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:3099 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,099 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,704 | ProTherm | 2.93 | DSC | Thermal | glycine-HCl | 50 mM | null | 62.5 | null | null | null | 102.06 | 1.46 | 102.06 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":2.93,"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"}] | [{"datasets":[],"id":72473,"numValue":62.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72474,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72475,"numValue":1.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72476,"numValue":102.06,"references... | |||||||||||||||||||||||||
fireprotdb:3101 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,101 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,709 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | 114.1 | 1.58 | 120.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 389 | ARTICLE | The structure, stability, and folding process of amyloidogenic mutant human lysozyme. | 1,996 | 10.1093/oxfordjournals.jbchem.a021544 | 9010773 | J Biochem;120;1216-23 | 5 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72489,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72490,"numValue":114.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72491,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72492,"numValue":120.1,"references":... | |||||||||||||||||||||||||
fireprotdb:3102 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,102 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,721 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | 114.1 | 1.58 | 120.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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"}] | [{"datasets":[],"id":72527,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72528,"numValue":114.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72529,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72530,"numValue":120.1,"references":... | |||||||||||||||||||||||||
fireprotdb:3103 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,103 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,740 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 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 | 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"}] | [{"datasets":[],"id":72573,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72574,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3104 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,104 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,741 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 64.9 | null | null | null | 114.01 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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"}] | [{"datasets":[],"id":72575,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72576,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72577,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72578,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:3105 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,105 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,865 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | 114.01 | 1.55 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori 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"}] | [{"datasets":[],"id":72967,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72968,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72969,"numValue":1.55,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72970,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:3106 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,106 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,134 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | 68.8 | null | null | null | null | 120.1 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":73799,"numValue":120.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73800,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":73801,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3107 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,107 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,135 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | null | null | null | null | 114.1 | 1.58 | 120.1 | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DHVH|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":73802,"numValue":114.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73803,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":73804,"numValue":120.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":73805,"numValue":null,"references... | |||||||||||||||||||||||||
fireprotdb:3108 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,108 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,145 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | 57 | null | null | 4.6 | null | 100.6 | 1.55 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":73828,"numValue":100.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73829,"numValue":1.55,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":73830,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73831,"numValue":null,"references":[]... | |||||||||||||||||||||||||
fireprotdb:3110 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,110 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,305 | ProTherm | 3 | DSC | GdnHCl | glycine-HCl | 50 mM | 25 | null | null | 9.49 | null | null | null | null | 2.9 | 3.23 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER... | [{"datasets":[],"id":77504,"numValue":9.49,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77505,"numValue":3.23,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77506,"numValue":2.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77507,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:3111 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,111 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,306 | ProTherm | 4 | DSC | GdnHCl | glycine-HCl | 50 mM | 25 | null | null | 12.86 | null | null | null | null | 3.8 | 3.37 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER... | [{"datasets":[],"id":77508,"numValue":12.86,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77509,"numValue":3.37,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77510,"numValue":3.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77511,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:3112 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,112 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,307 | ProTherm | 7 | DSC | GdnHCl | Sodium phosphate | 50 mM | 25 | null | null | 12.05 | null | null | null | null | 4 | 3.01 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":77512,"numValue":12.05,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77513,"numValue":3.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77514,"numValue":4.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77515,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:3113 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,113 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,308 | ProTherm | 3 | DSC | GdnHCl | glycine-HCl | 50 mM | 25 | null | null | 6.19 | null | null | null | null | 2.1 | 3.01 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER... | [{"datasets":[],"id":77516,"numValue":6.19,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77517,"numValue":3.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77518,"numValue":2.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77519,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:3114 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,114 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,309 | ProTherm | 4 | DSC | GdnHCl | glycine-HCl | 50 mM | 25 | null | null | 8.25 | null | null | null | null | 2.8 | 2.96 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER... | [{"datasets":[],"id":77520,"numValue":8.25,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77521,"numValue":2.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77522,"numValue":2.