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:3213 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,213 | train | mutant | 1,723 | 48 | 1,933 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20A | V20A | 1 | 1 | 0 | 0 | 20 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 7,743 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:V2A | null | null | null | 1.51 | null | 1.44 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":49.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":26600,"numValue":1.44,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26601,"numValue":1.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26602,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3214 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,214 | train | mutant | 44 | 48 | 49 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E25Q | E25Q | 1 | 1 | 0 | 0 | 25 | E | Q | 6 | CONSERVATION | 1LZ1 | 405 | null | 25 | A | H | false | false | 55.123798 | 17.856667 | 44 | ProTherm | 2.2 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | 1LZ1_A:E7Q | 57.8 | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:E7Q... | [{"datasets":[],"id":151,"numValue":57.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":152,"numValue":0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":153,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6980,"numValue":6.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3215 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,215 | train | mutant | 44 | 48 | 49 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E25Q | E25Q | 1 | 1 | 0 | 0 | 25 | E | Q | 6 | CONSERVATION | 1LZ1 | 405 | null | 25 | A | H | false | false | 55.123798 | 17.856667 | 50 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | null | 1LZ1_A:E7Q | 76.2 | -3.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:E7Q","type... | [{"datasets":[],"id":169,"numValue":76.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":170,"numValue":-3.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":171,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6980,"numValue":6.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3216 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,216 | train | mutant | 44 | 48 | 49 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E25Q | E25Q | 1 | 1 | 0 | 0 | 25 | E | Q | 6 | CONSERVATION | 1LZ1 | 405 | null | 25 | A | H | false | false | 55.123798 | 17.856667 | 56 | ProTherm | 2.3 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | KCl | 0.2 M | 1LZ1_A:E7Q | 54.6 | -1.6 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type... | [{"datasets":[],"id":187,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":188,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":189,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6980,"numValue":6.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3217 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,217 | train | mutant | 44 | 48 | 49 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E25Q | E25Q | 1 | 1 | 0 | 0 | 25 | E | Q | 6 | CONSERVATION | 1LZ1 | 405 | null | 25 | A | H | false | false | 55.123798 | 17.856667 | 60 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | null | KCl | 0.2 M | 1LZ1_A:E7Q | 75.5 | -2.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"... | [{"datasets":[],"id":199,"numValue":75.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":200,"numValue":-2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":201,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6980,"numValue":6.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3218 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,218 | train | mutant | 44 | 48 | 49 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E25Q | E25Q | 1 | 1 | 0 | 0 | 25 | E | Q | 6 | CONSERVATION | 1LZ1 | 405 | null | 25 | A | H | false | false | 55.123798 | 17.856667 | 6,837 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | 65 | 1LZ1_A:E7Q | null | null | 3.99 | 1.43 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":65.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"B... | [{"datasets":[],"id":24209,"numValue":3.99,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":24210,"numValue":1.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24211,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6980,"numValue":6.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3219 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,219 | train | mutant | 44 | 48 | 49 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E25Q | E25Q | 1 | 1 | 0 | 0 | 25 | E | Q | 6 | CONSERVATION | 1LZ1 | 405 | null | 25 | A | H | false | false | 55.123798 | 17.856667 | 6,843 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | 65 | KCl | 0.2 M | 1LZ1_A:E7Q | null | null | 2.77 | 1.29 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":65.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"B... | [{"datasets":[],"id":24227,"numValue":2.77,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":24228,"numValue":1.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24229,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6980,"numValue":6.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3220 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,220 | train | mutant | 172 | 48 | 200 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | L26T | L26T | 1 | 1 | 0 | 0 | 26 | L | T | 7 | CONSERVATION | 1LZ1 | 405 | null | 26 | A | H | false | false | 0.134371 | 9.8925 | 311 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:L8T | 52.5 | -12.4 | null | null | null | 1.39 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:L8T","type":"_PDB... | [{"datasets":[],"id":1280,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1281,"numValue":-12.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1282,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"i... | [{"id":6981,"numValue":7.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3221 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,221 | train | mutant | 172 | 48 | 200 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | L26T | L26T | 1 | 1 | 0 | 0 | 26 | L | T | 7 | CONSERVATION | 1LZ1 | 405 | null | 26 | A | H | false | false | 0.134371 | 9.8925 | 6,847 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:L8T | null | null | null | null | 106.6 | 1.39 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24239,"numValue":106.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24240,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24241,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6981,"numValue":7.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3222 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,222 | train | mutant | 172 | 48 | 200 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | L26T | L26T | 1 | 1 | 0 | 0 | 26 | L | T | 7 | CONSERVATION | 1LZ1 | 405 | null | 26 | A | H | false | false | 0.134371 | 9.8925 | 6,855 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:L8T | null | null | null | 3.73 | 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 | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24263,"numValue":3.73,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24264,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6981,"numValue":7.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3223 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,223 | train | mutant | 173 | 48 | 201 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A27S | A27S | 1 | 1 | 0 | 0 | 27 | A | S | 8 | CONSERVATION | 1LZ1 | 405 | null | 27 | A | H | false | false | 0 | 9.74 | 312 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:A9S | 64.8 | -0.1 | null | null | null | 1.27 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:A9S","type":"_PDB... | [{"datasets":[],"id":1284,"numValue":64.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1285,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1286,"numValue":1.27,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6982,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3224 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,224 | train | mutant | 173 | 48 | 201 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A27S | A27S | 1 | 1 | 0 | 0 | 27 | A | S | 8 | CONSERVATION | 1LZ1 | 405 | null | 27 | A | H | false | false | 0 | 9.74 | 6,848 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:A9S | null | null | null | null | 106.12 | 1.27 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24242,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24243,"numValue":1.27,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24244,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6982,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3226 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,226 | train | mutant | 1,937 | 48 | 2,166 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T29A | T29A | 1 | 1 | 0 | 0 | 29 | T | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 29 | A | H | true | false | 26.66619 | 11.711429 | 3,712 | ProTherm | 3.22 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T11A | 73.4 | null | null | null | 119.26 | null | 119.98 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.22,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T11A","type"... | [{"datasets":[],"id":13693,"numValue":73.