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:1662 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,662 | train | mutant | 7,102 | 41 | 7,755 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C|C54T | I3C|C54T | 2 | 2 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|54 | A | H|L | true | false | 14.680993 | 20.872738 | 15,597 | ProTherm | 5 | CD | GdnHCl | Sodium phosphate | 2 mM | 20 | 2LZM_A:I3C 2LZM_A:C54T | null | null | 13.2 | null | null | null | null | 3.03 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 925 | ARTICLE | Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies. | 1,989 | 10.1021/bi00428a041 | 2653427 | Biochemistry;28;685-91 | 2 | Schellman J A|Chen B L | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"2 mM","type":"BUF... | [{"datasets":[],"id":57227,"numValue":13.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":57228,"numValue":3.03,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":57229,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1663 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,663 | train | mutant | 7,102 | 41 | 7,755 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C|C54T | I3C|C54T | 2 | 2 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|54 | A | H|L | true | false | 14.680993 | 20.872738 | 15,611 | ProTherm | 5 | CD | GdnHCl | Sodium phosphate | 2 mM | 12 | 2LZM_A:I3C 2LZM_A:C54T | null | null | 14.8 | null | null | null | null | 3.15 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 925 | ARTICLE | Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies. | 1,989 | 10.1021/bi00428a041 | 2653427 | Biochemistry;28;685-91 | 2 | Schellman J A|Chen B L | [{"numValue":5.0,"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":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"2 mM","type":"BUF... | [{"datasets":[],"id":57278,"numValue":14.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":57279,"numValue":3.15,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":57280,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1665 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,665 | train | mutant | 1,122 | 41 | 1,266 | 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 | M6A | M6A | 1 | 1 | 0 | 0 | 6 | M | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6 | A | H | false | false | 0 | 11.909375 | 2,016 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:M6A | 60.8 | -4.5 | null | null | null | null | 121 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|Saraboji_S1396.csv|EASE-MM_S1676.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7522,"numValue":60.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1667 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,667 | train | mutant | 1,122 | 41 | 1,266 | 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 | M6A | M6A | 1 | 1 | 0 | 0 | 6 | M | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6 | A | H | false | false | 0 | 11.909375 | 6,783 | 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:M6A | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24051,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24052,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24053,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1668 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,668 | train | mutant | 1,122 | 41 | 1,266 | 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 | M6A | M6A | 1 | 1 | 0 | 0 | 6 | M | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6 | A | H | false | false | 0 | 11.909375 | 7,571 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:M6A | null | null | null | 1.9 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26186,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26187,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26188,"numV... | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1669 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,669 | train | mutant | 1,616 | 41 | 1,817 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M6I | M6I | 1 | 1 | 0 | 0 | 6 | M | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6 | A | H | false | false | 0 | 11.909375 | 3,029 | ProTherm | 6 | CD | Thermal | Unknown | null | 2LZM_A:M6I | 62.1 | -3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 272 | ARTICLE | Protein stability curves. | 1,987 | 10.1002/bip.360261104 | 3689874 | Biopolymers;26;1859-77 | 2 | Schellman J A|Becktel W J | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:M6I","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11008,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":11009,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"},{"... | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1670 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,670 | train | mutant | 1,616 | 41 | 1,817 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M6I | M6I | 1 | 1 | 0 | 0 | 6 | M | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6 | A | H | false | false | 0 | 11.909375 | 6,763 | ProTherm | 6 | CD | Thermal | Unknown | 65.5 | 2LZM_A:M6I | null | null | null | 1.38 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 272 | ARTICLE | Protein stability curves. | 1,987 | 10.1002/bip.360261104 | 3689874 | Biopolymers;26;1859-77 | 2 | Schellman J A|Becktel W J | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":65.5,"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":"2LZM_A:M6I","type":"_PDB_... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23996,"numValue":1.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23997,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,671 | train | mutant | 1,616 | 41 | 1,817 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M6I | M6I | 1 | 1 | 0 | 0 | 6 | M | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6 | A | H | false | false | 0 | 11.909375 | 12,602 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:M6I | null | null | null | 4.78 | null | null | null | 3.9 | 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":45709,"numValue":4.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45710,"numValue":3.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45711,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1672 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,672 | train | mutant | 1,680 | 41 | 1,889 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M6L | M6L | 1 | 1 | 0 | 0 | 6 | M | L | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6 | A | H | false | false | 0 | 11.909375 | 3,146 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:M6L | 41.1 | -10.6 | null | null | null | null | 61 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 291 | ARTICLE | Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. | 1,998 | 10.1002/pro.5560070326 | 9541409 | Protein Sci;7;765-73 | 5 | Baase W A|Gassner N C|Lipscomb L A|Snow S D|Eldridge A M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":[],"id":11482,"numValue":41.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11483,"numValue":-10.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11484,"numValue":61.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[... | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1673 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,673 | train | mutant | 1,680 | 41 | 1,889 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M6L | M6L | 1 | 1 | 0 | 0 | 6 | M | L | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6 | A | H | false | false | 0 | 11.909375 | 7,811 | ProTherm | 3 | CD | Thermal | phosphoric acid, Potassium phosphate | 3 mM, 17 mM | 47 | KCl | 25 mM | 2LZM_A:M6L | null | null | null | 2.8 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 291 | ARTICLE | Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. | 1,998 | 10.1002/pro.5560070326 | 9541409 | Protein Sci;7;765-73 | 5 | Baase W A|Gassner N C|Lipscomb L A|Snow S D|Eldridge A M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid, Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValu... | [{"datasets":[],"id":26757,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26758,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26759,"numValue":null,"references... | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,674 | train | mutant | 6,849 | 41 | 7,491 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M6I|R96H | M6I|R96H | 2 | 2 | 0 | 0 | 6 | M | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6|96 | A | H | false | false | 38.366511 | 15.64696 | 14,679 | ProTherm | 6 | CD | Thermal | Unknown | null | 2LZM_A:M6I 2LZM_A:R96H | 51.8 | -13.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 272 | ARTICLE | Protein stability curves. | 1,987 | 10.1002/bip.360261104 | 3689874 | Biopolymers;26;1859-77 | 2 | Schellman J A|Becktel W J | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:M6I 2LZM_A:R96H","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":54289,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54290,"numValue":-13.