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:2877 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,877 | train | mutant | 1,774 | 41 | 1,987 | 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 | N144E | N144E | 1 | 1 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 3,411 | ProTherm | 5.5 | CD | Thermal | acetate | 10 mM | null | KCl | 0.15 M | 2LZM_A:N144E | 66.8 | 1.4 | null | null | null | null | 136 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | ION_CONC|PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|_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":"0.15 M","type":"ION_CONC"},{"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"}... | [{"datasets":[],"id":12583,"numValue":66.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12584,"numValue":1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12585,"numValue":136.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2878 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,878 | train | mutant | 1,774 | 41 | 1,987 | 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 | N144E | N144E | 1 | 1 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 3,412 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:N144E | 64.5 | 1.5 | null | null | null | null | 138 | 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 | 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":[],"id":12587,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12588,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12589,"numValue":138.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2879 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,879 | train | mutant | 1,774 | 41 | 1,987 | 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 | N144E | N144E | 1 | 1 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 6,717 | ProTherm | 5.5 | CD | Thermal | acetate | 10 mM | 66.7 | KCl | 0.15 M | 2LZM_A:N144E | 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":5.5,"strValue":null,"type":"PH"},{"numValue":66.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"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_CON... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":23877,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23878,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2880 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,880 | train | mutant | 1,774 | 41 | 1,987 | 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 | N144E | N144E | 1 | 1 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 7,022 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 64.5 | KCl | 0.15 M | 2LZM_A:N144E | 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":6.5,"strValue":null,"type":"PH"},{"numValue":64.5,"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":24704,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24705,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2881 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,881 | train | mutant | 1,774 | 41 | 1,987 | 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 | N144E | N144E | 1 | 1 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 8,080 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 40.4 | KCl | 0.15 M | 2LZM_A:N144E | null | null | null | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | 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":40.4,"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":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27478,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27479,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2883 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,883 | train | mutant | 6,769 | 41 | 7,411 | 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 | N144E|K147M | N144E|K147M | 2 | 2 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144|147 | A | H | true | false | 96.702985 | 25.270799 | 14,549 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:N144E 2LZM_A:K147M | 66.6 | 1.2 | null | null | null | null | 139 | 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":53786,"numValue":66.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53787,"numValue":1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53788,"numValue":139.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53789,"numValue":null,"references":... | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2884 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,884 | train | mutant | 6,769 | 41 | 7,411 | 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 | N144E|K147M | N144E|K147M | 2 | 2 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144|147 | A | H | true | false | 96.702985 | 25.270799 | 14,550 | ProTherm | 6.5 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:N144E 2LZM_A:K147M | 64.2 | 1.2 | null | null | null | null | 134 | 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":53790,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53791,"numValue":1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53792,"numValue":134.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53793,"numValue":null,"references":... | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2885 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,885 | train | mutant | 6,769 | 41 | 7,411 | 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 | N144E|K147M | N144E|K147M | 2 | 2 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144|147 | A | H | true | false | 96.702985 | 25.270799 | 14,907 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | 65.4 | KCl | 0.15 M | 2LZM_A:N144E 2LZM_A:K147M | null | null | null | -0.5 | 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":5.5,"strValue":null,"type":"PH"},{"numValue":65.4,"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":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":54958,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54959,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2886 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,886 | train | mutant | 6,769 | 41 | 7,411 | 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 | N144E|K147M | N144E|K147M | 2 | 2 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144|147 | A | H | true | false | 96.702985 | 25.270799 | 14,936 | ProTherm | 6.5 | CD | Thermal | HCl | 10 mM | 63 | KCl | 0.15 M | 2LZM_A:N144E 2LZM_A:K147M | null | null | null | -0.4 | 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":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":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":55027,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55028,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2887 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,887 | train | mutant | 6,769 | 41 | 7,411 | 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 | N144E|K147M | N144E|K147M | 2 | 2 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144|147 | A | H | true | false | 96.702985 | 25.270799 | 15,143 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 28.5 | KCl | 0.15 M | 2LZM_A:N144E 2LZM_A:K147M | null | null | null | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|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":[],"id":55561,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55562,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2888 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,888 | train | mutant | 135 | 41 | 153 | 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 | A146T | A146T | 1 | 1 | 0 | 0 | 146 | A | T | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 248 | ProTherm | 3 | CD | Thermal | Unknown | null | 2LZM_A:A146T | 46.85 | null | null | null | null | 2.5 | 56.8 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 22 | ARTICLE | Mutations and protein stability. | 1,981 | 10.1002/bip.1981.360200921 | 7306671 | Biopolymers;20;1989-99 | 4 | Lindorfer M|Hawkes R|Grutter M|Schellman J A | [{"numValue":3.0,"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":"2LZM_A:A146T","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":1014,"numValue":46.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1015,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1016,"numValue":56.