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:2436 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,436 | train | mutant | 6,742 | 41 | 7,384 | 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 | L99F|M102L|V111I|F153L | L99F|M102L|V111I|F153L | 4 | 4 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|111|153 | A | H | true | false | 0.933049 | 16.19821 | 14,927 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 64.89 | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:V111I 2LZM_A:F153L | null | null | null | 0.65 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.89,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_... | [{"datasets":[],"id":55008,"numValue":0.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55009,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2437 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,437 | train | mutant | 6,742 | 41 | 7,384 | 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 | L99F|M102L|V111I|F153L | L99F|M102L|V111I|F153L | 4 | 4 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|111|153 | A | H | true | false | 0.933049 | 16.19821 | 15,007 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:V111I 2LZM_A:F153L | null | null | null | 0.54 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":[],"id":55196,"numValue":0.54,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55197,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2438 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,438 | train | mutant | 6,920 | 41 | 7,562 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L99A|E108V | L99A|E108V | 2 | 2 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|108 | A | H | true | true | 24.582114 | 27.856111 | 14,767 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99A 2LZM_A:E108V | 41.4 | -10.3 | null | null | null | null | 91 | null | null | null | null | null | null | null | null | null | yes(>95%) | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J 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":54566,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54567,"numValue":-10.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54568,"numValue":91.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54569,"numValue":null,"references"... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2439 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,439 | train | mutant | 6,920 | 41 | 7,562 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L99A|E108V | L99A|E108V | 2 | 2 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|108 | A | H | true | true | 24.582114 | 27.856111 | 14,769 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:L99A 2LZM_A:E108V | 56.6 | -8.6 | null | null | null | null | 114 | null | null | null | null | null | null | null | null | null | yes(>80%) | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"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":54574,"numValue":56.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54575,"numValue":-8.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54576,"numValue":114.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54577,"numValue":null,"references"... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2440 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,440 | train | mutant | 6,920 | 41 | 7,562 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L99A|E108V | L99A|E108V | 2 | 2 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|108 | A | H | true | true | 24.582114 | 27.856111 | 14,913 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.2 | NaCl | 0.10 M | 2LZM_A:L99A 2LZM_A:E108V | null | null | null | 3.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>80%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.2,"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":"BUF... | [{"datasets":[],"id":54975,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54976,"numValue":null,"references":[],"strValue":"yes(>80%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2441 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,441 | train | mutant | 6,920 | 41 | 7,562 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L99A|E108V | L99A|E108V | 2 | 2 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|108 | A | H | true | true | 24.582114 | 27.856111 | 15,017 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 25 mM | 2LZM_A:L99A 2LZM_A:E108V | null | null | null | 3.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>95%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.7,"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":[],"id":55217,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55218,"numValue":null,"references":[],"strValue":"yes(>95%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2442 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,442 | train | mutant | 6,921 | 41 | 7,563 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L99G|E108V | L99G|E108V | 2 | 2 | 0 | 0 | 99 | L | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|108 | A | H | true | true | 24.582114 | 27.856111 | 14,768 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99G 2LZM_A:E108V | 30.4 | -21.3 | null | null | null | null | 69 | null | null | null | null | null | null | null | null | null | yes(>95%) | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J 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":54570,"numValue":30.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54571,"numValue":-21.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54572,"numValue":69.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54573,"numValue":null,"references"... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2444 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,444 | train | mutant | 6,921 | 41 | 7,563 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L99G|E108V | L99G|E108V | 2 | 2 | 0 | 0 | 99 | L | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|108 | A | H | true | true | 24.582114 | 27.856111 | 14,914 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.2 | NaCl | 0.10 M | 2LZM_A:L99G 2LZM_A:E108V | null | null | null | 5.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>80%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.2,"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":"BUF... | [{"datasets":[],"id":54977,"numValue":5.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54978,"numValue":null,"references":[],"strValue":"yes(>80%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2445 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,445 | train | mutant | 6,921 | 41 | 7,563 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L99G|E108V | L99G|E108V | 2 | 2 | 0 | 0 | 99 | L | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|108 | A | H | true | true | 24.582114 | 27.856111 | 15,018 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 25 mM | 2LZM_A:L99G 2LZM_A:E108V | null | null | null | 6.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>95%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.7,"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":[],"id":55219,"numValue":6.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55220,"numValue":null,"references":[],"strValue":"yes(>95%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2446 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,446 | train | mutant | 164 | 41 | 192 | 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 | I100M | I100M | 1 | 1 | 0 | 0 | 100 | I | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 100 | A | H | false | false | 9.674708 | 11.033125 | 301 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:I100M | 60.8 | -4.5 | null | null | null | 2.5 | 125 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":1230,"numValue":60.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1231,"numValue":-4.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1232,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6891,"numValue":6.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2447 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,447 | train | mutant | 164 | 41 | 192 | 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 | I100M | I100M | 1 | 1 | 0 | 0 | 100 | I | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 100 | A | H | false | false | 9.674708 | 11.033125 | 2,043 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I100M | 60.8 | -4.5 | null | null | null | null | 125 | 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|EASE-MM_S1676.csv|PoPMuSiC-2.0_S2648.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":7657,"numValue":60.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":6891,"numValue":6.