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54291,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:1675 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,675 | train | mutant | 6,849 | 41 | 7,491 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M6I|R96H | M6I|R96H | 2 | 2 | 0 | 0 | 6 | M | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 6|96 | A | H | false | false | 38.366511 | 15.64696 | 14,906 | ProTherm | 6 | CD | Thermal | Unknown | 65.5 | 2LZM_A:M6I 2LZM_A:R96H | null | null | null | 5.08 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 272 | ARTICLE | Protein stability curves. | 1,987 | 10.1002/bip.360261104 | 3689874 | Biopolymers;26;1859-77 | 2 | Schellman J A|Becktel W J | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":65.5,"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":"2LZM_A:M6I 2LZM_A:R96H","... | [{"datasets":[],"id":54956,"numValue":5.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54957,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6797,"numValue":8.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:1676 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,676 | train | mutant | 1,123 | 41 | 1,267 | 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 | L7A | L7A | 1 | 1 | 0 | 0 | 7 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 7 | A | H | false | false | 0 | 13.963125 | 2,017 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L7A | 59 | -6.3 | null | null | null | null | 112 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7527,"numValue":59.0,"references":[],"strValue":null,"type":"TM"}... | [{"id":6798,"numValue":9.0,"position":7,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1677 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,677 | train | mutant | 1,123 | 41 | 1,267 | 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 | L7A | L7A | 1 | 1 | 0 | 0 | 7 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 7 | A | H | false | false | 0 | 13.963125 | 3,141 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L7A | 43.6 | -8.1 | null | null | null | 1.8 | 90 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11457,"numValue":43.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11458,"numValue":-8.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11459,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6798,"numValue":9.0,"position":7,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1678 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,678 | train | mutant | 1,123 | 41 | 1,267 | 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 | L7A | L7A | 1 | 1 | 0 | 0 | 7 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 7 | A | H | false | false | 0 | 13.963125 | 6,784 | 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:L7A | null | null | null | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24054,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24055,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24056,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6798,"numValue":9.0,"position":7,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1679 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,679 | train | mutant | 1,123 | 41 | 1,267 | 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 | L7A | L7A | 1 | 1 | 0 | 0 | 7 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 7 | A | H | false | false | 0 | 13.963125 | 7,575 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:L7A | null | null | null | 2.6 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26198,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26199,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26200,"numV... | [{"id":6798,"numValue":9.0,"position":7,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,681 | train | mutant | 1,123 | 41 | 1,267 | 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 | L7A | L7A | 1 | 1 | 0 | 0 | 7 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 7 | A | H | false | false | 0 | 13.963125 | 10,028 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:L7A | null | null | 7.5 | 3.7 | null | null | null | null | 2.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | 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":34449,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34450,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34451,"numValue":2.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34452,"numValue":null,"references":[],"st... | [{"id":6798,"numValue":9.0,"position":7,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1682 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,682 | train | mutant | 531 | 41 | 582 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11F | E11F | 1 | 1 | 0 | 0 | 11 | E | F | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 913 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:E11F | 70.78 | 4.3 | null | null | null | 3.5 | 138 | 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":3396,"numValue":70.78,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3397,"numValue":4.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3398,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1683 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,683 | train | mutant | 531 | 41 | 582 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11F | E11F | 1 | 1 | 0 | 0 | 11 | E | F | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 6,728 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:E11F | null | null | null | -1.7 | 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":23906,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23907,"numValue":-1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23908,"numValue":null,"reference... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,684 | train | mutant | 532 | 41 | 583 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11M | E11M | 1 | 1 | 0 | 0 | 11 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 914 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:E11M | 70.58 | 4.1 | 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|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":3401,"numValue":70.58,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3402,"numValue":4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3403,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1685 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,685 | train | mutant | 532 | 41 | 583 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11M | E11M | 1 | 1 | 0 | 0 | 11 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 6,729 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:E11M | null | null | null | -1.6 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":23909,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23910,"numValue":-1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23911,"numValue":null,"reference... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1686 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,686 | train | mutant | 533 | 41 | 584 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11A | E11A | 1 | 1 | 0 | 0 | 11 | E | A | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 915 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:E11A | 69.08 | 2.6 | null | null | null | 3.5 | 137 | 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":3406,"numValue":69.08,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3407,"numValue":2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3408,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1687 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,687 | train | mutant | 533 | 41 | 584 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11A | E11A | 1 | 1 | 0 | 0 | 11 | E | A | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 6,730 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:E11A | null | null | null | -1.1 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|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":23912,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23913,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23914,"num... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,689 | train | mutant | 541 | 41 | 592 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11H | E11H | 1 | 1 | 0 | 0 | 11 | E | H | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 6,830 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 65.1 | NaCl | 100 mM | 2LZM_A:E11H | null | null | null | -0.1 | 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":65.1,"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":24189,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24190,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24191,"numValue":null,"reference... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,690 | train | mutant | 542 | 41 | 593 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11N | E11N | 1 | 1 | 0 | 0 | 11 | E | N | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 925 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:E11N | 64.5 | -0.6 | null | null | null | 3.5 | 119 | 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":3456,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3457,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3458,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,691 | train | mutant | 542 | 41 | 593 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E11N | E11N | 1 | 1 | 0 | 0 | 11 | E | N | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 11 | A | H | true | true | 38.175398 | 18.361667 | 6,831 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 65.1 | NaCl | 100 mM | 2LZM_A:E11N | null | null | null | 0.1 | 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":65.1,"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":24192,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24193,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24194,"numValue":null,"references... | [{"id":18,"numValue":null,"position":11,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6802,"numValue":9.