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13694,"numValue":119.26,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13695,"numValue":119.98,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13696,"numValue":null,"reference... | [{"id":6984,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3227 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,227 | train | mutant | 1,937 | 48 | 2,166 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T29A | T29A | 1 | 1 | 0 | 0 | 29 | T | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 29 | A | H | true | false | 26.66619 | 11.711429 | 3,713 | ProTherm | 3.02 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T11A | 71.4 | null | null | null | 115.92 | null | 119.02 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T11A","type"... | [{"datasets":[],"id":13697,"numValue":71.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13698,"numValue":115.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13699,"numValue":119.02,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13700,"numValue":null,"reference... | [{"id":6984,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3228 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,228 | train | mutant | 1,937 | 48 | 2,166 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T29A | T29A | 1 | 1 | 0 | 0 | 29 | T | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 29 | A | H | true | false | 26.66619 | 11.711429 | 3,714 | ProTherm | 2.82 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T11A | 68.5 | null | null | null | 114.96 | null | 115.92 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.82,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T11A","type"... | [{"datasets":[],"id":13701,"numValue":68.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13702,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13703,"numValue":115.92,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13704,"numValue":null,"reference... | [{"id":6984,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3229 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,229 | train | mutant | 1,937 | 48 | 2,166 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T29A | T29A | 1 | 1 | 0 | 0 | 29 | T | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 29 | A | H | true | false | 26.66619 | 11.711429 | 3,715 | ProTherm | 2.74 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T11A | 66.8 | null | null | null | 112.09 | null | 114.96 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.74,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T11A","type"... | [{"datasets":[],"id":13705,"numValue":66.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13706,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13707,"numValue":114.96,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13708,"numValue":null,"reference... | [{"id":6984,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3231 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,231 | train | mutant | 1,942 | 48 | 2,171 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T29V | T29V | 1 | 1 | 0 | 0 | 29 | T | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 29 | A | H | true | false | 26.66619 | 11.711429 | 3,736 | ProTherm | 3.19 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T11V | 73 | null | null | null | 117.11 | null | 120.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.19,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T11V","type"... | [{"datasets":["STRUM_Q3421.csv"],"id":13789,"numValue":73.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13790,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13791,"numValue":120.94,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":6984,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3232 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,232 | train | mutant | 1,942 | 48 | 2,171 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T29V | T29V | 1 | 1 | 0 | 0 | 29 | T | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 29 | A | H | true | false | 26.66619 | 11.711429 | 3,737 | ProTherm | 2.81 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T11V | 68.7 | null | null | null | 114.01 | null | 117.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.81,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T11V","type"... | [{"datasets":["STRUM_Q3421.csv"],"id":13793,"numValue":68.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13794,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13795,"numValue":117.11,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":6984,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3233 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,233 | train | mutant | 1,942 | 48 | 2,171 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T29V | T29V | 1 | 1 | 0 | 0 | 29 | T | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 29 | A | H | true | false | 26.66619 | 11.711429 | 3,738 | ProTherm | 2.71 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T11V | 66.2 | null | null | null | 109.94 | null | 112.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.71,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T11V","type"... | [{"datasets":["STRUM_Q3421.csv"],"id":13797,"numValue":66.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13798,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13799,"numValue":112.09,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":6984,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3234 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,234 | train | mutant | 1,942 | 48 | 2,171 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T29V | T29V | 1 | 1 | 0 | 0 | 29 | T | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 29 | A | H | true | false | 26.66619 | 11.711429 | 3,739 | ProTherm | 2.51 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T11V | 62.9 | null | null | null | 103.97 | null | 107.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.51,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T11V","type"... | [{"datasets":["STRUM_Q3421.csv"],"id":13801,"numValue":62.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13802,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13803,"numValue":107.07,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":6984,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3235 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,235 | train | mutant | 287 | 48 | 319 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G34A | G34A | 1 | 1 | 0 | 0 | 34 | G | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 34 | A | T | false | false | 41.707278 | 12.7375 | 505 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G16A | 60.3 | null | null | null | 96.32 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G16A","type":"_PD... | [{"datasets":[],"id":2034,"numValue":60.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2035,"numValue":96.32,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2036,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6989,"numValue":5.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3236 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,236 | train | mutant | 287 | 48 | 319 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G34A | G34A | 1 | 1 | 0 | 0 | 34 | G | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 34 | A | T | false | false | 41.707278 | 12.7375 | 529 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G16A | 60.3 | -4.6 | null | null | 103.49 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G16A","type":"_PD... | [{"datasets":[],"id":2106,"numValue":60.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2107,"numValue":-4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2108,"numValue":103.49,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2109,"numValue":null,"references":[],"... | [{"id":6989,"numValue":5.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3237 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,237 | train | mutant | 287 | 48 | 319 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G34A | G34A | 1 | 1 | 0 | 0 | 34 | G | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 34 | A | T | false | false | 41.707278 | 12.7375 | 6,872 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:G16A | null | null | null | 1.39 | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24297,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24298,"numValue":1.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24299,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":6989,"numValue":5.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3238 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,238 | train | mutant | 45 | 48 | 50 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D36N | D36N | 1 | 1 | 0 | 0 | 36 | D | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 36 | A | T | false | false | 70.451131 | 19.0925 | 45 | ProTherm | 2.2 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | 1LZ1_A:D18N | 56 | -1.5 | 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 | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:D18... | [{"datasets":[],"id":154,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":155,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":156,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6991,"numValue":5.0,"position":36,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3239 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,239 | train | mutant | 45 | 48 | 50 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D36N | D36N | 1 | 1 | 0 | 0 | 36 | D | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 36 | A | T | false | false | 70.451131 | 19.0925 | 51 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | null | 1LZ1_A:D18N | 75.5 | -4.