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2448 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,448 | train | mutant | 164 | 41 | 192 | 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 | I100M | I100M | 1 | 1 | 0 | 0 | 100 | I | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 100 | A | H | false | false | 9.674708 | 11.033125 | 6,772 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:I100M | null | null | null | 1.6 | 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":24018,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24019,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24020,"numValue":null,"references... | [{"id":6891,"numValue":6.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2449 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,449 | train | mutant | 164 | 41 | 192 | 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 | I100M | I100M | 1 | 1 | 0 | 0 | 100 | I | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 100 | A | H | false | false | 9.674708 | 11.033125 | 6,810 | 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:I100M | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|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":24132,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24133,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24134,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6891,"numValue":6.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2452 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,452 | train | mutant | 1,133 | 41 | 1,277 | 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 | I100A | I100A | 1 | 1 | 0 | 0 | 100 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 100 | A | H | false | false | 9.674708 | 11.033125 | 2,028 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I100A | 58.2 | -7.1 | null | null | null | null | 118 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|EASE-MM_S1676.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|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":["M47andM8_S1810.csv","M47andM8_S2760.csv"],"id":7582,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7583,"numValue":-7.1,"references":[],"strValue":null,"type":"DT... | [{"id":6891,"numValue":6.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2453 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,453 | train | mutant | 1,133 | 41 | 1,277 | 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 | I100A | I100A | 1 | 1 | 0 | 0 | 100 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 100 | A | H | false | false | 9.674708 | 11.033125 | 3,130 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I100A | 41 | -10.7 | null | null | null | 1.8 | 85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11402,"numValue":41.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11403,"numValue":-10.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11404,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":6891,"numValue":6.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2454 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,454 | train | mutant | 1,133 | 41 | 1,277 | 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 | I100A | I100A | 1 | 1 | 0 | 0 | 100 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 100 | A | H | false | false | 9.674708 | 11.033125 | 6,795 | 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:I100A | null | null | null | 2.5 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24087,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24088,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24089,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6891,"numValue":6.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2455 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,455 | train | mutant | 1,133 | 41 | 1,277 | 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 | I100A | I100A | 1 | 1 | 0 | 0 | 100 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 100 | A | H | false | false | 9.674708 | 11.033125 | 7,564 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:I100A | null | null | null | 3.4 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26165,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26166,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26167,"numV... | [{"id":6891,"numValue":6.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2456 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,456 | train | mutant | 204 | 41 | 233 | 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 | N101A | N101A | 1 | 1 | 0 | 0 | 101 | N | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 101 | A | H | false | false | 0.381578 | 13.87375 | 385 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:N101A | 61.6 | -3.7 | 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":1583,"numValue":61.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1584,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1585,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6892,"numValue":8.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2457 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,457 | train | mutant | 204 | 41 | 233 | 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 | N101A | N101A | 1 | 1 | 0 | 0 | 101 | N | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 101 | A | H | false | false | 0.381578 | 13.87375 | 7,118 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:N101A | 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":24969,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24970,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6892,"numValue":8.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2458 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,458 | train | mutant | 134 | 41 | 152 | 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 | M102V | M102V | 1 | 1 | 0 | 0 | 102 | M | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 247 | ProTherm | 3 | CD | Thermal | Unknown | null | 2LZM_A:M102V | 46.85 | null | null | null | null | 2.33 | 65.3 | 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:M102V","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":1010,"numValue":46.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1011,"numValue":2.33,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1012,"numValue":65.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1013,"numValue":null,"references":[],... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:2459 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,459 | train | mutant | 134 | 41 | 152 | 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 | M102V | M102V | 1 | 1 | 0 | 0 | 102 | M | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 252 | ProTherm | 3 | CD | Thermal | Unknown | null | 2LZM_A:M102V | 46 | -13 | null | null | null | 2.33 | 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|_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:M102V","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":1030,"numValue":46.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1031,"numValue":-13.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1032,"numValue":2.33,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"i... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2460 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,460 | train | mutant | 134 | 41 | 152 | 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 | M102V | M102V | 1 | 1 | 0 | 0 | 102 | M | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 479 | ProTherm | 3 | CD | Thermal | Unknown | null | NaCl | 0.2 M | 2LZM_A:M102V | 44.1 | -12.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|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":1922,"numValue":44.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1923,"numValue":-12.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1924,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2461 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,461 | train | mutant | 134 | 41 | 152 | 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 | M102V | M102V | 1 | 1 | 0 | 0 | 102 | M | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 482 | ProTherm | 3 | CD | Thermal | Unknown | null | NaCl | 0.2 M | 2LZM_A:M102V | 44.1 | -12.7 | null | 3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DDG|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.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":1932,"numValue":44.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1933,"numValue":-12.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":1934,"numValue":3.... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2463 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,463 | train | mutant | 284 | 41 | 316 | 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 | M102L | M102L | 1 | 1 | 0 | 0 | 102 | M | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 502 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:M102L | 62.58 | -2.31 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":[],"id":2025,"numValue":62.58,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2026,"numValue":-2.31,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2027,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2464 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,464 | train | mutant | 284 | 41 | 316 | 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 | M102L | M102L | 1 | 1 | 0 | 0 | 102 | M | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 1,424 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:M102L | 63.2 | -2.3 | null | null | null | null | 118 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.10 M, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":5199,"numValue":63.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5200,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5201,"numValue":118.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5202,"numValue":null,"references":[],... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2465 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,465 | train | mutant | 284 | 41 | 316 | 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 | M102L | M102L | 1 | 1 | 0 | 0 | 102 | M | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 6,968 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 64.89 | KCl | 0.2 M | 2LZM_A:M102L | null | null | null | 0.82 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.89,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24570,"numValue":0.82,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24571,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2466 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,466 | train | mutant | 284 | 41 | 316 | 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 | M102L | M102L | 1 | 1 | 0 | 0 | 102 | M | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 7,080 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | 61 | 2LZM_A:M102L | null | null | null | 1 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":61.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":24839,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24840,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24841,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2467 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,467 | train | mutant | 284 | 41 | 316 | 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 | M102L | M102L | 1 | 1 | 0 | 0 | 102 | M | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 7,506 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:M102L | null | null | null | 0.74 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26014,"numValue":0.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26015,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2468 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,468 | train | mutant | 339 | 41 | 378 | 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 | M102K | M102K | 1 | 1 | 0 | 0 | 102 | M | K | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 595 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:M102K | 16.6 | -35 | null | null | null | 1.8 | 12.4 | 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 | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F 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":2360,"numValue":16.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2361,"numValue":-35.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2362,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2469 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,469 | train | mutant | 339 | 41 | 378 | 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 | M102K | M102K | 1 | 1 | 0 | 0 | 102 | M | K | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 598 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:M102K | 45 | -20.3 | null | null | null | 1.8 | 53 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|EASE-MM_S238.csv|M47andM8_S2760.csv|Saraboji_S1791.csv|STRUM_Q3421.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"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":2375,"numValue":45.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","EASE-MM_S238.csv","M47andM8_S2760.csv","Saraboji_S1791.csv","STRUM_Q3421.csv"],"id":2376,"numValue":-20.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S238.csv","M47andM8_S181... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2470 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,470 | train | mutant | 339 | 41 | 378 | 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 | M102K | M102K | 1 | 1 | 0 | 0 | 102 | M | K | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 600 | ProTherm | 10.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:M102K | 37.8 | -10.1 | null | null | null | 1.8 | 77.4 | null | null | null | null | null | null | null | null | null | yes(20%) | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":10.4,"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":"... | [{"datasets":[],"id":2385,"numValue":37.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2386,"numValue":-10.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2387,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2471 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,471 | train | mutant | 339 | 41 | 378 | 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 | M102K | M102K | 1 | 1 | 0 | 0 | 102 | M | K | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 6,782 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 65.3 | KCl | 25 mM | 2LZM_A:M102K | null | null | null | 6.9 | null | 1.8 | 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 | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":5.3,"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":24048,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":24049,"numValue":6.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24050,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2472 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,472 | train | mutant | 339 | 41 | 378 | 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 | M102K | M102K | 1 | 1 | 0 | 0 | 102 | M | K | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 7,580 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.6 | KCl | 25 mM | 2LZM_A:M102K | null | null | null | 8.9 | null | 1.8 | 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 | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.6,"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":26213,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26214,"numValue":8.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26215,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2473 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,473 | train | mutant | 339 | 41 | 378 | 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 | M102K | M102K | 1 | 1 | 0 | 0 | 102 | M | K | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 7,784 | ProTherm | 10.4 | CD | Thermal | Potassium phosphate | 20 mM | 47.9 | KCl | 25 mM | 2LZM_A:M102K | null | null | null | 2.2 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(20%) | 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 | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":47.9,"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":[],"id":26693,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26694,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26695,"numValue":null,"references":[],"strValue":"yes(20%)","type":"... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2474 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,474 | train | mutant | 360 | 41 | 399 | 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 | M102T | M102T | 1 | 1 | 0 | 0 | 102 | M | T | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 622 | ProTherm | 3 | CD | Thermal | HCl | null | 2LZM_A:M102T | 38.6 | -13 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|_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:M102T","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":2472,"numValue":38.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2473,"numValue":-13.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2474,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2475 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,475 | train | mutant | 1,132 | 41 | 1,276 | 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 | M102A | M102A | 1 | 1 | 0 | 0 | 102 | M | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 2,027 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:M102A | 57.1 | -8.2 | 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_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.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","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7577,"numValue":57.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.c... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2476 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,476 | train | mutant | 1,132 | 41 | 1,276 | 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 | M102A | M102A | 1 | 1 | 0 | 0 | 102 | M | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102 | A | H | false | false | 2.598931 | 15.57875 | 6,794 | 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:M102A | null | null | null | 2.9 | 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":24084,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24085,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24086,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2477 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,477 | train | mutant | 6,737 | 41 | 7,379 | 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 | M102L|V111F | M102L|V111F | 2 | 2 | 0 | 0 | 102 | M | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102|111 | A | H | false | false | 1.400244 | 17.489375 | 14,496 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:M102L 2LZM_A:V111F | 46.27 | -5.49 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53587,"numValue":46.27,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53588,"numValue":-5.49,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53589,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2479 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,479 | train | mutant | 6,737 | 41 | 7,379 | 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 | M102L|V111F | M102L|V111F | 2 | 2 | 0 | 0 | 102 | M | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102|111 | A | H | false | false | 1.400244 | 17.489375 | 14,922 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 64.89 | KCl | 0.2 M | 2LZM_A:M102L 2LZM_A:V111F | null | null | null | 2.11 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.89,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_... | [{"datasets":[],"id":54998,"numValue":2.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54999,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2480 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,480 | train | mutant | 6,737 | 41 | 7,379 | 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 | M102L|V111F | M102L|V111F | 2 | 2 | 0 | 0 | 102 | M | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102|111 | A | H | false | false | 1.400244 | 17.489375 | 15,002 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:M102L 2LZM_A:V111F | null | null | null | 1.51 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":[],"id":55186,"numValue":1.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55187,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2481 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,481 | train | mutant | 6,827 | 41 | 7,469 | 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 | M102A|M106A | M102A|M106A | 2 | 2 | 0 | 0 | 102 | M | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102|106 | A | H | true | true | 28.660713 | 21.91375 | 14,650 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:M102A 1L63_A:M106A | 54.5 | -10.8 | null | null | null | null | 101 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | 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":[],"id":54175,"numValue":54.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54176,"numValue":-10.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54177,"numValue":101.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54178,"numValue":2.0,"references"... | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2482 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,482 | train | mutant | 6,827 | 41 | 7,469 | 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 | M102A|M106A | M102A|M106A | 2 | 2 | 0 | 0 | 102 | M | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 102|106 | A | H | true | true | 28.660713 | 21.91375 | 14,911 | 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:M102A 1L63_A:M106A | null | null | null | 3.7 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | 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":[],"id":54969,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54970,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":54971,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2483 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,483 | train | mutant | 165 | 41 | 193 | 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 | V103M | V103M | 1 | 1 | 0 | 0 | 103 | V | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 302 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:V103M | 62.2 | -3.1 | null | null | null | 2.5 | 117 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | METHOD|PH|MEASURE|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":null,"strValue":"Thermal","type":"METHOD"},{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"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":1235,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1236,"numValue":-3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1237,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2484 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,484 | train | mutant | 165 | 41 | 193 | 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 | V103M | V103M | 1 | 1 | 0 | 0 | 103 | V | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 6,773 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:V103M | null | null | null | 1.2 | 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":24021,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24022,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24023,"numValue":null,"references... | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2485 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,485 | train | mutant | 808 | 41 | 912 | 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 | V103I | V103I | 1 | 1 | 0 | 0 | 103 | V | I | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 1,425 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:V103I | 64 | -1.5 | null | null | null | null | 130 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.10 M, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":5203,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5204,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5205,"numValue":130.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5206,"numValue":null,"references":[],... | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2486 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,486 | train | mutant | 808 | 41 | 912 | 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 | V103I | V103I | 1 | 1 | 0 | 0 | 103 | V | I | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 7,081 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | 61 | 2LZM_A:V103I | null | null | null | 0.5 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":61.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":24842,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24843,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24844,"numValue":null,"references":[],"strValue":"Unknown",... | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2487 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,487 | train | mutant | 1,134 | 41 | 1,278 | 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 | V103A | V103A | 1 | 1 | 0 | 0 | 103 | V | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 2,029 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:V103A | 60.9 | -4.4 | null | null | null | null | 122 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7587,"numValue":60.9,"references":[],"strValue":null,"type":"TM"}... | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2488 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,488 | train | mutant | 1,134 | 41 | 1,278 | 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 | V103A | V103A | 1 | 1 | 0 | 0 | 103 | V | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 3,134 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V103A | 45.1 | -6.6 | null | null | null | 1.8 | 94 | 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":11422,"numValue":45.