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1017,"numValue":null,"references":[],"... | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:2890 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,890 | train | mutant | 135 | 41 | 153 | 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 | A146T | A146T | 1 | 1 | 0 | 0 | 146 | A | T | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 480 | ProTherm | 3 | CD | Thermal | Unknown | null | NaCl | 0.2 M | 2LZM_A:A146T | 47.4 | -9.4 | 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 | 51 | ARTICLE | Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. | 1,984 | 10.1016/0022-2836(84)90474-1 | 6726809 | J Mol Biol;175;195-212 | 3 | Hawkes R|Schellman J|Grutter M G | [{"numValue":3.0,"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":"NaCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":1925,"numValue":47.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1926,"numValue":-9.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1927,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2891 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,891 | train | mutant | 135 | 41 | 153 | 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 | A146T | A146T | 1 | 1 | 0 | 0 | 146 | A | T | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 623 | ProTherm | 3 | CD | Thermal | HCl | null | 2LZM_A:A146T | 42.6 | -9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 68 | ARTICLE | Structure and thermal stability of phage T4 lysozyme. | 1,987 | 10.1016/0076-6879(87)54093-9 | 3323816 | Methods Enzymol;154;511-33 | 2 | Alber T|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":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:A146T","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":2475,"numValue":42.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2476,"numValue":-9.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2477,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2892 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,892 | train | mutant | 135 | 41 | 153 | 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 | A146T | A146T | 1 | 1 | 0 | 0 | 146 | A | T | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 817 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:A146T | 59 | -6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"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":3098,"numValue":59.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3099,"numValue":-6.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3100,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2893 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,893 | train | mutant | 135 | 41 | 153 | 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 | A146T | A146T | 1 | 1 | 0 | 0 | 146 | A | T | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 6,645 | ProTherm | 6.5 | CD | Thermal | Unknown | 70 | KCl | 0.2 M | 2LZM_A:A146T | null | null | null | 1.5 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23697,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23698,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2894 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,894 | train | mutant | 135 | 41 | 153 | 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 | A146T | A146T | 1 | 1 | 0 | 0 | 146 | A | T | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 7,797 | ProTherm | 3 | CD | Thermal | Unknown | 47 | NaCl | 0.2 M | 2LZM_A:A146T | null | null | 0.06 | 2.29 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 51 | ARTICLE | Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. | 1,984 | 10.1016/0022-2836(84)90474-1 | 6726809 | J Mol Biol;175;195-212 | 3 | Hawkes R|Schellman J|Grutter M G | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"num... | [{"datasets":[],"id":26728,"numValue":0.06,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":26729,"numValue":2.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26730,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2895 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,895 | train | mutant | 135 | 41 | 153 | 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 | A146T | A146T | 1 | 1 | 0 | 0 | 146 | A | T | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 12,620 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:A146T | null | null | null | 2.87 | null | null | null | 4.9 | 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":45763,"numValue":2.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45764,"numValue":4.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45765,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2896 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,896 | train | mutant | 1,876 | 41 | 2,104 | 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 | A146C | A146C | 1 | 1 | 0 | 0 | 146 | A | C | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 3,620 | ProTherm | 2.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A146C | 32.3 | -4.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 338 | ARTICLE | Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. | 1,992 | 10.1021/bi00149a004 | 1510962 | Biochemistry;31;7765-72 | 4 | Lu J|Baase W A|Dahlquist F W|Muchmore D C | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13311,"numValue":32.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":13312,"numValue":-4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMU... | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2897 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,897 | train | mutant | 1,876 | 41 | 2,104 | 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 | A146C | A146C | 1 | 1 | 0 | 0 | 146 | A | C | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 3,628 | ProTherm | 5.3 | CD | Thermal | Potassium acetate | 100 mM | null | 2LZM_A:A146C | 58.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 338 | ARTICLE | Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. | 1,992 | 10.1021/bi00149a004 | 1510962 | Biochemistry;31;7765-72 | 4 | Lu J|Baase W A|Dahlquist F W|Muchmore D C | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A146C","... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13335,"numValue":58.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13336,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2898 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,898 | train | mutant | 5,836 | 41 | 6,401 | 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 | A146I | A146I | 1 | 1 | 0 | 0 | 146 | A | I | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 12,619 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:A146I | null | null | null | 4.31 | null | null | null | 4.2 | 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":45760,"numValue":4.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45761,"numValue":4.2,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45762,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2899 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,899 | train | mutant | 5,837 | 41 | 6,402 | 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 | A146V | A146V | 1 | 1 | 0 | 0 | 146 | A | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 146 | A | H | false | false | 0 | 16.387 | 12,621 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:A146V | null | null | null | 4.31 | null | null | null | 4.1 | 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":45766,"numValue":4.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45767,"numValue":4.