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77523,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:3116 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,116 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,767 | ProTherm | 5.2 | CD | GdnHCl | Sodium acetate | 20 mM | 20 | null | null | 14.7 | null | null | null | null | 4.12 | 3.6 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 936 | ARTICLE | Effect of an alternative disulfide bond on the structure, stability, and folding of human lysozyme. | 2,000 | 10.1021/bi9921945 | 10727242 | Biochemistry;39;3472-9 | 7 | Kanaya E|Arai M|Kuwajima K|Hamel P|Inaka K|Miki K|Kikuchi M | [{"numValue":5.2,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":78943,"numValue":14.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78944,"numValue":3.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78945,"numValue":4.12,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78946,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:3117 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,117 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,995 | ProTherm | 4 | CD | GdnHCl | glycine-HCl | 40 mM | 10 | null | null | 14 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | MEASURE|PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC | 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":null,"strValue":"CD","type":"MEASURE"},{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":79667,"numValue":14.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79668,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:3118 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,118 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,996 | ProTherm | 3 | Fluorescence | GdnHCl | glycine-HCl | 40 mM | 10 | null | null | 11.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":79669,"numValue":11.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79670,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:3119 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,119 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,997 | ProTherm | 4 | CD | GdnHCl | glycine-HCl | 40 mM | 10 | null | null | 14.34 | null | null | null | null | 3.96 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":79671,"numValue":14.34,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79672,"numValue":3.96,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79673,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3120 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,120 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,332 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 64.9 | null | null | null | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":80641,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80642,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":80643,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3121 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,121 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,333 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 64.9 | null | null | null | null | 1.58 | 114.01 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":80644,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80645,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":80646,"numValue":114.01,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":80647,"numValue":null,"references... | |||||||||||||||||||||||||
fireprotdb:3122 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,122 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,488 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 64.9 | null | null | null | 114.01 | 1.58 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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"}] | [{"datasets":[],"id":81095,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":81096,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":81097,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":81098,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:3124 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,124 | train | mutant | 2,158 | 48 | 2,446 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19M | K19M | 1 | 1 | 0 | 0 | 19 | K | M | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 4,242 | ProTherm | 2.5 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:K1M | 61.7 | null | null | null | 88.43 | null | 90.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori 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:K1M","type":"_PDB... | [{"datasets":[],"id":15731,"numValue":61.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15732,"numValue":88.43,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15733,"numValue":90.11,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":15734,"numValue":null,"references"... | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3126 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,126 | train | mutant | 2,158 | 48 | 2,446 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19M | K19M | 1 | 1 | 0 | 0 | 19 | K | M | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 4,244 | ProTherm | 2.95 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:K1M | 69.1 | null | null | null | 95.36 | null | 97.51 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.95,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:K1M","type":"_PD... | [{"datasets":[],"id":15739,"numValue":69.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15740,"numValue":95.36,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15741,"numValue":97.51,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":15742,"numValue":null,"references"... | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3127 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,127 | train | mutant | 2,158 | 48 | 2,446 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19M | K19M | 1 | 1 | 0 | 0 | 19 | K | M | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 4,245 | ProTherm | 3.22 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:K1M | 70.1 | null | null | null | 98.47 | null | 106.12 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":3.22,"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:K1M","type":"_PD... | [{"datasets":[],"id":15743,"numValue":70.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15744,"numValue":98.47,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15745,"numValue":106.12,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":15746,"numValue":null,"references... | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3128 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,128 | train | mutant | 2,158 | 48 | 2,446 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19M | K19M | 1 | 1 | 0 | 0 | 19 | K | M | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 4,249 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:K1M | 64.4 | -0.5 | null | null | 91.78 | 1.03 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori 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:K1M","type":"_PDB... | [{"datasets":[],"id":15759,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15760,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15761,"numValue":91.78,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15762,"numValue":1.03,"references":[... | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3129 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,129 | train | mutant | 2,158 | 48 | 2,446 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19M | K19M | 1 | 1 | 0 | 0 | 19 | K | M | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 4,251 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:K1M | 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 | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori 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:K1M","type":"_PDB... | [{"datasets":[],"id":15769,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15770,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3130 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,130 | train | mutant | 2,158 | 48 | 2,446 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19M | K19M | 1 | 1 | 0 | 0 | 19 | K | M | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 6,937 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:K1M | 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 | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori 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","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24484,"numValue":0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24485,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3131 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,131 | train | mutant | 2,159 | 48 | 2,447 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19A | K19A | 1 | 1 | 0 | 0 | 19 | K | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 4,246 | ProTherm | 2.58 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:K1A | 60.9 | null | null | null | 90.58 | null | 98.71 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.58,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:K1A","type":"_PD... | [{"datasets":[],"id":15747,"numValue":60.