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11423,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11424,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2489 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,489 | train | mutant | 1,134 | 41 | 1,278 | 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 | V103A | V103A | 1 | 1 | 0 | 0 | 103 | V | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 6,796 | 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:V103A | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24090,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24091,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24092,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2490 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,490 | train | mutant | 1,134 | 41 | 1,278 | 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 | V103A | V103A | 1 | 1 | 0 | 0 | 103 | V | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 7,568 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:V103A | null | null | null | 2.2 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 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":26177,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26178,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26179,"numValue":null,"references":[],"strValue":"Unknown","type":"R... | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2491 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,491 | train | mutant | 1,134 | 41 | 1,278 | 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 | V103A | V103A | 1 | 1 | 0 | 0 | 103 | V | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 103 | A | H | true | true | 8.832081 | 15.769285 | 12,615 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:V103A | null | null | null | 1.91 | null | null | null | 5.3 | 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":45748,"numValue":1.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45749,"numValue":5.3,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45750,"numValue":null,"references":[],"strValue":"... | [{"id":6894,"numValue":7.0,"position":103,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2492 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,492 | train | mutant | 1,135 | 41 | 1,279 | 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 | F104A | F104A | 1 | 1 | 0 | 0 | 104 | F | A | 9 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 104 | A | H | true | true | 32.369368 | 13.143182 | 2,030 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:F104A | 57.8 | -7.5 | null | null | null | null | 109 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv|PON-TStab_dataset.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7592,"numValue":57.8,"references":[],"strValue":null,"type":"TM"}... | [{"id":21,"numValue":null,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6895,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2493 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,493 | train | mutant | 1,135 | 41 | 1,279 | 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 | F104A | F104A | 1 | 1 | 0 | 0 | 104 | F | A | 9 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 104 | A | H | true | true | 32.369368 | 13.143182 | 3,140 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:F104A | 42 | -9.7 | null | null | null | 1.8 | 82 | 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":11452,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11453,"numValue":-9.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11454,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":21,"numValue":null,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6895,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2494 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,494 | train | mutant | 1,135 | 41 | 1,279 | 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 | F104A | F104A | 1 | 1 | 0 | 0 | 104 | F | A | 9 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 104 | A | H | true | true | 32.369368 | 13.143182 | 6,797 | 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:F104A | null | null | null | 2.7 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24093,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24094,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24095,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":21,"numValue":null,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6895,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2495 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,495 | train | mutant | 1,135 | 41 | 1,279 | 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 | F104A | F104A | 1 | 1 | 0 | 0 | 104 | F | A | 9 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 104 | A | H | true | true | 32.369368 | 13.143182 | 7,574 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:F104A | null | null | null | 3.1 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26195,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26196,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26197,"numV... | [{"id":21,"numValue":null,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6895,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2496 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,496 | train | mutant | 1,143 | 41 | 1,287 | 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 | F104M | F104M | 1 | 1 | 0 | 0 | 104 | F | M | 9 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 104 | A | H | true | true | 32.369368 | 13.143182 | 2,044 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:F104M | 64.5 | -0.8 | null | null | null | null | 121 | 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 | 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":7662,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":21,"numValue":null,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6895,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2497 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,497 | train | mutant | 1,143 | 41 | 1,287 | 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 | F104M | F104M | 1 | 1 | 0 | 0 | 104 | F | M | 9 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 104 | A | H | true | true | 32.369368 | 13.143182 | 6,811 | 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:F104M | null | null | null | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|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":24135,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24136,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24137,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":21,"numValue":null,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6895,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2498 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,498 | train | mutant | 200 | 41 | 229 | 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 | Q105A | Q105A | 1 | 1 | 0 | 0 | 105 | Q | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 378 | ProTherm | 2.1 | CD | Thermal | H3PO4 | 17 mM | null | KCl | 0.15 M | 2LZM_A:Q105A | 38.5 | -3.5 | 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 | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":2.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValu... | [{"datasets":[],"id":1555,"numValue":38.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1556,"numValue":-3.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1557,"numValue":77.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2500 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,500 | train | mutant | 200 | 41 | 229 | 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 | Q105A | Q105A | 1 | 1 | 0 | 0 | 105 | Q | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 6,743 | ProTherm | 5.8 | CD | Thermal | KH2PO4 | 10 mM | 66.3 | KCl | 0.15 M | 2LZM_A:Q105A | null | null | null | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":66.3,"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_CONC... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23955,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23956,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2501 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,501 | train | mutant | 200 | 41 | 229 | 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 | Q105A | Q105A | 1 | 1 | 0 | 0 | 105 | Q | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 8,013 | ProTherm | 2.1 | CD | Thermal | H3PO4 | 17 mM | 42 | KCl | 0.15 M | 2LZM_A:Q105A | null | null | null | 0.9 | 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 | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":2.1,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM","type":"BUFFER_CONC"... | [{"datasets":["capriotti_S1615_map.csv"],"id":27339,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27340,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2502 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,502 | train | mutant | 201 | 41 | 230 | 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 | Q105E | Q105E | 1 | 1 | 0 | 0 | 105 | Q | E | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 379 | ProTherm | 2.1 | CD | Thermal | H3PO4 | 17 mM | null | KCl | 0.15 M | 2LZM_A:Q105E | 39.9 | -2.1 | null | null | null | null | 82 | 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 | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":2.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValu... | [{"datasets":[],"id":1559,"numValue":39.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1560,"numValue":-2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1561,"numValue":82.