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:4417 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,417 | train | mutant | 3,646 | 55 | 4,091 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E53H | E53H | 1 | 1 | 0 | 0 | 53 | E | H | 8 | ACTIVE_SITE|CONSERVATION | 4LYZ | 453 | null | 53 | A | H | true | false | 33.857927 | 5.92 | 8,376 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:E35H | null | null | 8.74 | 0.61 | null | null | null | 2.7 | 3.24 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 570 | ARTICLE | Stabilization of a protein by removal of unfavorable abnormal pKa: substitution of undissociable residue for glutamic acid-35 in chicken lysozyme. | 1,992 | 10.1021/bi00152a018 | 1390669 | Biochemistry;31;8816-21 | 5 | Yamada H|Hashimoto Y|Hamaguchi K|Inoue M|Yasukochi T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFF... | [{"datasets":[],"id":28458,"numValue":8.74,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28459,"numValue":0.61,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28460,"numValue":3.24,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28461,"numValue":2.7,"references":[],"... | [{"id":26,"numValue":null,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7156,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,418 | train | mutant | 611 | 55 | 662 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S | T58S | 1 | 1 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58 | A | S | true | false | 0.403113 | 5.998571 | 1,026 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T40S | 73.3 | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T40S","... | [{"datasets":[],"id":3826,"numValue":73.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3827,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3828,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4419 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,419 | train | mutant | 611 | 55 | 662 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S | T58S | 1 | 1 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58 | A | S | true | false | 0.403113 | 5.998571 | 6,598 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:T40S | null | null | null | 0.27 | 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 | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23571,"numValue":0.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23572,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4420 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,420 | train | mutant | 614 | 55 | 665 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58I | T58I | 1 | 1 | 0 | 0 | 58 | T | I | 9 | CONSERVATION | 4LYZ | 453 | null | 58 | A | S | true | false | 0.403113 | 5.998571 | 1,029 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T40I | 68.2 | -5.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T40I","... | [{"datasets":[],"id":3835,"numValue":68.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3836,"numValue":-5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3837,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,421 | train | mutant | 614 | 55 | 665 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58I | T58I | 1 | 1 | 0 | 0 | 58 | T | I | 9 | CONSERVATION | 4LYZ | 453 | null | 58 | A | S | true | false | 0.403113 | 5.998571 | 6,601 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:T40I | null | null | null | 2.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23577,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23578,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,422 | train | mutant | 6,786 | 55 | 7,428 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S|S109T | T58S|S109T | 2 | 2 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58|109 | A | S|H | true | false | 0.631488 | 6.164286 | 14,583 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T40S 4LYZ_A:S91T | 75.6 | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T40S 4L... | [{"datasets":[],"id":53930,"numValue":75.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53931,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53932,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4423 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,423 | train | mutant | 6,786 | 55 | 7,428 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S|S109T | T58S|S109T | 2 | 2 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58|109 | A | S|H | true | false | 0.631488 | 6.164286 | 14,872 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:T40S 4LYZ_A:S91T | null | null | null | -0.61 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54875,"numValue":-0.61,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54876,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4424 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,424 | train | mutant | 6,788 | 55 | 7,430 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S|I73V|S109T | T58S|I73V|S109T | 3 | 3 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58|73|109 | A | S|T|H | true | false | 1.316799 | 6.20619 | 14,585 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T40S 4LYZ_A:I55V 4LYZ_A:S91T | 73.2 | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T40S 4L... | [{"datasets":[],"id":53936,"numValue":73.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53937,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53938,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange"... | |||||||||||||
fireprotdb:4425 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,425 | train | mutant | 6,788 | 55 | 7,430 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S|I73V|S109T | T58S|I73V|S109T | 3 | 3 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58|73|109 | A | S|T|H | true | false | 1.316799 | 6.20619 | 14,874 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:T40S 4LYZ_A:I55V 4LYZ_A:S91T | null | null | null | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54879,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54880,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange"... | |||||||||||||
fireprotdb:4428 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,428 | train | mutant | 6,790 | 55 | 7,432 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S|S109A | T58S|S109A | 2 | 2 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58|109 | A | S|H | true | false | 0.631488 | 6.164286 | 14,587 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T40S 4LYZ_A:S91A | 71.7 | -2.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T40S 4L... | [{"datasets":[],"id":53942,"numValue":71.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53943,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53944,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,429 | train | mutant | 6,790 | 55 | 7,432 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S|S109A | T58S|S109A | 2 | 2 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58|109 | A | S|H | true | false | 0.631488 | 6.164286 | 14,876 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:T40S 4LYZ_A:S91A | null | null | null | 0.87 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54883,"numValue":0.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54884,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,431 | train | mutant | 6,793 | 55 | 7,435 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S|I73V | T58S|I73V | 2 | 2 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58|73 | A | S|T | true | false | 1.545266 | 6.144286 | 14,879 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:T40S 4LYZ_A:I55V | null | null | null | 1.33 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54889,"numValue":1.33,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54890,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4432 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,432 | train | mutant | 6,794 | 55 | 7,436 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58S|I73V|S109A | T58S|I73V|S109A | 3 | 3 | 0 | 0 | 58 | T | S | 9 | CONSERVATION | 4LYZ | 453 | null | 58|73|109 | A | S|T|H | true | false | 1.316799 | 6.20619 | 14,591 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T40S 4LYZ_A:I55V 4LYZ_A:S91A | 69.6 | -4.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T40S 4L... | [{"datasets":[],"id":53954,"numValue":69.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53955,"numValue":-4.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53956,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7161,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange"... | |||||||||||||