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1692 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,692 | train | mutant | 6,766 | 41 | 7,408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K60H|L13D | K60H|L13D | 2 | 2 | 0 | 0 | 60 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 13|60 | A | L|H | false | false | 74.58361 | 32.977569 | 14,539 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:L13D 2LZM_A:K60H | 32.4 | -6.1 | null | null | null | null | 71 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53746,"numValue":32.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53747,"numValue":-6.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53748,"numValue":71.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53749,"numValue":null,"references":... | [{"id":6804,"numValue":3.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1693 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,693 | train | mutant | 6,766 | 41 | 7,408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K60H|L13D | K60H|L13D | 2 | 2 | 0 | 0 | 60 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 13|60 | A | L|H | false | false | 74.58361 | 32.977569 | 14,540 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:L13D 2LZM_A:K60H | 58.3 | -7.1 | null | null | null | null | 101 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53750,"numValue":58.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53751,"numValue":-7.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53752,"numValue":101.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53753,"numValue":null,"references"... | [{"id":6804,"numValue":3.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1694 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,694 | train | mutant | 6,766 | 41 | 7,408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K60H|L13D | K60H|L13D | 2 | 2 | 0 | 0 | 60 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 13|60 | A | L|H | false | false | 74.58361 | 32.977569 | 14,541 | ProTherm | 6.5 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:L13D 2LZM_A:K60H | 55.9 | -7.1 | null | null | null | null | 82 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53754,"numValue":55.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53755,"numValue":-7.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53756,"numValue":82.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53757,"numValue":null,"references":... | [{"id":6804,"numValue":3.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,695 | train | mutant | 6,766 | 41 | 7,408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K60H|L13D | K60H|L13D | 2 | 2 | 0 | 0 | 60 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 13|60 | A | L|H | false | false | 74.58361 | 32.977569 | 14,894 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | 66.7 | KCl | 0.15 M | 2LZM_A:L13D 2LZM_A:K60H | null | null | null | 2.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":66.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":54923,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54924,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6804,"numValue":3.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,696 | train | mutant | 6,766 | 41 | 7,408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K60H|L13D | K60H|L13D | 2 | 2 | 0 | 0 | 60 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 13|60 | A | L|H | false | false | 74.58361 | 32.977569 | 14,929 | ProTherm | 6.5 | CD | Thermal | HCl | 10 mM | 64.6 | KCl | 0.15 M | 2LZM_A:L13D 2LZM_A:K60H | null | null | null | 2.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":55013,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55014,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6804,"numValue":3.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1697 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,697 | train | mutant | 6,766 | 41 | 7,408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K60H|L13D | K60H|L13D | 2 | 2 | 0 | 0 | 60 | K | H | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 13|60 | A | L|H | false | false | 74.58361 | 32.977569 | 15,109 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 40.4 | KCl | 0.15 M | 2LZM_A:L13D 2LZM_A:K60H | null | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | ION|PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue... | [{"datasets":[],"id":55440,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55441,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6804,"numValue":3.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,698 | train | mutant | 95 | 41 | 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 | R14K | R14K | 1 | 1 | 0 | 0 | 14 | R | K | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 14 | A | E | true | true | 126.371833 | 37.752273 | 189 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:R14K | 65.07 | -0.08 | null | null | null | 3.5 | 135 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":772,"numValue":65.07,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":773,"numValue":-0.08,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":774,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":6805,"numValue":6.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,699 | train | mutant | 95 | 41 | 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 | R14K | R14K | 1 | 1 | 0 | 0 | 14 | R | K | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 14 | A | E | true | true | 126.371833 | 37.752273 | 201 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:R14K | 61.66 | -0.53 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|HotMuSiC_S1626.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":[],"id":832,"numValue":61.66,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":833,"numValue":-0.53,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":834,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"}... | [{"id":6805,"numValue":6.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,700 | train | mutant | 95 | 41 | 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 | R14K | R14K | 1 | 1 | 0 | 0 | 14 | R | K | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 14 | A | E | true | true | 126.371833 | 37.752273 | 6,818 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:R14K | null | null | null | 0.03 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.15,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":24153,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24154,"numValue":0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24155,"numValue":null,"reference... | [{"id":6805,"numValue":6.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,701 | train | mutant | 7,377 | 41 | 8,047 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | R14A|K16A|I17A|K19A|T21A|E22A | R14A|K16A|I17A|K19A|T21A|E22A | 6 | 6 | 0 | 0 | 14 | R | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 14|16|17|19|21|22 | A | E|T | true | true | 94.440597 | 34.170276 | 15,766 | ProTherm | 3.02 | CD | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:R14A 2LZM_A:K16A 2LZM_A:I17A 2LZM_A:K19A 2LZM_A:T21A 2LZM_A:E22A | 44 | -7.6 | null | null | null | 2.5 | 60 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:R14A 2LZM_A:K1... | [{"datasets":[],"id":57884,"numValue":44.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57885,"numValue":-7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57886,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57887,"numValue":60.0,"references":[]... | [{"id":6805,"numValue":6.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6808,"numValue":5.0,"position":17,"positionArray":null,"positionRange":... | |||||||||||||
fireprotdb:1702 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,702 | train | mutant | 7,377 | 41 | 8,047 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | R14A|K16A|I17A|K19A|T21A|E22A | R14A|K16A|I17A|K19A|T21A|E22A | 6 | 6 | 0 | 0 | 14 | R | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 14|16|17|19|21|22 | A | E|T | true | true | 94.440597 | 34.170276 | 16,787 | ProTherm | 3.02 | CD | Thermal | glycine-HCl | 20 mM | 51.6 | 2LZM_A:R14A 2LZM_A:K16A 2LZM_A:I17A 2LZM_A:K19A 2LZM_A:T21A 2LZM_A:E22A | null | null | null | 3 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":51.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFE... | [{"datasets":[],"id":61696,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61697,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61698,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6805,"numValue":6.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6808,"numValue":5.0,"position":17,"positionArray":null,"positionRange":... | |||||||||||||
