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:9700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,700 | train | mutant | 2,070 | 183 | 2,311 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | V74A | V74A | 1 | 1 | 0 | 0 | 74 | V | A | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,665 | ProTherm | 3 | CD | Thermal | Gly-HCl buffer | 10 mM | null | NaCl | 0.1 M | 2RN2_A:V74A | null | -7.6 | null | 2.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DTM|DDG|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 458 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. | 1,993 | 8390295 | Biochemistry;32;6171-8 | 4 | Kanaya S|Nakamura H|Ishikawa K|Morikawa K | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl buffer","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17250,"numValue":-7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":17251,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":17252,"numValue":null,"ref... | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,701 | train | mutant | 2,070 | 183 | 2,311 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | V74A | V74A | 1 | 1 | 0 | 0 | 74 | V | A | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,668 | ProTherm | 5.5 | CD | Thermal | sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:V74A | null | -12.7 | null | 3.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DTM|DDG|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|capriotti_S1615_map.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 458 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. | 1,993 | 8390295 | Biochemistry;32;6171-8 | 4 | Kanaya S|Nakamura H|Ishikawa K|Morikawa K | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17259,"numValue":-12.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["capriotti_S1615_map.csv"],"id":17260,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":17261,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9702 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,702 | train | mutant | 2,070 | 183 | 2,311 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | V74A | V74A | 1 | 1 | 0 | 0 | 74 | V | A | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 7,469 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52 | NaCl | 0.1 M | 2RN2_A:V74A | null | null | null | 3.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25934,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25935,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9703 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,703 | train | mutant | 2,070 | 183 | 2,311 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | V74A | V74A | 1 | 1 | 0 | 0 | 74 | V | A | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 7,737 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | NaCl | 0.1 M | 2RN2_A:V74A | null | null | null | 2.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26583,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26584,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,704 | train | mutant | 2,074 | 183 | 2,315 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q76L | Q76L | 1 | 1 | 0 | 0 | 76 | Q | L | 5 | CONSERVATION | 2RN2 | 76 | null | 76 | A | H | false | false | 58.272096 | 18.828889 | 4,086 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:Q76L | 53.8 | 1.1 | null | null | null | null | 81.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":15092,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15093,"numValue":1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15094,"numValue":81.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16585,"numValue":5.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,705 | train | mutant | 2,074 | 183 | 2,315 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q76L | Q76L | 1 | 1 | 0 | 0 | 76 | Q | L | 5 | CONSERVATION | 2RN2 | 76 | null | 76 | A | H | false | false | 58.272096 | 18.828889 | 4,099 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:Q76L | 50.9 | 0.8 | null | null | null | null | 110.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":15144,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15145,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15146,"numValue":110.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16585,"numValue":5.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9706 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,706 | train | mutant | 2,074 | 183 | 2,315 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q76L | Q76L | 1 | 1 | 0 | 0 | 76 | Q | L | 5 | CONSERVATION | 2RN2 | 76 | null | 76 | A | H | false | false | 58.272096 | 18.828889 | 7,660 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:Q76L | null | null | null | -0.24 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26385,"numValue":-0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26386,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16585,"numValue":5.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,707 | train | mutant | 2,065 | 183 | 2,305 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 77 | A | H | false | false | 0 | 17.545 | 4,054 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:G77A | 46.9 | -2.9 | 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|_PDB_CHAIN_MUTATION | 373 | ARTICLE | Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution. | 1,993 | 10.1021/bi00079a010 | 8393706 | Biochemistry;32;7136-42 | 5 | Kanaya S|Nakamura H|Kimura S|Ishikawa K|Morikawa K | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:G77A","type":"_... | [{"datasets":[],"id":14979,"numValue":46.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14980,"numValue":-2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14981,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16586,"numValue":8.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9708 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,708 | train | mutant | 2,065 | 183 | 2,305 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 77 | A | H | false | false | 0 | 17.545 | 7,731 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:G77A | null | null | null | 0.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 373 | ARTICLE | Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution. | 1,993 | 10.1021/bi00079a010 | 8393706 | Biochemistry;32;7136-42 | 5 | Kanaya S|Nakamura H|Kimura S|Ishikawa K|Morikawa K | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26571,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26572,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16586,"numValue":8.