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:2767 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,767 | train | mutant | 171 | 41 | 199 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129M | A129M | 1 | 1 | 0 | 0 | 129 | A | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 6,780 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.10 M | 2LZM_A:A129M | null | null | null | 1.9 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM... | [{"datasets":[],"id":24042,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24043,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24044,"numValue":null,"references... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2768 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,768 | train | mutant | 171 | 41 | 199 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129M | A129M | 1 | 1 | 0 | 0 | 129 | A | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 6,813 | 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:A129M | 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|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":24141,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24142,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24143,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2769 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,769 | train | mutant | 435 | 41 | 481 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129V | A129V | 1 | 1 | 0 | 0 | 129 | A | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 708 | ProTherm | 1.99 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:A129V | 38.5 | -2.9 | null | null | null | null | 78 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":1.99,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":2748,"numValue":38.... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2770 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,770 | train | mutant | 435 | 41 | 481 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129V | A129V | 1 | 1 | 0 | 0 | 129 | A | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 710 | ProTherm | 2.8 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:A129V | 50.2 | -1.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2755,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2756,"numValue":-1.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2757,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2771 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,771 | train | mutant | 435 | 41 | 481 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129V | A129V | 1 | 1 | 0 | 0 | 129 | A | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 7,463 | ProTherm | 2.8 | CD | Thermal | Unknown | 52.1 | KCl | 0.2 M | 2LZM_A:A129V | null | null | null | 0.7 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":52.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25922,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25923,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2772 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,772 | train | mutant | 435 | 41 | 481 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129V | A129V | 1 | 1 | 0 | 0 | 129 | A | V | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 8,056 | ProTherm | 1.99 | CD | Thermal | Unknown | 41.4 | KCl | 0.2 M | 2LZM_A:A129V | null | null | null | 0.8 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":1.99,"strValue":null,"type":"PH"},{"numValue":41.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27427,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27428,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2773 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,773 | train | mutant | 1,966 | 41 | 2,196 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129F | A129F | 1 | 1 | 0 | 0 | 129 | A | F | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 3,786 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A129F | 49.4 | -2.3 | null | null | null | null | 94 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 350 | ARTICLE | The introduction of strain and its effects on the structure and stability of T4 lysozyme. | 2,000 | 10.1006/jmbi.1999.3300 | 10623513 | J Mol Biol;295;127-45 | 3 | Liu R|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":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":["STRUM_Q3421.csv"],"id":13978,"numValue":49.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv","STRUM_Q3421.csv"],"id":13979,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q3421.csv"],"id":13980,"numValue":94.0,"referenc... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2774 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,774 | train | mutant | 1,967 | 41 | 2,197 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129W | A129W | 1 | 1 | 0 | 0 | 129 | A | W | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 3,787 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A129W | 46.6 | -5.1 | null | null | null | null | 80 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 350 | ARTICLE | The introduction of strain and its effects on the structure and stability of T4 lysozyme. | 2,000 | 10.1006/jmbi.1999.3300 | 10623513 | J Mol Biol;295;127-45 | 3 | Liu R|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":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":13982,"numValue":46.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv","STRUM_Q3421.csv"],"id":13983,"numValue":-5.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q342... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2775 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,775 | train | mutant | 6,720 | 41 | 7,362 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129M|F153A | A129M|F153A | 2 | 2 | 0 | 0 | 129 | A | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129|153 | A | H | true | false | 0.53304 | 17.304545 | 14,479 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.10 M | 2LZM_A:A129M 2LZM_A:F153A | 52.6 | -12.7 | null | null | null | 2.5 | 94 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53535,"numValue":52.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53536,"numValue":-12.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53537,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53538,"numValue":94.0,"references":[... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2776 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,776 | train | mutant | 6,720 | 41 | 7,362 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129M|F153A | A129M|F153A | 2 | 2 | 0 | 0 | 129 | A | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129|153 | A | H | true | false | 0.53304 | 17.304545 | 14,910 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.10 M | 2LZM_A:A129M 2LZM_A:F153A | null | null | null | 4.3 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM... | [{"datasets":[],"id":54966,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54967,"numValue":4.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54968,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2777 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,777 | train | mutant | 236 | 41 | 266 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A130S | A130S | 1 | 1 | 0 | 0 | 130 | A | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 130 | A | H | true | false | 9.026523 | 18.654 | 422 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A130S | 48.66 | -2.89 | null | null | null | null | 107 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1739,"numValue":48.66,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1740,"numValue":-2.89,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1741,"numValue":107.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6921,"numValue":7.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2778 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,778 | train | mutant | 236 | 41 | 266 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A130S | A130S | 1 | 1 | 0 | 0 | 130 | A | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 130 | A | H | true | false | 9.026523 | 18.654 | 7,591 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:A130S | null | null | null | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26239,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26240,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6921,"numValue":7.