fireprotdb:4434 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,434 | train | mutant | 3,643 | 55 | 4,088 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N64D | N64D | 1 | 1 | 0 | 0 | 64 | N | D | 4 | CONSERVATION | 4LYZ | 453 | null | 64 | A | L | false | false | 70.494953 | 3.88125 | 8,357 | ProTherm | 3.5 | CD | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:N46D | null | null | 7.8 | -0.46 | null | null | null | 2.88 | 2.71 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 569 | ARTICLE | Left-sided substrate binding of lysozyme: evidence for the involvement of asparagine-46 in the initial binding of substrate to chicken lysozyme. | 1,992 | 10.1021/bi00157a021 | 1420152 | Biochemistry;31;10322-30 | 6 | Imoto T|Yamada H|Miki T|Inoue M|Yasukochi T|Horiuchi T | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFF... | [{"datasets":[],"id":28363,"numValue":7.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28364,"numValue":-0.46,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28365,"numValue":2.71,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28366,"numValue":2.88,"references":[],... | [{"id":7167,"numValue":4.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,435 | train | mutant | 3,643 | 55 | 4,088 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N64D | N64D | 1 | 1 | 0 | 0 | 64 | N | D | 4 | CONSERVATION | 4LYZ | 453 | null | 64 | A | L | false | false | 70.494953 | 3.88125 | 8,358 | ProTherm | 4 | CD | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:N46D | null | null | 8.86 | -0.03 | null | null | null | 3.27 | 2.71 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 569 | ARTICLE | Left-sided substrate binding of lysozyme: evidence for the involvement of asparagine-46 in the initial binding of substrate to chicken lysozyme. | 1,992 | 10.1021/bi00157a021 | 1420152 | Biochemistry;31;10322-30 | 6 | Imoto T|Yamada H|Miki T|Inoue M|Yasukochi T|Horiuchi T | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFF... | [{"datasets":[],"id":28368,"numValue":8.86,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28369,"numValue":-0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28370,"numValue":2.71,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28371,"numValue":3.27,"references":[]... | [{"id":7167,"numValue":4.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4436 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,436 | train | mutant | 3,643 | 55 | 4,088 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N64D | N64D | 1 | 1 | 0 | 0 | 64 | N | D | 4 | CONSERVATION | 4LYZ | 453 | null | 64 | A | L | false | false | 70.494953 | 3.88125 | 8,359 | ProTherm | 4.5 | CD | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:N46D | null | null | 9.3 | 0.69 | null | null | null | 3.43 | 2.71 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 569 | ARTICLE | Left-sided substrate binding of lysozyme: evidence for the involvement of asparagine-46 in the initial binding of substrate to chicken lysozyme. | 1,992 | 10.1021/bi00157a021 | 1420152 | Biochemistry;31;10322-30 | 6 | Imoto T|Yamada H|Miki T|Inoue M|Yasukochi T|Horiuchi T | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFF... | [{"datasets":[],"id":28373,"numValue":9.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":28374,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28375,"numValue":2.71,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28376,"numValue":3.43,... | [{"id":7167,"numValue":4.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4437 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,437 | train | mutant | 3,643 | 55 | 4,088 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N64D | N64D | 1 | 1 | 0 | 0 | 64 | N | D | 4 | CONSERVATION | 4LYZ | 453 | null | 64 | A | L | false | false | 70.494953 | 3.88125 | 8,360 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:N46D | null | null | 9.08 | 0.76 | null | null | null | 3.35 | 2.71 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 569 | ARTICLE | Left-sided substrate binding of lysozyme: evidence for the involvement of asparagine-46 in the initial binding of substrate to chicken lysozyme. | 1,992 | 10.1021/bi00157a021 | 1420152 | Biochemistry;31;10322-30 | 6 | Imoto T|Yamada H|Miki T|Inoue M|Yasukochi T|Horiuchi T | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFF... | [{"datasets":[],"id":28378,"numValue":9.08,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":28379,"numValue":0.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28380,"numValue":2.71,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28... | [{"id":7167,"numValue":4.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4440 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,440 | train | mutant | 50 | 55 | 56 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G67A | G67A | 1 | 1 | 0 | 0 | 67 | G | A | 5 | CONSERVATION | 4LYZ | 453 | null | 67 | A | S | false | false | 20.917358 | 5.1625 | 6,758 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 65.6 | 4LYZ_A:G49A | null | null | null | 1.89 | 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 | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":65.6,"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":23986,"numValue":1.89,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23987,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7170,"numValue":5.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4441 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,441 | train | mutant | 50 | 55 | 56 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G67A | G67A | 1 | 1 | 0 | 0 | 67 | G | A | 5 | CONSERVATION | 4LYZ | 453 | null | 67 | A | S | false | false | 20.917358 | 5.1625 | 8,350 | ProTherm | 5.5 | Fluorescence | GdnHCl | potassium phosphate | 0.05 M | 35 | 4LYZ_A:G49A | null | null | 8.48 | -1.92 | null | null | null | 3.01 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 566 | ARTICLE | Stabilization of lysozyme against irreversible inactivation by alterations of the Asp-Gly sequences. | 1,995 | 10.1093/protein/8.10.1023 | 8771183 | Protein Eng;8;1023-8 | 4 | Imoto T|Tomizawa H|Yamada H|Hashimoto Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05... | [{"datasets":[],"id":28336,"numValue":8.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":28337,"numValue":-1.92,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28338,"numValue":3.01,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28339,"numValue":n... | [{"id":7170,"numValue":5.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4442 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,442 | train | mutant | 5,874 | 55 | 6,444 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G67N | G67N | 1 | 1 | 0 | 0 | 67 | G | N | 5 | CONSERVATION | 4LYZ | 453 | null | 67 | A | S | false | false | 20.917358 | 5.1625 | 12,716 | ProTherm | 9.5 | CD | Thermal | sodium carbonate | 50 mM | 20 | 4LYZ_A:G49N | null | null | 11.71 | 0.96 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|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 | 819 | ARTICLE | Conformational changes in mutant lysozymes detected with monoclonal antibody. | 1,995 | 10.1016/0014-5793(95)00846-2 | 7664875 | FEBS Lett;371;17-20 | 3 | Kato A|Shimizu T|Saga S | [{"numValue":9.5,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium carbonate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":46117,"numValue":11.71,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":46118,"numValue":0.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46119,"numValue":null,"referenc... | [{"id":7170,"numValue":5.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4443 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,443 | train | mutant | 612 | 55 | 663 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73L | I73L | 1 | 1 | 0 | 0 | 73 | I | L | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 1,027 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55L | 72.8 | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55L","... | [{"datasets":[],"id":3829,"numValue":72.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3830,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3831,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4444 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,444 | train | mutant | 612 | 55 | 663 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73L | I73L | 1 | 1 | 0 | 0 | 73 | I | L | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 6,599 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55L | null | null | null | 0.45 | 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 | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23573,"numValue":0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23574,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4445 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,445 | train | mutant | 613 | 55 | 664 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73V | I73V | 1 | 1 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 1,028 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55V | 71.6 | -2.4 | 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 | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55V","... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":3832,"numValue":71.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":3833,"numValue":-2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.cs... | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4446 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,446 | train | mutant | 613 | 55 | 664 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73V | I73V | 1 | 1 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 6,600 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55V | null | null | null | 0.91 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23575,"numValue":0.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":23576,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4447 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,447 | train | mutant | 615 | 55 | 666 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73M | I73M | 1 | 1 | 0 | 0 | 73 | I | M | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 1,030 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55M | 68 | -6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55M","... | [{"datasets":[],"id":3838,"numValue":68.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3839,"numValue":-6.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3840,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4448 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,448 | train | mutant | 615 | 55 | 666 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73M | I73M | 1 | 1 | 0 | 0 | 73 | I | M | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 6,602 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55M | null | null | null | 2.27 | 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 | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23579,"numValue":2.