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:2102 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,102 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 907 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:A82P | 67.85 | 1.34 | null | null | null | 2.5 | 142 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3366,"numValue":67.85,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3367,"numValue":1.34,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3368,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2103 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,103 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 2,995 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:A82P | 42.7 | 0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A82P","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10876,"numValue":42.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv","STRUM_Q3421.csv"],"id":10877,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S196... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2104 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,104 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 4,658 | ProTherm | 2 | CD | Thermal | Phosphate buffer | 50 mM | null | 2LZM_A:A82P | 42.7 | 0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A82P","typ... | [{"datasets":[],"id":17224,"numValue":42.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17225,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17226,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2105 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,105 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 6,722 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:A82P | null | null | null | -0.57 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23888,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S983.csv"],"id":23889,"numValue":-0.57,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23890,"numValue":null,"references":[],"strVal... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2106 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,106 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 6,982 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | 64.7 | KCl | 100 mM | 2LZM_A:A82P | null | null | null | -0.8 | null | 2 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24609,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":24610,"numValue":-0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24611,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2107 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,107 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 7,001 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 64.7 | KCl | 0.15 M | 2LZM_A:A82P | null | null | null | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":24648,"numValue":-0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24649,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2108 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,108 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 7,328 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:A82P | null | null | null | -1.27 | null | 2.39 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":25565,"numValue":2.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25566,"numValue":-1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25567,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2109 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,109 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 7,337 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:A82P | null | null | null | -0.45 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":25592,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25593,"numValue":-0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25594,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2110 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,110 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 7,846 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.2 | KCl | 25 mM | 2LZM_A:A82P | null | null | null | -0.51 | null | 2.39 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26840,"numValue":2.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26841,"numValue":-0.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26842,"numValue":null,"references":[],"strValue":"yes","type":... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2111 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,111 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 8,030 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | 41.9 | KCl | 100 mM | 2LZM_A:A82P | null | null | null | -0.3 | null | 2 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CON... | [{"datasets":[],"id":27374,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":27375,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27376,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2112 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,112 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 8,048 | ProTherm | 2 | CD | Thermal | H3PO4,HCl | 10 mM,10 mM | 41.9 | KCl | 0.2 M | 2LZM_A:A82P | null | null | null | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM","type":"BU... | [{"datasets":["capriotti_S1615_map.csv"],"id":27411,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27412,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2113 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,113 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 8,210 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:A82P | null | null | null | 0.07 | null | 2.39 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":27810,"numValue":2.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27811,"numValue":0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27812,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2114 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,114 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 12,610 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:A82P | null | null | null | 0.72 | null | null | null | 5.9 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["SAAFEC_S1262.csv"],"id":45733,"numValue":0.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45734,"numValue":5.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45735,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2115 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,115 | train | mutant | 328 | 41 | 364 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 13,903 | ProTherm | 5.7 | CD | GdnHCl | Phosphate buffer | 50 mM | 12 | 2LZM_A:A82P | null | null | 18.6 | null | null | null | null | 2.58 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":12.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":51453,"numValue":18.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51454,"numValue":2.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":51455,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":51456,"numValue":null,"references":[... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2116 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,116 | train | mutant | 1,777 | 41 | 1,990 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H | K83H | 1 | 1 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83 | A | T | false | false | 127.692366 | 41.88 | 3,418 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:K83H | 36.3 | -2.2 | null | null | null | null | 80 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12611,"numValue":36.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":12612,"numValue":-2.2,"references":[... | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2117 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,117 | train | mutant | 1,777 | 41 | 1,990 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H | K83H | 1 | 1 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83 | A | T | false | false | 127.692366 | 41.88 | 3,419 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:K83H | 62 | -1 | null | null | null | null | 122 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Broom_S605.csv|Saraboji_S1791.