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2779 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,779 | train | mutant | 4,336 | 41 | 4,845 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A130G | A130G | 1 | 1 | 0 | 0 | 130 | A | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 130 | A | H | true | false | 9.026523 | 18.654 | 10,026 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:A130G | null | null | 12.8 | 2.1 | null | null | null | null | 2.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 664 | ARTICLE | Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway. | 2,007 | 10.1110/ps.062632807 | 17400925 | Protein Sci;16;852-62 | 3 | Marqusee Susan|Cellitti Jason|Bernstein Rachel | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"B... | [{"datasets":[],"id":34441,"numValue":12.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34442,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34443,"numValue":2.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34444,"numValue":null,... | [{"id":6921,"numValue":7.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2780 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,780 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 583 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:V131A | 41.25 | 1 | null | null | null | 2.4 | 88.7 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":2320,"numValue":41.25,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2321,"numValue":1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2322,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2781 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,781 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 903 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131A | 54.14 | 0.72 | null | null | null | 1.8 | 123 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3346,"numValue":54.14,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3347,"numValue":0.72,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3348,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2782 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,782 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 910 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:V131A | 67.38 | 0.87 | null | null | null | 2.5 | 140 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3381,"numValue":67.38,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3382,"numValue":0.87,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3383,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2783 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,783 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 949 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131A | 53.74 | 0.66 | null | null | null | null | 128 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3557,"numValue":53.74,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3558,"numValue":0.66,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3559,"numValue":128.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2784 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,784 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 993 | ProTherm | 2.03 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:V131A | 42.03 | 0.56 | null | null | null | null | 84.8 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.03,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":3721,"numValue":42.03,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3722,"numValue":0.56,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3723,"numValue":84.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2785 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,785 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 996 | ProTherm | 2.83 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:V131A | 52 | 0.9 | null | null | null | null | 106.3 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":3733,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3734,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3735,"numValue":106.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2787 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,787 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 6,725 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:V131A | null | null | null | -0.39 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23897,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":23898,"numValue":-0.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23899,"numValue":null,"references":[],"st... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2788 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,788 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,340 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:V131A | null | null | null | -0.33 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":25601,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25602,"numValue":-0.33,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25603,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2789 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,789 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,387 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.08 | KCl | 25 mM | 2LZM_A:V131A | null | null | null | -0.26 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":53.08,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":25727,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25728,"numValue":-0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25729,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2790 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,790 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,611 | ProTherm | 2.83 | CD | Thermal | K2HPO4, NaH2PO4 | 1.05 M, 1.26 M | 51.1 | KCl | 0.2 M | 2LZM_A:V131A | null | null | null | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":51.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"K2HPO4, NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"1.05 M, 1.26 M",... | [{"datasets":["capriotti_S1615_map.csv"],"id":26287,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26288,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2791 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,791 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 8,052 | ProTherm | 2.03 | CD | Thermal | K2HPO4, NaH2PO4 | 1.05 M, 1.26 M | 41.47 | KCl | 0.2 M | 2LZM_A:V131A | null | null | null | -0.15 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.03,"strValue":null,"type":"PH"},{"numValue":41.47,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"K2HPO4, NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"1.05 M, 1.26 M"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27419,"numValue":-0.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27420,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2792 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,792 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 8,069 | ProTherm | 2 | CD | Thermal | HCl | 40.8 | KCl | 0.20 M | 2LZM_A:V131A | null | null | null | -0.26 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.8,"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":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv"],"id":27453,"numValue":-0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27454,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2793 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,793 | train | mutant | 334 | 41 | 372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A | V131A | 1 | 1 | 0 | 0 | 131 | V | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 8,071 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:V131A | null | null | null | -0.27 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":27458,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":27459,"numValue":-0.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27460,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2794 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,794 | train | mutant | 565 | 41 | 616 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131L | V131L | 1 | 1 | 0 | 0 | 131 | V | L | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 950 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131L | 53.31 | 0.23 | null | null | null | null | 121 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3561,"numValue":53.31,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3562,"numValue":0.23,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3563,"numValue":121.