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9709 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,709 | train | mutant | 2,075 | 183 | 2,316 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q80L | Q80L | 1 | 1 | 0 | 0 | 80 | Q | L | 4 | CONSERVATION | 2RN2 | 76 | null | 80 | A | H | false | false | 106.540235 | 22.504444 | 4,087 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:Q80L | 53.5 | 0.8 | null | null | null | null | 94.6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":15096,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15097,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15098,"numValue":94.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16589,"numValue":4.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9710 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,710 | train | mutant | 2,075 | 183 | 2,316 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q80L | Q80L | 1 | 1 | 0 | 0 | 80 | Q | L | 4 | CONSERVATION | 2RN2 | 76 | null | 80 | A | H | false | false | 106.540235 | 22.504444 | 4,100 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:Q80L | 51.1 | 1 | null | null | null | null | 114.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":15148,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15149,"numValue":1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15150,"numValue":114.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16589,"numValue":4.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9712 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,712 | train | mutant | 6,932 | 183 | 7,574 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q80L|K117R | Q80L|K117R | 2 | 2 | 0 | 0 | 80 | Q | L | 4 | CONSERVATION | 2RN2 | 76 | null | 80|117 | A | H|E | true | false | 109.675415 | 23.177778 | 14,785 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:Q80L 2RN2_A:K117R | 53.5 | 0.8 | null | null | null | null | 83.1 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":54624,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54625,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54626,"numValue":83.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54627,"numValue":null,"references":[... | [{"id":16589,"numValue":4.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16626,"numValue":1.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9713 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,713 | train | mutant | 6,932 | 183 | 7,574 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q80L|K117R | Q80L|K117R | 2 | 2 | 0 | 0 | 80 | Q | L | 4 | CONSERVATION | 2RN2 | 76 | null | 80|117 | A | H|E | true | false | 109.675415 | 23.177778 | 14,789 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:Q80L 2RN2_A:K117R | 50 | -0.1 | null | null | null | null | 103.6 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":54640,"numValue":50.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54641,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54642,"numValue":103.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54643,"numValue":null,"references"... | [{"id":16589,"numValue":4.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16626,"numValue":1.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9714 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,714 | train | mutant | 6,932 | 183 | 7,574 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q80L|K117R | Q80L|K117R | 2 | 2 | 0 | 0 | 80 | Q | L | 4 | CONSERVATION | 2RN2 | 76 | null | 80|117 | A | H|E | true | false | 109.675415 | 23.177778 | 15,048 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:Q80L 2RN2_A:K117R | null | null | null | 0.03 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"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":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55285,"numValue":0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55286,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16589,"numValue":4.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16626,"numValue":1.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,715 | train | mutant | 2,045 | 183 | 2,284 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H83A | H83A | 1 | 1 | 0 | 0 | 83 | H | A | 1 | CONSERVATION | 2RN2 | 76 | null | 83 | A | H | true | false | 120.300698 | 30.325999 | 3,965 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:H83A | 51.5 | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H83A","type":"_... | [{"datasets":[],"id":14598,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14599,"numValue":2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14600,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16592,"numValue":1.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9716 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,716 | train | mutant | 2,045 | 183 | 2,284 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H83A | H83A | 1 | 1 | 0 | 0 | 83 | H | A | 1 | CONSERVATION | 2RN2 | 76 | null | 83 | A | H | true | false | 120.300698 | 30.325999 | 3,969 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:H83A | 52.8 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H83A","type"... | [{"datasets":[],"id":14610,"numValue":52.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14611,"numValue":0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14612,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16592,"numValue":1.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9717 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,717 | train | mutant | 2,045 | 183 | 2,284 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H83A | H83A | 1 | 1 | 0 | 0 | 83 | H | A | 1 | CONSERVATION | 2RN2 | 76 | null | 83 | A | H | true | false | 120.300698 | 30.325999 | 3,972 | ProTherm | 7.8 | CD | Thermal | Sodium phosphate | 20 mM | null | 2RN2_A:H83A | 50 | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H83A","typ... | [{"datasets":[],"id":14619,"numValue":50.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14620,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14621,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16592,"numValue":1.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9719 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,719 | train | mutant | 2,045 | 183 | 2,284 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H83A | H83A | 1 | 1 | 0 | 0 | 83 | H | A | 1 | CONSERVATION | 2RN2 | 76 | null | 83 | A | H | true | false | 120.300698 | 30.325999 | 11,065 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 25 | 2RN2_A:H83A | null | null | 9.43 | -0.22 | null | null | null | 1.83 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":38091,"numValue":9.43,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38092,"numValue":-0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38093,"numValue":1.83,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38094,"numValue":null,"references":[... | [{"id":16592,"numValue":1.