fireprotdb:1704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,704 | train | mutant | 55 | 41 | 61 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E | K16E | 1 | 1 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16 | A | E | false | false | 107.320435 | 43.815 | 74 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E | 67.8 | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | potapov_with_uniprot_mapping.csv|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":["potapov_with_uniprot_mapping.csv"],"id":251,"numValue":67.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","potapov_with_uniprot_mapping.csv","Saraboji_S1791.csv"],"id":252,"numValue":1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["potapov_with_uniprot_mapp... | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,705 | train | mutant | 55 | 41 | 61 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E | K16E | 1 | 1 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16 | A | E | false | false | 107.320435 | 43.815 | 6,710 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:K16E | null | null | null | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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","potapov_with_uniprot_mapping.csv"],"id":23863,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":23864,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1706 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,706 | train | mutant | 55 | 41 | 61 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E | K16E | 1 | 1 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16 | A | E | false | false | 107.320435 | 43.815 | 7,614 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K16E | null | null | null | 0.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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","potapov_with_uniprot_mapping.csv"],"id":26293,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":26294,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,707 | train | mutant | 6,700 | 41 | 7,342 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R119E | K16E|R119E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|119 | A | E|H | false | false | 113.015913 | 45.003864 | 14,441 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R119E | 49.1 | -1.8 | 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":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":53391,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53392,"numValue":-1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53393,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1708 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,708 | train | mutant | 6,700 | 41 | 7,342 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R119E | K16E|R119E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|119 | A | E|H | false | false | 113.015913 | 45.003864 | 14,449 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R119E | 67.6 | 0.9 | 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":53415,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53416,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53417,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1709 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,709 | train | mutant | 6,700 | 41 | 7,342 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R119E | K16E|R119E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|119 | A | E|H | false | false | 113.015913 | 45.003864 | 14,886 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R119E | null | null | null | -0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":54907,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54908,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1710 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,710 | train | mutant | 6,700 | 41 | 7,342 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R119E | K16E|R119E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|119 | A | E|H | false | false | 113.015913 | 45.003864 | 15,033 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R119E | null | null | null | 0.6 | 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":55255,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55256,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1711 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,711 | train | mutant | 6,701 | 41 | 7,343 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|K135E | K16E|K135E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|135 | A | E|S | true | false | 127.009872 | 37.196111 | 14,442 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:K135E | 48.3 | -2.6 | 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":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":53394,"numValue":48.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53395,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53396,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1712 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,712 | train | mutant | 6,701 | 41 | 7,343 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|K135E | K16E|K135E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|135 | A | E|S | true | false | 127.009872 | 37.196111 | 14,450 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:K135E | 65.1 | -1.6 | 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":53418,"numValue":65.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53419,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53420,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1714 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,714 | train | mutant | 6,701 | 41 | 7,343 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|K135E | K16E|K135E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|135 | A | E|S | true | false | 127.009872 | 37.196111 | 15,034 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:K135E | null | null | null | 0.9 | 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":55257,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55258,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,715 | train | mutant | 6,702 | 41 | 7,344 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R154E | K16E|R154E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|154 | A | E|H | true | false | 101.426041 | 41.479091 | 14,443 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R154E | 51.1 | 0.2 | 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":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":53397,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53398,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53399,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6945,"numValue":5.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1716 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,716 | train | mutant | 6,702 | 41 | 7,344 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R154E | K16E|R154E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|154 | A | E|H | true | false | 101.426041 | 41.479091 | 14,451 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R154E | 64.8 | -1.9 | 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":53421,"numValue":64.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53422,"numValue":-1.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53423,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6945,"numValue":5.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1717 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,717 | train | mutant | 6,702 | 41 | 7,344 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R154E | K16E|R154E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|154 | A | E|H | true | false | 101.426041 | 41.479091 | 14,888 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R154E | null | null | null | 0.8 | 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":54911,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54912,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6945,"numValue":5.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1718 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,718 | train | mutant | 6,702 | 41 | 7,344 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R154E | K16E|R154E | 2 | 2 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|154 | A | E|H | true | false | 101.426041 | 41.479091 | 15,035 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R154E | null | null | null | -0.1 | 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":55259,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55260,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6945,"numValue":5.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1719 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,719 | train | mutant | 6,705 | 41 | 7,347 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|K135E|K147E | K16E|K135E|K147E | 3 | 3 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|135|147 | A | E|S|H | true | false | 115.206934 | 35.158148 | 14,446 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:K135E 2LZM_A:K147E | 48.4 | -2.5 | 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":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":53406,"numValue":48.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53407,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53408,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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... | |||||||||||