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15748,"numValue":90.58,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15749,"numValue":98.71,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":15750,"numValue":null,"references"... | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3132 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,132 | train | mutant | 2,159 | 48 | 2,447 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19A | K19A | 1 | 1 | 0 | 0 | 19 | K | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 4,247 | ProTherm | 2.77 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:K1A | 63.7 | null | null | null | 95.12 | null | 99.43 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.77,"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:K1A","type":"_PD... | [{"datasets":[],"id":15751,"numValue":63.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15752,"numValue":95.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15753,"numValue":99.43,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":15754,"numValue":null,"references"... | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3134 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,134 | train | mutant | 2,159 | 48 | 2,447 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | K19A | K19A | 1 | 1 | 0 | 0 | 19 | K | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 19 | A | L | true | false | 67.324975 | 20.721111 | 4,250 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:K1A | 62.7 | -2.2 | null | null | 96.8 | 1.6 | 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 | 406 | ARTICLE | Effect of foreign N-terminal residues on the conformational stability of human lysozyme. | 1,999 | 10.1046/j.1432-1327.1999.00918.x | 10561612 | Eur J Biochem;266;675-82 | 4 | Takano K|Tsuchimori 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:K1A","type":"_PDB... | [{"datasets":[],"id":15764,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15765,"numValue":-2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15766,"numValue":96.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":6974,"numValue":6.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3137 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,137 | train | mutant | 670 | 48 | 726 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20G | V20G | 1 | 1 | 0 | 0 | 20 | V | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,100 | ProTherm | 2.65 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2G | 56.63 | null | null | null | 95.6 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.65,"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:V2G","type":... | [{"datasets":[],"id":4121,"numValue":56.63,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4122,"numValue":95.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4123,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3138 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,138 | train | mutant | 670 | 48 | 726 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20G | V20G | 1 | 1 | 0 | 0 | 20 | V | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,101 | ProTherm | 2.83 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2G | 59.46 | null | null | null | 99.67 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.83,"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:V2G","type":... | [{"datasets":[],"id":4124,"numValue":59.46,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4125,"numValue":99.67,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4126,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3139 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,139 | train | mutant | 670 | 48 | 726 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20G | V20G | 1 | 1 | 0 | 0 | 20 | V | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,102 | ProTherm | 3.08 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2G | 63.75 | null | null | null | 104.92 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.08,"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:V2G","type":... | [{"datasets":[],"id":4127,"numValue":63.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4128,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4129,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3140 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,140 | train | mutant | 670 | 48 | 726 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20G | V20G | 1 | 1 | 0 | 0 | 20 | V | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,103 | ProTherm | 3.19 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2G | 65.7 | null | null | null | 108.03 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.19,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2G","type":... | [{"datasets":[],"id":4130,"numValue":65.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4131,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4132,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3141 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,141 | train | mutant | 670 | 48 | 726 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20G | V20G | 1 | 1 | 0 | 0 | 20 | V | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,104 | ProTherm | 3.4 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2G | 69.03 | null | null | null | 112.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.4,"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:V2G","type":"... | [{"datasets":[],"id":4133,"numValue":69.03,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4134,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4135,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3142 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,142 | train | mutant | 670 | 48 | 726 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20G | V20G | 1 | 1 | 0 | 0 | 20 | V | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,166 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2G | 57.4 | -7.5 | null | null | 106.6 | 1.31 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2G","type":"... | [{"datasets":[],"id":4319,"numValue":57.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4320,"numValue":-7.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4321,"numValue":106.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3143 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,143 | train | mutant | 670 | 48 | 726 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20G | V20G | 1 | 1 | 0 | 0 | 20 | V | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,181 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2G | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2G","type":"... | [{"datasets":[],"id":4394,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4395,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3144 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,144 | train | mutant | 670 | 48 | 726 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20G | V20G | 1 | 1 | 0 | 0 | 20 | V | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,939 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V2G | null | null | null | 2.29 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24488,"numValue":2.