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23580,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4449 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,449 | train | mutant | 617 | 55 | 668 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73F | I73F | 1 | 1 | 0 | 0 | 73 | I | F | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 1,032 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55F | 67.5 | -6.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55F","... | [{"datasets":[],"id":3844,"numValue":67.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3845,"numValue":-6.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3846,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4451 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,451 | train | mutant | 619 | 55 | 670 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73A | I73A | 1 | 1 | 0 | 0 | 73 | I | A | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 1,034 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55A | 62.4 | -11.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55A","... | [{"datasets":[],"id":3850,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3851,"numValue":-11.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3852,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4453 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,453 | train | mutant | 620 | 55 | 671 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73T | I73T | 1 | 1 | 0 | 0 | 73 | I | T | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 1,035 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55T | 60.9 | -13.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|EASE-MM_S1676.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55T","... | [{"datasets":[],"id":3853,"numValue":60.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3854,"numValue":-13.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","... | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4454 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,454 | train | mutant | 620 | 55 | 671 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73T | I73T | 1 | 1 | 0 | 0 | 73 | I | T | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 6,607 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55T | null | null | null | 4.96 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23589,"numValue":4.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23590,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4455 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,455 | train | mutant | 620 | 55 | 671 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73T | I73T | 1 | 1 | 0 | 0 | 73 | I | T | 8 | CONSERVATION | 4LYZ | 453 | null | 73 | A | T | true | false | 2.687419 | 6.29 | 8,868 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 0.1 M | 25 | 4LYZ_A:I55T | null | null | 6.9 | 3.3 | null | null | null | 2.57 | 2.6 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":5.0,"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFF... | [{"datasets":[],"id":30039,"numValue":6.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30040,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30041,"numValue":2.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30042,"numValue":2.57,"... | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4456 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,456 | train | mutant | 6,785 | 55 | 7,427 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73L|S109T | I73L|S109T | 2 | 2 | 0 | 0 | 73 | I | L | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,582 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55L 4LYZ_A:S91T | 77.3 | 3.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55L 4L... | [{"datasets":[],"id":53927,"numValue":77.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53928,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53929,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4457 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,457 | train | mutant | 6,785 | 55 | 7,427 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73L|S109T | I73L|S109T | 2 | 2 | 0 | 0 | 73 | I | L | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,871 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55L 4LYZ_A:S91T | null | null | null | -1.25 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54873,"numValue":-1.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54874,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4458 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,458 | train | mutant | 6,787 | 55 | 7,429 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73V|S109T | I73V|S109T | 2 | 2 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,584 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55V 4LYZ_A:S91T | 74 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55V 4L... | [{"datasets":[],"id":53933,"numValue":74.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53934,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53935,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4459 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,459 | train | mutant | 6,787 | 55 | 7,429 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73V|S109T | I73V|S109T | 2 | 2 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,873 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55V 4LYZ_A:S91T | null | null | null | 0 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54877,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54878,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4460 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,460 | train | mutant | 6,791 | 55 | 7,433 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73V|S109A | I73V|S109A | 2 | 2 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,588 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55V 4LYZ_A:S91A | 70.7 | -3.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55V 4L... | [{"datasets":[],"id":53945,"numValue":70.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53946,"numValue":-3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53947,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4461 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,461 | train | mutant | 6,791 | 55 | 7,433 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73V|S109A | I73V|S109A | 2 | 2 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,877 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55V 4LYZ_A:S91A | null | null | null | 1.25 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54885,"numValue":1.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54886,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4462 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,462 | train | mutant | 6,792 | 55 | 7,434 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73V|S109V | I73V|S109V | 2 | 2 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,589 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55V 4LYZ_A:S91V | 70.7 | -3.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55V 4L... | [{"datasets":[],"id":53948,"numValue":70.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53949,"numValue":-3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53950,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4463 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,463 | train | mutant | 6,792 | 55 | 7,434 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73V|S109V | I73V|S109V | 2 | 2 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,878 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55V 4LYZ_A:S91V | null | null | null | 1.25 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54887,"numValue":1.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54888,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4464 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,464 | train | mutant | 6,795 | 55 | 7,437 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73A|S109T | I73A|S109T | 2 | 2 | 0 | 0 | 73 | I | A | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,592 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:I55A 4LYZ_A:S91T | 66.7 | -7.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:I55A 4L... | [{"datasets":[],"id":53957,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53958,"numValue":-7.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53959,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4465 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,465 | train | mutant | 6,795 | 55 | 7,437 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I73A|S109T | I73A|S109T | 2 | 2 | 0 | 0 | 73 | I | A | 8 | CONSERVATION | 4LYZ | 453 | null | 73|109 | A | T|H | true | false | 1.773641 | 6.31 | 14,881 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:I55A 4LYZ_A:S91T | null | null | null | 2.77 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":54893,"numValue":2.77,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54894,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7176,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4466 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,466 | train | mutant | 3,638 | 55 | 4,083 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I76M | I76M | 1 | 1 | 0 | 0 | 76 | I | M | 9 | CONSERVATION | 4LYZ | 453 | null | 76 | A | E | true | false | 3.762386 | 6.0025 | 8,352 | ProTherm | 5.5 | Fluorescence | GdnHCl | sodium acetate | 0.1 M | 35 | HCl | 4LYZ_A:I58M | null | null | null | 1.18 | null | null | null | 2.98 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|_PDB_CHAIN_MUTATION | 567 | ARTICLE | Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme. | 2,001 | 10.1093/protein/14.6.421 | 11477222 | Protein Eng;14;421-5 | 4 | Ueda T|Imoto T|Ohmura T|Hashimoto Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":["SAAFEC_S1262.csv"],"id":28344,"numValue":1.18,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28345,"numValue":2.98,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28346,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7179,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:4467 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,467 | train | mutant | 6,954 | 55 | 7,605 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C82A|C98A | C82A|C98A | 2 | 2 | 0 | 0 | 82 | C | A | 9 | CONSERVATION | 4LYZ | 453 | null | 82|98 | A | L|G | true | false | 0.322747 | 7.54 | 14,812 | ProTherm | 3 | DSC | Thermal | Sodium acetate | 0.1 M | null | 4LYZ_A:C64A 4LYZ_A:C80A | 37.