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2503 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,503 | train | mutant | 201 | 41 | 230 | 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 | Q105E | Q105E | 1 | 1 | 0 | 0 | 105 | Q | E | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 382 | ProTherm | 5.8 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 0.15 M | 2LZM_A:Q105E | 63.3 | -3 | null | null | null | null | 124 | 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 | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":5.8,"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":1571,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1572,"numValue":-3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1573,"numValue":124.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2504 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,504 | train | mutant | 201 | 41 | 230 | 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 | Q105E | Q105E | 1 | 1 | 0 | 0 | 105 | Q | E | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 6,744 | ProTherm | 5.8 | CD | Thermal | KH2PO4 | 10 mM | 66.3 | KCl | 0.15 M | 2LZM_A:Q105E | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":66.3,"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_CONC... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":23957,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23958,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2505 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,505 | train | mutant | 201 | 41 | 230 | 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 | Q105E | Q105E | 1 | 1 | 0 | 0 | 105 | Q | E | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 8,014 | ProTherm | 2.1 | CD | Thermal | H3PO4 | 17 mM | 42 | KCl | 0.15 M | 2LZM_A:Q105E | null | null | null | 0.5 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":2.1,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM","type":"BUFFER_CONC"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27341,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27342,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2506 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,506 | train | mutant | 202 | 41 | 231 | 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 | Q105G | Q105G | 1 | 1 | 0 | 0 | 105 | Q | G | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 380 | ProTherm | 2.1 | CD | Thermal | H3PO4 | 17 mM | null | KCl | 0.15 M | 2LZM_A:Q105G | 34.8 | -7.2 | null | null | null | null | 72 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":2.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValu... | [{"datasets":[],"id":1563,"numValue":34.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1564,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1565,"numValue":72.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2507 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,507 | train | mutant | 202 | 41 | 231 | 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 | Q105G | Q105G | 1 | 1 | 0 | 0 | 105 | Q | G | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 383 | ProTherm | 5.8 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 0.15 M | 2LZM_A:Q105G | 62.4 | -3.9 | 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 | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":5.8,"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":1575,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1576,"numValue":-3.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1577,"numValue":132.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2508 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,508 | train | mutant | 202 | 41 | 231 | 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 | Q105G | Q105G | 1 | 1 | 0 | 0 | 105 | Q | G | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 6,745 | ProTherm | 5.8 | CD | Thermal | KH2PO4 | 10 mM | 66.3 | KCl | 0.15 M | 2LZM_A:Q105G | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":66.3,"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_CONC... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23959,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23960,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2509 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,509 | train | mutant | 202 | 41 | 231 | 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 | Q105G | Q105G | 1 | 1 | 0 | 0 | 105 | Q | G | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 8,015 | ProTherm | 2.1 | CD | Thermal | H3PO4 | 17 mM | 42 | KCl | 0.15 M | 2LZM_A:Q105G | null | null | null | 1.7 | 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 | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":2.1,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM","type":"BUFFER_CONC"... | [{"datasets":["capriotti_S1615_map.csv"],"id":27343,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27344,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2510 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,510 | train | mutant | 202 | 41 | 231 | 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 | Q105G | Q105G | 1 | 1 | 0 | 0 | 105 | Q | G | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 12,616 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:Q105G | null | null | null | 3.11 | null | null | null | 4.7 | 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":45751,"numValue":3.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45752,"numValue":4.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45753,"numValue":null,"references":[],"strValue":"... | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2511 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,511 | train | mutant | 205 | 41 | 234 | 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 | Q105M | Q105M | 1 | 1 | 0 | 0 | 105 | Q | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 386 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:Q105M | 62.6 | -2.7 | 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":1587,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1588,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1589,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2512 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,512 | train | mutant | 205 | 41 | 234 | 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 | Q105M | Q105M | 1 | 1 | 0 | 0 | 105 | Q | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 105 | A | H | true | true | 60.450739 | 18.97 | 7,119 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:Q105M | null | null | null | 1.2 | 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":24971,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24972,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6896,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2513 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,513 | train | mutant | 809 | 41 | 913 | 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 | M106I | M106I | 1 | 1 | 0 | 0 | 106 | M | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 1,426 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:M106I | 66.1 | 0.6 | null | null | null | null | 132 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.10 M, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":5207,"numValue":66.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5208,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5209,"numValue":132.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5210,"numValue":null,"references":[],"... | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,514 | train | mutant | 809 | 41 | 913 | 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 | M106I | M106I | 1 | 1 | 0 | 0 | 106 | M | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 7,082 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | 61 | 2LZM_A:M106I | null | null | null | -0.2 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":61.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":24845,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24846,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24847,"numValue":null,"references":[],"strValue":"Unknown"... | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2515 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,515 | train | mutant | 1,136 | 41 | 1,280 | 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 | M106A | M106A | 1 | 1 | 0 | 0 | 106 | M | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 2,031 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:M106A | 60.1 | -5.2 | null | null | null | null | 114 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | EASE-MM_S1676.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["EASE-MM_S1676.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv"],"id":7597,"numValue":60.