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24489,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3145 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,145 | train | mutant | 671 | 48 | 727 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20I | V20I | 1 | 1 | 0 | 0 | 20 | V | I | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,105 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2I | 65.06 | null | null | null | 108.03 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2I","type":"... | [{"datasets":[],"id":4136,"numValue":65.06,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4137,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4138,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3146 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,146 | train | mutant | 671 | 48 | 727 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20I | V20I | 1 | 1 | 0 | 0 | 20 | V | I | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,106 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2I | 67.98 | null | null | null | 114.01 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2I","type":"... | [{"datasets":[],"id":4139,"numValue":67.98,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4140,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4141,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3147 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,147 | train | mutant | 671 | 48 | 727 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20I | V20I | 1 | 1 | 0 | 0 | 20 | V | I | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,107 | ProTherm | 2.92 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2I | 72.23 | null | null | null | 119.02 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.92,"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:V2I","type":... | [{"datasets":[],"id":4142,"numValue":72.23,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4143,"numValue":119.02,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4144,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3148 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,148 | train | mutant | 671 | 48 | 727 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20I | V20I | 1 | 1 | 0 | 0 | 20 | V | I | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,108 | ProTherm | 3.13 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2I | 75.47 | null | null | null | 125 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.13,"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:V2I","type":... | [{"datasets":[],"id":4145,"numValue":75.47,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4146,"numValue":125.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4147,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3149 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,149 | train | mutant | 671 | 48 | 727 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20I | V20I | 1 | 1 | 0 | 0 | 20 | V | I | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,167 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2I | 68.3 | 3.4 | null | null | 108.03 | 1.58 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2I","type":"... | [{"datasets":[],"id":4324,"numValue":68.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4325,"numValue":3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4326,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3150 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,150 | train | mutant | 671 | 48 | 727 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20I | V20I | 1 | 1 | 0 | 0 | 20 | V | I | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,182 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2I | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2I","type":"... | [{"datasets":[],"id":4396,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4397,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3151 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,151 | train | mutant | 671 | 48 | 727 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20I | V20I | 1 | 1 | 0 | 0 | 20 | V | I | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,940 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V2I | null | null | null | -1.1 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24490,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24491,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3153 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,153 | train | mutant | 672 | 48 | 728 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20L | V20L | 1 | 1 | 0 | 0 | 20 | V | L | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,110 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2L | 64.55 | null | null | null | 108.99 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2L","type":"... | [{"datasets":[],"id":4151,"numValue":64.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4152,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4153,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3154 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,154 | train | mutant | 672 | 48 | 728 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20L | V20L | 1 | 1 | 0 | 0 | 20 | V | L | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,111 | ProTherm | 3.05 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2L | 70.39 | null | null | null | 116.16 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.05,"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:V2L","type":... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4154,"numValue":70.39,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4155,"numValue":116.16,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4156,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3155 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,155 | train | mutant | 672 | 48 | 728 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20L | V20L | 1 | 1 | 0 | 0 | 20 | V | L | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,168 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2L | 64.7 | -0.2 | null | null | 109.46 | 1.22 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2L","type":"... | [{"datasets":[],"id":4329,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4330,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4331,"numValue":109.46,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3156 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,156 | train | mutant | 672 | 48 | 728 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20L | V20L | 1 | 1 | 0 | 0 | 20 | V | L | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,183 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2L | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2L","type":"... | [{"datasets":[],"id":4398,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4399,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3157 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,157 | train | mutant | 672 | 48 | 728 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20L | V20L | 1 | 1 | 0 | 0 | 20 | V | L | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,941 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V2L | null | null | null | 0.05 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24492,"numValue":0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24493,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3158 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,158 | train | mutant | 673 | 48 | 729 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20M | V20M | 1 | 1 | 0 | 0 | 20 | V | M | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,112 | ProTherm | 2.52 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2M | 60.62 | null | null | null | 106.12 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.52,"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:V2M","type":... | [{"datasets":[],"id":4157,"numValue":60.62,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4158,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4159,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3159 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,159 | train | mutant | 673 | 48 | 729 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20M | V20M | 1 | 1 | 0 | 0 | 20 | V | M | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,113 | ProTherm | 2.73 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2M | 64.55 | null | null | null | 112.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.73,"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:V2M","type":... | [{"datasets":[],"id":4160,"numValue":64.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4161,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4162,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3160 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,160 | train | mutant | 673 | 48 | 729 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20M | V20M | 1 | 1 | 0 | 0 | 20 | V | M | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,114 | ProTherm | 2.94 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2M | 68.26 | null | null | null | 118.07 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.94,"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:V2M","type":... | [{"datasets":[],"id":4163,"numValue":68.26,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4164,"numValue":118.