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2795 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,795 | train | mutant | 565 | 41 | 616 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131L | V131L | 1 | 1 | 0 | 0 | 131 | V | L | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,388 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.08 | KCl | 25 mM | 2LZM_A:V131L | null | null | null | -0.09 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":53.08,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":25730,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25731,"numValue":-0.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25732,"numValue":null,"referenc... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2796 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,796 | train | mutant | 566 | 41 | 617 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131M | V131M | 1 | 1 | 0 | 0 | 131 | V | M | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 951 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131M | 53.4 | 0.32 | null | null | null | null | 126 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3565,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3566,"numValue":0.32,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3567,"numValue":126.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2797 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,797 | train | mutant | 566 | 41 | 617 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131M | V131M | 1 | 1 | 0 | 0 | 131 | V | M | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,389 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.08 | KCl | 25 mM | 2LZM_A:V131M | null | null | null | -0.12 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":53.08,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":25733,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25734,"numValue":-0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25735,"numValue":null,"referenc... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2798 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,798 | train | mutant | 567 | 41 | 618 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131I | V131I | 1 | 1 | 0 | 0 | 131 | V | I | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 952 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131I | 53.49 | 0.41 | null | null | null | null | 127 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3569,"numValue":53.49,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3570,"numValue":0.41,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3571,"numValue":127.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2799 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,799 | train | mutant | 567 | 41 | 618 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131I | V131I | 1 | 1 | 0 | 0 | 131 | V | I | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,390 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.08 | KCl | 25 mM | 2LZM_A:V131I | null | null | null | -0.16 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":53.08,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":25736,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25737,"numValue":-0.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25738,"numValue":null,"referenc... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2800 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,800 | train | mutant | 568 | 41 | 619 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131T | V131T | 1 | 1 | 0 | 0 | 131 | V | T | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 953 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131T | 52.75 | -0.33 | null | null | null | null | 122 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3573,"numValue":52.75,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3574,"numValue":-0.33,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3575,"numValue":122.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2801 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,801 | train | mutant | 568 | 41 | 619 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131T | V131T | 1 | 1 | 0 | 0 | 131 | V | T | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 994 | ProTherm | 2.03 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:V131T | 41.06 | -0.41 | null | null | null | null | 82.4 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.03,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":3725,"numValue":41.06,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3726,"numValue":-0.41,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3727,"numValue":82.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2802 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,802 | train | mutant | 568 | 41 | 619 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131T | V131T | 1 | 1 | 0 | 0 | 131 | V | T | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 997 | ProTherm | 2.83 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:V131T | 50.95 | -0.1 | null | null | null | null | 106.3 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":3737,"numValue":50.95,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3738,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3739,"numValue":106.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2804 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,804 | train | mutant | 568 | 41 | 619 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131T | V131T | 1 | 1 | 0 | 0 | 131 | V | T | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,612 | ProTherm | 2.83 | CD | Thermal | K2HPO4, NaH2PO4 | 1.05 M, 1.26 M | 51.1 | KCl | 0.2 M | 2LZM_A:V131T | null | null | null | 0.05 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":51.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"K2HPO4, NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"1.05 M, 1.26 M",... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26289,"numValue":0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26290,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2805 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,805 | train | mutant | 568 | 41 | 619 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131T | V131T | 1 | 1 | 0 | 0 | 131 | V | T | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 8,053 | ProTherm | 2.03 | CD | Thermal | K2HPO4, NaH2PO4 | 1.05 M, 1.26 M | 41.47 | KCl | 0.2 M | 2LZM_A:V131T | null | null | null | 0.11 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.03,"strValue":null,"type":"PH"},{"numValue":41.47,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"K2HPO4, NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"1.05 M, 1.26 M"... | [{"datasets":["capriotti_S1615_map.csv"],"id":27421,"numValue":0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27422,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2806 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,806 | train | mutant | 569 | 41 | 620 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131E | V131E | 1 | 1 | 0 | 0 | 131 | V | E | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 954 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131E | 53.6 | 0.52 | null | null | null | null | 128 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3577,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3578,"numValue":0.52,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3579,"numValue":128.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2808 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,808 | train | mutant | 570 | 41 | 621 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131S | V131S | 1 | 1 | 0 | 0 | 131 | V | S | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 955 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131S | 52.96 | -0.12 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3581,"numValue":52.96,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3582,"numValue":-0.12,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3583,"numValue":124.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2809 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,809 | train | mutant | 570 | 41 | 621 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131S | V131S | 1 | 1 | 0 | 0 | 131 | V | S | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,393 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.08 | KCl | 25 mM | 2LZM_A:V131S | null | null | null | 0.05 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":53.08,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":25745,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25746,"numValue":0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25747,"numValue":null,"reference... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2810 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,810 | train | mutant | 571 | 41 | 622 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131D | V131D | 1 | 1 | 0 | 0 | 131 | V | D | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 956 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131D | 53.3 | 0.22 | null | null | null | null | 123 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3585,"numValue":53.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3586,"numValue":0.22,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3587,"numValue":123.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2811 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,811 | train | mutant | 571 | 41 | 622 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131D | V131D | 1 | 1 | 0 | 0 | 131 | V | D | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,394 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.08 | KCl | 25 mM | 2LZM_A:V131D | null | null | null | -0.08 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":53.08,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":25748,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25749,"numValue":-0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25750,"numValue":null,"referenc... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2812 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,812 | train | mutant | 572 | 41 | 623 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131G | V131G | 1 | 1 | 0 | 0 | 131 | V | G | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 957 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:V131G | 51.28 | -1.8 | null | null | null | null | 123 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3589,"numValue":51.28,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3590,"numValue":-1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3591,"numValue":123.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2813 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,813 | train | mutant | 572 | 41 | 623 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131G | V131G | 1 | 1 | 0 | 0 | 131 | V | G | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 131 | A | H | true | false | 94.547905 | 19.562143 | 7,395 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.08 | KCl | 25 mM | 2LZM_A:V131G | null | null | null | 0.68 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":53.08,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":25751,"numValue":2.4,"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":25752,"numValue":0.68,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25753,"num... | [{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2815 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,815 | train | mutant | 6,747 | 41 | 7,389 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|N132A | V131A|N132A | 2 | 2 | 0 | 0 | 131 | V | A | 2 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 131|132 | A | H | true | false | 68.516007 | 18.620759 | 14,719 | ProTherm | 2 | CD | Thermal | HCl | null | KCl | 0.20 M | 2LZM_A:V131A 2LZM_A:N132A | 43.1 | 2.3 | null | null | null | null | 82 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"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":"KCl","type":"ION"},{"numValue":null,"strValue":"0.20 M","type":"ION_CONC"},{"numValue":n... | [{"datasets":[],"id":54427,"numValue":43.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54428,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54429,"numValue":82.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54430,"numValue":null,"references":[... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6923,"numValue":6.0,"position":132,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2816 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,816 | train | mutant | 6,747 | 41 | 7,389 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|N132A | V131A|N132A | 2 | 2 | 0 | 0 | 131 | V | A | 2 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 131|132 | A | H | true | false | 68.516007 | 18.620759 | 15,100 | ProTherm | 2 | CD | Thermal | HCl | 40.8 | KCl | 0.20 M | 2LZM_A:V131A 2LZM_A:N132A | null | null | null | -0.62 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.8,"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":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":55415,"numValue":-0.62,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55416,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6923,"numValue":6.0,"position":132,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2817 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,817 | train | mutant | 6,747 | 41 | 7,389 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|N132A | V131A|N132A | 2 | 2 | 0 | 0 | 131 | V | A | 2 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 131|132 | A | H | true | false | 68.516007 | 18.620759 | 15,104 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:V131A 2LZM_A:N132A | null | null | null | -0.57 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":55425,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55426,"numValue":-0.57,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55427,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6923,"numValue":6.0,"position":132,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2818 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,818 | train | mutant | 538 | 41 | 589 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N132M | N132M | 1 | 1 | 0 | 0 | 132 | N | M | 6 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 132 | A | H | true | false | 42.48411 | 17.679375 | 921 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:N132M | 70.08 | 3.6 | null | null | null | 3.5 | 134 | 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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3436,"numValue":70.08,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3437,"numValue":3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3438,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6923,"numValue":6.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2819 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,819 | train | mutant | 538 | 41 | 589 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N132M | N132M | 1 | 1 | 0 | 0 | 132 | N | M | 6 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 132 | A | H | true | false | 42.48411 | 17.679375 | 6,736 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:N132M | null | null | null | -1.5 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.48,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23930,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23931,"numValue":-1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23932,"numValue":null,"reference... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6923,"numValue":6.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2820 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,820 | train | mutant | 539 | 41 | 590 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N132F | N132F | 1 | 1 | 0 | 0 | 132 | N | F | 6 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 132 | A | H | true | false | 42.48411 | 17.679375 | 922 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:N132F | 69.78 | 3.3 | null | null | null | 3.5 | 134 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3441,"numValue":69.78,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3442,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iP... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6923,"numValue":6.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2821 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,821 | train | mutant | 539 | 41 | 590 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N132F | N132F | 1 | 1 | 0 | 0 | 132 | N | F | 6 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 132 | A | H | true | false | 42.48411 | 17.679375 | 6,737 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:N132F | null | null | null | -1.3 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.48,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23933,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23934,"numValue":-1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23935,"numValue":null,"reference... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6923,"numValue":6.