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv"],"id":7598,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE... | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,516 | train | mutant | 1,136 | 41 | 1,280 | 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 | M106A | M106A | 1 | 1 | 0 | 0 | 106 | M | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 3,138 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:M106A | 44.6 | -7.1 | null | null | null | 1.8 | 89 | 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":11442,"numValue":44.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11443,"numValue":-7.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11444,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2517 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,517 | train | mutant | 1,136 | 41 | 1,280 | 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 | M106A | M106A | 1 | 1 | 0 | 0 | 106 | M | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 6,798 | 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:M106A | null | null | null | 1.9 | 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":24096,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24097,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24098,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2518 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,518 | train | mutant | 1,136 | 41 | 1,280 | 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 | M106A | M106A | 1 | 1 | 0 | 0 | 106 | M | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 7,572 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:M106A | null | null | null | 2.3 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26189,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26190,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26191,"numV... | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,519 | train | mutant | 1,681 | 41 | 1,890 | 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 | M106L | M106L | 1 | 1 | 0 | 0 | 106 | M | L | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 3,147 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:M106L | 53.4 | 1.7 | null | null | null | null | 111 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 291 | ARTICLE | Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. | 1,998 | 10.1002/pro.5560070326 | 9541409 | Protein Sci;7;765-73 | 5 | Baase W A|Gassner N C|Lipscomb L A|Snow S D|Eldridge A M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":[],"id":11486,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11487,"numValue":1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11488,"numValue":111.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2520 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,520 | train | mutant | 1,681 | 41 | 1,890 | 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 | M106L | M106L | 1 | 1 | 0 | 0 | 106 | M | L | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 7,812 | ProTherm | 3 | CD | Thermal | phosphoric acid, Potassium phosphate | 3 mM, 17 mM | 47 | KCl | 25 mM | 2LZM_A:M106L | null | null | null | -0.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | 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 | 291 | ARTICLE | Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. | 1,998 | 10.1002/pro.5560070326 | 9541409 | Protein Sci;7;765-73 | 5 | Baase W A|Gassner N C|Lipscomb L A|Snow S D|Eldridge A M | [{"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":"phosphoric acid, Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValu... | [{"datasets":[],"id":26760,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26761,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26762,"numValue":null,"reference... | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2522 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,522 | train | mutant | 1,683 | 41 | 1,892 | 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 | M106K | M106K | 1 | 1 | 0 | 0 | 106 | M | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 106 | A | H | true | true | 54.722496 | 28.24875 | 7,814 | ProTherm | 3 | CD | Thermal | phosphoric acid, Potassium phosphate | 3 mM, 17 mM | 47 | KCl | 25 mM | 2LZM_A:M106K | null | null | null | 3.4 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | 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 | 291 | ARTICLE | Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. | 1,998 | 10.1002/pro.5560070326 | 9541409 | Protein Sci;7;765-73 | 5 | Baase W A|Gassner N C|Lipscomb L A|Snow S D|Eldridge A M | [{"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":"phosphoric acid, Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValu... | [{"datasets":[],"id":26766,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26767,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26768,"numValue":null,"references... | [{"id":6897,"numValue":8.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,523 | train | mutant | 869 | 41 | 984 | 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 | E108V | E108V | 1 | 1 | 0 | 0 | 108 | E | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 108 | A | H | true | true | 48.962672 | 42.887222 | 1,498 | ProTherm | 3.02 | CD | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:E108V | 55.2 | 3.6 | null | null | null | 2.5 | 134 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:E108V","type":... | [{"datasets":[],"id":5484,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5485,"numValue":3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5486,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":5487,"numValue":134.0,"references":[],"st... | [{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2524 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,524 | train | mutant | 869 | 41 | 984 | 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 | E108V | E108V | 1 | 1 | 0 | 0 | 108 | E | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 108 | A | H | true | true | 48.962672 | 42.887222 | 3,823 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:E108V | 56 | 4.3 | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | yes(>95%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|STRUM_Q... | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J 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":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S2204.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id"... | [{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2527 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,527 | train | mutant | 869 | 41 | 984 | 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 | E108V | E108V | 1 | 1 | 0 | 0 | 108 | E | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 108 | A | H | true | true | 48.962672 | 42.887222 | 7,520 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 25 mM | 2LZM_A:E108V | null | null | null | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>95%) | DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.7,"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":["potapov_with_uniprot_mapping.csv"],"id":26052,"numValue":-1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26053,"numValue":null,"references":[],"strValue":"yes(>95%)","type":"REVERSIBILITY"}] | [{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,528 | train | mutant | 869 | 41 | 984 | 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 | E108V | E108V | 1 | 1 | 0 | 0 | 108 | E | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 108 | A | H | true | true | 48.962672 | 42.887222 | 7,582 | ProTherm | 3.02 | CD | Thermal | glycine-HCl | 20 mM | 51.6 | 2LZM_A:E108V | null | null | null | -1.4 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":51.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFE... | [{"datasets":[],"id":26219,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26220,"numValue":-1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26221,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6899,"numValue":5.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2529 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,529 | train | mutant | 505 | 41 | 555 | 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 | T109D | T109D | 1 | 1 | 0 | 0 | 109 | T | D | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 109 | A | H | false | true | 115.999562 | 32.585 | 820 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:T109D | 38.7 | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":3107,"numValue":38.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3108,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3109,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6900,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,530 | train | mutant | 505 | 41 | 555 | 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 | T109D | T109D | 1 | 1 | 0 | 0 | 109 | T | D | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 109 | A | H | false | true | 115.999562 | 32.585 | 825 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:T109D | 63.9 | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":3122,"numValue":63.