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:D18N","typ... | [{"datasets":[],"id":172,"numValue":75.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":173,"numValue":-4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":174,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6991,"numValue":5.0,"position":36,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3241 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,241 | train | mutant | 288 | 48 | 320 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G37A | G37A | 1 | 1 | 0 | 0 | 37 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 37 | A | T | false | false | 42.826369 | 13.9325 | 506 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G19A | 59.4 | null | null | null | 102.06 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G19A","type":"_PD... | [{"datasets":[],"id":2037,"numValue":59.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2038,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2039,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6992,"numValue":4.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3242 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,242 | train | mutant | 288 | 48 | 320 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G37A | G37A | 1 | 1 | 0 | 0 | 37 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 37 | A | T | false | false | 42.826369 | 13.9325 | 530 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G19A | 59.4 | -5.5 | null | null | 110.66 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G19A","type":"_PD... | [{"datasets":[],"id":2110,"numValue":59.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2111,"numValue":-5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2112,"numValue":110.66,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2113,"numValue":null,"references":[],"... | [{"id":6992,"numValue":4.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3243 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,243 | train | mutant | 288 | 48 | 320 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G37A | G37A | 1 | 1 | 0 | 0 | 37 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 37 | A | T | false | false | 42.826369 | 13.9325 | 6,873 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:G19A | null | null | null | 1.77 | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24300,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24301,"numValue":1.77,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24302,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":6992,"numValue":4.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3244 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,244 | train | mutant | 1,732 | 48 | 1,942 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y38F | Y38F | 1 | 1 | 0 | 0 | 38 | Y | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 38 | A | G | false | false | 51.187088 | 13.379167 | 3,262 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y20F | 63.4 | -1.5 | null | null | 111.5 | 1.35 | 119.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y20F","type":"_PD... | [{"datasets":[],"id":11960,"numValue":63.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11961,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11962,"numValue":111.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":6993,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3245 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,245 | train | mutant | 1,732 | 48 | 1,942 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y38F | Y38F | 1 | 1 | 0 | 0 | 38 | Y | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 38 | A | G | false | false | 51.187088 | 13.379167 | 3,268 | ProTherm | 3.18 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y20F | 72 | null | null | null | 122 | 0.6 | 129.19 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":3.18,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y20F","type":"_P... | [{"datasets":[],"id":11996,"numValue":72.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11997,"numValue":122.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11998,"numValue":0.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":11999,"numValue":129.19,"references":... | [{"id":6993,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3247 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,247 | train | mutant | 1,732 | 48 | 1,942 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y38F | Y38F | 1 | 1 | 0 | 0 | 38 | Y | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 38 | A | G | false | false | 51.187088 | 13.379167 | 3,270 | ProTherm | 2.89 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y20F | 66.8 | null | null | null | 115.1 | 1.7 | 123.21 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.89,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y20F","type":"_P... | [{"datasets":[],"id":12006,"numValue":66.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12007,"numValue":115.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12008,"numValue":1.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12009,"numValue":123.21,"references":... | [{"id":6993,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3249 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,249 | train | mutant | 1,732 | 48 | 1,942 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y38F | Y38F | 1 | 1 | 0 | 0 | 38 | Y | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 38 | A | G | false | false | 51.187088 | 13.379167 | 3,272 | ProTherm | 2.58 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y20F | 61.1 | null | null | null | 106.2 | 1.67 | 114.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.58,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y20F","type":"_P... | [{"datasets":[],"id":12016,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12017,"numValue":106.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12018,"numValue":1.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12019,"numValue":114.11,"references"... | [{"id":6993,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3250 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,250 | train | mutant | 1,732 | 48 | 1,942 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y38F | Y38F | 1 | 1 | 0 | 0 | 38 | Y | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 38 | A | G | false | false | 51.187088 | 13.379167 | 6,897 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:Y20F | null | null | null | 0.5 | null | 1.35 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24372,"numValue":1.35,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24373,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24374,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":6993,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3251 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,251 | train | mutant | 188 | 48 | 216 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39A | R39A | 1 | 1 | 0 | 0 | 39 | R | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 332 | ProTherm | 2.51 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R21A | 66.1 | null | null | null | 98.71 | null | 107.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.51,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R21A","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1362,"numValue":66.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1363,"numValue":98.71,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1364,"numValue":107.07,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["Ho... | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3252 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,252 | train | mutant | 188 | 48 | 216 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39A | R39A | 1 | 1 | 0 | 0 | 39 | R | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 333 | ProTherm | 2.71 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R21A | 69.8 | null | null | null | 106.12 | null | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.71,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R21A","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1366,"numValue":69.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1367,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1368,"numValue":113.05,"references":[],"strValue":null,"type":"DH... | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3254 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,254 | train | mutant | 188 | 48 | 216 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39A | R39A | 1 | 1 | 0 | 0 | 39 | R | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 335 | ProTherm | 3.23 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R21A | 77.6 | null | null | null | 119.98 | null | 129.06 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.23,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R21A","type":"_P... | [{"datasets":[],"id":1374,"numValue":77.