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:3650 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,650 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,959 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V74S | null | null | null | 0.38 | 108.03 | 1.22 | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24538,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24539,"numValue":1.22,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24540,"numValue":0.38,"references":[],"strValue":null,"t... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3651 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,651 | train | mutant | 724 | 48 | 790 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92Y | V92Y | 1 | 1 | 0 | 0 | 92 | V | Y | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,281 | ProTherm | 2.67 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74Y | 63.3 | null | null | null | 103.97 | null | 103.97 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.67,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74Y","type":"_P... | [{"datasets":[],"id":4716,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4717,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4718,"numValue":103.97,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4719,"numValue"... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3653 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,653 | train | mutant | 724 | 48 | 790 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92Y | V92Y | 1 | 1 | 0 | 0 | 92 | V | Y | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,283 | ProTherm | 3.02 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74Y | 70 | null | null | null | 114.96 | null | 116.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74Y","type":"_P... | [{"datasets":[],"id":4724,"numValue":70.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4725,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4726,"numValue":116.16,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4727,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3654 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,654 | train | mutant | 724 | 48 | 790 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92Y | V92Y | 1 | 1 | 0 | 0 | 92 | V | Y | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,284 | ProTherm | 3.21 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74Y | 73.3 | null | null | null | 119.98 | null | 119.98 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.21,"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:V74Y","type":"_P... | [{"datasets":[],"id":4728,"numValue":73.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4729,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4730,"numValue":119.98,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4731,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3655 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,655 | train | mutant | 724 | 48 | 790 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92Y | V92Y | 1 | 1 | 0 | 0 | 92 | V | Y | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,285 | ProTherm | 3.26 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74Y | 74.1 | null | null | null | 122.13 | null | 123.09 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.26,"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:V74Y","type":"_P... | [{"datasets":[],"id":4732,"numValue":74.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4733,"numValue":122.13,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4734,"numValue":123.09,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4735,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3656 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,656 | train | mutant | 724 | 48 | 790 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92Y | V92Y | 1 | 1 | 0 | 0 | 92 | V | Y | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,323 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74Y | 64 | -0.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74Y","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4880,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4881,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4882,"numValue":null,"re... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3657 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,657 | train | mutant | 724 | 48 | 790 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92Y | V92Y | 1 | 1 | 0 | 0 | 92 | V | Y | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,960 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V74Y | null | null | null | 0.24 | 106.6 | 1.65 | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24542,"numValue":106.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24543,"numValue":1.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24544,"numValue":0.24,"references":[],"strValue":null,"ty... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3658 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,658 | train | mutant | 725 | 48 | 791 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92D | V92D | 1 | 1 | 0 | 0 | 92 | V | D | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,286 | ProTherm | 2.6 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74D | 61.7 | null | null | null | 103.01 | null | 109.94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.6,"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:V74D","type":"_PD... | [{"datasets":[],"id":4736,"numValue":61.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4737,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4738,"numValue":109.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4739,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3659 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,659 | train | mutant | 725 | 48 | 791 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92D | V92D | 1 | 1 | 0 | 0 | 92 | V | D | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,287 | ProTherm | 2.83 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74D | 65.9 | null | null | null | 107.07 | null | 114.96 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74D","type":"_P... | [{"datasets":[],"id":4740,"numValue":65.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4741,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4742,"numValue":114.96,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4743,"numValue"... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3660 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,660 | train | mutant | 725 | 48 | 791 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92D | V92D | 1 | 1 | 0 | 0 | 92 | V | D | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,288 | ProTherm | 2.98 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74D | 68.1 | null | null | null | 112.09 | null | 118.07 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.98,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74D","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4744,"numValue":68.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4745,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4746,"numValue":118.07,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3661 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,661 | train | mutant | 725 | 48 | 791 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92D | V92D | 1 | 1 | 0 | 0 | 92 | V | D | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,289 | ProTherm | 3.1 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74D | 70.1 | null | null | null | 114.96 | null | 123.09 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74D","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4748,"numValue":70.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4749,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4750,"numValue":123.09,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3662 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,662 | train | mutant | 725 | 48 | 791 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92D | V92D | 1 | 1 | 0 | 0 | 92 | V | D | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,290 | ProTherm | 3.25 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74D | 72.5 | null | null | null | 119.98 | null | 126.91 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.25,"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:V74D","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4752,"numValue":72.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4753,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4754,"numValue":126.91,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3663 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,663 | train | mutant | 725 | 48 | 791 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92D | V92D | 1 | 1 | 0 | 0 | 92 | V | D | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,324 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74D | 63.5 | -1.