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4165,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3161 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,161 | train | mutant | 673 | 48 | 729 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20M | V20M | 1 | 1 | 0 | 0 | 20 | V | M | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,115 | ProTherm | 3.09 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2M | 70.56 | null | null | null | 121.89 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.09,"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:V2M","type":... | [{"datasets":[],"id":4166,"numValue":70.56,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4167,"numValue":121.89,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4168,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3162 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,162 | train | mutant | 673 | 48 | 729 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20M | V20M | 1 | 1 | 0 | 0 | 20 | V | M | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,116 | ProTherm | 3.31 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2M | 74.24 | null | null | null | 126.91 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.31,"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:V2M","type":... | [{"datasets":[],"id":4169,"numValue":74.24,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4170,"numValue":126.91,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4171,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3163 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,163 | train | mutant | 673 | 48 | 729 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20M | V20M | 1 | 1 | 0 | 0 | 20 | V | M | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,169 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2M | 63.9 | -1 | null | null | 112.57 | 1.55 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2M","type":"... | [{"datasets":[],"id":4334,"numValue":63.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4335,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4336,"numValue":112.57,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3165 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,165 | train | mutant | 673 | 48 | 729 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20M | V20M | 1 | 1 | 0 | 0 | 20 | V | M | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,942 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V2M | null | null | null | 0.31 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24494,"numValue":0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24495,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3166 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,166 | train | mutant | 674 | 48 | 730 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20F | V20F | 1 | 1 | 0 | 0 | 20 | V | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,117 | ProTherm | 2.68 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2F | 61.97 | null | null | null | 106.12 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.68,"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:V2F","type":... | [{"datasets":[],"id":4172,"numValue":61.97,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4173,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4174,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3167 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,167 | train | mutant | 674 | 48 | 730 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20F | V20F | 1 | 1 | 0 | 0 | 20 | V | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,118 | ProTherm | 2.87 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2F | 65.05 | null | null | null | 109.94 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.87,"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:V2F","type":... | [{"datasets":[],"id":4175,"numValue":65.05,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":4176,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4177,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3168 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,168 | train | mutant | 674 | 48 | 730 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20F | V20F | 1 | 1 | 0 | 0 | 20 | V | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,119 | ProTherm | 3.09 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2F | 68.6 | null | null | null | 115.92 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.09,"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:V2F","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":4178,"numValue":68.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4179,"numValue":115.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4180,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3169 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,169 | train | mutant | 674 | 48 | 730 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20F | V20F | 1 | 1 | 0 | 0 | 20 | V | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,120 | ProTherm | 3.22 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2F | 71.22 | null | null | null | 120.94 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.22,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2F","type":... | [{"datasets":[],"id":4181,"numValue":71.22,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":4182,"numValue":... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3170 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,170 | train | mutant | 674 | 48 | 730 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20F | V20F | 1 | 1 | 0 | 0 | 20 | V | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,170 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2F | 62.2 | -2.7 | null | null | 110.18 | 1.63 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2F","type":"... | [{"datasets":[],"id":4339,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4340,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4341,"numValue":110.18,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3171 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,171 | train | mutant | 674 | 48 | 730 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20F | V20F | 1 | 1 | 0 | 0 | 20 | V | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,185 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V2F | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2F","type":"... | [{"datasets":[],"id":4402,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4403,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3172 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,172 | train | mutant | 674 | 48 | 730 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20F | V20F | 1 | 1 | 0 | 0 | 20 | V | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,943 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V2F | null | null | null | 0.86 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24496,"numValue":0.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24497,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3173 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,173 | train | mutant | 718 | 48 | 784 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20S | V20S | 1 | 1 | 0 | 0 | 20 | V | S | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,254 | ProTherm | 2.65 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2S | 59.4 | null | null | null | 103.01 | null | 103.01 | 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":2.65,"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:V2S","type":"_PD... | [{"datasets":[],"id":4608,"numValue":59.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4609,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4610,"numValue":103.01,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4611,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3174 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,174 | train | mutant | 718 | 48 | 784 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20S | V20S | 1 | 1 | 0 | 0 | 20 | V | S | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,255 | ProTherm | 2.83 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2S | 62.9 | null | null | null | 108.03 | null | 107.07 | 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":2.83,"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:V2S","type":"_PD... | [{"datasets":[],"id":4612,"numValue":62.