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 918 | ARTICLE | The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge. | 2,000 | 10.1006/jmbi.1999.3442 | 10653703 | J Mol Biol;295;1275-88 | 7 | Yokota A|Izutani K|Takai M|Kubo Y|Noda Y|Koumoto Y|Tachibana H | [{"numValue":3.0,"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":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:C64A 4LYZ_A... | [{"datasets":[],"id":54698,"numValue":37.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54699,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7185,"numValue":9.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7201,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4468 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,468 | train | mutant | 6,954 | 55 | 7,605 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C82A|C98A | C82A|C98A | 2 | 2 | 0 | 0 | 82 | C | A | 9 | CONSERVATION | 4LYZ | 453 | null | 82|98 | A | L|G | true | false | 0.322747 | 7.54 | 14,816 | ProTherm | 3.9 | DSC | Thermal | Sodium acetate | 0.1 M | null | 4LYZ_A:C64A 4LYZ_A:C80A | 47.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 918 | ARTICLE | The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge. | 2,000 | 10.1006/jmbi.1999.3442 | 10653703 | J Mol Biol;295;1275-88 | 7 | Yokota A|Izutani K|Takai M|Kubo Y|Noda Y|Koumoto Y|Tachibana H | [{"numValue":3.9,"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":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:C64A 4LYZ_A... | [{"datasets":[],"id":54706,"numValue":47.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54707,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7185,"numValue":9.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7201,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4469 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,469 | train | mutant | 51 | 55 | 57 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G85A | G85A | 1 | 1 | 0 | 0 | 85 | G | A | 3 | CONSERVATION | 4LYZ | 453 | null | 85 | A | S | false | false | 72.112759 | 6.0575 | 65 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 4LYZ_A:G67A | 62.7 | -2.9 | null | null | 115.92 | 1.74 | 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 | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:G67A","type":"_PD... | [{"datasets":[],"id":216,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":217,"numValue":-2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":218,"numValue":115.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":... | [{"id":7188,"numValue":3.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4470 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,470 | train | mutant | 51 | 55 | 57 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G85A | G85A | 1 | 1 | 0 | 0 | 85 | G | A | 3 | CONSERVATION | 4LYZ | 453 | null | 85 | A | S | false | false | 72.112759 | 6.0575 | 6,759 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 65.6 | 4LYZ_A:G67A | null | null | null | 0.98 | 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 | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":65.6,"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":23988,"numValue":0.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23989,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7188,"numValue":3.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4471 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,471 | train | mutant | 51 | 55 | 57 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G85A | G85A | 1 | 1 | 0 | 0 | 85 | G | A | 3 | CONSERVATION | 4LYZ | 453 | null | 85 | A | S | false | false | 72.112759 | 6.0575 | 8,351 | ProTherm | 5.5 | Fluorescence | GdnHCl | potassium phosphate | 0.05 M | 35 | 4LYZ_A:G67A | null | null | 9.13 | -1.27 | null | null | null | 3.24 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 566 | ARTICLE | Stabilization of lysozyme against irreversible inactivation by alterations of the Asp-Gly sequences. | 1,995 | 10.1093/protein/8.10.1023 | 8771183 | Protein Eng;8;1023-8 | 4 | Imoto T|Tomizawa H|Yamada H|Hashimoto Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05... | [{"datasets":[],"id":28340,"numValue":9.13,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":28341,"numValue":-1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28342,"numValue":3.24,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28343,"numValue":n... | [{"id":7188,"numValue":3.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4472 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,472 | train | mutant | 589 | 55 | 640 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R86K | R86K | 1 | 1 | 0 | 0 | 86 | R | K | 3 | CONSERVATION | 4LYZ | 453 | null | 86 | A | S | false | false | 116.38812 | 6.15 | 1,004 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:R68K | 73.9 | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.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_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|Saraboji_S1791.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:R68K","... | [{"datasets":[],"id":3760,"numValue":73.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.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_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv"... | [{"id":7189,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4473 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,473 | train | mutant | 589 | 55 | 640 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R86K | R86K | 1 | 1 | 0 | 0 | 86 | R | K | 3 | CONSERVATION | 4LYZ | 453 | null | 86 | A | S | false | false | 116.38812 | 6.15 | 6,576 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:R68K | null | null | null | 0.04 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23508,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23509,"numValue":0.04,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23510,"numValue":null,"referenc... | [{"id":7189,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4474 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,474 | train | mutant | 5,875 | 55 | 6,445 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P88N | P88N | 1 | 1 | 0 | 0 | 88 | P | N | 1 | CONSERVATION | 4LYZ | 453 | null | 88 | A | T | false | false | 124.587302 | 4.788571 | 12,717 | ProTherm | 9.5 | CD | Thermal | sodium carbonate | 50 mM | 20 | 4LYZ_A:P70N | null | null | 10.52 | 2.15 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|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 | 819 | ARTICLE | Conformational changes in mutant lysozymes detected with monoclonal antibody. | 1,995 | 10.1016/0014-5793(95)00846-2 | 7664875 | FEBS Lett;371;17-20 | 3 | Kato A|Shimizu T|Saga S | [{"numValue":9.5,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium carbonate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":46120,"numValue":10.52,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":46121,"numValue":2.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46122,"numValue":null,"referenc... | [{"id":7191,"numValue":1.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4475 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,475 | train | mutant | 6,994 | 55 | 7,646 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P88G|G89P | P88G|G89P | 2 | 2 | 0 | 0 | 88 | P | G | 1 | CONSERVATION | 4LYZ | 453 | null | 88|89 | A | T | false | false | 79.09645 | 4.408036 | 15,132 | ProTherm | 5.5 | Fluorescence | GdnHCl | acetate | 0.1 M | 35 | 4LYZ_A:P70G 4LYZ_A:G71P | null | null | 8.8 | 1 | null | null | null | 3.25 | 2.7 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 572 | ARTICLE | Correlation between the differences in the free energy change and conformational energy in the folded state of hen lysozymes with Gly-Pro and Pro-Gly sequences introduced to the same site. | 1,995 | 10.1093/oxfordjournals.jbchem.a124999 | 8720127 | J Biochem;118;1138-44 | 5 | Ueda T|Motoshima H|Imoto T|Hashimoto Y|Tsutsumi M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"B... | [{"datasets":[],"id":55514,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55515,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55516,"numValue":2.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55517,"numValue":3.25,"references":[],"st... | [{"id":7191,"numValue":1.