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74D","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4883,"numValue":63.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4884,"numValue":-1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4885,"numValue":null,"re... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3664 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,664 | train | mutant | 725 | 48 | 791 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92D | V92D | 1 | 1 | 0 | 0 | 92 | V | D | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,961 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V74D | null | null | null | 0.43 | 106.84 | 1.58 | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24546,"numValue":106.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24547,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24548,"numValue":0.43,"references":[],"strValue":null,"t... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3665 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,665 | train | mutant | 726 | 48 | 792 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92N | V92N | 1 | 1 | 0 | 0 | 92 | V | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,291 | ProTherm | 2.65 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74N | 63 | null | null | null | 109.94 | null | 114.01 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.65,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74N","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4756,"numValue":63.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4757,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4758,"numValue":114.01,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3666 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,666 | train | mutant | 726 | 48 | 792 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92N | V92N | 1 | 1 | 0 | 0 | 92 | V | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,292 | ProTherm | 2.84 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74N | 66.2 | null | null | null | 114.01 | null | 115.92 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.84,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74N","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4760,"numValue":66.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4761,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4762,"numValue":115.92,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3668 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,668 | train | mutant | 726 | 48 | 792 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92N | V92N | 1 | 1 | 0 | 0 | 92 | V | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,325 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74N | 63.9 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74N","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4886,"numValue":63.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4887,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4888,"numValue":null,"re... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3669 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,669 | train | mutant | 726 | 48 | 792 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92N | V92N | 1 | 1 | 0 | 0 | 92 | V | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,962 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V74N | null | null | null | 0.33 | 115.44 | 1.1 | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24550,"numValue":115.44,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24551,"numValue":1.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24552,"numValue":0.33,"references":[],"strValue":null,"ty... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3670 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,670 | train | mutant | 727 | 48 | 793 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92R | V92R | 1 | 1 | 0 | 0 | 92 | V | R | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,294 | ProTherm | 2.66 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74R | 63.8 | null | null | null | 102.06 | null | 100.14 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.66,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74R","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4768,"numValue":63.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4769,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4770,"numValue":100.14,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,671 | train | mutant | 727 | 48 | 793 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92R | V92R | 1 | 1 | 0 | 0 | 92 | V | R | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,295 | ProTherm | 2.85 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74R | 67.3 | null | null | null | 108.03 | null | 105.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.85,"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:V74R","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4772,"numValue":67.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4773,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4774,"numValue":105.16,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3672 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,672 | train | mutant | 727 | 48 | 793 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92R | V92R | 1 | 1 | 0 | 0 | 92 | V | R | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,296 | ProTherm | 3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74R | 69.5 | null | null | null | 112.09 | null | 108.99 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":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:V74R","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4776,"numValue":69.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4777,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4778,"numValue":108.99,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3673 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,673 | train | mutant | 727 | 48 | 793 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92R | V92R | 1 | 1 | 0 | 0 | 92 | V | R | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,297 | ProTherm | 3.18 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74R | 72.8 | null | null | null | 117.11 | null | 114.01 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.18,"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:V74R","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4780,"numValue":72.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4781,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4782,"numValue":114.01,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,674 | train | mutant | 727 | 48 | 793 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92R | V92R | 1 | 1 | 0 | 0 | 92 | V | R | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,298 | ProTherm | 3.22 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74R | 73.2 | null | null | null | 118.07 | null | 116.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.22,"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:V74R","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4784,"numValue":73.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4785,"numValue":118.07,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4786,"numValue":116.16,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3675 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,675 | train | mutant | 727 | 48 | 793 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92R | V92R | 1 | 1 | 0 | 0 | 92 | V | R | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,326 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74R | 64.6 | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74R","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4889,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4890,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4891,"numValue":null,"re... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3676 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,676 | train | mutant | 727 | 48 | 793 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92R | V92R | 1 | 1 | 0 | 0 | 92 | V | R | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,963 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V74R | null | null | null | 0.07 | 103.97 | 1.67 | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24554,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24555,"numValue":1.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24556,"numValue":0.07,"references":[],"strValue":null,"t... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3677 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,677 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,190 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74A | 47.3 | -1.9 | null | null | 73.68 | 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 | 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:V74A","type":"_PD... | [{"datasets":[],"id":11658,"numValue":47.