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv"],"id":12615,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":12616,"numValue":-1.0,"references":[],"strValu... | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2118 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,118 | train | mutant | 1,777 | 41 | 1,990 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H | K83H | 1 | 1 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83 | A | T | false | false | 127.692366 | 41.88 | 7,040 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63 | KCl | 0.15 M | 2LZM_A:K83H | null | null | null | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24747,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24748,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2119 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,119 | train | mutant | 1,777 | 41 | 1,990 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H | K83H | 1 | 1 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83 | A | T | false | false | 127.692366 | 41.88 | 8,427 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 28.5 | KCl | 0.15 M | 2LZM_A:K83H | null | null | null | 0.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":28.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":28656,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28657,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2120 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,120 | train | mutant | 6,768 | 41 | 7,410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H|A112D | K83H|A112D | 2 | 2 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83|112 | A | T|H | false | false | 72.298039 | 36.551 | 14,545 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:K83H 2LZM_A:A112D | 33.7 | -4.8 | null | null | null | null | 73 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53770,"numValue":33.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53771,"numValue":-4.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53772,"numValue":73.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53773,"numValue":null,"references":... | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6903,"numValue":6.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2121 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,121 | train | mutant | 6,768 | 41 | 7,410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H|A112D | K83H|A112D | 2 | 2 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83|112 | A | T|H | false | false | 72.298039 | 36.551 | 14,546 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:K83H 2LZM_A:A112D | 62 | -3.4 | null | null | null | null | 122 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53774,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53775,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53776,"numValue":122.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53777,"numValue":null,"references"... | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6903,"numValue":6.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2123 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,123 | train | mutant | 6,768 | 41 | 7,410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H|A112D | K83H|A112D | 2 | 2 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83|112 | A | T|H | false | false | 72.298039 | 36.551 | 14,933 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 64.6 | KCl | 0.15 M | 2LZM_A:K83H 2LZM_A:A112D | null | null | null | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":64.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":55021,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55022,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6903,"numValue":6.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2124 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,124 | train | mutant | 6,768 | 41 | 7,410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H|A112D | K83H|A112D | 2 | 2 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83|112 | A | T|H | false | false | 72.298039 | 36.551 | 14,934 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | 64.6 | KCl | 0.15 M | 2LZM_A:K83H 2LZM_A:A112D | null | null | null | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":64.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":55023,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55024,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6903,"numValue":6.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2125 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,125 | train | mutant | 6,768 | 41 | 7,410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K83H|A112D | K83H|A112D | 2 | 2 | 0 | 0 | 83 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 83|112 | A | T|H | false | false | 72.298039 | 36.551 | 14,935 | ProTherm | 6.5 | CD | Thermal | HCl | 10 mM | 64.6 | KCl | 0.15 M | 2LZM_A:K83H 2LZM_A:A112D | null | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":55025,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55026,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6874,"numValue":3.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6903,"numValue":6.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2126 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,126 | train | mutant | 161 | 41 | 189 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84M | L84M | 1 | 1 | 0 | 0 | 84 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84 | A | H | true | false | 0 | 17.8475 | 298 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:L84M | 60.4 | -4.9 | null | null | null | 2.5 | 110 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":1215,"numValue":60.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1216,"numValue":-4.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1217,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2127 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,127 | train | mutant | 161 | 41 | 189 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84M | L84M | 1 | 1 | 0 | 0 | 84 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84 | A | H | true | false | 0 | 17.8475 | 6,769 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:L84M | null | null | null | 1.9 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 m... | [{"datasets":[],"id":24009,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24010,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24011,"numValue":null,"references... | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2128 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,128 | train | mutant | 1,129 | 41 | 1,273 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84A | L84A | 1 | 1 | 0 | 0 | 84 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84 | A | H | true | false | 0 | 17.8475 | 2,023 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L84A | 54.8 | -10.5 | null | null | null | null | 101 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7557,"numValue":54.8,"references":[],"strValue":null,"type":"TM"}... | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2129 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,129 | train | mutant | 1,129 | 41 | 1,273 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84A | L84A | 1 | 1 | 0 | 0 | 84 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84 | A | H | true | false | 0 | 17.8475 | 3,144 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L84A | 38.3 | -13.4 | null | null | null | 1.8 | 67 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11472,"numValue":38.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11473,"numValue":-13.