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45768,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6937,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2900 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,900 | train | mutant | 58 | 41 | 64 | 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 | K147E | K147E | 1 | 1 | 0 | 0 | 147 | K | E | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 147 | A | H | true | false | 91.601057 | 31.082222 | 72 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K147E | 51.1 | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"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":245,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":246,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":247,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2902 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,902 | train | mutant | 58 | 41 | 64 | 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 | K147E | K147E | 1 | 1 | 0 | 0 | 147 | K | E | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 147 | A | H | true | false | 91.601057 | 31.082222 | 6,713 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:K147E | null | null | null | 0.7 | 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 | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":66.7,"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":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":23869,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23870,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2903 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,903 | train | mutant | 58 | 41 | 64 | 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 | K147E | K147E | 1 | 1 | 0 | 0 | 147 | K | E | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 147 | A | H | true | false | 91.601057 | 31.082222 | 7,617 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K147E | 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 | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":50.9,"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","khan_protherm_data_mapped.csv"],"id":26299,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26300,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2906 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,906 | train | mutant | 206 | 41 | 235 | 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 | V149A | V149A | 1 | 1 | 0 | 0 | 149 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 2,035 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:V149A | 56.3 | -9 | null | null | null | null | 106 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | METHOD|PH|MEASURE|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":null,"strValue":"Thermal","type":"METHOD"},{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"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","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7617,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2907 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,907 | train | mutant | 206 | 41 | 235 | 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 | V149A | V149A | 1 | 1 | 0 | 0 | 149 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 3,136 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V149A | 40.7 | -11 | null | null | null | 1.8 | 66 | 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":11432,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11433,"numValue":-11.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11434,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2909 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,909 | train | mutant | 206 | 41 | 235 | 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 | V149A | V149A | 1 | 1 | 0 | 0 | 149 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,120 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:V149A | null | null | null | 3.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24973,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24974,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2910 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,910 | train | mutant | 206 | 41 | 235 | 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 | V149A | V149A | 1 | 1 | 0 | 0 | 149 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,570 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:V149A | null | null | null | 3.2 | 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 | 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":26183,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26184,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26185,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2911 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,911 | train | mutant | 206 | 41 | 235 | 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 | V149A | V149A | 1 | 1 | 0 | 0 | 149 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 12,622 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:V149A | null | null | null | 2.87 | null | null | null | 4.9 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|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":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":45769,"numValue":2.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45770,"numValue":4.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45771,"numValue":null,"references":[],"strValue":"... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2912 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,912 | train | mutant | 207 | 41 | 236 | 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 | V149S | V149S | 1 | 1 | 0 | 0 | 149 | V | S | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 388 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:V149S | 52.1 | -13.2 | null | null | null | null | 94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1595,"numValue":52.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1596,"numValue":-13.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1597,"numValue":94.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2913 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,913 | train | mutant | 207 | 41 | 236 | 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 | V149S | V149S | 1 | 1 | 0 | 0 | 149 | V | S | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,121 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:V149S | null | null | null | 4.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24975,"numValue":4.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24976,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2914 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,914 | train | mutant | 208 | 41 | 237 | 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 | V149C | V149C | 1 | 1 | 0 | 0 | 149 | V | C | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 389 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:V149C | 59.8 | -5.5 | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1599,"numValue":59.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1600,"numValue":-5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1601,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2915 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,915 | train | mutant | 208 | 41 | 237 | 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 | V149C | V149C | 1 | 1 | 0 | 0 | 149 | V | C | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 992 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V149C | 49 | -5.1 | null | null | null | null | 109.8 | 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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"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":3717,"numValue":49.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3718,"numValue":-5.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3719,"numValue":109.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2916 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,916 | train | mutant | 208 | 41 | 237 | 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 | V149C | V149C | 1 | 1 | 0 | 0 | 149 | V | C | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,122 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:V149C | null | null | null | 2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24977,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24978,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2917 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,917 | train | mutant | 208 | 41 | 237 | 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 | V149C | V149C | 1 | 1 | 0 | 0 | 149 | V | C | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 8,096 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 40 | KCl | 25 mM | 2LZM_A:V149C | null | null | null | 2.2 | null | 2.41 | 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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":40.0,"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":"20 mM","type"... | [{"datasets":[],"id":27527,"numValue":2.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27528,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27529,"numValue":null,"references":[],"strValue":"yes","type":"R... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2918 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,918 | train | mutant | 209 | 41 | 238 | 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 | V149T | V149T | 1 | 1 | 0 | 0 | 149 | V | T | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 390 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:V149T | 57 | -8.3 | null | null | null | null | 110 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1603,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1604,"numValue":-8.