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2823 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,823 | train | mutant | 540 | 41 | 591 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N132I | N132I | 1 | 1 | 0 | 0 | 132 | N | I | 6 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 132 | A | H | true | false | 42.48411 | 17.679375 | 6,738 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:N132I | null | null | null | -1.2 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.48,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23936,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23937,"numValue":-1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23938,"numValue":null,"reference... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6923,"numValue":6.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2824 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,824 | train | mutant | 42 | 41 | 46 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133A | L133A | 1 | 1 | 0 | 0 | 133 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 42 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | null | KCl | 0.025 M | 2LZM_A:L133A | 42.9 | -8.9 | null | null | null | 2.5 | 91.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.020 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type"... | [{"datasets":[],"id":141,"numValue":42.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":142,"numValue":-8.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":143,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2825 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,825 | train | mutant | 42 | 41 | 46 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133A | L133A | 1 | 1 | 0 | 0 | 133 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 584 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:L133A | 23.75 | -17 | null | null | null | 2.4 | 53 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | M47andM8_S2760.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | MEASURE|PH|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":["M47andM8_S2760.csv"],"id":2325,"numValue":23.75,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2326,"numValue":-17.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2327,"numValue":2.4,"references":[],"strValue":null,"type":"DCP... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2826 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,826 | train | mutant | 42 | 41 | 46 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133A | L133A | 1 | 1 | 0 | 0 | 133 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 7,503 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | 51.8 | KCl | 0.025 M | 2LZM_A:L133A | null | null | null | 4.3 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.8,"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":"0.020 M","ty... | [{"datasets":[],"id":26006,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":26007,"numValue":4.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26008,"numValue":null,"references":[],"strV... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2827 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,827 | train | mutant | 42 | 41 | 46 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133A | L133A | 1 | 1 | 0 | 0 | 133 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 8,072 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:L133A | null | null | null | 4.19 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":27461,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27462,"numValue":4.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27463,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2828 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,828 | train | mutant | 168 | 41 | 196 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133M | L133M | 1 | 1 | 0 | 0 | 133 | L | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 305 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:L133M | 64.3 | -1 | null | null | null | 2.5 | 128 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":1250,"numValue":64.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1251,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1252,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2829 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,829 | train | mutant | 168 | 41 | 196 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133M | L133M | 1 | 1 | 0 | 0 | 133 | L | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 6,776 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:L133M | null | null | null | 0.4 | 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":24030,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24031,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24032,"numValue":null,"references... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2830 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,830 | train | mutant | 340 | 41 | 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 | L133D | L133D | 1 | 1 | 0 | 0 | 133 | L | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 596 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L133D | 36.7 | -14.9 | null | null | null | 1.8 | 47.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":2365,"numValue":36.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2366,"numValue":-14.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2367,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2832 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,832 | train | mutant | 340 | 41 | 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 | L133D | L133D | 1 | 1 | 0 | 0 | 133 | L | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 599 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L133D | 44 | -17.9 | null | null | null | 1.8 | 50.8 | null | null | null | null | null | null | null | null | null | yes(50-75%) | 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":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":2380,"numValue":44.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2381,"numValue":-17.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2382,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2833 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,833 | train | mutant | 340 | 41 | 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 | L133D | L133D | 1 | 1 | 0 | 0 | 133 | L | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 601 | ProTherm | 10.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L133D | 28.9 | -19 | null | null | null | 1.8 | 47.1 | null | null | null | null | null | null | null | null | null | yes(20%) | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.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":2390,"numValue":28.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2391,"numValue":-19.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":2392,"numValue":1.8,"refe... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2834 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,834 | train | mutant | 340 | 41 | 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 | L133D | L133D | 1 | 1 | 0 | 0 | 133 | L | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 7,005 | ProTherm | 4.4 | CD | Thermal | Potassium phosphate | 20 mM | 64.6 | KCl | 25 mM | 2LZM_A:L133D | null | null | null | 5.5 | 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":4.4,"strValue":null,"type":"PH"},{"numValue":64.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":24656,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":24657,"numValue":5.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24658,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2835 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,835 | train | mutant | 340 | 41 | 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 | L133D | L133D | 1 | 1 | 0 | 0 | 133 | L | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 7,075 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 20 mM | 61.9 | KCl | 25 mM | 2LZM_A:L133D | null | null | null | 5.7 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(50-75%) | 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":6.5,"strValue":null,"type":"PH"},{"numValue":61.9,"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":24824,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":24825,"numValue":5.