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11474,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2130 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,130 | train | mutant | 1,129 | 41 | 1,273 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84A | L84A | 1 | 1 | 0 | 0 | 84 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84 | A | H | true | false | 0 | 17.8475 | 6,790 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:L84A | null | null | null | 3.7 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24072,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24073,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24074,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2131 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,131 | train | mutant | 1,129 | 41 | 1,273 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84A | L84A | 1 | 1 | 0 | 0 | 84 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84 | A | H | true | false | 0 | 17.8475 | 7,578 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:L84A | null | null | null | 3.9 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26207,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26208,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26209,"numV... | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2132 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,132 | train | mutant | 6,900 | 41 | 7,542 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84M|L91M|L99M | L84M|L91M|L99M | 3 | 3 | 0 | 0 | 84 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84|91|99 | A | H|S | true | false | 2.100846 | 15.070208 | 14,742 | ProTherm | 5.42 | DSC | Thermal | Sodium acetate,Acetic acid, | 8.6 mM,1.4 mM, | null | NaCl | 0.10 M | 2LZM_A:L84M 2LZM_A:L91M 2LZM_A:L99M | 56.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 913 | ARTICLE | Substitution with selenomethionine can enhance the stability of methionine-rich proteins. | 1,999 | 10.1006/jmbi.1999.3220 | 10556025 | J Mol Biol;294;17-20 | 4 | Baase W A|Matthews B W|Gassner N C|Hausrath A C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"8.6 mM,1.4 mM,","type":"BUFFER_CONC"},{"numValue":null,"strVal... | [{"datasets":[],"id":54505,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54506,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:2133 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,133 | train | mutant | 6,901 | 41 | 7,543 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84M|L91M|L99M|L118M|L121M | L84M|L91M|L99M|L118M|L121M | 5 | 5 | 0 | 0 | 84 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84|91|99|118|121 | A | H|S | true | false | 3.970357 | 16.666625 | 14,743 | ProTherm | 5.42 | DSC | Thermal | Sodium acetate,Acetic acid, | 8.6 mM,1.4 mM, | null | NaCl | 0.10 M | 2LZM_A:L84M 2LZM_A:L91M 2LZM_A:L99M 2LZM_A:L118M 2LZM_A:L121M | 53 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 913 | ARTICLE | Substitution with selenomethionine can enhance the stability of methionine-rich proteins. | 1,999 | 10.1006/jmbi.1999.3220 | 10556025 | J Mol Biol;294;17-20 | 4 | Baase W A|Matthews B W|Gassner N C|Hausrath A C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"8.6 mM,1.4 mM,","type":"BUFFER_CONC"},{"numValue":null,"strVal... | [{"datasets":[],"id":54507,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54508,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:2134 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,134 | train | mutant | 6,902 | 41 | 7,544 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84M|L91M|L99M|L118M|L121M|L133M|F153M | L84M|L91M|L99M|L118M|L121M|L133M|F153M | 7 | 7 | 0 | 0 | 84 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84|91|99|118|121|133|153 | A | H|S | true | false | 3.180225 | 16.583531 | 14,744 | ProTherm | 5.42 | DSC | Thermal | Sodium acetate,Acetic acid, | 8.6 mM,1.4 mM, | null | NaCl | 0.10 M | 2LZM_A:L84M 2LZM_A:L91M 2LZM_A:L99M 2LZM_A:L118M 2LZM_A:L121M 2LZM_A:L133M 2LZM_A:F153M | 50.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 913 | ARTICLE | Substitution with selenomethionine can enhance the stability of methionine-rich proteins. | 1,999 | 10.1006/jmbi.1999.3220 | 10556025 | J Mol Biol;294;17-20 | 4 | Baase W A|Matthews B W|Gassner N C|Hausrath A C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"8.6 mM,1.4 mM,","type":"BUFFER_CONC"},{"numValue":null,"strVal... | [{"datasets":[],"id":54509,"numValue":50.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54510,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:2135 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,135 | train | mutant | 6,903 | 41 | 7,545 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L84M|L91M|L99M|L118M|L121M|V111M|L133M | L84M|L91M|L99M|L118M|L121M|V111M|L133M | 7 | 7 | 0 | 0 | 84 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 84|91|99|111|118|121|133 | A | H|S | true | false | 3.104711 | 16.927946 | 14,745 | ProTherm | 5.42 | DSC | Thermal | Sodium acetate,Acetic acid, | 8.6 mM,1.4 mM, | null | NaCl | 0.10 M | 2LZM_A:L84M 2LZM_A:L91M 2LZM_A:L99M 2LZM_A:V111M 2LZM_A:L118M 2LZM_A:L121M 2LZM_A:L133M | 53.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 913 | ARTICLE | Substitution with selenomethionine can enhance the stability of methionine-rich proteins. | 1,999 | 10.1006/jmbi.1999.3220 | 10556025 | J Mol Biol;294;17-20 | 4 | Baase W A|Matthews B W|Gassner N C|Hausrath A C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"8.6 mM,1.4 mM,","type":"BUFFER_CONC"},{"numValue":null,"strVal... | [{"datasets":[],"id":54511,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54512,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6875,"numValue":8.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:2137 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,137 | train | mutant | 1,452 | 41 | 1,639 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K85A | K85A | 1 | 1 | 0 | 0 | 85 | K | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 85 | A | H | false | false | 81.320475 | 27.995 | 2,791 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:K85A | null | -1 | null | null | null | null | 126 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10195,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10196,"numValue":126.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10197,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6876,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2138 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,138 | train | mutant | 1,452 | 41 | 1,639 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K85A | K85A | 1 | 1 | 0 | 0 | 85 | K | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 85 | A | H | false | false | 81.320475 | 27.995 | 2,812 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:K85A | null | 0.9 | null | null | null | null | 134 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10258,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10259,"numValue":134.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10260,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6876,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2140 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,140 | train | mutant | 1,452 | 41 | 1,639 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K85A | K85A | 1 | 1 | 0 | 0 | 85 | K | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 85 | A | H | false | false | 81.320475 | 27.995 | 7,991 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:K85A | null | null | null | -0.1 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":27276,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27277,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27278,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6876,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2141 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,141 | train | mutant | 7,606 | 41 | 8,309 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K85A|R96H | K85A|R96H | 2 | 2 | 0 | 0 | 85 | K | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 85|96 | A | H | false | false | 79.026749 | 23.689773 | 16,137 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:K85A 2LZM_A:R96H | null | -9.8 | null | null | null | null | 122 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":59117,"numValue":-9.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":59118,"numValue":122.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":59119,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6876,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2142 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,142 | train | mutant | 7,606 | 41 | 8,309 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K85A|R96H | K85A|R96H | 2 | 2 | 0 | 0 | 85 | K | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 85|96 | A | H | false | false | 79.026749 | 23.689773 | 16,139 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:K85A 2LZM_A:R96H | null | -8.3 | null | null | null | null | 109 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":59123,"numValue":-8.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":59124,"numValue":109.