fireprotdb:1720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,720 | train | mutant | 6,705 | 41 | 7,347 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|K135E|K147E | K16E|K135E|K147E | 3 | 3 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|135|147 | A | E|S|H | true | false | 115.206934 | 35.158148 | 14,454 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:K135E 2LZM_A:K147E | 62.7 | -4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | ION|PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|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":null,"strValue":"KCl","type":"ION"},{"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_CO... | [{"datasets":[],"id":53430,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53431,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53432,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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... | |||||||||||
fireprotdb:1721 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,721 | train | mutant | 6,705 | 41 | 7,347 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|K135E|K147E | K16E|K135E|K147E | 3 | 3 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|135|147 | A | E|S|H | true | false | 115.206934 | 35.158148 | 14,891 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:K135E 2LZM_A:K147E | null | null | null | 1.7 | 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":54917,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54918,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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... | |||||||||||
fireprotdb:1722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,722 | train | mutant | 6,705 | 41 | 7,347 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|K135E|K147E | K16E|K135E|K147E | 3 | 3 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|135|147 | A | E|S|H | true | false | 115.206934 | 35.158148 | 15,038 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:K135E 2LZM_A:K147E | null | null | null | 0.8 | 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":55265,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55266,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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... | |||||||||||
fireprotdb:1723 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,723 | train | mutant | 6,707 | 41 | 7,349 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R119E|K135E|K147E | K16E|R119E|K135E|K147E | 4 | 4 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|119|135|147 | A | E|H|S | true | false | 116.083048 | 37.916793 | 14,448 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R119E 2LZM_A:K135E 2LZM_A:K147E | 48.3 | -2.6 | 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":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":53412,"numValue":48.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53413,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53414,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:1724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,724 | train | mutant | 6,707 | 41 | 7,349 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R119E|K135E|K147E | K16E|R119E|K135E|K147E | 4 | 4 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|119|135|147 | A | E|H|S | true | false | 116.083048 | 37.916793 | 14,456 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R119E 2LZM_A:K135E 2LZM_A:K147E | 64.2 | -2.5 | 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":53436,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53437,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53438,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:1725 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,725 | train | mutant | 6,707 | 41 | 7,349 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R119E|K135E|K147E | K16E|R119E|K135E|K147E | 4 | 4 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|119|135|147 | A | E|H|S | true | false | 116.083048 | 37.916793 | 14,893 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R119E 2LZM_A:K135E 2LZM_A:K147E | null | null | null | 1 | 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":54921,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54922,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:1726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,726 | train | mutant | 6,707 | 41 | 7,349 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K16E|R119E|K135E|K147E | K16E|R119E|K135E|K147E | 4 | 4 | 0 | 0 | 16 | K | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 16|119|135|147 | A | E|H|S | true | false | 116.083048 | 37.916793 | 15,040 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:K16E 2LZM_A:R119E 2LZM_A:K135E 2LZM_A:K147E | null | null | null | 0.9 | 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":55269,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55270,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6807,"numValue":4.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:1727 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,727 | train | mutant | 1,124 | 41 | 1,268 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I17A | I17A | 1 | 1 | 0 | 0 | 17 | I | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 17 | A | E | true | false | 21.209591 | 23.52875 | 2,018 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I17A | 58.9 | -6.4 | null | null | null | null | 93 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7532,"numValue":58.9,"references":[],"strValue":null,"type":"TM"}... | [{"id":6808,"numValue":5.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1728 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,728 | train | mutant | 1,124 | 41 | 1,268 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I17A | I17A | 1 | 1 | 0 | 0 | 17 | I | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 17 | A | E | true | false | 21.209591 | 23.52875 | 3,124 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I17A | 43.3 | -8.4 | null | null | null | 1.8 | 87 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11372,"numValue":43.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11373,"numValue":-8.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11374,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6808,"numValue":5.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,729 | train | mutant | 1,124 | 41 | 1,268 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I17A | I17A | 1 | 1 | 0 | 0 | 17 | I | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 17 | A | E | true | false | 21.209591 | 23.52875 | 6,785 | 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:I17A | null | null | null | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24057,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24058,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24059,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6808,"numValue":5.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1730 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,730 | train | mutant | 1,124 | 41 | 1,268 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I17A | I17A | 1 | 1 | 0 | 0 | 17 | I | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 17 | A | E | true | false | 21.209591 | 23.52875 | 7,558 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:I17A | null | null | null | 2.7 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26147,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26148,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26149,"numV... | [{"id":6808,"numValue":5.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,731 | train | mutant | 1,137 | 41 | 1,281 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I17M | I17M | 1 | 1 | 0 | 0 | 17 | I | M | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 17 | A | E | true | false | 21.209591 | 23.52875 | 2,037 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I17M | 59.4 | -5.9 | null | null | null | null | 102 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7627,"numValue":59.4,"references":[],"strValue":null,"type... | [{"id":6808,"numValue":5.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1732 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,732 | train | mutant | 1,137 | 41 | 1,281 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I17M | I17M | 1 | 1 | 0 | 0 | 17 | I | M | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 17 | A | E | true | false | 21.209591 | 23.52875 | 6,804 | 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:I17M | null | null | null | 2.2 | 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":24114,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24115,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24116,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6808,"numValue":5.