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11659,"numValue":-1.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11660,"numValue":73.68,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3678 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,678 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,223 | ProTherm | 3.16 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74A | 54.8 | null | null | null | 82.5 | null | 86.4 | 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":3.16,"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:V74A","type":"_P... | [{"datasets":[],"id":11801,"numValue":54.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11802,"numValue":82.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11803,"numValue":86.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11804,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3679 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,679 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,224 | ProTherm | 3.03 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74A | 52.8 | null | null | null | 79.2 | null | 86.4 | 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":3.03,"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:V74A","type":"_P... | [{"datasets":[],"id":11805,"numValue":52.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11806,"numValue":79.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11807,"numValue":86.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11808,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3680 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,680 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,225 | ProTherm | 2.85 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74A | 50.1 | null | null | null | 74.4 | null | 80.9 | 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":2.85,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74A","type":"_P... | [{"datasets":[],"id":11809,"numValue":50.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11810,"numValue":74.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11811,"numValue":80.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11812,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,681 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,226 | ProTherm | 2.69 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74A | 47.5 | null | null | null | 71.5 | null | 75.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.69,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74A","type":"_P... | [{"datasets":[],"id":11813,"numValue":47.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11814,"numValue":71.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11815,"numValue":75.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11816,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3682 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,682 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,227 | ProTherm | 2.51 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74A | 43.9 | null | null | null | 65.6 | null | 69.9 | 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":2.51,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74A","type":"_P... | [{"datasets":[],"id":11817,"numValue":43.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11818,"numValue":65.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11819,"numValue":69.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11820,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3683 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,683 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 4,166 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74A | 63.8 | -1.1 | null | null | 113.9 | 1.48 | 119.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 391 | ARTICLE | Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. | 1,997 | 10.1021/bi9621829 | 9020766 | Biochemistry;36;688-98 | 4 | Takano K|Yamagata Y|Yutani K|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74A","type":"_PD... | [{"datasets":[],"id":15430,"numValue":63.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15431,"numValue":-1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15432,"numValue":113.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,684 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,889 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V74A | null | null | null | 0.36 | null | 1.48 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 391 | ARTICLE | Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. | 1,997 | 10.1021/bi9621829 | 9020766 | Biochemistry;36;688-98 | 4 | Takano K|Yamagata Y|Yutani K|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24348,"numValue":1.48,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24349,"numValue":0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24350,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3685 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,685 | train | mutant | 1,724 | 48 | 1,934 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 7,744 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:V74A | null | null | null | 0.43 | null | 1.53 | 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":26603,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26604,"numValue":0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26605,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3686 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,686 | train | mutant | 3,555 | 48 | 3,974 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C95A | C95A | 1 | 1 | 0 | 0 | 95 | C | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 95 | A | T | true | false | 21.917963 | 14.905 | 7,164 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | 57 | 1LZ1_A:C77A | null | null | 0 | 4.6 | 94.8 | null | null | null | null | null | null | null | null | null | null | null | yes | DH|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 551 | ARTICLE | Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95. | 1,992 | 10.1021/bi00150a028 | 1525170 | Biochemistry;31;8323-8 | 5 | Kuroki R|Matsushima M|Inaka K|Kidokoro S|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":57.0,"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":25088,"numValue":94.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":25089,"numValue":0.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25090,"numValue":4.6,"references":... | [{"id":7050,"numValue":9.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3687 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,687 | train | mutant | 6,709 | 48 | 7,351 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C95A|C113A | C95A|C113A | 2 | 2 | 0 | 0 | 95 | C | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 95|113 | A | T|H | true | false | 11.949291 | 12.918333 | 14,459 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:C77A 1LZ1_A:C95A | 56.9 | -14.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 551 | ARTICLE | Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95. | 1,992 | 10.1021/bi00150a028 | 1525170 | Biochemistry;31;8323-8 | 5 | Kuroki R|Matsushima M|Inaka K|Kidokoro S|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:C77A 1LZ1_A:C... | [{"datasets":[],"id":53447,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53448,"numValue":-14.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53449,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7050,"numValue":9.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7068,"numValue":9.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3688 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,688 | train | mutant | 6,709 | 48 | 7,351 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C95A|C113A | C95A|C113A | 2 | 2 | 0 | 0 | 95 | C | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 95|113 | A | T|H | true | false | 11.949291 | 12.918333 | 14,971 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | 57 | 1LZ1_A:C77A 1LZ1_A:C95A | null | null | 0 | 4.6 | 90.8 | null | null | null | null | null | null | null | null | null | null | null | yes | DH|DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 551 | ARTICLE | Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95. | 1,992 | 10.1021/bi00150a028 | 1525170 | Biochemistry;31;8323-8 | 5 | Kuroki R|Matsushima M|Inaka K|Kidokoro S|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":57.0,"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":55110,"numValue":90.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":55111,"numValue":0.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55112,"numValue":4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55113,"numValue":null,"references":[],"... | [{"id":7050,"numValue":9.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7068,"numValue":9.