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":59125,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6876,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2144 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,144 | train | mutant | 7,606 | 41 | 8,309 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K85A|R96H | K85A|R96H | 2 | 2 | 0 | 0 | 85 | K | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 85|96 | A | H | false | false | 79.026749 | 23.689773 | 16,795 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:K85A 2LZM_A:R96H | null | null | null | 3.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":61720,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61721,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61722,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6876,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2145 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,145 | train | mutant | 508 | 41 | 558 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86A | P86A | 1 | 1 | 0 | 0 | 86 | P | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 830 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86A | 40 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3137,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3138,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3139,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2146 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,146 | train | mutant | 508 | 41 | 558 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86A | P86A | 1 | 1 | 0 | 0 | 86 | P | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 2,997 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:P86A | 40.6 | -1.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:P86A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10882,"numValue":40.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10883,"numValue":-1.3,"references":[],"strValue":nul... | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2148 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,148 | train | mutant | 508 | 41 | 558 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86A | P86A | 1 | 1 | 0 | 0 | 86 | P | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 13,902 | ProTherm | 5.7 | CD | GdnHCl | Phosphate buffer | 50 mM | 12 | 2LZM_A:P86A | null | null | 17.8 | null | null | null | null | 2.49 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":12.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":51449,"numValue":17.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51450,"numValue":2.49,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":51451,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":51452,"numValue":null,"references":[... | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2149 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,149 | train | mutant | 509 | 41 | 559 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86R | P86R | 1 | 1 | 0 | 0 | 86 | P | R | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 831 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86R | 40 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3140,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3141,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3142,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2150 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,150 | train | mutant | 509 | 41 | 559 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86R | P86R | 1 | 1 | 0 | 0 | 86 | P | R | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 840 | ProTherm | 4 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86R | 62 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3167,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3168,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3169,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2151 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,151 | train | mutant | 509 | 41 | 559 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86R | P86R | 1 | 1 | 0 | 0 | 86 | P | R | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 843 | ProTherm | 6 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86R | 63 | -3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3176,"numValue":63.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3177,"numValue":-3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3178,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2152 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,152 | train | mutant | 510 | 41 | 560 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86D | P86D | 1 | 1 | 0 | 0 | 86 | P | D | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 832 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86D | 42 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3143,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3144,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3145,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2153 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,153 | train | mutant | 510 | 41 | 560 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86D | P86D | 1 | 1 | 0 | 0 | 86 | P | D | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 841 | ProTherm | 4 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86D | 63 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3170,"numValue":63.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3171,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3172,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2154 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,154 | train | mutant | 510 | 41 | 560 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86D | P86D | 1 | 1 | 0 | 0 | 86 | P | D | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 844 | ProTherm | 6 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86D | 65 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3179,"numValue":65.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3180,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3181,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2156 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,156 | train | mutant | 512 | 41 | 562 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86G | P86G | 1 | 1 | 0 | 0 | 86 | P | G | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 834 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86G | 40 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3149,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3150,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3151,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2157 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,157 | train | mutant | 512 | 41 | 562 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86G | P86G | 1 | 1 | 0 | 0 | 86 | P | G | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 842 | ProTherm | 4 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86G | 62 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3173,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3174,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3175,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2159 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,159 | train | mutant | 513 | 41 | 563 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86H | P86H | 1 | 1 | 0 | 0 | 86 | P | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 835 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86H | 40 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3152,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3153,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3154,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2160 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,160 | train | mutant | 513 | 41 | 563 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86H | P86H | 1 | 1 | 0 | 0 | 86 | P | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 845 | ProTherm | 6 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86H | 62 | -4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3182,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3183,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3184,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2161 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,161 | train | mutant | 514 | 41 | 564 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86I | P86I | 1 | 1 | 0 | 0 | 86 | P | I | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 836 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86I | 40 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3155,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3156,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3157,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2162 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,162 | train | mutant | 515 | 41 | 565 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86L | P86L | 1 | 1 | 0 | 0 | 86 | P | L | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 837 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86L | 40 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3158,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3159,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3160,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2163 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,163 | train | mutant | 516 | 41 | 566 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86S | P86S | 1 | 1 | 0 | 0 | 86 | P | S | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 838 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86S | 41 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3161,"numValue":41.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3162,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3163,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2164 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,164 | train | mutant | 517 | 41 | 567 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P86T | P86T | 1 | 1 | 0 | 0 | 86 | P | T | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 86 | A | H | false | false | 56.381608 | 23.802857 | 839 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:P86T | 41 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3164,"numValue":41.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3165,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3166,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6877,"numValue":3.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2165 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,165 | train | mutant | 239 | 41 | 269 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87T | V87T | 1 | 1 | 0 | 0 | 87 | V | T | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 425 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V87T | 47 | -4.55 | null | null | null | null | 105 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1751,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1752,"numValue":-4.55,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1753,"numValue":105.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2166 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,166 | train | mutant | 239 | 41 | 269 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87T | V87T | 1 | 1 | 0 | 0 | 87 | V | T | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 7,594 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:V87T | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26245,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26246,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2167 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,167 | train | mutant | 806 | 41 | 910 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87I | V87I | 1 | 1 | 0 | 0 | 87 | V | I | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 1,422 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:V87I | 64.7 | -0.8 | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.10 M, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":5191,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5192,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5193,"numValue":127.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5194,"numValue":null,"references":[],... | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2168 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,168 | train | mutant | 806 | 41 | 910 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87I | V87I | 1 | 1 | 0 | 0 | 87 | V | I | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 7,078 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | 61 | 2LZM_A:V87I | null | null | null | 0.3 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":61.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":24833,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24834,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24835,"numValue":null,"references":[],"strValue":"Unknown",... | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2169 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,169 | train | mutant | 1,130 | 41 | 1,274 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87A | V87A | 1 | 1 | 0 | 0 | 87 | V | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 2,024 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:V87A | 61 | -4.3 | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7562,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets... | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2171 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,171 | train | mutant | 1,130 | 41 | 1,274 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87A | V87A | 1 | 1 | 0 | 0 | 87 | V | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 6,791 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:V87A | null | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24075,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24076,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24077,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2172 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,172 | train | mutant | 1,130 | 41 | 1,274 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87A | V87A | 1 | 1 | 0 | 0 | 87 | V | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 7,566 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:V87A | null | null | null | 1.7 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26171,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26172,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26173,"numV... | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2173 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,173 | train | mutant | 1,130 | 41 | 1,274 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87A | V87A | 1 | 1 | 0 | 0 | 87 | V | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 10,024 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:V87A | null | null | 12.1 | 2.8 | null | null | null | null | 2.5 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 664 | ARTICLE | Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway. | 2,007 | 10.1110/ps.062632807 | 17400925 | Protein Sci;16;852-62 | 3 | Marqusee Susan|Cellitti Jason|Bernstein Rachel | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"B... | [{"datasets":[],"id":34433,"numValue":12.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34434,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34435,"numValue":2.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34436,"numValue":null,... | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2174 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,174 | train | mutant | 1,142 | 41 | 1,286 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87M | V87M | 1 | 1 | 0 | 0 | 87 | V | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 2,042 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:V87M | 59 | -6.3 | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7652,"numValue":59.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":7653,"numValue":-6.