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4613,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4614,"numValue":107.07,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4615,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3175 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,175 | train | mutant | 718 | 48 | 784 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20S | V20S | 1 | 1 | 0 | 0 | 20 | V | S | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,256 | ProTherm | 3.09 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2S | 67.1 | null | null | null | 114.96 | null | 114.01 | 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":3.09,"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:V2S","type":"_PD... | [{"datasets":[],"id":4616,"numValue":67.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4617,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4618,"numValue":114.01,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4619,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3177 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,177 | train | mutant | 718 | 48 | 784 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20S | V20S | 1 | 1 | 0 | 0 | 20 | V | S | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,258 | ProTherm | 3.45 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2S | 73 | null | null | null | 124.04 | null | 125.96 | 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":3.45,"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:V2S","type":"_PD... | [{"datasets":[],"id":4624,"numValue":73.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4625,"numValue":124.04,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4626,"numValue":125.96,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4627,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3178 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,178 | train | mutant | 718 | 48 | 784 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20S | V20S | 1 | 1 | 0 | 0 | 20 | V | S | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,317 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2S | 60.5 | -4.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | 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:V2S","type":"_PDB... | [{"datasets":[],"id":4860,"numValue":60.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4861,"numValue":-4.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4862,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3179 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,179 | train | mutant | 718 | 48 | 784 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20S | V20S | 1 | 1 | 0 | 0 | 20 | V | S | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,954 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V2S | null | null | null | 1.41 | 111.14 | 1.55 | 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":24518,"numValue":111.14,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24519,"numValue":1.55,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24520,"numValue":1.41,"references":[],"strValue":null,"t... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3180 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,180 | train | mutant | 719 | 48 | 785 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20Y | V20Y | 1 | 1 | 0 | 0 | 20 | V | Y | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,259 | ProTherm | 2.83 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2Y | 65.9 | null | null | null | 108.03 | null | 110.18 | 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":2.83,"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:V2Y","type":"_PD... | [{"datasets":[],"id":4628,"numValue":65.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4629,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4630,"numValue":110.18,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4631,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3181 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,181 | train | mutant | 719 | 48 | 785 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20Y | V20Y | 1 | 1 | 0 | 0 | 20 | V | Y | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,260 | ProTherm | 2.91 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2Y | 67.4 | null | null | null | 111.14 | null | 112.09 | 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":2.91,"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:V2Y","type":"_PD... | [{"datasets":[],"id":4632,"numValue":67.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4633,"numValue":111.14,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4634,"numValue":112.09,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4635,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3182 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,182 | train | mutant | 719 | 48 | 785 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20Y | V20Y | 1 | 1 | 0 | 0 | 20 | V | Y | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,261 | ProTherm | 3.2 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2Y | 72.3 | null | null | null | 119.02 | 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":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2Y","type":"_PDB... | [{"datasets":[],"id":4636,"numValue":72.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4637,"numValue":119.02,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4638,"numValue":119.98,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4639,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3183 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,183 | train | mutant | 719 | 48 | 785 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20Y | V20Y | 1 | 1 | 0 | 0 | 20 | V | Y | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,262 | ProTherm | 3.21 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2Y | 72 | 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:V2Y","type":"_PD... | [{"datasets":[],"id":4640,"numValue":72.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4641,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4642,"numValue":119.98,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4643,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3184 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,184 | train | mutant | 719 | 48 | 785 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20Y | V20Y | 1 | 1 | 0 | 0 | 20 | V | Y | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,263 | ProTherm | 3.24 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2Y | 73 | null | null | null | 121.18 | null | 122.13 | 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":3.24,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2Y","type":"_PD... | [{"datasets":[],"id":4644,"numValue":73.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4645,"numValue":121.18,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4646,"numValue":122.13,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4647,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3186 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,186 | train | mutant | 719 | 48 | 785 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20Y | V20Y | 1 | 1 | 0 | 0 | 20 | V | Y | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,955 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V2Y | null | null | null | 0.36 | 106.12 | 1.82 | 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":24522,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24523,"numValue":1.82,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24524,"numValue":0.36,"references":[],"strValue":null,"t... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3187 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,187 | train | mutant | 720 | 48 | 786 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20D | V20D | 1 | 1 | 0 | 0 | 20 | V | D | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,264 | ProTherm | 2.66 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2D | 59.6 | null | null | null | 103.01 | null | 99.9 | 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":2.66,"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:V2D","type":"_PD... | [{"datasets":[],"id":4648,"numValue":59.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4649,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4650,"numValue":99.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4651,"numValue":null,"references":[],... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3188 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,188 | train | mutant | 720 | 48 | 786 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20D | V20D | 1 | 1 | 0 | 0 | 20 | V | D | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,265 | ProTherm | 2.96 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2D | 64.9 | null | null | null | 112.09 | null | 108.03 | 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":2.96,"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:V2D","type":"_PD... | [{"datasets":[],"id":4652,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4653,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4654,"numValue":108.03,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4655,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3189 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,189 | train | mutant | 720 | 48 | 786 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20D | V20D | 1 | 1 | 0 | 0 | 20 | V | D | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,266 | ProTherm | 3.01 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2D | 65.7 | null | null | null | 113.05 | null | 108.99 | 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":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2D","type":"_PD... | [{"datasets":[],"id":4656,"numValue":65.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4657,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4658,"numValue":108.99,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4659,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3190 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,190 | train | mutant | 720 | 48 | 786 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20D | V20D | 1 | 1 | 0 | 0 | 20 | V | D | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,267 | ProTherm | 3.14 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2D | 68 | null | null | null | 115.92 | null | 113.05 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":3.14,"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:V2D","type":"_PD... | [{"datasets":[],"id":4660,"numValue":68.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4661,"numValue":115.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4662,"numValue":113.05,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.cs... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3191 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,191 | train | mutant | 720 | 48 | 786 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20D | V20D | 1 | 1 | 0 | 0 | 20 | V | D | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,268 | ProTherm | 3.3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2D | 70.2 | null | null | null | 119.98 | null | 118.07 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|EASE-MM_S1676.csv|PON-TStab_dataset.csv|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":3.3,"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:V2D","type":"_PDB... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":4664,"numValue":70.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3192 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,192 | train | mutant | 720 | 48 | 786 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20D | V20D | 1 | 1 | 0 | 0 | 20 | V | D | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,319 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2D | 60.4 | -4.5 | 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:V2D","type":"_PDB... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4866,"numValue":60.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4867,"numValue":-4.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4868,"numValue":null,"re... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3193 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,193 | train | mutant | 720 | 48 | 786 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20D | V20D | 1 | 1 | 0 | 0 | 20 | V | D | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,956 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V2D | null | null | null | 1.43 | 111.38 | 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":24526,"numValue":111.38,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24527,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24528,"numValue":1.43,"references":[],"strValue":null,"t... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3194 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,194 | train | mutant | 721 | 48 | 787 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20N | V20N | 1 | 1 | 0 | 0 | 20 | V | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,269 | ProTherm | 2.6 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2N | 59.1 | null | null | null | 103.97 | null | 99.9 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | 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:V2N","type":"_PDB... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":4668,"numValue":5... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3195 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,195 | train | mutant | 721 | 48 | 787 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20N | V20N | 1 | 1 | 0 | 0 | 20 | V | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,270 | ProTherm | 2.82 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2N | 62.7 | null | null | null | 109.94 | null | 104.92 | 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":2.82,"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:V2N","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4672,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4673,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4674,"numValue":104.92,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4675,"numValue"... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3197 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,197 | train | mutant | 721 | 48 | 787 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20N | V20N | 1 | 1 | 0 | 0 | 20 | V | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,272 | ProTherm | 3.01 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2N | 66.3 | null | null | null | 117.11 | null | 110.9 | 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":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2N","type":"_PD... | [{"datasets":[],"id":4680,"numValue":66.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4681,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4682,"numValue":110.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4683,"numValue":null,"references":[]... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3198 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,198 | train | mutant | 721 | 48 | 787 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20N | V20N | 1 | 1 | 0 | 0 | 20 | V | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,320 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2N | 60.8 | -4.1 | 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:V2N","type":"_PDB... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4869,"numValue":60.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4870,"numValue":-4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4871,"numValue":null,"re... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3199 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,199 | train | mutant | 721 | 48 | 787 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20N | V20N | 1 | 1 | 0 | 0 | 20 | V | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,957 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V2N | null | null | null | 1.34 | 113.77 | 1.7 | 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":24530,"numValue":113.77,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24531,"numValue":1.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24532,"numValue":1.34,"references":[],"strValue":null,"ty... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3200 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,200 | train | mutant | 722 | 48 | 788 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20R | V20R | 1 | 1 | 0 | 0 | 20 | V | R | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,273 | ProTherm | 2.6 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2R | 62.1 | null | null | null | 103.01 | null | 109.94 | 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":2.6,"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:V2R","type":"_PDB... | [{"datasets":[],"id":4684,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4685,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4686,"numValue":109.