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24826,"numValue":null,"references":[],"strValue":"yes(50-75%)","type":"REVERSIBILITY"}] | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2836 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,836 | train | mutant | 340 | 41 | 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 | L133D | L133D | 1 | 1 | 0 | 0 | 133 | L | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 7,581 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.6 | KCl | 25 mM | 2LZM_A:L133D | null | null | null | 4.9 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":26216,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26217,"numValue":4.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26218,"numValue":null,"references":[],"strValue":"yes","type":"REVER... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2837 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,837 | train | mutant | 434 | 41 | 480 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133F | L133F | 1 | 1 | 0 | 0 | 133 | L | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 707 | ProTherm | 1.99 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:L133F | 40.7 | -0.7 | null | null | null | null | 83 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":1.99,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":2744,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2745,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2746,"numValue":83.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUT... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2838 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,838 | train | mutant | 434 | 41 | 480 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133F | L133F | 1 | 1 | 0 | 0 | 133 | L | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 709 | ProTherm | 2.86 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:L133F | 51.3 | -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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":2.86,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":2752,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2753,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2754,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2839 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,839 | train | mutant | 434 | 41 | 480 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133F | L133F | 1 | 1 | 0 | 0 | 133 | L | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 1,429 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:L133F | 64.8 | -0.7 | null | null | null | null | 130 | 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|_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":5219,"numValue":64.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":5220,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5221,"numValue":130.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2840 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,840 | train | mutant | 434 | 41 | 480 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133F | L133F | 1 | 1 | 0 | 0 | 133 | L | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 7,085 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | 61 | 2LZM_A:L133F | null | null | null | 0.3 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | 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":24854,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24855,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24856,"numValue":null,"references":[],"strValue":"Unknown","type"... | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2841 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,841 | train | mutant | 434 | 41 | 480 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133F | L133F | 1 | 1 | 0 | 0 | 133 | L | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 7,462 | ProTherm | 2.86 | CD | Thermal | Unknown | 52.1 | KCl | 0.2 M | 2LZM_A:L133F | null | null | null | 0.3 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":2.86,"strValue":null,"type":"PH"},{"numValue":52.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25920,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25921,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2842 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,842 | train | mutant | 434 | 41 | 480 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L133F | L133F | 1 | 1 | 0 | 0 | 133 | L | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 133 | A | H | true | false | 1.679637 | 15.7625 | 8,055 | ProTherm | 1.99 | CD | Thermal | Unknown | 41.4 | KCl | 0.2 M | 2LZM_A:L133F | null | null | null | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":1.99,"strValue":null,"type":"PH"},{"numValue":41.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27425,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27426,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2843 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,843 | train | mutant | 237 | 41 | 267 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A134S | A134S | 1 | 1 | 0 | 0 | 134 | A | S | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 134 | A | H | true | false | 29.453611 | 17.493 | 423 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A134S | 51.11 | -0.44 | null | null | null | null | 111 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1743,"numValue":51.11,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1744,"numValue":-0.44,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1745,"numValue":111.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6925,"numValue":6.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2844 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,844 | train | mutant | 237 | 41 | 267 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A134S | A134S | 1 | 1 | 0 | 0 | 134 | A | S | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 134 | A | H | true | false | 29.453611 | 17.493 | 7,592 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:A134S | 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 | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26241,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26242,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6925,"numValue":6.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2845 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,845 | train | mutant | 57 | 41 | 63 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135E | K135E | 1 | 1 | 0 | 0 | 135 | K | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135 | A | S | true | false | 146.699309 | 30.577222 | 71 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K135E | 50.2 | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":242,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":243,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":244,"numValue":null,"references":[],"strValue":"yes","type":"REVERS... | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2846 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,846 | train | mutant | 57 | 41 | 63 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135E | K135E | 1 | 1 | 0 | 0 | 135 | K | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135 | A | S | true | false | 146.699309 | 30.577222 | 76 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K135E | 64.4 | -2.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":257,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":258,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":259,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2847 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,847 | train | mutant | 57 | 41 | 63 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135E | K135E | 1 | 1 | 0 | 0 | 135 | K | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135 | A | S | true | false | 146.699309 | 30.577222 | 6,712 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:K135E | null | null | null | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":66.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":23867,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23868,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2848 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,848 | train | mutant | 57 | 41 | 63 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135E | K135E | 1 | 1 | 0 | 0 | 135 | K | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135 | A | S | true | false | 146.699309 | 30.577222 | 7,616 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K135E | null | null | null | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":50.