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1375,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1376,"numValue":129.06,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1377,"numValue":null,"references":[... | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3255 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,255 | train | mutant | 188 | 48 | 216 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39A | R39A | 1 | 1 | 0 | 0 | 39 | R | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 363 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R21A | 69.4 | 4.5 | null | null | 96.56 | 1.82 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R21A","type":"_PD... | [{"datasets":[],"id":1486,"numValue":69.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1487,"numValue":4.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1488,"numValue":96.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id"... | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3257 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,257 | train | mutant | 189 | 48 | 217 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39G | R39G | 1 | 1 | 0 | 0 | 39 | R | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 336 | ProTherm | 2.5 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R21G | 64.6 | null | null | null | 102.06 | null | 107.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R21G","type":"_PD... | [{"datasets":[],"id":1378,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1379,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1380,"numValue":107.07,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1381,"numValue":null,"references":[... | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3258 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,258 | train | mutant | 189 | 48 | 217 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39G | R39G | 1 | 1 | 0 | 0 | 39 | R | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 337 | ProTherm | 2.69 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R21G | 68.2 | null | null | null | 108.99 | null | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.69,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R21G","type":"_P... | [{"datasets":[],"id":1382,"numValue":68.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1383,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1384,"numValue":113.05,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["HotMuSiC_S1626.csv"],... | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3259 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,259 | train | mutant | 189 | 48 | 217 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39G | R39G | 1 | 1 | 0 | 0 | 39 | R | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 338 | ProTherm | 2.81 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R21G | 70.9 | null | null | null | 113.05 | null | 115.92 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.81,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R21G","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1386,"numValue":70.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1387,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1388,"numValue":115.92,"references":[],"strValue":null,"type":"DH... | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3260 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,260 | train | mutant | 189 | 48 | 217 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39G | R39G | 1 | 1 | 0 | 0 | 39 | R | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 364 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R21G | 68.6 | 3.7 | null | null | 102.77 | 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 | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R21G","type":"_PD... | [{"datasets":[],"id":1491,"numValue":68.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1492,"numValue":3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1493,"numValue":102.77,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3261 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,261 | train | mutant | 189 | 48 | 217 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R39G | R39G | 1 | 1 | 0 | 0 | 39 | R | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 39 | A | G | false | false | 152.342116 | 41.366364 | 6,864 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:R21G | null | null | null | -1.15 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24281,"numValue":-1.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24282,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6994,"numValue":3.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3262 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,262 | train | mutant | 289 | 48 | 321 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G40A | G40A | 1 | 1 | 0 | 0 | 40 | G | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 40 | A | G | false | false | 73.710906 | 10.7675 | 507 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G22A | 57.7 | null | null | null | 76.96 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G22A","type":"_PD... | [{"datasets":[],"id":2040,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2041,"numValue":76.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2042,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6995,"numValue":5.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3263 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,263 | train | mutant | 289 | 48 | 321 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G40A | G40A | 1 | 1 | 0 | 0 | 40 | G | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 40 | A | G | false | false | 73.710906 | 10.7675 | 531 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G22A | 57.7 | -7.2 | null | null | 88.43 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G22A","type":"_PD... | [{"datasets":[],"id":2114,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2115,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2116,"numValue":88.43,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2117,"numValue":null,"references":[],"s... | [{"id":6995,"numValue":5.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3265 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,265 | train | mutant | 1,718 | 48 | 1,928 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41V | I41V | 1 | 1 | 0 | 0 | 41 | I | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 3,184 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23V | 47.6 | -1.6 | null | null | 80.86 | 1.82 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23V","type":"_PD... | [{"datasets":[],"id":11628,"numValue":47.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11629,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11630,"numValue":80.86,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3266 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,266 | train | mutant | 1,718 | 48 | 1,928 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41V | I41V | 1 | 1 | 0 | 0 | 41 | I | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 3,198 | ProTherm | 3.09 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23V | 55 | null | null | null | 91.1 | null | 95 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.09,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23V","type":"_P... | [{"datasets":[],"id":11698,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11699,"numValue":91.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11700,"numValue":95.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11701,"numValue":null,"references":[... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3267 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,267 | train | mutant | 1,718 | 48 | 1,928 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41V | I41V | 1 | 1 | 0 | 0 | 41 | I | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 3,199 | ProTherm | 2.96 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23V | 52.3 | null | null | null | 85.4 | null | 89.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.96,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23V","type":"_P... | [{"datasets":[],"id":11702,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11703,"numValue":85.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11704,"numValue":89.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11705,"numValue":null,"references":[... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3268 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,268 | train | mutant | 1,718 | 48 | 1,928 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41V | I41V | 1 | 1 | 0 | 0 | 41 | I | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 3,200 | ProTherm | 2.78 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23V | 49.6 | null | null | null | 83.5 | null | 85.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23V","type":"_P... | [{"datasets":[],"id":11706,"numValue":49.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11707,"numValue":83.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11708,"numValue":85.