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUT... | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2175 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,175 | train | mutant | 1,142 | 41 | 1,286 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V87M | V87M | 1 | 1 | 0 | 0 | 87 | V | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 87 | A | H | false | false | 3.426459 | 17.118571 | 6,809 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:V87M | null | null | null | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24129,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24130,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24131,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6878,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2176 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,176 | train | mutant | 1,453 | 41 | 1,640 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D89A | D89A | 1 | 1 | 0 | 0 | 89 | D | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 89 | A | H | false | false | 72.445193 | 19.800625 | 2,792 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:D89A | null | -1.3 | null | null | null | null | 133 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10198,"numValue":-1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10199,"numValue":133.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10200,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6880,"numValue":4.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2177 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,177 | train | mutant | 1,453 | 41 | 1,640 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D89A | D89A | 1 | 1 | 0 | 0 | 89 | D | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 89 | A | H | false | false | 72.445193 | 19.800625 | 2,813 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:D89A | null | -1.3 | null | null | null | null | 135 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10261,"numValue":-1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10262,"numValue":135.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10263,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6880,"numValue":4.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2179 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,179 | train | mutant | 1,453 | 41 | 1,640 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D89A | D89A | 1 | 1 | 0 | 0 | 89 | D | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 89 | A | H | false | false | 72.445193 | 19.800625 | 7,992 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:D89A | null | null | null | 0.7 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":27279,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27280,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27281,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6880,"numValue":4.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2180 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,180 | train | mutant | 7,607 | 41 | 8,310 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D89A|R96H | D89A|R96H | 2 | 2 | 0 | 0 | 89 | D | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 89|96 | A | H | false | false | 74.589108 | 19.592585 | 16,138 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:D89A 2LZM_A:R96H | null | -10.2 | null | null | null | null | 119 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":59120,"numValue":-10.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":59121,"numValue":119.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":59122,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6880,"numValue":4.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2181 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,181 | train | mutant | 7,607 | 41 | 8,310 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D89A|R96H | D89A|R96H | 2 | 2 | 0 | 0 | 89 | D | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 89|96 | A | H | false | false | 74.589108 | 19.592585 | 16,140 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:D89A 2LZM_A:R96H | null | -11.2 | null | null | null | null | 87 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":59126,"numValue":-11.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":59127,"numValue":87.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":59128,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6880,"numValue":4.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2182 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,182 | train | mutant | 7,607 | 41 | 8,310 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D89A|R96H | D89A|R96H | 2 | 2 | 0 | 0 | 89 | D | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 89|96 | A | H | false | false | 74.589108 | 19.592585 | 16,762 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 58 | 2LZM_A:D89A 2LZM_A:R96H | null | null | null | 3.8 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":58.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":61621,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61622,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61623,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6880,"numValue":4.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2183 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,183 | train | mutant | 7,607 | 41 | 8,310 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D89A|R96H | D89A|R96H | 2 | 2 | 0 | 0 | 89 | D | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 89|96 | A | H | false | false | 74.589108 | 19.592585 | 16,796 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:D89A 2LZM_A:R96H | null | null | null | 4.3 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":61723,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61724,"numValue":4.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61725,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6880,"numValue":4.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2184 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,184 | train | mutant | 1,776 | 41 | 1,989 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H | S90H | 1 | 1 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90 | A | H | false | false | 36.619849 | 13.475833 | 3,415 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:S90H | 34.4 | -4.1 | null | null | null | null | 72 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":12599,"numValue":34.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12600,"numValue":-4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12601,"numValue":72.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["... | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2185 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,185 | train | mutant | 1,776 | 41 | 1,989 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H | S90H | 1 | 1 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90 | A | H | false | false | 36.619849 | 13.475833 | 3,416 | ProTherm | 5.5 | CD | Thermal | acetate | 10 mM | null | KCl | 0.15 M | 2LZM_A:S90H | 62.7 | -2.7 | null | null | null | null | 128 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Broom_S605.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":["AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12603,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12604,"num... | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2186 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,186 | train | mutant | 1,776 | 41 | 1,989 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H | S90H | 1 | 1 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90 | A | H | false | false | 36.619849 | 13.475833 | 3,417 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:S90H | 60.1 | -2.9 | null | null | null | null | 117 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12607,"numValue":60.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"... | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2188 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,188 | train | mutant | 1,776 | 41 | 1,989 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H | S90H | 1 | 1 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90 | A | H | false | false | 36.619849 | 13.475833 | 7,039 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63 | KCl | 0.15 M | 2LZM_A:S90H | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24745,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24746,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2189 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,189 | train | mutant | 1,776 | 41 | 1,989 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H | S90H | 1 | 1 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90 | A | H | false | false | 36.619849 | 13.475833 | 8,426 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 28.5 | KCl | 0.15 M | 2LZM_A:S90H | null | null | null | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":28.