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1605,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2919 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,919 | train | mutant | 209 | 41 | 238 | 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 | V149T | V149T | 1 | 1 | 0 | 0 | 149 | V | T | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 426 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V149T | 41.47 | -10.08 | null | null | null | null | 77 | 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":1755,"numValue":41.47,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1756,"numValue":-10.08,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1757,"numValue":77.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2920 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,920 | train | mutant | 209 | 41 | 238 | 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 | V149T | V149T | 1 | 1 | 0 | 0 | 149 | V | T | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,123 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:V149T | null | null | null | 3 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv"],"id":24979,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24980,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2921 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,921 | train | mutant | 209 | 41 | 238 | 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 | V149T | V149T | 1 | 1 | 0 | 0 | 149 | V | T | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,595 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:V149T | null | null | null | 2.8 | 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":26247,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26248,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2922 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,922 | train | mutant | 210 | 41 | 239 | 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 | V149I | V149I | 1 | 1 | 0 | 0 | 149 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 391 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:V149I | 65.25 | -0.05 | null | null | null | null | 123 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":1607,"numValue":65.25,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":1608,"numValue":-0.05,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2923 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,923 | train | mutant | 210 | 41 | 239 | 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 | V149I | V149I | 1 | 1 | 0 | 0 | 149 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 1,430 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:V149I | 65.2 | -0.3 | null | null | null | null | 128 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv | 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":["khan_protherm_data_mapped.csv"],"id":5223,"numValue":65.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":5224,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":5225,"numValue":128.0,"references... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2924 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,924 | train | mutant | 210 | 41 | 239 | 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 | V149I | V149I | 1 | 1 | 0 | 0 | 149 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,086 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | 61 | 2LZM_A:V149I | null | null | null | 0 | 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":["khan_protherm_data_mapped.csv"],"id":24857,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24858,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"i... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2925 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,925 | train | mutant | 210 | 41 | 239 | 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 | V149I | V149I | 1 | 1 | 0 | 0 | 149 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,124 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:V149I | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24981,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":24982,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2927 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,927 | train | mutant | 211 | 41 | 240 | 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 | V149G | V149G | 1 | 1 | 0 | 0 | 149 | V | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 7,125 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:V149G | null | null | null | 4.9 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24983,"numValue":4.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24984,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2928 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,928 | train | mutant | 1,145 | 41 | 1,289 | 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 | V149M | V149M | 1 | 1 | 0 | 0 | 149 | V | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 2,047 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:V149M | 57.5 | -7.8 | null | null | null | null | 111 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|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","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7677,"numValue":57.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2929 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,929 | train | mutant | 1,145 | 41 | 1,289 | 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 | V149M | V149M | 1 | 1 | 0 | 0 | 149 | V | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 149 | A | H | false | false | 0.268742 | 12.753571 | 6,814 | 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:V149M | null | null | null | 2.8 | 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":24144,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24145,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24146,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2930 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,930 | train | mutant | 4,337 | 41 | 4,846 | 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 | I150V | I150V | 1 | 1 | 0 | 0 | 150 | I | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 150 | A | H | true | false | 12.496498 | 15.660625 | 10,027 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:I150V | null | null | 12.8 | 2.1 | 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":34445,"numValue":12.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34446,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34447,"numValue":2.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34448,"numValue":null,... | [{"id":6941,"numValue":7.0,"position":150,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2931 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,931 | train | mutant | 104 | 41 | 114 | 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 | T151S | T151S | 1 | 1 | 0 | 0 | 151 | T | S | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 151 | A | H | true | false | 33.128167 | 16.873572 | 198 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:T151S | 66.08 | 0.93 | null | null | null | 3.5 | 141 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|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":817,"numValue":66.08,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":818,"numValue":0.93,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":819,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":8... | [{"id":6942,"numValue":3.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2932 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,932 | train | mutant | 104 | 41 | 114 | 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 | T151S | T151S | 1 | 1 | 0 | 0 | 151 | T | S | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 151 | A | H | true | false | 33.128167 | 16.873572 | 210 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:T151S | 63.16 | 0.97 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|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":869,"numValue":63.16,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":870,"numValue":0.97,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":871,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":8... | [{"id":6942,"numValue":3.