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11709,"numValue":null,"references":[... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3269 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,269 | train | mutant | 1,718 | 48 | 1,928 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41V | I41V | 1 | 1 | 0 | 0 | 41 | I | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 3,201 | ProTherm | 2.66 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23V | 46.7 | null | null | null | 76.3 | null | 80.4 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.66,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23V","type":"_P... | [{"datasets":[],"id":11710,"numValue":46.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11711,"numValue":76.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11712,"numValue":80.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11713,"numValue":null,"references":[... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3271 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,271 | train | mutant | 1,718 | 48 | 1,928 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41V | I41V | 1 | 1 | 0 | 0 | 41 | I | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 4,153 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23V | 63.8 | -1.1 | null | null | 112 | 1.39 | 120.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 388 | ARTICLE | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. | 1,995 | 10.1006/jmbi.1995.0599 | 7473760 | J Mol Biol;254;62-76 | 6 | Takano K|Yamagata Y|Ogasahara K|Fujii S|Kaneda H|Kanaya E | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23V","type":"_PD... | [{"datasets":[],"id":15364,"numValue":63.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15365,"numValue":-1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15366,"numValue":112.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3272 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,272 | train | mutant | 1,718 | 48 | 1,928 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41V | I41V | 1 | 1 | 0 | 0 | 41 | I | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 6,882 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I23V | null | null | null | 0.36 | null | 1.39 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 388 | ARTICLE | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. | 1,995 | 10.1006/jmbi.1995.0599 | 7473760 | J Mol Biol;254;62-76 | 6 | Takano K|Yamagata Y|Ogasahara K|Fujii S|Kaneda H|Kanaya E | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24327,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24328,"numValue":0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24329,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3273 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,273 | train | mutant | 1,718 | 48 | 1,928 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41V | I41V | 1 | 1 | 0 | 0 | 41 | I | V | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 7,738 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:I23V | null | null | null | 0.41 | null | 1.82 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":49.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":26585,"numValue":1.82,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26586,"numValue":0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26587,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3274 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,274 | train | mutant | 1,753 | 48 | 1,966 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41A | I41A | 1 | 1 | 0 | 0 | 41 | I | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 3,328 | ProTherm | 2.96 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23A | 62 | null | null | null | 105 | 1.08 | 111 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.96,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23A","type":"_P... | [{"datasets":[],"id":12239,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12240,"numValue":105.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12241,"numValue":1.08,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12242,"numValue":111.0,"references":... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3275 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,275 | train | mutant | 1,753 | 48 | 1,966 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41A | I41A | 1 | 1 | 0 | 0 | 41 | I | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 3,329 | ProTherm | 2.67 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23A | 56.2 | null | null | null | 98.1 | 1.51 | 103.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.67,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23A","type":"_P... | [{"datasets":[],"id":12244,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12245,"numValue":98.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12246,"numValue":1.51,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12247,"numValue":103.1,"references":[... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3276 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,276 | train | mutant | 1,753 | 48 | 1,966 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41A | I41A | 1 | 1 | 0 | 0 | 41 | I | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 3,356 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I23A | 56.8 | -8.1 | null | null | null | 1.2 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I23A","type":"_PD... | [{"datasets":[],"id":12376,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12377,"numValue":-8.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12378,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3277 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,277 | train | mutant | 1,753 | 48 | 1,966 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I41A | I41A | 1 | 1 | 0 | 0 | 41 | I | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 41 | A | B | false | false | 14.646433 | 10.845 | 6,903 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I23A | null | null | null | 2.54 | 108.6 | 1.2 | 115.5 | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DHVH|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24390,"numValue":108.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24391,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24392,"numValue":115.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_... | [{"id":6996,"numValue":3.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3278 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,278 | train | mutant | 1,888 | 48 | 2,117 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S42A | S42A | 1 | 1 | 0 | 0 | 42 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 42 | A | L | false | false | 45.64644 | 11.015 | 3,636 | ProTherm | 3.09 | DSC | Thermal | glycine | 0.05 M | null | -- | 1LZ1_A:S24A | 70.3 | null | null | null | 118.07 | 1.41 | 123.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":3.09,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"--","type":"ION_CONC"},... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13359,"numValue":70.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13360,"numValue":118.07,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":6997,"numValue":5.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3279 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,279 | train | mutant | 1,888 | 48 | 2,117 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S42A | S42A | 1 | 1 | 0 | 0 | 42 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 42 | A | L | false | false | 45.64644 | 11.015 | 3,637 | ProTherm | 2.82 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S24A | 65.7 | null | null | null | 112.09 | 1.55 | 117.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.82,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S24A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13364,"numValue":65.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13365,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":6997,"numValue":5.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3280 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,280 | train | mutant | 1,888 | 48 | 2,117 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S42A | S42A | 1 | 1 | 0 | 0 | 42 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 42 | A | L | false | false | 45.64644 | 11.015 | 3,638 | ProTherm | 2.66 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S24A | 62.5 | null | null | null | 106.12 | 1.67 | 110.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.66,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S24A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13369,"numValue":62.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13370,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":6997,"numValue":5.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3281 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,281 | train | mutant | 1,888 | 48 | 2,117 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S42A | S42A | 1 | 1 | 0 | 0 | 42 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 42 | A | L | false | false | 45.64644 | 11.015 | 3,639 | ProTherm | 2.46 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S24A | 58.8 | null | null | null | 101.1 | 1.46 | 104.92 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.46,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S24A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13374,"numValue":58.