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":28654,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28655,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2190 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,190 | train | mutant | 6,767 | 41 | 7,409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H|Q122D | S90H|Q122D | 2 | 2 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90|122 | A | H | false | false | 59.604379 | 24.524583 | 14,542 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:S90H 2LZM_A:Q122D | 32.7 | -5.8 | null | null | null | null | 67 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53758,"numValue":32.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53759,"numValue":-5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53760,"numValue":67.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53761,"numValue":null,"references":... | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2191 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,191 | train | mutant | 6,767 | 41 | 7,409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H|Q122D | S90H|Q122D | 2 | 2 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90|122 | A | H | false | false | 59.604379 | 24.524583 | 14,543 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:S90H 2LZM_A:Q122D | 61.3 | -4.1 | null | null | null | null | 128 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53762,"numValue":61.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53763,"numValue":-4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53764,"numValue":128.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53765,"numValue":null,"references"... | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2192 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,192 | train | mutant | 6,767 | 41 | 7,409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H|Q122D | S90H|Q122D | 2 | 2 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90|122 | A | H | false | false | 59.604379 | 24.524583 | 14,544 | ProTherm | 6.5 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:S90H 2LZM_A:Q122D | 57.3 | -5.7 | null | null | null | null | 116 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53766,"numValue":57.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53767,"numValue":-5.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53768,"numValue":116.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53769,"numValue":null,"references"... | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2193 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,193 | train | mutant | 6,767 | 41 | 7,409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H|Q122D | S90H|Q122D | 2 | 2 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90|122 | A | H | false | false | 59.604379 | 24.524583 | 14,930 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 64.6 | KCl | 0.15 M | 2LZM_A:S90H 2LZM_A:Q122D | null | null | null | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":64.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":55015,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55016,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2194 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,194 | train | mutant | 6,767 | 41 | 7,409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H|Q122D | S90H|Q122D | 2 | 2 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90|122 | A | H | false | false | 59.604379 | 24.524583 | 14,931 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | 64.6 | KCl | 0.15 M | 2LZM_A:S90H 2LZM_A:Q122D | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | METHOD|MEASURE|PH|EXP_TEMPERATURE|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":64.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":55017,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55018,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2195 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,195 | train | mutant | 6,767 | 41 | 7,409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S90H|Q122D | S90H|Q122D | 2 | 2 | 0 | 0 | 90 | S | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 90|122 | A | H | false | false | 59.604379 | 24.524583 | 14,932 | ProTherm | 6.5 | CD | Thermal | HCl | 10 mM | 64.6 | KCl | 0.15 M | 2LZM_A:S90H 2LZM_A:Q122D | null | null | null | 2.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":55019,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55020,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6881,"numValue":3.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2196 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,196 | train | mutant | 162 | 41 | 190 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L91M | L91M | 1 | 1 | 0 | 0 | 91 | L | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 91 | A | S | false | false | 6.100983 | 14.538125 | 299 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:L91M | 63.3 | -2 | null | null | null | 2.5 | 125 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":1220,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1221,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1222,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2197 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,197 | train | mutant | 162 | 41 | 190 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L91M | L91M | 1 | 1 | 0 | 0 | 91 | L | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 91 | A | S | false | false | 6.100983 | 14.538125 | 6,770 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:L91M | null | null | null | 0.8 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 m... | [{"datasets":[],"id":24012,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24013,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24014,"numValue":null,"references... | [{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2198 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,198 | train | mutant | 1,131 | 41 | 1,275 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L91A | L91A | 1 | 1 | 0 | 0 | 91 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 91 | A | S | false | false | 6.100983 | 14.538125 | 2,025 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L91A | 57.9 | -7.4 | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7567,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets... | [{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2199 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,199 | train | mutant | 1,131 | 41 | 1,275 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L91A | L91A | 1 | 1 | 0 | 0 | 91 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 91 | A | S | false | false | 6.100983 | 14.538125 | 3,145 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L91A | 42 | -9.7 | null | null | null | 1.8 | 85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11477,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11478,"numValue":-9.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11479,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2200 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,200 | train | mutant | 1,131 | 41 | 1,275 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L91A | L91A | 1 | 1 | 0 | 0 | 91 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 91 | A | S | false | false | 6.100983 | 14.538125 | 6,792 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:L91A | null | null | null | 2.6 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24078,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24079,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24080,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2202 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,202 | train | mutant | 2,066 | 41 | 2,306 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L91P | L91P | 1 | 1 | 0 | 0 | 91 | L | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 91 | A | S | false | false | 6.100983 | 14.538125 | 4,055 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:L91P | 30.7 | -34.