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2933 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,933 | train | mutant | 104 | 41 | 114 | 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 | T151S | T151S | 1 | 1 | 0 | 0 | 151 | T | S | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 151 | A | H | true | false | 33.128167 | 16.873572 | 1,229 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:T151S | 66.03 | 0.93 | 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":4531,"numValue":66.03,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4532,"numValue":0.93,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4533,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6942,"numValue":3.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2934 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,934 | train | mutant | 104 | 41 | 114 | 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 | T151S | T151S | 1 | 1 | 0 | 0 | 151 | T | S | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 151 | A | H | true | false | 33.128167 | 16.873572 | 6,827 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:T151S | null | null | null | -0.39 | null | 3.5 | 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 | 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":24180,"numValue":3.5,"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":24181,"numValue":-0.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24182,"nu... | [{"id":6942,"numValue":3.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2935 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,935 | train | mutant | 212 | 41 | 241 | 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 | T152A | T152A | 1 | 1 | 0 | 0 | 152 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 393 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:T152A | 61.3 | -4 | null | null | null | null | 115 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1615,"numValue":61.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1616,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1617,"numValue":115.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2936 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,936 | train | mutant | 212 | 41 | 241 | 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 | T152A | T152A | 1 | 1 | 0 | 0 | 152 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 7,126 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:T152A | null | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24985,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24986,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2937 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,937 | train | mutant | 213 | 41 | 242 | 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 | T152S | T152S | 1 | 1 | 0 | 0 | 152 | T | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 394 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:T152S | 59.8 | -5.5 | null | null | null | null | 117 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1619,"numValue":59.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1620,"numValue":-5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1621,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2938 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,938 | train | mutant | 213 | 41 | 242 | 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 | T152S | T152S | 1 | 1 | 0 | 0 | 152 | T | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 991 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T152S | 47.5 | -6.6 | null | null | null | null | 106.6 | 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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"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":3713,"numValue":47.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3714,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3715,"numValue":106.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2939 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,939 | train | mutant | 213 | 41 | 242 | 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 | T152S | T152S | 1 | 1 | 0 | 0 | 152 | T | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 7,127 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:T152S | null | null | null | 2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24987,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24988,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2940 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,940 | train | mutant | 213 | 41 | 242 | 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 | T152S | T152S | 1 | 1 | 0 | 0 | 152 | T | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 8,095 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 40 | KCl | 25 mM | 2LZM_A:T152S | null | null | null | 2.6 | null | 2.41 | null | null | null | null | null | null | null | null | null | null | yes | DCP|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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":40.0,"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":"20 mM","type"... | [{"datasets":[],"id":27524,"numValue":2.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":27525,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27526,"numValue":null,"references":[],"str... | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2941 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,941 | train | mutant | 214 | 41 | 243 | 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 | T152C | T152C | 1 | 1 | 0 | 0 | 152 | T | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 395 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:T152C | 63.9 | -1.4 | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1623,"numValue":63.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1624,"numValue":-1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1625,"numValue":127.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2942 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,942 | train | mutant | 214 | 41 | 243 | 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 | T152C | T152C | 1 | 1 | 0 | 0 | 152 | T | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 7,128 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:T152C | null | null | null | 0.5 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24989,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24990,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2943 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,943 | train | mutant | 215 | 41 | 244 | 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 | T152V | T152V | 1 | 1 | 0 | 0 | 152 | T | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 396 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:T152V | 66.1 | 0.8 | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1627,"numValue":66.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1628,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1629,"numValue":127.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2944 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,944 | train | mutant | 215 | 41 | 244 | 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 | T152V | T152V | 1 | 1 | 0 | 0 | 152 | T | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 7,129 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:T152V | null | null | null | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24991,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24992,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2945 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,945 | train | mutant | 216 | 41 | 245 | 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 | T152I | T152I | 1 | 1 | 0 | 0 | 152 | T | I | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 397 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:T152I | 64.3 | -1 | null | null | null | null | 125 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"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":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1631,"numValue":64.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1632,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1633,"numValue":125.