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13375,"numValue":101.1,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S19... | [{"id":6997,"numValue":5.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3282 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,282 | train | mutant | 1,888 | 48 | 2,117 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S42A | S42A | 1 | 1 | 0 | 0 | 42 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 42 | A | L | false | false | 45.64644 | 11.015 | 3,660 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S24A | 63.3 | -1.6 | null | null | 110.18 | 1.51 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S24A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13479,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13480,"numValue":-1.6,"references":[],"strValue":nul... | [{"id":6997,"numValue":5.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3283 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,283 | train | mutant | 2,016 | 48 | 2,252 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N45L | N45L | 1 | 1 | 0 | 0 | 45 | N | L | 6 | CONSERVATION | 1LZ1 | 405 | null | 45 | A | H | false | false | 31.521804 | 11.42625 | 3,878 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:N27L | 65.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:N27L","type":"_PD... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":14273,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","M47and... | [{"id":7000,"numValue":6.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3284 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,284 | train | mutant | 2,016 | 48 | 2,252 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N45L | N45L | 1 | 1 | 0 | 0 | 45 | N | L | 6 | CONSERVATION | 1LZ1 | 405 | null | 45 | A | H | false | false | 31.521804 | 11.42625 | 3,905 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:N27L | 65.3 | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|EASE-MM_S1676.csv|Saraboji_S1791.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:N27L","type":"_PD... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":14379,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","A... | [{"id":7000,"numValue":6.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3285 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,285 | train | mutant | 174 | 48 | 202 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50S | A50S | 1 | 1 | 0 | 0 | 50 | A | S | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 313 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:A32S | 63.9 | -1 | null | null | null | 1.65 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:A32S","type":"_PD... | [{"datasets":[],"id":1288,"numValue":63.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1289,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1290,"numValue":1.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3286 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,286 | train | mutant | 174 | 48 | 202 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50S | A50S | 1 | 1 | 0 | 0 | 50 | A | S | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 6,849 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:A32S | null | null | null | null | 110.66 | 1.65 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24245,"numValue":110.66,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24246,"numValue":1.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24247,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3287 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,287 | train | mutant | 174 | 48 | 202 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50S | A50S | 1 | 1 | 0 | 0 | 50 | A | S | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 6,857 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:A32S | null | null | null | 0.33 | 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 | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24267,"numValue":0.33,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24268,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3288 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,288 | train | mutant | 2,017 | 48 | 2,253 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50L | A50L | 1 | 1 | 0 | 0 | 50 | A | L | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 3,879 | ProTherm | 2.61 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A32L | 63.1 | null | null | null | 94.89 | null | 97.75 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv|PON-TStab_dataset.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.61,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:A32L","type":"_P... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":14275,"numValue":63.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","M47and... | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3289 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,289 | train | mutant | 2,017 | 48 | 2,253 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50L | A50L | 1 | 1 | 0 | 0 | 50 | A | L | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 3,880 | ProTherm | 2.83 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A32L | 66.9 | null | null | null | 102.06 | null | 103.97 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:A32L","type":"_P... | [{"datasets":[],"id":14279,"numValue":66.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14280,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14281,"numValue":103.97,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14282,"numValue":null,"reference... | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,290 | train | mutant | 2,017 | 48 | 2,253 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50L | A50L | 1 | 1 | 0 | 0 | 50 | A | L | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 3,881 | ProTherm | 3.23 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A32L | 73.2 | null | null | null | 108.03 | null | 110.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":3.23,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:A32L","type":"_P... | [{"datasets":[],"id":14283,"numValue":73.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14284,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14285,"numValue":110.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14286,"numValue":null,"references... | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3291 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,291 | train | mutant | 2,017 | 48 | 2,253 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50L | A50L | 1 | 1 | 0 | 0 | 50 | A | L | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 3,906 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A32L | 64.6 | -0.3 | null | null | 98.23 | 1.27 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:A32L","type":"_PD... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":14382,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOM... | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3292 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,292 | train | mutant | 2,017 | 48 | 2,253 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50L | A50L | 1 | 1 | 0 | 0 | 50 | A | L | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 3,915 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A32L | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:A32L","type":"_PD... | [{"datasets":[],"id":14427,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14428,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3293 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,293 | train | mutant | 2,017 | 48 | 2,253 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A50L | A50L | 1 | 1 | 0 | 0 | 50 | A | L | 7 | CONSERVATION | 1LZ1 | 405 | null | 50 | A | H | false | false | 0.134371 | 11.534 | 6,909 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:A32L | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24420,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24421,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7005,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,294 | train | mutant | 2,018 | 48 | 2,254 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E53L | E53L | 1 | 1 | 0 | 0 | 53 | E | L | 8 | ACTIVE_SITE|CONSERVATION | 1LZ1 | 405 | null | 53 | A | H | true | true | 37.49267 | 15.478889 | 3,882 | ProTherm | 2.56 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:E35L | 61.2 | null | null | null | 94.89 | null | 104.92 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.56,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:E35L","type":"_P... | [{"datasets":[],"id":14287,"numValue":61.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14288,"numValue":94.89,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14289,"numValue":104.92,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14290,"numValue":null,"references... | [{"id":24,"numValue":null,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7008,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3295 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,295 | train | mutant | 2,018 | 48 | 2,254 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E53L | E53L | 1 | 1 | 0 | 0 | 53 | E | L | 8 | ACTIVE_SITE|CONSERVATION | 1LZ1 | 405 | null | 53 | A | H | true | true | 37.49267 | 15.478889 | 3,883 | ProTherm | 3.25 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:E35L | 70.8 | null | null | null | 104.92 | null | 109.