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3123,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3124,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6900,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2531 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,531 | train | mutant | 505 | 41 | 555 | 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 | T109D | T109D | 1 | 1 | 0 | 0 | 109 | T | D | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 109 | A | H | false | true | 115.999562 | 32.585 | 7,064 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | 62.4 | KCl | 200 mM | 2LZM_A:T109D | null | null | null | -0.6 | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv"],"id":24802,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24803,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6900,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,532 | train | mutant | 505 | 41 | 555 | 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 | T109D | T109D | 1 | 1 | 0 | 0 | 109 | T | D | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 109 | A | H | false | true | 115.999562 | 32.585 | 8,159 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 39.5 | KCl | 200 mM | 2LZM_A:T109D | null | null | null | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":39.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27708,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27709,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6900,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2533 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,533 | train | mutant | 506 | 41 | 556 | 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 | T109N | T109N | 1 | 1 | 0 | 0 | 109 | T | N | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 109 | A | H | false | true | 115.999562 | 32.585 | 821 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:T109N | 39.4 | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":3110,"numValue":39.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":3111,"numValue":-0.1,"references":[],"strValue":null,"typ... | [{"id":6900,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2534 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,534 | train | mutant | 506 | 41 | 556 | 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 | T109N | T109N | 1 | 1 | 0 | 0 | 109 | T | N | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 109 | A | H | false | true | 115.999562 | 32.585 | 826 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:T109N | 62.7 | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":3125,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":3126,"numValue":0.3,"references":[],"strValue":null,"type... | [{"id":6900,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,535 | train | mutant | 506 | 41 | 556 | 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 | T109N | T109N | 1 | 1 | 0 | 0 | 109 | T | N | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 109 | A | H | false | true | 115.999562 | 32.585 | 7,065 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | 62.4 | KCl | 200 mM | 2LZM_A:T109N | 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|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24804,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24805,"numValue":null,"references":[],"strValue":"yes","type":... | [{"id":6900,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2537 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,537 | train | mutant | 285 | 41 | 317 | 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 | V111F | V111F | 1 | 1 | 0 | 0 | 111 | V | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 500 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V111F | 46.99 | -4.77 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":2019,"numValue":46.99,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2020,"numValue":-4.77,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2021,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2539 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,539 | train | mutant | 285 | 41 | 317 | 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 | V111F | V111F | 1 | 1 | 0 | 0 | 111 | V | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 6,969 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 64.89 | KCl | 0.2 M | 2LZM_A:V111F | null | null | null | 1.69 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.89,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv"],"id":24572,"numValue":1.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24573,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2540 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,540 | train | mutant | 285 | 41 | 317 | 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 | V111F | V111F | 1 | 1 | 0 | 0 | 111 | V | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 7,507 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:V111F | null | null | null | 1.43 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26016,"numValue":1.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26017,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2541 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,541 | train | mutant | 286 | 41 | 318 | 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 | V111I | V111I | 1 | 1 | 0 | 0 | 111 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 501 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V111I | 49.44 | -2.32 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":2022,"numValue":49.44,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2023,"numValue":-2.32,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2024,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,542 | train | mutant | 286 | 41 | 318 | 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 | V111I | V111I | 1 | 1 | 0 | 0 | 111 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 504 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:V111I | 62.29 | -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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":[],"id":2031,"numValue":62.29,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2032,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2033,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2544 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,544 | train | mutant | 286 | 41 | 318 | 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 | V111I | V111I | 1 | 1 | 0 | 0 | 111 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 7,508 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:V111I | null | null | null | 0.69 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26018,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26019,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2545 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,545 | train | mutant | 810 | 41 | 914 | 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 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 1,427 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:V111A | 62.6 | -2.9 | null | null | null | null | 121 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.10 M, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":5211,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5212,"numValue":-2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5213,"numValue":121.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5214,"numValue":null,"references":[],... | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2546 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,546 | train | mutant | 810 | 41 | 914 | 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 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 2,032 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:V111A | 62.4 | -2.9 | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | EASE-MM_S1676.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["EASE-MM_S1676.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv"],"id":7602,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","... | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2547 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,547 | train | mutant | 810 | 41 | 914 | 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 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 3,135 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V111A | 48 | -3.7 | null | null | null | 1.8 | 100 | 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":11427,"numValue":48.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11428,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11429,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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