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,734 | train | mutant | 6,763 | 41 | 7,405 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T26Q|Y18D | T26Q|Y18D | 2 | 2 | 0 | 0 | 26 | T | Q | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 18|26 | A | E | true | true | 18.526058 | 21.42747 | 14,535 | ProTherm | 5.31 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:Y18D 2LZM_A:T26Q | 61.3 | -4 | 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 | 67 | ARTICLE | Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft. | 1,991 | 10.1021/bi00219a037 | 1991123 | Biochemistry;30;1425-32 | 4 | Nicholson H|Matthews B W|Poteete A R|Sun D P | [{"numValue":5.31,"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":53734,"numValue":61.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53735,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53736,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6809,"numValue":9.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6817,"numValue":9.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1735 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,735 | train | mutant | 543 | 41 | 594 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D20N | D20N | 1 | 1 | 0 | 0 | 20 | D | N | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 20 | A | L | true | true | 46.749846 | 25.468125 | 926 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:D20N | 68.2 | 3.1 | null | null | null | 3.5 | 139 | 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":3461,"numValue":68.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3462,"numValue":3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3463,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":19,"numValue":null,"position":20,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6811,"numValue":9.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,736 | train | mutant | 543 | 41 | 594 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D20N | D20N | 1 | 1 | 0 | 0 | 20 | D | N | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 20 | A | L | true | true | 46.749846 | 25.468125 | 6,832 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 65.1 | NaCl | 100 mM | 2LZM_A:D20N | 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":65.1,"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":24195,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24196,"numValue":-1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24197,"numValue":null,"reference... | [{"id":19,"numValue":null,"position":20,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6811,"numValue":9.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1737 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,737 | train | mutant | 544 | 41 | 595 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D20T | D20T | 1 | 1 | 0 | 0 | 20 | D | T | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 20 | A | L | true | true | 46.749846 | 25.468125 | 927 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:D20T | 67.3 | 2.2 | null | null | null | 3.5 | 135 | 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":3466,"numValue":67.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3467,"numValue":2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3468,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":19,"numValue":null,"position":20,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6811,"numValue":9.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1738 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,738 | train | mutant | 544 | 41 | 595 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D20T | D20T | 1 | 1 | 0 | 0 | 20 | D | T | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 20 | A | L | true | true | 46.749846 | 25.468125 | 6,833 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 65.1 | NaCl | 100 mM | 2LZM_A:D20T | null | null | null | -0.9 | 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":65.1,"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":24198,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24199,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24200,"numValue":null,"reference... | [{"id":19,"numValue":null,"position":20,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6811,"numValue":9.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1739 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,739 | train | mutant | 545 | 41 | 596 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D20S | D20S | 1 | 1 | 0 | 0 | 20 | D | S | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 20 | A | L | true | true | 46.749846 | 25.468125 | 928 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:D20S | 66.7 | 1.6 | null | null | null | 3.5 | 129 | 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":3471,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3472,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3473,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":19,"numValue":null,"position":20,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6811,"numValue":9.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1740 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,740 | train | mutant | 545 | 41 | 596 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D20S | D20S | 1 | 1 | 0 | 0 | 20 | D | S | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 20 | A | L | true | true | 46.749846 | 25.468125 | 6,834 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 65.1 | NaCl | 100 mM | 2LZM_A:D20S | null | null | null | -0.7 | 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":65.1,"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":24201,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24202,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24203,"numValue":null,"reference... | [{"id":19,"numValue":null,"position":20,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6811,"numValue":9.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1741 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,741 | train | mutant | 546 | 41 | 597 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D20A | D20A | 1 | 1 | 0 | 0 | 20 | D | A | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 20 | A | L | true | true | 46.749846 | 25.468125 | 929 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:D20A | 64.3 | -0.8 | null | null | null | 3.5 | 127 | 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":3476,"numValue":64.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3477,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3478,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":19,"numValue":null,"position":20,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6811,"numValue":9.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1742 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,742 | train | mutant | 546 | 41 | 597 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D20A | D20A | 1 | 1 | 0 | 0 | 20 | D | A | 9 | ACTIVE_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 20 | A | L | true | true | 46.749846 | 25.468125 | 6,835 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 65.1 | NaCl | 100 mM | 2LZM_A:D20A | null | null | null | 0.3 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|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":65.1,"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":24204,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24205,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24206,"numV... | [{"id":19,"numValue":null,"position":20,"positionArray":null,"positionRange":null,"strValue":"Proton donor/acceptor","type":"ACTIVE_SITE"},{"id":6811,"numValue":9.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1743 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,743 | train | mutant | 96 | 41 | 106 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E22K | E22K | 1 | 1 | 0 | 0 | 22 | E | K | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 22 | A | T | true | true | 81.033875 | 34.892778 | 190 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:E22K | 66.52 | 1.37 | null | null | null | 3.5 | 141 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":777,"numValue":66.52,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":778,"numValue":1.37,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":779,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":7... | [{"id":6813,"numValue":6.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1744 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,744 | train | mutant | 96 | 41 | 106 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E22K | E22K | 1 | 1 | 0 | 0 | 22 | E | K | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 22 | A | T | true | true | 81.033875 | 34.892778 | 202 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:E22K | 63.77 | 1.58 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":["HotMuSiC_S1626.csv"],"id":836,"numValue":63.77,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":837,"numValue":1.58,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":838,"numValue":3.5,"references":[],"strValue"... | [{"id":6813,"numValue":6.