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 374 | ARTICLE | Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: leucine 66 to proline and leucine 91 to proline. | 1,996 | 10.1002/pro.5560050419 | 8845764 | Protein Sci;5;742-51 | 5 | Blankespoor S|Born T|Jagar R|Gray T M|Arnoys E J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":14982,"numValue":30.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14983,"numValue":-34.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14984,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2203 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,203 | train | mutant | 2,066 | 41 | 2,306 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L91P | L91P | 1 | 1 | 0 | 0 | 91 | L | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 91 | A | S | false | false | 6.100983 | 14.538125 | 11,099 | ProTherm | 7 | CD | Urea | Potassium phosphate | 10 mM | 25 | KCl | 0.15 M | 2LZM_A:L91P | null | null | 5.57 | 10.98 | null | null | null | 2.09 | 2.67 | null | null | null | null | null | null | null | no | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 374 | ARTICLE | Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: leucine 66 to proline and leucine 91 to proline. | 1,996 | 10.1002/pro.5560050419 | 8845764 | Protein Sci;5;742-51 | 5 | Blankespoor S|Born T|Jagar R|Gray T M|Arnoys E J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":38214,"numValue":5.57,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38215,"numValue":10.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38216,"numValue":2.67,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38217,"numValue":2.09,"references":[]... | [{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2204 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,204 | train | mutant | 2,066 | 41 | 2,306 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L91P | L91P | 1 | 1 | 0 | 0 | 91 | L | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 91 | A | S | false | false | 6.100983 | 14.538125 | 12,612 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:L91P | null | null | null | 8.13 | null | null | null | 2.2 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":[],"id":45739,"numValue":8.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45740,"numValue":2.2,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45741,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6882,"numValue":7.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2205 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,205 | train | mutant | 504 | 41 | 554 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D92N | D92N | 1 | 1 | 0 | 0 | 92 | D | N | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 92 | A | L | false | false | 57.933268 | 17.383125 | 819 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:D92N | 39.2 | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":3104,"numValue":39.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3105,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3106,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6883,"numValue":7.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2206 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,206 | train | mutant | 504 | 41 | 554 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D92N | D92N | 1 | 1 | 0 | 0 | 92 | D | N | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 92 | A | L | false | false | 57.933268 | 17.383125 | 824 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:D92N | 58.7 | -3.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":3119,"numValue":58.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3120,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3121,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6883,"numValue":7.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2207 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,207 | train | mutant | 504 | 41 | 554 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D92N | D92N | 1 | 1 | 0 | 0 | 92 | D | N | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 92 | A | L | false | false | 57.933268 | 17.383125 | 7,063 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | 62.4 | KCl | 200 mM | 2LZM_A:D92N | null | null | null | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24800,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24801,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6883,"numValue":7.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2208 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,208 | train | mutant | 504 | 41 | 554 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D92N | D92N | 1 | 1 | 0 | 0 | 92 | D | N | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 92 | A | L | false | false | 57.933268 | 17.383125 | 8,158 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 39.5 | KCl | 200 mM | 2LZM_A:D92N | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":39.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27706,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27707,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6883,"numValue":7.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2209 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,209 | train | mutant | 101 | 41 | 111 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A93T | A93T | 1 | 1 | 0 | 0 | 93 | A | T | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 93 | A | H | false | false | 80.345611 | 17.627 | 195 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:A93T | 65.28 | 0.13 | null | null | null | 3.5 | 138 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":802,"numValue":65.28,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":803,"numValue":0.13,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":804,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":8... | [{"id":6884,"numValue":1.0,"position":93,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2210 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,210 | train | mutant | 101 | 41 | 111 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A93T | A93T | 1 | 1 | 0 | 0 | 93 | A | T | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 93 | A | H | false | false | 80.345611 | 17.627 | 207 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:A93T | 62.35 | 0.16 | null | null | null | 3.5 | 138 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":[],"id":856,"numValue":62.35,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":857,"numValue":0.16,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":858,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":8... | [{"id":6884,"numValue":1.0,"position":93,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2211 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,211 | train | mutant | 101 | 41 | 111 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A93T | A93T | 1 | 1 | 0 | 0 | 93 | A | T | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 93 | A | H | false | false | 80.345611 | 17.627 | 1,228 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:A93T | 65.2 | 0.13 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 125 | ARTICLE | Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent. | 1,993 | 10.1002/pro.5560021222 | 8298466 | Protein Sci;2;2226-32 | 2 | Matthews B W|Pjura P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":4528,"numValue":65.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4529,"numValue":0.13,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4530,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6884,"numValue":1.0,"position":93,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2212 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,212 | train | mutant | 101 | 41 | 111 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A93T | A93T | 1 | 1 | 0 | 0 | 93 | A | T | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 93 | A | H | false | false | 80.345611 | 17.627 | 6,824 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:A93T | null | null | null | -0.06 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.15,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":24171,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24172,"numValue":-0.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24173,"numValue":null,"referenc... | [{"id":6884,"numValue":1.0,"position":93,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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