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2946 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,946 | train | mutant | 216 | 41 | 245 | 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 | T152I | T152I | 1 | 1 | 0 | 0 | 152 | T | I | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 152 | A | H | false | false | 0.134371 | 14.754286 | 7,130 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:T152I | null | null | null | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"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":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24993,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24994,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2947 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,947 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 43 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | null | KCl | 0.025 M | 2LZM_A:F153A | 39.5 | -12.3 | null | null | null | 2.5 | 74.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"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":"0.020 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type"... | [{"datasets":[],"id":146,"numValue":39.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":147,"numValue":-12.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":148,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2948 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,948 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 310 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.10 M | 2LZM_A:F153A | 55.6 | -9.3 | null | null | null | 2.5 | 117 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"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":1275,"numValue":55.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1276,"numValue":-9.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1277,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2949 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,949 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 963 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:F153A | 39.46 | -12.3 | null | null | null | null | 75 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3613,"numValue":39.46,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3614,"numValue":-12.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3615,"numValue":75.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2950 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,950 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 973 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:F153A | 55.58 | -9.3 | null | null | null | null | 117 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3653,"numValue":55.58,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3654,"numValue":-9.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3655,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2951 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,951 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 2,036 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:F153A | 55.6 | -9.7 | null | null | null | null | 108 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv|PON-TStab_dataset.csv|STRUM_Q3421.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","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7622,"numValue":55.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2952 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,952 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 6,781 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.10 M | 2LZM_A:F153A | null | null | null | 3.4 | null | 2.5 | 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 | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"numValue":5.4,"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 mM... | [{"datasets":[],"id":24045,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24046,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24047,"numValue":null,"references":[],"strValue":"yes","type":"REVER... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2953 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,953 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 6,803 | 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:F153A | null | null | null | 3.4 | 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":24111,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24112,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24113,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2954 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,954 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 6,976 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:F153A | null | null | null | 3.8 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24591,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24592,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24593,"numValue":null,"references":[],"strV... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2956 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,956 | train | mutant | 43 | 41 | 47 | 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 | F153A | F153A | 1 | 1 | 0 | 0 | 153 | F | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 7,514 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:F153A | null | null | null | 3.5 | null | 2.5 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER_CO... | [{"datasets":[],"id":26035,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26036,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26037,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2957 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,957 | train | mutant | 105 | 41 | 115 | 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 | F153L | F153L | 1 | 1 | 0 | 0 | 153 | F | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 199 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:F153L | 66.03 | 0.88 | null | null | null | 3.5 | 137 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|Saraboji_S1791.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 | 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":822,"numValue":66.03,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","Saraboji_S1791.csv"... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2958 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,958 | train | mutant | 105 | 41 | 115 | 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 | F153L | F153L | 1 | 1 | 0 | 0 | 153 | F | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 211 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:F153L | 62.7 | 0.51 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|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":873,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":874,"numValue":0.51,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":875,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":87... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2959 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,959 | train | mutant | 105 | 41 | 115 | 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 | F153L | F153L | 1 | 1 | 0 | 0 | 153 | F | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 966 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:F153L | 52.36 | 0.6 | null | null | null | null | 115 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3625,"numValue":52.36,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3626,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3627,"numValue":115.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2960 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,960 | train | mutant | 105 | 41 | 115 | 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 | F153L | F153L | 1 | 1 | 0 | 0 | 153 | F | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 976 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:F153L | 65.68 | 0.8 | null | null | null | null | 135 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3665,"numValue":65.68,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3666,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3667,"numValue":135.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2962 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,962 | train | mutant | 105 | 41 | 115 | 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 | F153L | F153L | 1 | 1 | 0 | 0 | 153 | F | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 6,979 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:F153L | null | null | null | -0.3 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24600,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24601,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24602,"numValue":null,"references":[],"str... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2963 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,963 | train | mutant | 105 | 41 | 115 | 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 | F153L | F153L | 1 | 1 | 0 | 0 | 153 | F | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 7,517 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:F153L | null | null | null | -0.2 | null | 2.5 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER_CO... | [{"datasets":[],"id":26044,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26045,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26046,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2964 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,964 | train | mutant | 169 | 41 | 197 | 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 | F153M | F153M | 1 | 1 | 0 | 0 | 153 | F | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 306 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:F153M | 63.7 | -1.6 | null | null | null | 2.5 | 128 | 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":1255,"numValue":63.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1256,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1257,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2965 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,965 | train | mutant | 169 | 41 | 197 | 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 | F153M | F153M | 1 | 1 | 0 | 0 | 153 | F | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 967 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:F153M | 49.36 | -2.4 | null | null | null | null | 107 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3629,"numValue":49.36,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3630,"numValue":-2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3631,"numValue":107.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2966 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,966 | train | mutant | 169 | 41 | 197 | 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 | F153M | F153M | 1 | 1 | 0 | 0 | 153 | F | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 977 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:F153M | 63.28 | -1.6 | null | null | null | null | 132 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3669,"numValue":63.28,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3670,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3671,"numValue":132.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2967 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,967 | train | mutant | 169 | 41 | 197 | 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 | F153M | F153M | 1 | 1 | 0 | 0 | 153 | F | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 6,777 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:F153M | null | null | null | 0.6 | 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":24033,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24034,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24035,"numValue":null,"references... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2968 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,968 | train | mutant | 169 | 41 | 197 | 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 | F153M | F153M | 1 | 1 | 0 | 0 | 153 | F | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 6,980 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:F153M | null | null | null | 0.6 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24603,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24604,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24605,"numValue":null,"references... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2969 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,969 | train | mutant | 169 | 41 | 197 | 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 | F153M | F153M | 1 | 1 | 0 | 0 | 153 | F | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 7,518 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:F153M | null | null | null | 0.8 | null | 2.5 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER_CO... | [{"datasets":[],"id":26047,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26048,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26049,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2970 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,970 | train | mutant | 576 | 41 | 627 | 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 | F153V | F153V | 1 | 1 | 0 | 0 | 153 | F | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 964 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:F153V | 45.66 | -6.1 | null | null | null | null | 85 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3617,"numValue":45.66,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3618,"numValue":-6.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3619,"numValue":85.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2971 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,971 | train | mutant | 576 | 41 | 627 | 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 | F153V | F153V | 1 | 1 | 0 | 0 | 153 | F | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 974 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:F153V | 60.38 | -4.5 | null | null | null | null | 123 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3657,"numValue":60.38,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3658,"numValue":-4.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3659,"numValue":123.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2973 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,973 | train | mutant | 576 | 41 | 627 | 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 | F153V | F153V | 1 | 1 | 0 | 0 | 153 | F | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 7,515 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:F153V | null | null | null | 1.8 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER_CO... | [{"datasets":[],"id":26038,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26039,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26040,"numValue":null,"references... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2975 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,975 | train | mutant | 577 | 41 | 628 | 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 | F153I | F153I | 1 | 1 | 0 | 0 | 153 | F | I | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 975 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:F153I | 64.38 | -0.5 | null | null | null | null | 128 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3661,"numValue":64.38,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3662,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3663,"numValue":128.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2976 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,976 | train | mutant | 577 | 41 | 628 | 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 | F153I | F153I | 1 | 1 | 0 | 0 | 153 | F | I | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 6,978 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:F153I | null | null | null | 0.2 | null | 3.5 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24597,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24598,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24599,"numValue":null,"references":[],"strValue":"yes","type":"REVER... | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2977 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,977 | train | mutant | 577 | 41 | 628 | 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 | F153I | F153I | 1 | 1 | 0 | 0 | 153 | F | I | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 153 | A | H | true | false | 0.730152 | 16.989091 | 7,516 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:F153I | null | null | null | 0.5 | null | 2.5 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER_CO... | [{"datasets":[],"id":26041,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26042,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26043,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2979 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,979 | train | mutant | 59 | 41 | 65 | 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 | R154E | R154E | 1 | 1 | 0 | 0 | 154 | R | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 154 | A | H | true | false | 95.531647 | 39.143182 | 73 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R154E | 51.5 | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|HotMuSiC_S1626.