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26297,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26298,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2849 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,849 | train | mutant | 57 | 41 | 63 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135E | K135E | 1 | 1 | 0 | 0 | 135 | K | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135 | A | S | true | false | 146.699309 | 30.577222 | 11,154 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 25 | KCl | 25 mM | 2LZM_A:K135E | null | null | null | 1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 750 | ARTICLE | Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. | 2,000 | 10.1110/ps.9.7.1395 | 10933506 | Protein Sci;9;1395-8 | 3 | Pace C N|Shaw K L|Alston R W | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":38362,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38363,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2850 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,850 | train | mutant | 1,882 | 41 | 2,110 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135C | K135C | 1 | 1 | 0 | 0 | 135 | K | C | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135 | A | S | true | false | 146.699309 | 30.577222 | 3,627 | ProTherm | 2.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K135C | 33.8 | -2.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Broom_S605.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 338 | ARTICLE | Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. | 1,992 | 10.1021/bi00149a004 | 1510962 | Biochemistry;31;7765-72 | 4 | Lu J|Baase W A|Dahlquist F W|Muchmore D C | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13332,"numValue":33.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13333,"numValue":-2.6,"references":... | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2852 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,852 | train | mutant | 6,704 | 41 | 7,346 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135E|K147E | K135E|K147E | 2 | 2 | 0 | 0 | 135 | K | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135|147 | A | S|H | true | false | 119.150183 | 30.829722 | 14,453 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K135E 2LZM_A:K147E | 63 | -3.7 | 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 | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53427,"numValue":63.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53428,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53429,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2853 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,853 | train | mutant | 6,704 | 41 | 7,346 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135E|K147E | K135E|K147E | 2 | 2 | 0 | 0 | 135 | K | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135|147 | A | S|H | true | false | 119.150183 | 30.829722 | 14,890 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:K135E 2LZM_A:K147E | null | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":66.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":54915,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54916,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2854 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,854 | train | mutant | 6,704 | 41 | 7,346 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K135E|K147E | K135E|K147E | 2 | 2 | 0 | 0 | 135 | K | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 135|147 | A | S|H | true | false | 119.150183 | 30.829722 | 15,037 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K135E 2LZM_A:K147E | null | null | null | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":50.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55263,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55264,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2855 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,855 | train | mutant | 132 | 41 | 150 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y | W138Y | 1 | 1 | 0 | 0 | 138 | W | Y | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 138 | A | H | true | true | 14.821883 | 15.446786 | 244 | ProTherm | 2 | CD | Thermal | Unknown | null | 2LZM_A:W138Y | 46.85 | null | null | null | null | 2.1 | 104 | 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":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:W138Y","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":998,"numValue":46.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":999,"numValue":2.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1000,"numValue":104.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1001,"numValue":null,"references":[],"s... | [{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:2856 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,856 | train | mutant | 132 | 41 | 150 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y | W138Y | 1 | 1 | 0 | 0 | 138 | W | Y | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 138 | A | H | true | true | 14.821883 | 15.446786 | 249 | ProTherm | 2 | CD | Thermal | Unknown | null | 2LZM_A:W138Y | 34 | -3 | null | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.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":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:W138Y","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":1018,"numValue":34.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1019,"numValue":-3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1020,"numValue":2.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":["EASE-... | [{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2859 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,859 | train | mutant | 132 | 41 | 150 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y | W138Y | 1 | 1 | 0 | 0 | 138 | W | Y | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 138 | A | H | true | true | 14.821883 | 15.446786 | 12,618 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:W138Y | null | null | null | 2.87 | null | null | null | 4.9 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["SAAFEC_S1262.csv"],"id":45757,"numValue":2.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45758,"numValue":4.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45759,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2860 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,860 | train | mutant | 1,877 | 41 | 2,105 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T142C | T142C | 1 | 1 | 0 | 0 | 142 | T | C | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 142 | A | S | true | true | 25.225749 | 14.916429 | 3,621 | ProTherm | 2.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T142C | 35.9 | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|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|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 338 | ARTICLE | Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. | 1,992 | 10.1021/bi00149a004 | 1510962 | Biochemistry;31;7765-72 | 4 | Lu J|Baase W A|Dahlquist F W|Muchmore D C | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13314,"numValue":35.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":13315,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMU... | [{"id":6933,"numValue":9.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2861 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,861 | train | mutant | 1,600 | 41 | 1,800 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P143A | P143A | 1 | 1 | 0 | 0 | 143 | P | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 143 | A | H | false | false | 55.024902 | 16.895714 | 2,999 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:P143A | 36.9 | -5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:P143A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10888,"numValue":36.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":10889,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"... | [{"id":6934,"numValue":5.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2862 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,862 | train | mutant | 1,600 | 41 | 1,800 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P143A | P143A | 1 | 1 | 0 | 0 | 143 | P | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 143 | A | H | false | false | 55.024902 | 16.895714 | 4,656 | ProTherm | 2 | CD | Thermal | Phosphate buffer | 50 mM | null | 2LZM_A:P143A | 36.9 | -5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:P143A","ty... | [{"datasets":[],"id":17216,"numValue":36.