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7192,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4476 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,476 | train | mutant | 52 | 55 | 58 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G89A | G89A | 1 | 1 | 0 | 0 | 89 | G | A | 1 | CONSERVATION | 4LYZ | 453 | null | 89 | A | T | false | false | 33.605598 | 4.0275 | 66 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 4LYZ_A:G71A | 64.4 | -1.2 | null | null | 111.85 | 2.29 | 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 | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:G71A","type":"_PD... | [{"datasets":[],"id":221,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":222,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":223,"numValue":111.85,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":... | [{"id":7192,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4477 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,477 | train | mutant | 52 | 55 | 58 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G89A | G89A | 1 | 1 | 0 | 0 | 89 | G | A | 1 | CONSERVATION | 4LYZ | 453 | null | 89 | A | T | false | false | 33.605598 | 4.0275 | 6,760 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 65.6 | 4LYZ_A:G71A | null | null | null | 0.38 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":65.6,"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":23990,"numValue":0.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23991,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7192,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4478 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,478 | train | mutant | 590 | 55 | 641 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R91K | R91K | 1 | 1 | 0 | 0 | 91 | R | K | 4 | CONSERVATION | 4LYZ | 453 | null | 91 | A | L | false | false | 152.638706 | 3.116364 | 1,005 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:R73K | 74.6 | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:R73K","... | [{"datasets":[],"id":3763,"numValue":74.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3764,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3765,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7194,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4479 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,479 | train | mutant | 590 | 55 | 641 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R91K | R91K | 1 | 1 | 0 | 0 | 91 | R | K | 4 | CONSERVATION | 4LYZ | 453 | null | 91 | A | L | false | false | 152.638706 | 3.116364 | 6,577 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:R73K | null | null | null | -0.23 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23511,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23512,"numValue":-0.23,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23513,"numValue":null,"referen... | [{"id":7194,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4480 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,480 | train | mutant | 6,955 | 55 | 7,606 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C94A|C112A | C94A|C112A | 2 | 2 | 0 | 0 | 94 | C | A | 9 | CONSERVATION | 4LYZ | 453 | null | 94|112 | A | S|H | true | false | 12.615633 | 8.2775 | 14,813 | ProTherm | 2.9 | DSC | Thermal | Sodium acetate | 0.1 M | null | 4LYZ_A:C76A 4LYZ_A:C94A | 41.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 918 | ARTICLE | The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge. | 2,000 | 10.1006/jmbi.1999.3442 | 10653703 | J Mol Biol;295;1275-88 | 7 | Yokota A|Izutani K|Takai M|Kubo Y|Noda Y|Koumoto Y|Tachibana H | [{"numValue":2.9,"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":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:C76A 4LYZ_A... | [{"datasets":[],"id":54700,"numValue":41.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54701,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7197,"numValue":9.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7215,"numValue":9.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4481 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,481 | train | mutant | 6,955 | 55 | 7,606 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C94A|C112A | C94A|C112A | 2 | 2 | 0 | 0 | 94 | C | A | 9 | CONSERVATION | 4LYZ | 453 | null | 94|112 | A | S|H | true | false | 12.615633 | 8.2775 | 14,817 | ProTherm | 3.9 | DSC | Thermal | Sodium acetate | 0.1 M | null | 4LYZ_A:C76A 4LYZ_A:C94A | 51.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 918 | ARTICLE | The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge. | 2,000 | 10.1006/jmbi.1999.3442 | 10653703 | J Mol Biol;295;1275-88 | 7 | Yokota A|Izutani K|Takai M|Kubo Y|Noda Y|Koumoto Y|Tachibana H | [{"numValue":3.9,"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":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:C76A 4LYZ_A... | [{"datasets":[],"id":54708,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54709,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7197,"numValue":9.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7215,"numValue":9.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4482 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,482 | train | mutant | 591 | 55 | 642 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N95H | N95H | 1 | 1 | 0 | 0 | 95 | N | H | 4 | CONSERVATION | 4LYZ | 453 | null | 95 | A | L | false | false | 126.002624 | 5.08625 | 1,006 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:N77H | 73 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:N77H","... | [{"datasets":[],"id":3766,"numValue":73.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3767,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3768,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7198,"numValue":4.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4484 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,484 | train | mutant | 3,639 | 55 | 4,084 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I96M | I96M | 1 | 1 | 0 | 0 | 96 | I | M | 6 | CONSERVATION | 4LYZ | 453 | null | 96 | A | S | true | false | 52.530151 | 5.06125 | 8,353 | ProTherm | 5.5 | Fluorescence | GdnHCl | sodium acetate | 0.1 M | 35 | HCl | 4LYZ_A:I78M | null | null | null | 0.9 | null | null | null | 3.08 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|_PDB_CHAIN_MUTATION | 567 | ARTICLE | Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme. | 2,001 | 10.1093/protein/14.6.421 | 11477222 | Protein Eng;14;421-5 | 4 | Ueda T|Imoto T|Ohmura T|Hashimoto Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":["SAAFEC_S1262.csv"],"id":28347,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28348,"numValue":3.08,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28349,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7199,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:4485 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,485 | train | mutant | 6,944 | 55 | 7,586 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T107A|N111A|I116A|S118A | T107A|N111A|I116A|S118A | 4 | 4 | 0 | 0 | 107 | T | A | 4 | CONSERVATION | 4LYZ | 453 | null | 107|111|116|118 | A | H|T | true | false | 44.220051 | 6.211801 | 14,802 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T89A 4LYZ_A:N93A 4LYZ_A:I98A 4LYZ_A:S100A | 66 | 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 | 916 | ARTICLE | Role of the minor energetic determinants of chicken egg white lysozyme (HEWL) to the stability of the HEWL.antibody scFv-10 complex. | 2,000 | 10813830 | Proteins;40;49-57 | 2 | Rajpal A|Kirsch J F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T89A 4L... | [{"datasets":[],"id":54674,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54675,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7210,"numValue":4.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7214,"numValue":1.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7219,"numValue":8.0,"position":116,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:4486 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,486 | train | mutant | 6,947 | 55 | 7,589 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T107A|N111A|S118A | T107A|N111A|S118A | 3 | 3 | 0 | 0 | 107 | T | A | 4 | CONSERVATION | 4LYZ | 453 | null | 107|111|118 | A | H|T | true | false | 55.708438 | 6.073234 | 14,805 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T89A 4LYZ_A:N93A 4LYZ_A:S100A | 74.6 | 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 | 916 | ARTICLE | Role of the minor energetic determinants of chicken egg white lysozyme (HEWL) to the stability of the HEWL.antibody scFv-10 complex. | 2,000 | 10813830 | Proteins;40;49-57 | 2 | Rajpal A|Kirsch J F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T89A 4L... | [{"datasets":[],"id":54680,"numValue":74.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54681,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7210,"numValue":4.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7214,"numValue":1.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7221,"numValue":3.0,"position":118,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:4487 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,487 | train | mutant | 6,948 | 55 | 7,590 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T107A|N111A|I116A | T107A|N111A|I116A | 3 | 3 | 0 | 0 | 107 | T | A | 4 | CONSERVATION | 4LYZ | 453 | null | 107|111|116 | A | H | true | false | 48.393287 | 6.361845 | 14,806 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:T89A 4LYZ_A:N93A 4LYZ_A:I98A | 66.9 | 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 | 916 | ARTICLE | Role of the minor energetic determinants of chicken egg white lysozyme (HEWL) to the stability of the HEWL.antibody scFv-10 complex. | 2,000 | 10813830 | Proteins;40;49-57 | 2 | Rajpal A|Kirsch J F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:T89A 4L... | [{"datasets":[],"id":54682,"numValue":66.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54683,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7210,"numValue":4.