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":3.25,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:E35L","type":"_P... | [{"datasets":[],"id":14291,"numValue":70.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14292,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14293,"numValue":109.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14294,"numValue":null,"reference... | [{"id":24,"numValue":null,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7008,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,296 | train | mutant | 2,018 | 48 | 2,254 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E53L | E53L | 1 | 1 | 0 | 0 | 53 | E | L | 8 | ACTIVE_SITE|CONSERVATION | 1LZ1 | 405 | null | 53 | A | H | true | true | 37.49267 | 15.478889 | 3,907 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:E35L | 63.1 | -1.8 | null | null | 98.95 | 1.05 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|EASE-MM_S1676.csv|M47andM8_S1810.csv|Saraboji_S1791.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:E35L","type":"_PD... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":14387,"numValue":63.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1925.csv","E... | [{"id":24,"numValue":null,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7008,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3297 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,297 | train | mutant | 2,018 | 48 | 2,254 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E53L | E53L | 1 | 1 | 0 | 0 | 53 | E | L | 8 | ACTIVE_SITE|CONSERVATION | 1LZ1 | 405 | null | 53 | A | H | true | true | 37.49267 | 15.478889 | 3,916 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:E35L | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:E35L","type":"_PD... | [{"datasets":[],"id":14429,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14430,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":24,"numValue":null,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7008,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,298 | train | mutant | 2,018 | 48 | 2,254 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | E53L | E53L | 1 | 1 | 0 | 0 | 53 | E | L | 8 | ACTIVE_SITE|CONSERVATION | 1LZ1 | 405 | null | 53 | A | H | true | true | 37.49267 | 15.478889 | 6,910 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:E35L | null | null | null | 0.53 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24422,"numValue":0.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24423,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":24,"numValue":null,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7008,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,299 | train | mutant | 1,889 | 48 | 2,118 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S54A | S54A | 1 | 1 | 0 | 0 | 54 | S | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 54 | A | H | false | false | 18.016374 | 12.48 | 3,640 | ProTherm | 3.09 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S36A | 68.7 | null | null | null | 114.01 | 1.22 | 119.02 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":3.09,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S36A","type":"_P... | [{"datasets":[],"id":13379,"numValue":68.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13380,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13381,"numValue":1.22,"... | [{"id":7009,"numValue":9.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,300 | train | mutant | 1,889 | 48 | 2,118 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S54A | S54A | 1 | 1 | 0 | 0 | 54 | S | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 54 | A | H | false | false | 18.016374 | 12.48 | 3,641 | ProTherm | 2.84 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S36A | 64 | null | null | null | 107.07 | 1.24 | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | EASE-MM_S238.csv|PON-TStab_dataset.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.84,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S36A","type":"_P... | [{"datasets":[],"id":13384,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv"],"id":13385,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13386,"numValue":1.24,"references":[],"strValue":null,"type":"DCP"},{"datasets":[... | [{"id":7009,"numValue":9.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3301 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,301 | train | mutant | 1,889 | 48 | 2,118 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S54A | S54A | 1 | 1 | 0 | 0 | 54 | S | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 54 | A | H | false | false | 18.016374 | 12.48 | 3,642 | ProTherm | 2.67 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S36A | 60.8 | null | null | null | 103.97 | 1.31 | 108.99 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.67,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S36A","type":"_P... | [{"datasets":[],"id":13389,"numValue":60.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13390,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13391,"numValue":1.31,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":13392,"numValue":108.99,"references... | [{"id":7009,"numValue":9.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,302 | train | mutant | 1,889 | 48 | 2,118 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S54A | S54A | 1 | 1 | 0 | 0 | 54 | S | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 54 | A | H | false | false | 18.016374 | 12.48 | 3,643 | ProTherm | 2.47 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S36A | 57.1 | null | null | null | 98.47 | 1.31 | 103.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.47,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S36A","type":"_P... | [{"datasets":[],"id":13394,"numValue":57.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13395,"numValue":98.47,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13396,"numValue":1.31,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":13397,"numValue":103.01,"references"... | [{"id":7009,"numValue":9.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,303 | train | mutant | 1,889 | 48 | 2,118 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S54A | S54A | 1 | 1 | 0 | 0 | 54 | S | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 54 | A | H | false | false | 18.016374 | 12.48 | 3,661 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S36A | 61.4 | -3.5 | null | null | 108.75 | 1.31 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S36A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13484,"numValue":61.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13485,"numValue":-3.5,"references":[],"strValue":nul... | [{"id":7009,"numValue":9.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,304 | train | mutant | 290 | 48 | 322 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55A | G55A | 1 | 1 | 0 | 0 | 55 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 508 | ProTherm | 2.38 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G37A | 58.1 | null | null | null | 97.04 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.38,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37A","type":"_P... | [{"datasets":[],"id":2043,"numValue":58.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2044,"numValue":97.04,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2045,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,305 | train | mutant | 290 | 48 | 322 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55A | G55A | 1 | 1 | 0 | 0 | 55 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 509 | ProTherm | 2.6 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G37A | 62.4 | null | null | null | 103.97 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37A","type":"_PD... | [{"datasets":[],"id":2046,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2047,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":2048,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3306 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,306 | train | mutant | 290 | 48 | 322 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55A | G55A | 1 | 1 | 0 | 0 | 55 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 510 | ProTherm | 3.18 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G37A | 72.4 | null | null | null | 119.02 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.18,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37A","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":2049,"numValue":72.