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,689 | train | mutant | 6,709 | 48 | 7,351 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C95A|C113A | C95A|C113A | 2 | 2 | 0 | 0 | 95 | C | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 95|113 | A | T|H | true | false | 11.949291 | 12.918333 | 15,619 | ProTherm | 4 | CD | GdnHCl | glycine-HCl | 40 mM | 10 | 1LZ1_A:C77A 1LZ1_A:C95A | null | null | 8.2 | 5.8 | 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 | 941 | ARTICLE | Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast. | 1,992 | 1537844 | J Biol Chem;267;4619-24 | 4 | Yutani K|Ogasahara K|Kikuchi M|Taniyama Y | [{"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":57312,"numValue":8.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":57313,"numValue":5.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57314,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7050,"numValue":9.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7068,"numValue":9.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:3690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,690 | train | mutant | 6,709 | 48 | 7,351 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | C95A|C113A | C95A|C113A | 2 | 2 | 0 | 0 | 95 | C | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 95|113 | A | T|H | true | false | 11.949291 | 12.918333 | 15,620 | ProTherm | 3 | Fluorescence | GdnHCl | glycine-HCl | 40 mM | 10 | 1LZ1_A:C77A 1LZ1_A:C95A | null | null | 6.1 | 5.7 | 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 | 941 | ARTICLE | Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast. | 1,992 | 1537844 | J Biol Chem;267;4619-24 | 4 | Yutani K|Ogasahara K|Kikuchi M|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type... | [{"datasets":[],"id":57315,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":57316,"numValue":5.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57317,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7050,"numValue":9.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7068,"numValue":9.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:3691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,691 | train | mutant | 194 | 48 | 222 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96A | H96A | 1 | 1 | 0 | 0 | 96 | H | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 352 | ProTherm | 2.5 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:H78A | 61.1 | null | null | null | 97.51 | 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:H78A","type":"_PD... | [{"datasets":[],"id":1442,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1443,"numValue":97.51,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1444,"numValue":107.07,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1445,"numValue":null,"references":[]... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3692 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,692 | train | mutant | 194 | 48 | 222 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96A | H96A | 1 | 1 | 0 | 0 | 96 | H | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 353 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:H78A | 64.3 | null | null | null | 103.01 | null | 112.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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:H78A","type":"_PD... | [{"datasets":[],"id":1446,"numValue":64.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1447,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1448,"numValue":112.09,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1449,"numValue":null,"references":[... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3693 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,693 | train | mutant | 194 | 48 | 222 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96A | H96A | 1 | 1 | 0 | 0 | 96 | H | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 354 | ProTherm | 3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:H78A | 69.5 | null | null | null | 109.94 | null | 117.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|SVM-WIN31_SVM-3D12_S499.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:H78A","type":"_PD... | [{"datasets":[],"id":1450,"numValue":69.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1451,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":1452,"numValue":117.11,"referen... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,695 | train | mutant | 194 | 48 | 222 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96A | H96A | 1 | 1 | 0 | 0 | 96 | H | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 369 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:H78A | 64.4 | -0.5 | null | null | 103.49 | 1.51 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:H78A","type":"_PD... | [{"datasets":[],"id":1516,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1517,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1518,"numValue":103.49,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,696 | train | mutant | 194 | 48 | 222 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96A | H96A | 1 | 1 | 0 | 0 | 96 | H | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 6,869 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:H78A | null | null | null | 0.14 | 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":24291,"numValue":0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24292,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3697 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,697 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 3,896 | ProTherm | 2.53 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:H78G | 61.5 | null | null | null | 103.01 | 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":2.53,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:H78G","type":"_P... | [{"datasets":[],"id":14343,"numValue":61.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14344,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14345,"numValue":108.03,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14346,"numValue":null,"reference... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,698 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 3,897 | ProTherm | 2.75 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:H78G | 65.2 | null | null | null | 109.94 | null | 112.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":2.75,"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:H78G","type":"_P... | [{"datasets":[],"id":14347,"numValue":65.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14348,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14349,"numValue":112.09,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14350,"numValue":null,"reference... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,699 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 3,898 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:H78G | 71 | null | null | null | 118.07 | 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 | 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":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:H78G","type":"_PD... | [{"datasets":[],"id":14351,"numValue":71.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14352,"numValue":118.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14353,"numValue":119.98,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14354,"numValue":null,"reference... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,700 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 3,912 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:H78G | 64.4 | -0.5 | null | null | 108.75 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|PoPMuSiC-2.0_S2648.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:H78G","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14412,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":14413,"numValue":-0.5,"references":[],"strVal... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,701 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 3,921 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:H78G | 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:H78G","type":"_PD... | [{"datasets":[],"id":14439,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14440,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3703 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,703 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 4,207 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:H78G | 64.9 | null | null | null | 108.75 | 1.58 | 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:H78G","type":... | [{"datasets":[],"id":15595,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15596,"numValue":108.75,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15597,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":15598,"numValue":null,"references":... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,704 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 6,915 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:H78G | null | null | null | 0.12 | 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":24432,"numValue":0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24433,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,705 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 6,935 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:H78G | null | null | null | 0.12 | 108.75 | 1.58 | 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":24476,"numValue":108.75,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24477,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24478,"numValue":0.12,"references":[],"strValue":null,"t... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3706 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,706 | train | mutant | 2,022 | 48 | 2,258 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | H96G | H96G | 1 | 1 | 0 | 0 | 96 | H | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 96 | A | L | true | false | 155.073405 | 34.33 | 14,095 | ProTherm | 4 | CD | GdnHCl | glycine-HCl | 40 mM | 10 | 1LZ1_A:H78G | null | null | 13.81 | 0.53 | null | null | null | 3.81 | 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":52138,"numValue":13.81,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":52139,"numValue":0.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":52140,"numValue":3.81,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":52141,"numValue":null,"references":[... | [{"id":7051,"numValue":4.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,707 | train | mutant | 1,892 | 48 | 2,121 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S98A | S98A | 1 | 1 | 0 | 0 | 98 | S | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 98 | A | B | false | false | 60.891818 | 13.39 | 3,652 | ProTherm | 3.11 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S80A | 73.6 | null | null | null | 129.06 | 1.39 | 135.04 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|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":3.11,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S80A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13439,"numValue":73.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13440,"numValue":129.06,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7053,"numValue":4.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3708 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,708 | train | mutant | 1,892 | 48 | 2,121 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S98A | S98A | 1 | 1 | 0 | 0 | 98 | S | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 98 | A | B | false | false | 60.891818 | 13.39 | 3,653 | ProTherm | 2.85 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S80A | 69.1 | null | null | null | 121.89 | 1.34 | 129.06 | 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":2.85,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S80A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13444,"numValue":69.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13445,"numValue":121.89,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7053,"numValue":4.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3709 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,709 | train | mutant | 1,892 | 48 | 2,121 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S98A | S98A | 1 | 1 | 0 | 0 | 98 | S | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 98 | A | B | false | false | 60.891818 | 13.39 | 3,654 | ProTherm | 2.69 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S80A | 66.2 | null | null | null | 119.02 | 1.34 | 125.96 | 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":2.69,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S80A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13449,"numValue":66.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13450,"numValue":119.02,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7053,"numValue":4.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3710 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,710 | train | mutant | 1,892 | 48 | 2,121 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S98A | S98A | 1 | 1 | 0 | 0 | 98 | S | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 98 | A | B | false | false | 60.891818 | 13.39 | 3,655 | ProTherm | 2.5 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S80A | 62.7 | null | null | null | 113.05 | 1.41 | 119.98 | 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":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S80A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13454,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13455,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7053,"numValue":4.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3711 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,711 | train | mutant | 1,892 | 48 | 2,121 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S98A | S98A | 1 | 1 | 0 | 0 | 98 | S | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 98 | A | B | false | false | 60.891818 | 13.39 | 3,664 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S80A | 66.3 | 1.4 | null | null | 116.4 | 1.43 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | 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:S80A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13499,"numValue":66.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13500,"numValue":1.4,"references":[],"strValue":null... | [{"id":7053,"numValue":4.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3712 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,712 | train | mutant | 1,893 | 48 | 2,122 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S100A | S100A | 1 | 1 | 0 | 0 | 100 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 100 | A | G | false | false | 72.985047 | 13.99 | 3,656 | ProTherm | 3.12 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S82A | 73.5 | null | null | null | 125 | 1.41 | 132.89 | 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":3.12,"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:S82A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13459,"numValue":73.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13460,"numValue":125.0,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S19... | [{"id":7055,"numValue":5.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3713 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,713 | train | mutant | 1,893 | 48 | 2,122 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S100A | S100A | 1 | 1 | 0 | 0 | 100 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 100 | A | G | false | false | 72.985047 | 13.99 | 3,657 | ProTherm | 2.85 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S82A | 68.9 | null | null | null | 119.98 | 1.2 | 128.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.85,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S82A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13464,"numValue":68.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13465,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7055,"numValue":5.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,715 | train | mutant | 1,893 | 48 | 2,122 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S100A | S100A | 1 | 1 | 0 | 0 | 100 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 100 | A | G | false | false | 72.985047 | 13.99 | 3,659 | ProTherm | 2.51 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S82A | 62.5 | null | null | null | 110.9 | 1.41 | 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 | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.51,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S82A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13474,"numValue":62.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13475,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":1... | [{"id":7055,"numValue":5.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3716 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,716 | train | mutant | 1,893 | 48 | 2,122 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S100A | S100A | 1 | 1 | 0 | 0 | 100 | S | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 100 | A | G | false | false | 72.985047 | 13.99 | 3,665 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S82A | 66 | 1.1 | null | null | 114.48 | 1.27 | 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:S82A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13504,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13505,"numValue":1.1,"references":[],"strValue":null... | [{"id":7055,"numValue":5.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3717 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,717 | train | mutant | 1,721 | 48 | 1,931 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107V | I107V | 1 | 1 | 0 | 0 | 107 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,187 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89V | 46.5 | -2.7 | null | null | 78.47 | 1.84 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I89V","type":"_PD... | [{"datasets":[],"id":11643,"numValue":46.