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7214,"numValue":1.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7219,"numValue":8.0,"position":116,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:4489 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,489 | train | mutant | 608 | 55 | 659 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S109T | S109T | 1 | 1 | 0 | 0 | 109 | S | T | 7 | CONSERVATION | 4LYZ | 453 | null | 109 | A | H | true | false | 0.859864 | 6.33 | 6,595 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:S91T | null | null | null | -0.99 | 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 | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23565,"numValue":-0.99,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23566,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4490 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,490 | train | mutant | 609 | 55 | 660 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S109V | S109V | 1 | 1 | 0 | 0 | 109 | S | V | 7 | CONSERVATION | 4LYZ | 453 | null | 109 | A | H | true | false | 0.859864 | 6.33 | 1,024 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:S91V | 73.8 | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|HotMuSiC_S1626.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:S91V","... | [{"datasets":[],"id":3820,"numValue":73.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":3821,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":3822,"numValue":null,"references":[],"strVal... | [{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4491 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,491 | train | mutant | 609 | 55 | 660 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S109V | S109V | 1 | 1 | 0 | 0 | 109 | S | V | 7 | CONSERVATION | 4LYZ | 453 | null | 109 | A | H | true | false | 0.859864 | 6.33 | 6,596 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:S91V | null | null | null | 0.08 | 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 | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23567,"numValue":0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23568,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4494 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,494 | train | mutant | 616 | 55 | 667 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S109D | S109D | 1 | 1 | 0 | 0 | 109 | S | D | 7 | CONSERVATION | 4LYZ | 453 | null | 109 | A | H | true | false | 0.859864 | 6.33 | 1,031 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:S91D | 67.9 | -6.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:S91D","... | [{"datasets":[],"id":3841,"numValue":67.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3842,"numValue":-6.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3843,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4495 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,495 | train | mutant | 616 | 55 | 667 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S109D | S109D | 1 | 1 | 0 | 0 | 109 | S | D | 7 | CONSERVATION | 4LYZ | 453 | null | 109 | A | H | true | false | 0.859864 | 6.33 | 6,603 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:S91D | null | null | null | 2.31 | 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 | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23581,"numValue":2.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23582,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4497 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,497 | train | mutant | 618 | 55 | 669 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S109Y | S109Y | 1 | 1 | 0 | 0 | 109 | S | Y | 7 | CONSERVATION | 4LYZ | 453 | null | 109 | A | H | true | false | 0.859864 | 6.33 | 6,605 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:S91Y | null | null | null | 3.07 | 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 | 105 | ARTICLE | Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. | 1,995 | 10.1002/pro.5560041010 | 8535241 | Protein Sci;4;2050-62 | 3 | Shih P|Kirsch J F|Holland D R | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23585,"numValue":3.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23586,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7212,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4498 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,498 | train | mutant | 6,946 | 55 | 7,588 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N111A|I116A|S118A | N111A|I116A|S118A | 3 | 3 | 0 | 0 | 111 | N | A | 1 | CONSERVATION | 4LYZ | 453 | null | 111|116|118 | A | H|T | true | false | 41.07122 | 6.187639 | 14,804 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:N93A 4LYZ_A:I98A 4LYZ_A:S100A | 65.4 | 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 | 916 | ARTICLE | Role of the minor energetic determinants of chicken egg white lysozyme (HEWL) to the stability of the HEWL.antibody scFv-10 complex. | 2,000 | 10813830 | Proteins;40;49-57 | 2 | Rajpal A|Kirsch J F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:N93A 4L... | [{"datasets":[],"id":54678,"numValue":65.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54679,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7214,"numValue":1.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7219,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7221,"numValue":3.0,"position":118,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:4499 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,499 | train | mutant | 5,876 | 55 | 6,446 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C112A | C112A | 1 | 1 | 0 | 0 | 112 | C | A | 9 | CONSERVATION | 4LYZ | 453 | null | 112 | A | H | true | false | 3.090532 | 8.298333 | 12,718 | ProTherm | 9.5 | CD | Thermal | sodium carbonate | 50 mM | 20 | 4LYZ_A:C94A | null | null | 7.89 | 4.78 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|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 | 819 | ARTICLE | Conformational changes in mutant lysozymes detected with monoclonal antibody. | 1,995 | 10.1016/0014-5793(95)00846-2 | 7664875 | FEBS Lett;371;17-20 | 3 | Kato A|Shimizu T|Saga S | [{"numValue":9.5,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium carbonate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":46123,"numValue":7.89,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":46124,"numValue":4.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46125,"numValue":null,"reference... | [{"id":7215,"numValue":9.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4500 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,500 | train | mutant | 3,640 | 55 | 4,085 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I116M | I116M | 1 | 1 | 0 | 0 | 116 | I | M | 8 | CONSERVATION | 4LYZ | 453 | null | 116 | A | H | false | false | 9.75489 | 6.6275 | 8,354 | ProTherm | 5.5 | Fluorescence | GdnHCl | sodium acetate | 0.1 M | 35 | HCl | 4LYZ_A:I98M | null | null | null | 0.9 | null | null | null | 3.08 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|_PDB_CHAIN_MUTATION | 567 | ARTICLE | Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme. | 2,001 | 10.1093/protein/14.6.421 | 11477222 | Protein Eng;14;421-5 | 4 | Ueda T|Imoto T|Ohmura T|Hashimoto Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":["SAAFEC_S1262.csv"],"id":28350,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28351,"numValue":3.08,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28352,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7219,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:4501 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,501 | train | mutant | 592 | 55 | 643 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119G | D119G | 1 | 1 | 0 | 0 | 119 | D | G | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 1,007 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:D101G | 75.2 | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:D101G",... | [{"datasets":[],"id":3769,"numValue":75.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3770,"numValue":1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3771,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4502 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,502 | train | mutant | 592 | 55 | 643 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119G | D119G | 1 | 1 | 0 | 0 | 119 | D | G | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 6,579 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:D101G | null | null | null | -0.45 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23517,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23518,"numValue":-0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23519,"n... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4503 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,503 | train | mutant | 600 | 55 | 651 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119S | D119S | 1 | 1 | 0 | 0 | 119 | D | S | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 1,015 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:D101S | 76.3 | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:D101S",... | [{"datasets":[],"id":3793,"numValue":76.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3794,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3795,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4504 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,504 | train | mutant | 600 | 55 | 651 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119S | D119S | 1 | 1 | 0 | 0 | 119 | D | S | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 6,587 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:D101S | null | null | null | -0.87 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23541,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23542,"numValue":-0.