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":2050,"numValue":119.02,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":2051,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,307 | train | mutant | 290 | 48 | 322 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55A | G55A | 1 | 1 | 0 | 0 | 55 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 532 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G37A | 64 | -0.9 | null | null | 107.55 | 1.53 | 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 | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37A","type":"_PD... | [{"datasets":[],"id":2118,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2119,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2120,"numValue":107.55,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,309 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 3,884 | ProTherm | 2.48 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:G37Q | 60.7 | null | null | null | 102.06 | null | 108.03 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.48,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37Q","type":"_P... | [{"datasets":[],"id":14295,"numValue":60.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14296,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14297,"numValue":108.03,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14298,"numValue":null,"reference... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3310 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,310 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 3,885 | ProTherm | 2.73 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:G37Q | 64.5 | null | null | null | 108.03 | null | 110.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.73,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37Q","type":"_P... | [{"datasets":[],"id":14299,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14300,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14301,"numValue":110.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14302,"numValue":null,"references... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,311 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 3,886 | ProTherm | 3.09 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:G37Q | 70.1 | null | null | null | 113.05 | null | 118.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":3.09,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37Q","type":"_P... | [{"datasets":[],"id":14303,"numValue":70.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14304,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14305,"numValue":118.07,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14306,"numValue":null,"reference... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,312 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 3,908 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:G37Q | 64.1 | -0.8 | null | null | 107.55 | 1.15 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37Q","type":"_PD... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":14392,"numValue":64.1,"references":[],"strValue":null,"type... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,313 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 3,917 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:G37Q | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37Q","type":"_PD... | [{"datasets":[],"id":14431,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14432,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3315 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,315 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 4,208 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:G37Q | 64.9 | null | null | null | 107.55 | 1.15 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 397 | ARTICLE | Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. | 2,000 | 10.1021/bi9928694 | 10913274 | Biochemistry;39;8655-65 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G37Q","type":... | [{"datasets":[],"id":15599,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15600,"numValue":107.55,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15601,"numValue":1.15,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":15602,"numValue":null,"references":... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3316 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,316 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 6,911 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:G37Q | null | null | null | 0.26 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24424,"numValue":0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24425,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,317 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 6,936 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:G37Q | null | null | null | 0.26 | 107.55 | 1.15 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 397 | ARTICLE | Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. | 2,000 | 10.1021/bi9928694 | 10913274 | Biochemistry;39;8655-65 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":[],"id":24480,"numValue":107.55,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24481,"numValue":1.15,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24482,"numValue":0.26,"references":[],"strValue":null,"t... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3318 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,318 | train | mutant | 2,019 | 48 | 2,255 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G55Q | G55Q | 1 | 1 | 0 | 0 | 55 | G | Q | 4 | CONSERVATION | 1LZ1 | 405 | null | 55 | A | T | false | false | 37.416485 | 14.7525 | 14,096 | ProTherm | 4 | CD | GdnHCl | glycine-HCl | 40 mM | 10 | 1LZ1_A:G37Q | null | null | 13.48 | 0.86 | null | null | null | 3.79 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 397 | ARTICLE | Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. | 2,000 | 10.1021/bi9928694 | 10913274 | Biochemistry;39;8655-65 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":52142,"numValue":13.48,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":52143,"numValue":0.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":52144,"numValue":3.79,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":52145,"numValue":null,"references":[... | [{"id":7010,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,319 | train | mutant | 190 | 48 | 218 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56A | Y56A | 1 | 1 | 0 | 0 | 56 | Y | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 339 | ProTherm | 2.72 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Y38A | 56.3 | null | null | null | 87.95 | null | 89.15 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.72,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y38A","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1390,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1391,"numValue":87.95,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1392,"numValue":89.15,"references":[],"strValue":null,"type":"DHVH... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3320 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,320 | train | mutant | 190 | 48 | 218 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56A | Y56A | 1 | 1 | 0 | 0 | 56 | Y | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 340 | ProTherm | 3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Y38A | 61.7 | null | null | null | 94.41 | null | 96.32 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y38A","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1394,"numValue":61.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1395,"numValue":94.41,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1396,"numValue":96.32,"references":[],"strValue":null,"type":"DHVH... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,321 | train | mutant | 190 | 48 | 218 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56A | Y56A | 1 | 1 | 0 | 0 | 56 | Y | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 341 | ProTherm | 3.18 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Y38A | 65 | null | null | null | 96.32 | null | 97.51 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.18,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y38A","type":"_P... | [{"datasets":[],"id":1398,"numValue":65.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1399,"numValue":96.32,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1400,"numValue":97.51,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1401,"numValue":null,"references":[],... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3322 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,322 | train | mutant | 190 | 48 | 218 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56A | Y56A | 1 | 1 | 0 | 0 | 56 | Y | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 365 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Y38A | 56 | -8.9 | null | null | 96.8 | 0.98 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y38A","type":"_PD... | [{"datasets":[],"id":1496,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1497,"numValue":-8.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1498,"numValue":96.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id"... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,323 | train | mutant | 190 | 48 | 218 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56A | Y56A | 1 | 1 | 0 | 0 | 56 | Y | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 6,865 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:Y38A | null | null | null | 2.49 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24283,"numValue":2.49,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24284,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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