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["H... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3201 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,201 | train | mutant | 722 | 48 | 788 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20R | V20R | 1 | 1 | 0 | 0 | 20 | V | R | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,274 | ProTherm | 2.88 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2R | 66.4 | null | null | null | 108.03 | 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":2.88,"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:V2R","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4688,"numValue":66.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4689,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4690,"numValue":114.96,"references":[],"strValue":null,"type":"DH... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3203 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,203 | train | mutant | 722 | 48 | 788 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20R | V20R | 1 | 1 | 0 | 0 | 20 | V | R | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,276 | ProTherm | 3.15 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2R | 70.7 | null | null | null | 114.01 | 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":3.15,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2R","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4696,"numValue":70.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4697,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4698,"numValue":123.09,"references":[],"strValue":null,"type":"DH... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3204 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,204 | train | mutant | 722 | 48 | 788 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20R | V20R | 1 | 1 | 0 | 0 | 20 | V | R | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,277 | ProTherm | 3.3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2R | 74.1 | null | null | null | 119.98 | null | 125.96 | 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":3.3,"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:V2R","type":"_PDB... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4700,"numValue":74.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4701,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4702,"numValue":125.96,"references":[],"strValue":null,"type":"DH... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3205 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,205 | train | mutant | 722 | 48 | 788 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20R | V20R | 1 | 1 | 0 | 0 | 20 | V | R | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 1,321 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V2R | 63.6 | -1.3 | 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:V2R","type":"_PDB... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4872,"numValue":63.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4873,"numValue":-1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4874,"numValue":null,"re... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3206 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,206 | train | mutant | 722 | 48 | 788 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20R | V20R | 1 | 1 | 0 | 0 | 20 | V | R | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,958 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V2R | null | null | null | 0.38 | 106.36 | 1.41 | 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":24534,"numValue":106.36,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24535,"numValue":1.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24536,"numValue":0.38,"references":[],"strValue":null,"t... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3207 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,207 | train | mutant | 1,723 | 48 | 1,933 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20A | V20A | 1 | 1 | 0 | 0 | 20 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 3,189 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V2A | 41.3 | -7.9 | null | null | 65.55 | 1.44 | 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:V2A","type":"_PDB... | [{"datasets":[],"id":11653,"numValue":41.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11654,"numValue":-7.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11655,"numValue":65.55,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3208 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,208 | train | mutant | 1,723 | 48 | 1,933 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20A | V20A | 1 | 1 | 0 | 0 | 20 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 3,220 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V2A | 48.3 | null | null | null | 65.1 | null | 70.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":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:V2A","type":"_PDB... | [{"datasets":[],"id":11789,"numValue":48.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11790,"numValue":65.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11791,"numValue":70.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11792,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3209 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,209 | train | mutant | 1,723 | 48 | 1,933 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20A | V20A | 1 | 1 | 0 | 0 | 20 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 3,221 | ProTherm | 3.02 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V2A | 47.3 | null | null | null | 62 | null | 67.5 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.02,"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:V2A","type":"_PD... | [{"datasets":[],"id":11793,"numValue":47.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11794,"numValue":62.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11795,"numValue":67.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11796,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3210 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,210 | train | mutant | 1,723 | 48 | 1,933 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20A | V20A | 1 | 1 | 0 | 0 | 20 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 3,222 | ProTherm | 2.71 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V2A | 41.4 | null | null | null | 54.5 | null | 60.3 | 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":2.71,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V2A","type":"_PD... | [{"datasets":[],"id":11797,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11798,"numValue":54.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11799,"numValue":60.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11800,"numValue":null,"references":[... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3211 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,211 | train | mutant | 1,723 | 48 | 1,933 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20A | V20A | 1 | 1 | 0 | 0 | 20 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 4,165 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V2A | 60.3 | -4.6 | null | null | 111.96 | 1.56 | 114.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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:V2A","type":"_PDB... | [{"datasets":[],"id":15424,"numValue":60.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15425,"numValue":-4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15426,"numValue":111.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3212 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,212 | train | mutant | 1,723 | 48 | 1,933 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V20A | V20A | 1 | 1 | 0 | 0 | 20 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 20 | A | B | false | false | 103.225621 | 17.771429 | 6,888 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V2A | null | null | null | 1.51 | null | 1.56 | 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":24345,"numValue":1.56,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24346,"numValue":1.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24347,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":6975,"numValue":4.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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