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23543,"numValue":null,"referen... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4505 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,505 | train | mutant | 601 | 55 | 652 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119A | D119A | 1 | 1 | 0 | 0 | 119 | D | A | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 1,016 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:D101A | 76 | 2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|HotMuSiC_S1626.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:D101A",... | [{"datasets":[],"id":3796,"numValue":76.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":3797,"numValue":2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3798,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4507 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,507 | train | mutant | 602 | 55 | 653 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119F | D119F | 1 | 1 | 0 | 0 | 119 | D | F | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 1,017 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:D101F | 75.9 | 1.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:D101F",... | [{"datasets":["HotMuSiC_S1626.csv"],"id":3799,"numValue":75.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3800,"numValue":1.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3801,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4508 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,508 | train | mutant | 602 | 55 | 653 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119F | D119F | 1 | 1 | 0 | 0 | 119 | D | F | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 6,589 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:D101F | null | null | null | -0.72 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23547,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23548,"numValue":-0.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23549,"numValue":null,"referen... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4509 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,509 | train | mutant | 603 | 55 | 654 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119R | D119R | 1 | 1 | 0 | 0 | 119 | D | R | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 1,018 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:D101R | 74.7 | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:D101R",... | [{"datasets":[],"id":3802,"numValue":74.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3803,"numValue":0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3804,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4510 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,510 | train | mutant | 603 | 55 | 654 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119R | D119R | 1 | 1 | 0 | 0 | 119 | D | R | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 6,590 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:D101R | null | null | null | -0.27 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23550,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23551,"numValue":-0.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23552,"numValue":null,"referen... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4513 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,513 | train | mutant | 605 | 55 | 656 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119N | D119N | 1 | 1 | 0 | 0 | 119 | D | N | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 1,020 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:D101N | 74.1 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:D101N",... | [{"datasets":[],"id":3808,"numValue":74.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3809,"numValue":0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3810,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,514 | train | mutant | 605 | 55 | 656 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119N | D119N | 1 | 1 | 0 | 0 | 119 | D | N | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 6,592 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:D101N | null | null | null | -0.04 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23556,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23557,"numValue":-0.04,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23558,"n... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,516 | train | mutant | 606 | 55 | 657 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119E | D119E | 1 | 1 | 0 | 0 | 119 | D | E | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 6,593 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:D101E | null | null | null | 0 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23559,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23560,"numValue":0.0,"refer... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4517 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,517 | train | mutant | 607 | 55 | 658 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119Q | D119Q | 1 | 1 | 0 | 0 | 119 | D | Q | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 1,022 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:D101Q | 73.8 | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:D101Q",... | [{"datasets":[],"id":3814,"numValue":73.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3815,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3816,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4518 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,518 | train | mutant | 607 | 55 | 658 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119Q | D119Q | 1 | 1 | 0 | 0 | 119 | D | Q | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 6,594 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:D101Q | null | null | null | 0.08 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23562,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23563,"numValue":0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23564,"numValue":null,"referenc... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,519 | train | mutant | 3,641 | 55 | 4,086 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119P | D119P | 1 | 1 | 0 | 0 | 119 | D | P | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119 | A | T | false | false | 95.265192 | 3.10125 | 8,355 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.1 M | 35 | 4LYZ_A:D101P | null | null | 7.7 | 2.4 | null | null | null | 2.7 | 2.7 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 568 | ARTICLE | Stabilization of lysozyme by the introduction of Gly-Pro sequence. | 1,993 | 10.1093/protein/6.2.183 | 8475043 | Protein Eng;6;183-7 | 7 | Ueda T|Imoto T|Yamada H|Hashimoto Y|Tamura T|Maeda Y|Miki T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC... | [{"datasets":[],"id":28353,"numValue":7.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":28354,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28355,"numValue":2.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28356,"numValue":2.7,"r... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4520 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,520 | train | mutant | 6,993 | 55 | 7,645 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D119G|G120P | D119G|G120P | 2 | 2 | 0 | 0 | 119 | D | G | 4 | BINDING_SITE|CONSERVATION | 4LYZ | 453 | null | 119|120 | A | T|S | false | false | 78.276238 | 4.253125 | 15,131 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.1 M | 35 | 4LYZ_A:D101G 4LYZ_A:G102P | null | null | 11 | -0.9 | null | null | null | 3.95 | 2.8 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 568 | ARTICLE | Stabilization of lysozyme by the introduction of Gly-Pro sequence. | 1,993 | 10.1093/protein/6.2.183 | 8475043 | Protein Eng;6;183-7 | 7 | Ueda T|Imoto T|Yamada H|Hashimoto Y|Tamura T|Maeda Y|Miki T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC... | [{"datasets":[],"id":55509,"numValue":11.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55510,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55511,"numValue":2.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55512,"numValue":3.95,"references":[],"... | [{"id":28,"numValue":null,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7222,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7223,"numValue":3.0,"position":120,"positionArray":null,"positionRange... | |||||||||||||