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1745 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,745 | train | mutant | 96 | 41 | 106 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E22K | E22K | 1 | 1 | 0 | 0 | 22 | E | K | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 22 | A | T | true | true | 81.033875 | 34.892778 | 6,819 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:E22K | null | null | null | -0.57 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.15,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":24156,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24157,"numValue":-0.57,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24158,"numValue":null,"referenc... | [{"id":6813,"numValue":6.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1747 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,747 | train | mutant | 7,378 | 41 | 8,048 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Y24A|Y25A|T26A|I27A | Y24A|Y25A|T26A|I27A | 4 | 4 | 0 | 0 | 24 | Y | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 24|25|26|27 | A | L|E | true | true | 25.173688 | 24.361704 | 16,788 | ProTherm | 3.05 | CD | Thermal | glycine-HCl | 20 mM | 51.6 | 2LZM_A:Y24A 2LZM_A:Y25A 2LZM_A:T26A 2LZM_A:I27A | null | null | null | 5.5 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":51.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFE... | [{"datasets":[],"id":61699,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61700,"numValue":5.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61701,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6815,"numValue":5.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6816,"numValue":3.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6817,"numValue":9.0,"position":26,"positionArray":null,"positionRange":... | |||||||||||||
fireprotdb:1748 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,748 | train | mutant | 5,830 | 41 | 6,395 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Y25G | Y25G | 1 | 1 | 0 | 0 | 25 | Y | G | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 25 | A | E | true | false | 27.930277 | 25.1725 | 12,603 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:Y25G | null | null | null | 4.55 | null | null | null | 4 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":45712,"numValue":4.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45713,"numValue":4.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45714,"numValue":null,"references":[],"strValue":"... | [{"id":6816,"numValue":3.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1749 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,749 | train | mutant | 97 | 41 | 107 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T26S | T26S | 1 | 1 | 0 | 0 | 26 | T | S | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 26 | A | E | true | true | 4.734318 | 19.147857 | 191 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:T26S | 66.5 | 1.35 | null | null | null | 3.5 | 143 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":782,"numValue":66.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":783,"numValue":1.35,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":784,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":78... | [{"id":6817,"numValue":9.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1750 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,750 | train | mutant | 97 | 41 | 107 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T26S | T26S | 1 | 1 | 0 | 0 | 26 | T | S | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 26 | A | E | true | true | 4.734318 | 19.147857 | 203 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:T26S | 63.54 | 1.35 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":[],"id":840,"numValue":63.54,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":841,"numValue":1.35,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":842,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{... | [{"id":6817,"numValue":9.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1751 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,751 | train | mutant | 97 | 41 | 107 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T26S | T26S | 1 | 1 | 0 | 0 | 26 | T | S | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 26 | A | E | true | true | 4.734318 | 19.147857 | 1,227 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:T26S | 66.45 | 1.35 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 125 | ARTICLE | Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent. | 1,993 | 10.1002/pro.5560021222 | 8298466 | Protein Sci;2;2226-32 | 2 | Matthews B W|Pjura P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":4525,"numValue":66.45,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4526,"numValue":1.35,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4527,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6817,"numValue":9.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1752 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,752 | train | mutant | 97 | 41 | 107 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T26S | T26S | 1 | 1 | 0 | 0 | 26 | T | S | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 26 | A | E | true | true | 4.734318 | 19.147857 | 6,820 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:T26S | null | null | null | -0.57 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.15,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":24159,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24160,"numValue":-0.57,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24161,"nu... | [{"id":6817,"numValue":9.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1753 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,753 | train | mutant | 358 | 41 | 397 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T26Q | T26Q | 1 | 1 | 0 | 0 | 26 | T | Q | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 26 | A | E | true | true | 4.734318 | 19.147857 | 619 | ProTherm | 5.31 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T26Q | 64.4 | -0.9 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 67 | ARTICLE | Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft. | 1,991 | 10.1021/bi00219a037 | 1991123 | Biochemistry;30;1425-32 | 4 | Nicholson H|Matthews B W|Poteete A R|Sun D P | [{"numValue":5.31,"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":2463,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2464,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2465,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6817,"numValue":9.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1754 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,754 | train | mutant | 1,138 | 41 | 1,282 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I27M | I27M | 1 | 1 | 0 | 0 | 27 | I | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 27 | A | E | false | false | 0 | 22.723125 | 2,038 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I27M | 55.2 | -10.1 | null | null | null | null | 62 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv|PoPMuSiC-2.0_S2648.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7632,"numValue":55.2,"references":[],"strValue":null,"type":"... | [{"id":6818,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1755 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,755 | train | mutant | 1,138 | 41 | 1,282 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I27M | I27M | 1 | 1 | 0 | 0 | 27 | I | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 27 | A | E | false | false | 0 | 22.723125 | 6,805 | 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:I27M | null | null | null | 3.1 | 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":24117,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24118,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24119,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6818,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1756 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,756 | train | mutant | 1,674 | 41 | 1,883 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I27A | I27A | 1 | 1 | 0 | 0 | 27 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 27 | A | E | false | false | 0 | 22.723125 | 3,125 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I27A | 41.6 | -10.1 | null | null | null | 1.8 | 76 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11377,"numValue":41.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11378,"numValue":-10.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11379,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":6818,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1757 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,757 | train | mutant | 1,674 | 41 | 1,883 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I27A | I27A | 1 | 1 | 0 | 0 | 27 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 27 | A | E | false | false | 0 | 22.723125 | 7,559 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:I27A | null | null | null | 3.1 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26150,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":26151,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":... | [{"id":6818,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1758 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,758 | train | mutant | 1,674 | 41 | 1,883 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I27A | I27A | 1 | 1 | 0 | 0 | 27 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 27 | A | E | false | false | 0 | 22.723125 | 10,020 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:I27A | null | null | 11 | 3.9 | null | null | null | null | 2.