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"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":248,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":249,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":250,"numValue":null,"references":[],"strValue":"yes","type":"REVERS... | [{"id":6945,"numValue":5.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2980 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,980 | train | mutant | 59 | 41 | 65 | 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 | R154E | R154E | 1 | 1 | 0 | 0 | 154 | R | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 154 | A | H | true | false | 95.531647 | 39.143182 | 78 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R154E | 64.1 | -2.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"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":263,"numValue":64.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":264,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":265,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6945,"numValue":5.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2981 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,981 | train | mutant | 59 | 41 | 65 | 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 | R154E | R154E | 1 | 1 | 0 | 0 | 154 | R | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 154 | A | H | true | false | 95.531647 | 39.143182 | 6,714 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:R154E | null | null | null | 1.1 | 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 | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":66.7,"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":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":23871,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23872,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6945,"numValue":5.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2982 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,982 | train | mutant | 59 | 41 | 65 | 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 | R154E | R154E | 1 | 1 | 0 | 0 | 154 | R | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 154 | A | H | true | false | 95.531647 | 39.143182 | 7,618 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:R154E | null | null | null | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":50.9,"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","khan_protherm_data_mapped.csv"],"id":26301,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26302,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6945,"numValue":5.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2983 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,983 | train | mutant | 7,188 | 41 | 7,843 | 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 | T155A|T157I | T155A|T157I | 2 | 2 | 0 | 0 | 155 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 155|157 | A | H|S | false | false | 52.22616 | 20.233214 | 15,490 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:T155A 2LZM_A:T157I | null | null | null | 4.31 | null | null | null | 4.2 | 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":56874,"numValue":4.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56875,"numValue":4.2,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56876,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6946,"numValue":7.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2984 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,984 | train | mutant | 361 | 41 | 400 | 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 | G156D | G156D | 1 | 1 | 0 | 0 | 156 | G | D | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 156 | A | S | false | false | 18.352523 | 19.815 | 624 | ProTherm | 3 | CD | Thermal | HCl | null | 2LZM_A:G156D | 46.6 | -5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 68 | ARTICLE | Structure and thermal stability of phage T4 lysozyme. | 1,987 | 10.1016/0076-6879(87)54093-9 | 3323816 | Methods Enzymol;154;511-33 | 2 | Alber T|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":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:G156D","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":2478,"numValue":46.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2479,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2480,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6947,"numValue":8.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2985 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,985 | train | mutant | 361 | 41 | 400 | 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 | G156D | G156D | 1 | 1 | 0 | 0 | 156 | G | D | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 156 | A | S | false | false | 18.352523 | 19.815 | 828 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:G156D | 36.8 | -5.1 | 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 | 90 | ARTICLE | Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid. | 1,987 | 10.2210/pdb1l16/pdb | 3680274 | J Biol Chem;262;16858-64 | 2 | Matthews B W|Gray T M | [{"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":3131,"numValue":36.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3132,"numValue":-5.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3133,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6947,"numValue":8.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2986 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,986 | train | mutant | 361 | 41 | 400 | 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 | G156D | G156D | 1 | 1 | 0 | 0 | 156 | G | D | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 156 | A | S | false | false | 18.352523 | 19.815 | 829 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:G156D | 58.6 | -6.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 90 | ARTICLE | Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid. | 1,987 | 10.2210/pdb1l16/pdb | 3680274 | J Biol Chem;262;16858-64 | 2 | Matthews B W|Gray T M | [{"numValue":6.5,"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":3134,"numValue":58.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3135,"numValue":-6.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3136,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6947,"numValue":8.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2987 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,987 | train | mutant | 361 | 41 | 400 | 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 | G156D | G156D | 1 | 1 | 0 | 0 | 156 | G | D | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 156 | A | S | false | false | 18.352523 | 19.815 | 7,004 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:G156D | null | null | null | 2.3 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 90 | ARTICLE | Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid. | 1,987 | 10.2210/pdb1l16/pdb | 3680274 | J Biol Chem;262;16858-64 | 2 | Matthews B W|Gray T M | [{"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":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":24654,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24655,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6947,"numValue":8.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2988 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,988 | train | mutant | 361 | 41 | 400 | 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 | G156D | G156D | 1 | 1 | 0 | 0 | 156 | G | D | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 156 | A | S | false | false | 18.352523 | 19.815 | 8,051 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:G156D | null | null | null | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 90 | ARTICLE | Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid. | 1,987 | 10.2210/pdb1l16/pdb | 3680274 | J Biol Chem;262;16858-64 | 2 | Matthews B W|Gray T M | [{"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":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27417,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27418,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6947,"numValue":8.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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