fireprotdb:4521 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,521 | train | mutant | 53 | 55 | 59 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G120A | G120A | 1 | 1 | 0 | 0 | 120 | G | A | 3 | CONSERVATION | 4LYZ | 453 | null | 120 | A | S | false | false | 61.287284 | 5.405 | 67 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 4LYZ_A:G102A | 65.6 | 0 | null | null | 113.29 | 2.01 | 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 | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:G102A","type":"_P... | [{"datasets":[],"id":226,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":227,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":228,"numValue":113.29,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2... | [{"id":7223,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,523 | train | mutant | 593 | 55 | 644 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G120V | G120V | 1 | 1 | 0 | 0 | 120 | G | V | 3 | CONSERVATION | 4LYZ | 453 | null | 120 | A | S | false | false | 61.287284 | 5.405 | 1,008 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:G102V | 73.9 | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:G102V",... | [{"datasets":[],"id":3772,"numValue":73.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3773,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3774,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7223,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4524 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,524 | train | mutant | 593 | 55 | 644 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G120V | G120V | 1 | 1 | 0 | 0 | 120 | G | V | 3 | CONSERVATION | 4LYZ | 453 | null | 120 | A | S | false | false | 61.287284 | 5.405 | 6,580 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:G102V | null | null | null | 0.04 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23520,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23521,"numValue":0.04,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23522,"numValue":null,"referenc... | [{"id":7223,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4525 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,525 | train | mutant | 594 | 55 | 645 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G120R | G120R | 1 | 1 | 0 | 0 | 120 | G | R | 3 | CONSERVATION | 4LYZ | 453 | null | 120 | A | S | false | false | 61.287284 | 5.405 | 1,009 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:G102R | 75 | 1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:G102R",... | [{"datasets":[],"id":3775,"numValue":75.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3776,"numValue":1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3777,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7223,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4527 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,527 | train | mutant | 3,642 | 55 | 4,087 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G120P | G120P | 1 | 1 | 0 | 0 | 120 | G | P | 3 | CONSERVATION | 4LYZ | 453 | null | 120 | A | S | false | false | 61.287284 | 5.405 | 8,356 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.1 M | 35 | 4LYZ_A:G102P | null | null | 10 | 0.1 | null | null | null | 3.5 | 2.7 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 568 | ARTICLE | Stabilization of lysozyme by the introduction of Gly-Pro sequence. | 1,993 | 10.1093/protein/6.2.183 | 8475043 | Protein Eng;6;183-7 | 7 | Ueda T|Imoto T|Yamada H|Hashimoto Y|Tamura T|Maeda Y|Miki T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC... | [{"datasets":[],"id":28358,"numValue":10.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":28359,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28360,"numValue":2.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":2836... | [{"id":7223,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,528 | train | mutant | 6,992 | 55 | 7,644 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G120A|G122A | G120A|G122A | 2 | 2 | 0 | 0 | 120 | G | A | 3 | CONSERVATION | 4LYZ | 453 | null | 120|122 | A | S|G | false | false | 35.402996 | 5.8475 | 15,130 | ProTherm | 5.5 | Fluorescence | GdnHCl | potassium phosphate | 0.05 M | 35 | 4LYZ_A:G102A 4LYZ_A:G104A | null | null | 8.4 | -2 | null | null | null | 2.98 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 566 | ARTICLE | Stabilization of lysozyme against irreversible inactivation by alterations of the Asp-Gly sequences. | 1,995 | 10.1093/protein/8.10.1023 | 8771183 | Protein Eng;8;1023-8 | 4 | Imoto T|Tomizawa H|Yamada H|Hashimoto Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05... | [{"datasets":[],"id":55505,"numValue":8.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55506,"numValue":-2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55507,"numValue":2.98,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":55508,"numValue":null,"references":[],... | [{"id":7223,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7225,"numValue":8.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4529 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,529 | train | mutant | 5,877 | 55 | 6,447 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N121D | N121D | 1 | 1 | 0 | 0 | 121 | N | D | 4 | CONSERVATION | 4LYZ | 453 | null | 121 | A | S | false | false | 100.736508 | 4.9575 | 12,719 | ProTherm | 9.5 | CD | Thermal | sodium carbonate | 50 mM | 20 | 4LYZ_A:N103D | null | null | 12.91 | -0.24 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|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 | 819 | ARTICLE | Conformational changes in mutant lysozymes detected with monoclonal antibody. | 1,995 | 10.1016/0014-5793(95)00846-2 | 7664875 | FEBS Lett;371;17-20 | 3 | Kato A|Shimizu T|Saga S | [{"numValue":9.5,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium carbonate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":46126,"numValue":12.91,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":46127,"numValue":-0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46128,"numValue":null,"referen... | [{"id":7224,"numValue":4.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,530 | train | mutant | 5,878 | 55 | 6,448 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | M123T | M123T | 1 | 1 | 0 | 0 | 123 | M | T | 7 | CONSERVATION | 4LYZ | 453 | null | 123 | A | G | true | false | 0 | 7.53625 | 12,720 | ProTherm | 9.5 | CD | Thermal | sodium carbonate | 50 mM | 20 | 4LYZ_A:M105T | null | null | 12.43 | 0.24 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|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 | 819 | ARTICLE | Conformational changes in mutant lysozymes detected with monoclonal antibody. | 1,995 | 10.1016/0014-5793(95)00846-2 | 7664875 | FEBS Lett;371;17-20 | 3 | Kato A|Shimizu T|Saga S | [{"numValue":9.5,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium carbonate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":46129,"numValue":12.43,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":46130,"numValue":0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46131,"numValue":null,"referenc... | [{"id":7226,"numValue":7.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4531 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,531 | train | mutant | 3,647 | 55 | 4,092 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Y | W126Y | 1 | 1 | 0 | 0 | 126 | W | Y | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,377 | ProTherm | 3.5 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Y | null | null | 5.61 | 1.41 | null | null | null | 1.76 | 3.19 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28463,"numValue":5.61,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28464,"numValue":1.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28465,"numValue":3.19,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28466,"numValue":1.76,"references":[],... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,532 | train | mutant | 3,647 | 55 | 4,092 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Y | W126Y | 1 | 1 | 0 | 0 | 126 | W | Y | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,379 | ProTherm | 4 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Y | null | null | 7.02 | 1.42 | null | null | null | 2.2 | 3.19 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28473,"numValue":7.02,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28474,"numValue":1.42,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28475,"numValue":3.19,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28476,"numValue":2.2,"references":[],"... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4533 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,533 | train | mutant | 3,647 | 55 | 4,092 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Y | W126Y | 1 | 1 | 0 | 0 | 126 | W | Y | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,381 | ProTherm | 4.5 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Y | null | null | 8.2 | 1.36 | null | null | null | 2.57 | 3.19 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28483,"numValue":8.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28484,"numValue":1.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28485,"numValue":3.19,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28486,"numValue":2.57,"references":[],"... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4534 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,534 | train | mutant | 3,647 | 55 | 4,092 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Y | W126Y | 1 | 1 | 0 | 0 | 126 | W | Y | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,383 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Y | null | null | 8.13 | 1.27 | null | null | null | 2.55 | 3.19 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28493,"numValue":8.13,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28494,"numValue":1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28495,"numValue":3.19,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28496,"numValue":2.55,"references":[],... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,535 | train | mutant | 3,647 | 55 | 4,092 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Y | W126Y | 1 | 1 | 0 | 0 | 126 | W | Y | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,385 | ProTherm | 5.5 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Y | null | null | 8.04 | 1.31 | null | null | null | 2.52 | 3.19 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28503,"numValue":8.04,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28504,"numValue":1.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28505,"numValue":3.19,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28506,"numValue":2.52,"references":[],... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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