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | 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":34417,"numValue":11.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34418,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34419,"numValue":2.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34420,"numValue":null,"references":[],"s... | [{"id":6818,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1759 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,759 | train | mutant | 1,674 | 41 | 1,883 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I27A | I27A | 1 | 1 | 0 | 0 | 27 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 27 | A | E | false | false | 0 | 22.723125 | 10,029 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:I27A | null | null | 8.8 | 2.4 | null | null | null | null | 2.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | 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":34453,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34454,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34455,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34456,"numValue":null,"references":[],"st... | [{"id":6818,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1760 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,760 | train | mutant | 6,828 | 41 | 7,470 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I27M|L33M | I27M|L33M | 2 | 2 | 0 | 0 | 27 | I | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 27|33 | A | E | false | true | 8.504509 | 20.8025 | 14,651 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I27M 1L63_A:L33M | 55 | -10.3 | null | null | null | null | 61 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":[],"id":54180,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54181,"numValue":-10.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54182,"numValue":61.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54183,"numValue":2.0,"references":... | [{"id":6818,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1761 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,761 | train | mutant | 6,828 | 41 | 7,470 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I27M|L33M | I27M|L33M | 2 | 2 | 0 | 0 | 27 | I | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 27|33 | A | E | false | true | 8.504509 | 20.8025 | 14,912 | 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:I27M 1L63_A:L33M | null | null | null | 3.1 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":[],"id":54972,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54973,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":54974,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6818,"numValue":8.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1763 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,763 | train | mutant | 870 | 41 | 985 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | G28A | G28A | 1 | 1 | 0 | 0 | 28 | G | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 28 | A | E | false | false | 0.483708 | 17.005 | 7,583 | ProTherm | 3.02 | CD | Thermal | glycine-HCl | 20 mM | 51.6 | 2LZM_A:G28A | null | null | null | 2 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":51.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFE... | [{"datasets":[],"id":26222,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26223,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26224,"numValue":null,"references":[],"strValue":"Unknown",... | [{"id":6819,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1764 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,764 | train | mutant | 7,379 | 41 | 8,049 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | G28A|I29A|G30A | G28A|I29A|G30A | 3 | 3 | 0 | 0 | 28 | G | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 28|29|30 | A | E|T | true | true | 7.878402 | 16.469792 | 15,768 | ProTherm | 3.05 | CD | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:G28A 2LZM_A:I29A 2LZM_A:G30A | 36 | -15.6 | null | null | null | 2.5 | 61 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:G28A 2LZM_A:I2... | [{"datasets":[],"id":57894,"numValue":36.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57895,"numValue":-15.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57896,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57897,"numValue":61.0,"references":[... | [{"id":6819,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6820,"numValue":7.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6821,"numValue":9.0,"position":30,"positionArray":null,"positionRange":... | |||||||||||||
fireprotdb:1765 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,765 | train | mutant | 7,379 | 41 | 8,049 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | G28A|I29A|G30A | G28A|I29A|G30A | 3 | 3 | 0 | 0 | 28 | G | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 28|29|30 | A | E|T | true | true | 7.878402 | 16.469792 | 16,789 | ProTherm | 3.05 | CD | Thermal | glycine-HCl | 20 mM | 51.6 | 2LZM_A:G28A 2LZM_A:I29A 2LZM_A:G30A | null | null | null | 5.5 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":51.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFE... | [{"datasets":[],"id":61702,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61703,"numValue":5.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61704,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6819,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6820,"numValue":7.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6821,"numValue":9.0,"position":30,"positionArray":null,"positionRange":... | |||||||||||||
fireprotdb:1766 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,766 | train | mutant | 1,675 | 41 | 1,884 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I29A | I29A | 1 | 1 | 0 | 0 | 29 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 29 | A | T | true | true | 5.636767 | 16.711875 | 3,126 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I29A | 43.5 | -8.2 | null | null | null | 1.8 | 85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11382,"numValue":43.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv","Saraboji... | [{"id":6820,"numValue":7.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1768 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,768 | train | mutant | 534 | 41 | 585 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | G30A | G30A | 1 | 1 | 0 | 0 | 30 | G | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 30 | A | T | true | true | 17.514731 | 15.6925 | 916 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:G30A | 66.58 | 0.1 | 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":3411,"numValue":66.58,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3412,"numValue":0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3413,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6821,"numValue":9.0,"position":30,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1769 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,769 | train | mutant | 534 | 41 | 585 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | G30A | G30A | 1 | 1 | 0 | 0 | 30 | G | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 30 | A | T | true | true | 17.514731 | 15.6925 | 6,731 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:G30A | null | null | null | -0.1 | 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":23915,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23916,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23917,"numValue":null,"reference... | [{"id":6821,"numValue":9.0,"position":30,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1770 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,770 | train | mutant | 535 | 41 | 586 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | G30F | G30F | 1 | 1 | 0 | 0 | 30 | G | F | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 30 | A | T | true | true | 17.514731 | 15.6925 | 917 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:G30F | 61.58 | -4.9 | null | null | null | 3.5 | 99 | 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":3416,"numValue":61.58,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3417,"numValue":-4.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3418,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6821,"numValue":9.0,"position":30,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1771 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,771 | train | mutant | 535 | 41 | 586 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | G30F | G30F | 1 | 1 | 0 | 0 | 30 | G | F | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 30 | A | T | true | true | 17.514731 | 15.6925 | 6,732 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:G30F | 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":23918,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23919,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23920,"numValue":null,"references... | [{"id":6821,"numValue":9.0,"position":30,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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