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11644,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11645,"numValue":78.47,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3718 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,718 | train | mutant | 1,721 | 48 | 1,931 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107V | I107V | 1 | 1 | 0 | 0 | 107 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,211 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89V | 53.8 | null | null | null | 87.3 | null | 88.3 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I89V","type":"_PD... | [{"datasets":[],"id":11752,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11753,"numValue":87.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11754,"numValue":88.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11755,"numValue":null,"references":[... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,720 | train | mutant | 1,721 | 48 | 1,931 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107V | I107V | 1 | 1 | 0 | 0 | 107 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,213 | ProTherm | 2.78 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89V | 48.4 | null | null | null | 77.3 | null | 82.3 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.78,"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:I89V","type":"_P... | [{"datasets":[],"id":11760,"numValue":48.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11761,"numValue":77.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11762,"numValue":82.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11763,"numValue":null,"references":[... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3721 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,721 | train | mutant | 1,721 | 48 | 1,931 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107V | I107V | 1 | 1 | 0 | 0 | 107 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,214 | ProTherm | 2.66 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89V | 45.5 | null | null | null | 71.8 | null | 76.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.66,"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:I89V","type":"_P... | [{"datasets":[],"id":11764,"numValue":45.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11765,"numValue":71.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11766,"numValue":76.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11767,"numValue":null,"references":[... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,722 | train | mutant | 1,721 | 48 | 1,931 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107V | I107V | 1 | 1 | 0 | 0 | 107 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,215 | ProTherm | 2.49 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89V | 42.5 | null | null | null | 66 | null | 72 | 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":2.49,"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:I89V","type":"_P... | [{"datasets":[],"id":11768,"numValue":42.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11769,"numValue":66.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11770,"numValue":72.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11771,"numValue":null,"references":[... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3723 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,723 | train | mutant | 1,721 | 48 | 1,931 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107V | I107V | 1 | 1 | 0 | 0 | 107 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 4,156 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89V | 63.5 | -1.4 | null | null | 115.8 | 1.91 | 121.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 388 | ARTICLE | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. | 1,995 | 10.1006/jmbi.1995.0599 | 7473760 | J Mol Biol;254;62-76 | 6 | Takano K|Yamagata Y|Ogasahara K|Fujii S|Kaneda H|Kanaya E | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I89V","type":"_PD... | [{"datasets":[],"id":15382,"numValue":63.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15383,"numValue":-1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15384,"numValue":115.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,724 | train | mutant | 1,721 | 48 | 1,931 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107V | I107V | 1 | 1 | 0 | 0 | 107 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 6,885 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I89V | null | null | null | 0.48 | null | 1.91 | 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 | 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":24336,"numValue":1.91,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":24337,"numValue":0.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24338,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3725 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,725 | train | mutant | 1,721 | 48 | 1,931 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107V | I107V | 1 | 1 | 0 | 0 | 107 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 7,741 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:I89V | null | null | null | 0.35 | null | 1.84 | 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":26594,"numValue":1.84,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26595,"numValue":0.35,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26596,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,726 | train | mutant | 1,755 | 48 | 1,968 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107A | I107A | 1 | 1 | 0 | 0 | 107 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,340 | ProTherm | 3.09 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89A | 62.9 | null | null | null | 106.2 | 1.51 | 110 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":3.09,"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:I89A","type":"_P... | [{"datasets":[],"id":12299,"numValue":62.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12300,"numValue":106.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12301,"numValue":1.51,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12302,"numValue":110.0,"references":... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3727 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,727 | train | mutant | 1,755 | 48 | 1,968 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107A | I107A | 1 | 1 | 0 | 0 | 107 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,341 | ProTherm | 2.95 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89A | 61.1 | null | null | null | 103.1 | 1.67 | 108.1 | 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":2.95,"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:I89A","type":"_P... | [{"datasets":[],"id":12304,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12305,"numValue":103.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12306,"numValue":1.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12307,"numValue":108.1,"references":... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3728 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,728 | train | mutant | 1,755 | 48 | 1,968 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107A | I107A | 1 | 1 | 0 | 0 | 107 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,342 | ProTherm | 2.8 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89A | 57.7 | null | null | null | 97.8 | 1.08 | 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":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I89A","type":"_PD... | [{"datasets":[],"id":12309,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12310,"numValue":97.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12311,"numValue":1.08,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12312,"numValue":103.1,"references":[... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,729 | train | mutant | 1,755 | 48 | 1,968 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107A | I107A | 1 | 1 | 0 | 0 | 107 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,343 | ProTherm | 2.66 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89A | 55.4 | null | null | null | 93.1 | 1.39 | 98.1 | 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":2.66,"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:I89A","type":"_P... | [{"datasets":[],"id":12314,"numValue":55.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12315,"numValue":93.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12316,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12317,"numValue":98.1,"references":[]... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3730 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,730 | train | mutant | 1,755 | 48 | 1,968 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107A | I107A | 1 | 1 | 0 | 0 | 107 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,344 | ProTherm | 2.5 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89A | 52.6 | null | null | null | 89.5 | 1.72 | 95.5 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I89A","type":"_PD... | [{"datasets":[],"id":12319,"numValue":52.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12320,"numValue":89.