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17217,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17218,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[]... | [{"id":6934,"numValue":5.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2863 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,863 | train | mutant | 1,600 | 41 | 1,800 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P143A | P143A | 1 | 1 | 0 | 0 | 143 | P | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 143 | A | H | false | false | 55.024902 | 16.895714 | 13,901 | ProTherm | 5.7 | CD | GdnHCl | Phosphate buffer | 50 mM | 12 | 2LZM_A:P143A | null | null | 17.2 | null | null | null | null | 3.01 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":12.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":51445,"numValue":17.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51446,"numValue":3.01,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":51447,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":51448,"numValue":null,"references":[... | [{"id":6934,"numValue":5.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2864 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,864 | train | mutant | 507 | 41 | 557 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144H | N144H | 1 | 1 | 0 | 0 | 144 | N | H | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 822 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:N144H | 37.2 | -2.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":3113,"numValue":37.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3114,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3115,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2865 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,865 | train | mutant | 507 | 41 | 557 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144H | N144H | 1 | 1 | 0 | 0 | 144 | N | H | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 827 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:N144H | 63.1 | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":3128,"numValue":63.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3129,"numValue":0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3130,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2866 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,866 | train | mutant | 507 | 41 | 557 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144H | N144H | 1 | 1 | 0 | 0 | 144 | N | H | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 7,066 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | 62.4 | KCl | 200 mM | 2LZM_A:N144H | 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":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"],"id":24806,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24807,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2867 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,867 | train | mutant | 507 | 41 | 557 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144H | N144H | 1 | 1 | 0 | 0 | 144 | N | H | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 8,161 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 39.5 | KCl | 200 mM | 2LZM_A:N144H | 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":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"],"id":27712,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27713,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2868 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,868 | train | mutant | 528 | 41 | 579 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144D | N144D | 1 | 1 | 0 | 0 | 144 | N | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 901 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:N144D | 54.36 | 0.94 | null | null | null | 1.8 | 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 | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3336,"numValue":54.36,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3337,"numValue":0.94,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3338,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2869 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,869 | train | mutant | 528 | 41 | 579 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144D | N144D | 1 | 1 | 0 | 0 | 144 | N | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 908 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:N144D | 67.5 | 0.99 | null | null | null | 2.5 | 142 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3371,"numValue":67.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3372,"numValue":0.99,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3373,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2870 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,870 | train | mutant | 528 | 41 | 579 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144D | N144D | 1 | 1 | 0 | 0 | 144 | N | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 3,298 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:N144D | 40.7 | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":12138,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12139,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12140,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2871 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,871 | train | mutant | 528 | 41 | 579 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144D | N144D | 1 | 1 | 0 | 0 | 144 | N | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 3,303 | ProTherm | 6.9 | CD | Thermal | phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:N144D | 67.5 | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|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":6.9,"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":12153,"numValue":67.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12154,"numValue":1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12155,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2872 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,872 | train | mutant | 528 | 41 | 579 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144D | N144D | 1 | 1 | 0 | 0 | 144 | N | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 6,723 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:N144D | null | null | null | -0.41 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23891,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":23892,"numValue":-0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23893,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2873 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,873 | train | mutant | 528 | 41 | 579 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144D | N144D | 1 | 1 | 0 | 0 | 144 | N | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 6,753 | ProTherm | 6.9 | CD | Thermal | phosphate | 10 mM | 66.1 | KCl | 150 mM | 2LZM_A:N144D | null | null | null | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.9,"strValue":null,"type":"PH"},{"numValue":66.1,"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_C... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":23976,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23977,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2875 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,875 | train | mutant | 528 | 41 | 579 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144D | N144D | 1 | 1 | 0 | 0 | 144 | N | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 8,067 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 40.9 | KCl | 200 mM | 2LZM_A:N144D | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.9,"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":27449,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27450,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2876 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,876 | train | mutant | 1,774 | 41 | 1,987 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N144E | N144E | 1 | 1 | 0 | 0 | 144 | N | E | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 144 | A | H | false | false | 101.804914 | 19.459375 | 3,410 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:N144E | 39.4 | 0.9 | null | null | null | null | 83 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":12579,"numValue":39.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12580,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12581,"numValue":83.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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