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12321,"numValue":1.72,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12322,"numValue":95.5,"references":[]... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,731 | train | mutant | 1,755 | 48 | 1,968 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107A | I107A | 1 | 1 | 0 | 0 | 107 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 3,359 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I89A | 56.2 | -8.7 | 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 | 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:I89A","type":"_PD... | [{"datasets":[],"id":12388,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12389,"numValue":-8.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12390,"numValue":1.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3732 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,732 | train | mutant | 1,755 | 48 | 1,968 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I107A | I107A | 1 | 1 | 0 | 0 | 107 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 107 | A | L | true | false | 6.819224 | 13.33125 | 6,906 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I89A | null | null | null | 2.7 | 109.6 | 1.65 | 113 | 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":24405,"numValue":109.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24406,"numValue":1.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24407,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["capriotti_S1615_map.csv","khan_protherm... | [{"id":7062,"numValue":8.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3733 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,733 | train | mutant | 633 | 48 | 685 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D109P | D109P | 1 | 1 | 0 | 0 | 109 | D | P | 4 | CONSERVATION | 1LZ1 | 405 | null | 109 | A | H | true | false | 50.384057 | 17.31125 | 1,050 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | null | 1LZ1_A:D91P | 67.7 | -1.1 | null | null | null | 1.57 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:D91P","type":"... | [{"datasets":[],"id":3924,"numValue":67.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3925,"numValue":-1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3926,"numValue":1.57,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":7064,"numValue":4.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,734 | train | mutant | 633 | 48 | 685 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D109P | D109P | 1 | 1 | 0 | 0 | 109 | D | P | 4 | CONSERVATION | 1LZ1 | 405 | null | 109 | A | H | true | false | 50.384057 | 17.31125 | 6,703 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | 68.8 | 1LZ1_A:D91P | null | null | null | 0.4 | 115.4 | 1.57 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":68.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":[],"id":23843,"numValue":115.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":23844,"numValue":1.57,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23845,"numValue":0.4,"reference... | [{"id":7064,"numValue":4.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3735 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,735 | train | mutant | 633 | 48 | 685 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D109P | D109P | 1 | 1 | 0 | 0 | 109 | D | P | 4 | CONSERVATION | 1LZ1 | 405 | null | 109 | A | H | true | false | 50.384057 | 17.31125 | 9,882 | ProTherm | 3 | CD | GdnHCl | glycine-HCl | 40 mM | 25 | 1LZ1_A:D91P | null | null | 8.9 | 0.8 | null | null | null | 2.78 | 5.42 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 658 | ARTICLE | Effects of proline mutations on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerization. | 1,991 | 10.1021/bi00105a011 | 1911779 | Biochemistry;30;9882-91 | 4 | Yutani K|Kikuchi M|Herning T|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":33969,"numValue":8.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33970,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33971,"numValue":5.42,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33972,"numValue":2.78,"references":[],"s... | [{"id":7064,"numValue":4.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,736 | train | mutant | 175 | 48 | 203 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A110S | A110S | 1 | 1 | 0 | 0 | 110 | A | S | 7 | CONSERVATION | 1LZ1 | 405 | null | 110 | A | H | true | false | 4.55114 | 12.656 | 314 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:A92S | 67.5 | 2.6 | null | null | null | 2.01 | 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:A92S","type":"_PD... | [{"datasets":[],"id":1292,"numValue":67.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1293,"numValue":2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1294,"numValue":2.01,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":7065,"numValue":7.0,"position":110,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3737 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,737 | train | mutant | 175 | 48 | 203 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A110S | A110S | 1 | 1 | 0 | 0 | 110 | A | S | 7 | CONSERVATION | 1LZ1 | 405 | null | 110 | A | H | true | false | 4.55114 | 12.656 | 6,850 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:A92S | null | null | null | null | 103.73 | 2.01 | 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":24248,"numValue":103.73,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24249,"numValue":2.01,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24250,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7065,"numValue":7.0,"position":110,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3739 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,739 | train | mutant | 176 | 48 | 204 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111T | V111T | 1 | 1 | 0 | 0 | 111 | V | T | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 315 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V93T | 62.6 | -2.3 | null | null | null | 1.12 | 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:V93T","type":"_PD... | [{"datasets":[],"id":1296,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1297,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1298,"numValue":1.12,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3740 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,740 | train | mutant | 176 | 48 | 204 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111T | V111T | 1 | 1 | 0 | 0 | 111 | V | T | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 6,851 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V93T | null | null | null | null | 100.62 | 1.12 | 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":24251,"numValue":100.62,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24252,"numValue":1.12,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24253,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3741 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,741 | train | mutant | 176 | 48 | 204 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111T | V111T | 1 | 1 | 0 | 0 | 111 | V | T | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 6,859 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V93T | null | null | null | 0.67 | 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":24271,"numValue":0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24272,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3742 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,742 | train | mutant | 1,725 | 48 | 1,935 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 3,191 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V93A | 44.8 | -4.4 | null | null | 76.32 | 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 | 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:V93A","type":"_PD... | [{"datasets":[],"id":11663,"numValue":44.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11664,"numValue":-4.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11665,"numValue":76.32,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3743 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,743 | train | mutant | 1,725 | 48 | 1,935 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 3,228 | ProTherm | 3.16 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V93A | 52.5 | null | null | null | 81.8 | null | 86.4 | 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":3.16,"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:V93A","type":"_P... | [{"datasets":[],"id":11821,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11822,"numValue":81.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11823,"numValue":86.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11824,"numValue":null,"references":[... | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3744 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,744 | train | mutant | 1,725 | 48 | 1,935 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 3,229 | ProTherm | 3.02 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V93A | 50.1 | null | null | null | 77.5 | null | 83 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V93A","type":"_P... | [{"datasets":[],"id":11825,"numValue":50.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11826,"numValue":77.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11827,"numValue":83.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11828,"numValue":null,"references":[... | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3746 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,746 | train | mutant | 1,725 | 48 | 1,935 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 3,231 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V93A | 45.2 | -4 | null | null | 71.1 | null | 77.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V93A","type":"_PD... | [{"datasets":[],"id":11833,"numValue":45.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11834,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11835,"numValue":71.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3747 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,747 | train | mutant | 1,725 | 48 | 1,935 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 3,232 | ProTherm | 2.5 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V93A | 41.2 | null | null | null | 64.1 | null | 71.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V93A","type":"_PD... | [{"datasets":[],"id":11838,"numValue":41.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11839,"numValue":64.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11840,"numValue":71.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11841,"numValue":null,"references":[... | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3748 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,748 | train | mutant | 1,725 | 48 | 1,935 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 4,167 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V93A | 62.6 | -2.3 | null | null | 111.5 | 1.53 | 119.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 391 | ARTICLE | Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. | 1,997 | 10.1021/bi9621829 | 9020766 | Biochemistry;36;688-98 | 4 | Takano K|Yamagata Y|Yutani K|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V93A","type":"_PD... | [{"datasets":[],"id":15436,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15437,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15438,"numValue":111.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3750 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,750 | train | mutant | 1,725 | 48 | 1,935 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 7 | CONSERVATION | 1LZ1 | 405 | null | 111 | A | H | false | false | 3.628015 | 10.895714 | 7,745 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:V93A | null | null | null | 1 | null | 1.53 | 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":26606,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26607,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26608,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7066,"numValue":7.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3751 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,751 | train | mutant | 177 | 48 | 205 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A114S | A114S | 1 | 1 | 0 | 0 | 114 | A | S | 8 | CONSERVATION | 1LZ1 | 405 | null | 114 | A | H | false | false | 0 | 11.73 | 316 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:A96S | 61.6 | -3.3 | null | null | null | 1.29 | 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:A96S","type":"_PD... | [{"datasets":[],"id":1300,"numValue":61.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1301,"numValue":-3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1302,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":7069,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3752 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,752 | train | mutant | 177 | 48 | 205 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A114S | A114S | 1 | 1 | 0 | 0 | 114 | A | S | 8 | CONSERVATION | 1LZ1 | 405 | null | 114 | A | H | false | false | 0 | 11.73 | 6,852 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:A96S | null | null | null | null | 103.25 | 1.29 | 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":24254,"numValue":103.25,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24255,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24256,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7069,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3753 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,753 | train | mutant | 177 | 48 | 205 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A114S | A114S | 1 | 1 | 0 | 0 | 114 | A | S | 8 | CONSERVATION | 1LZ1 | 405 | null | 114 | A | H | false | false | 0 | 11.73 | 6,860 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:A96S | null | null | null | 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 | 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":24273,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24274,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7069,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3754 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,754 | train | mutant | 2,023 | 48 | 2,259 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A114M | A114M | 1 | 1 | 0 | 0 | 114 | A | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 114 | A | H | false | false | 0 | 11.73 | 3,899 | ProTherm | 2.56 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A96M | 62.5 | null | null | null | 95.12 | null | 97.99 | 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:A96M","type":"_P... | [{"datasets":[],"id":14355,"numValue":62.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14356,"numValue":95.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14357,"numValue":97.99,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14358,"numValue":null,"references"... | [{"id":7069,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3756 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,756 | train | mutant | 2,023 | 48 | 2,259 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A114M | A114M | 1 | 1 | 0 | 0 | 114 | A | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 114 | A | H | false | false | 0 | 11.73 | 3,901 | ProTherm | 3.19 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A96M | 72.9 | null | null | null | 108.99 | null | 112.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":3.19,"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:A96M","type":"_P... | [{"datasets":[],"id":14363,"numValue":72.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14364,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14365,"numValue":112.09,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14366,"numValue":null,"reference... | [{"id":7069,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3757 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,757 | train | mutant | 2,023 | 48 | 2,259 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A114M | A114M | 1 | 1 | 0 | 0 | 114 | A | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 114 | A | H | false | false | 0 | 11.73 | 3,913 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A96M | 65 | 0.1 | null | null | 98.71 | 1.31 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.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:A96M","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":14417,"numValue":65.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":14418,"numValue":0.1,"references":[],"strValu... | [{"id":7069,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3758 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,758 | train | mutant | 2,023 | 48 | 2,259 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A114M | A114M | 1 | 1 | 0 | 0 | 114 | A | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 114 | A | H | false | false | 0 | 11.73 | 3,922 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:A96M | 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:A96M","type":"_PD... | [{"datasets":[],"id":14441,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14442,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7069,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3759 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,759 | train | mutant | 2,023 | 48 | 2,259 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A114M | A114M | 1 | 1 | 0 | 0 | 114 | A | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 114 | A | H | false | false | 0 | 11.73 | 6,916 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:A96M | null | null | null | -0.02 | 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":24434,"numValue":-0.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24435,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7069,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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