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,720 | train | mutant | 2,045 | 183 | 2,284 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H83A | H83A | 1 | 1 | 0 | 0 | 83 | H | A | 1 | CONSERVATION | 2RN2 | 76 | null | 83 | A | H | true | false | 120.300698 | 30.325999 | 11,069 | ProTherm | 8.2 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 2RN2_A:H83A | null | null | 8.4 | 0.09 | null | null | null | 1.63 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":8.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":38107,"numValue":8.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38108,"numValue":0.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38109,"numValue":1.63,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38110,"numValue":null,"references":[],... | [{"id":16592,"numValue":1.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9721 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,721 | train | mutant | 1,948 | 183 | 2,177 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R | K91R | 1 | 1 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91 | A | B | false | false | 80.200501 | 17.638889 | 3,760 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K91R | 49.8 | 0.5 | null | null | null | null | 119.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K91R","type":"_... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":13884,"numValue":49.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":13885,"numValue":0.5,"references":[],"strValue":null,"ty... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,722 | train | mutant | 1,948 | 183 | 2,177 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R | K91R | 1 | 1 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91 | A | B | false | false | 80.200501 | 17.638889 | 3,761 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:K91R | 52 | 0.1 | null | null | null | null | 96.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K91R","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":13888,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":13889,"numValue":0.1,"references":[],"strValue":null,"ty... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,724 | train | mutant | 1,948 | 183 | 2,177 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R | K91R | 1 | 1 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91 | A | B | false | false | 80.200501 | 17.638889 | 7,717 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 49.8 | 2RN2_A:K91R | null | null | null | 0 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26543,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26544,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9725 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,725 | train | mutant | 6,715 | 183 | 7,357 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|D94E | K91R|D94E | 2 | 2 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|94 | A | B|T | false | false | 90.353525 | 21.150695 | 14,471 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K91R 2RN2_A:D94E | 47.8 | -2 | null | null | null | null | 93.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K91R 2RN2_A:D94... | [{"datasets":[],"id":53501,"numValue":47.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53502,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53503,"numValue":93.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53504,"numValue":null,"references":... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,726 | train | mutant | 6,715 | 183 | 7,357 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|D94E | K91R|D94E | 2 | 2 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|94 | A | B|T | false | false | 90.353525 | 21.150695 | 14,472 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K91R 2RN2_A:D94E | 50.2 | -1.8 | null | null | null | null | 87.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K91R 2RN2_A:D94... | [{"datasets":[],"id":53505,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53506,"numValue":-1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53507,"numValue":87.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53508,"numValue":null,"references":... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9727 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,727 | train | mutant | 6,715 | 183 | 7,357 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|D94E | K91R|D94E | 2 | 2 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|94 | A | B|T | false | false | 90.353525 | 21.150695 | 15,052 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:K91R 2RN2_A:D94E | 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|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55295,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55296,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,729 | train | mutant | 6,717 | 183 | 7,359 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|K95G | K91R|K95G | 2 | 2 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|95 | A | B|S | false | false | 108.286048 | 19.812778 | 14,475 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K91R 2RN2_A:K95G | 55 | 5.2 | null | null | null | null | 114.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K91R 2RN2_A:K95... | [{"datasets":[],"id":53517,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53518,"numValue":5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53519,"numValue":114.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53520,"numValue":null,"references":... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9730 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,730 | train | mutant | 6,717 | 183 | 7,359 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|K95G | K91R|K95G | 2 | 2 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|95 | A | B|S | false | false | 108.286048 | 19.812778 | 14,476 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K91R 2RN2_A:K95G | 57.8 | 5.8 | null | null | null | null | 92 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K91R 2RN2_A:K95... | [{"datasets":[],"id":53521,"numValue":57.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53522,"numValue":5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53523,"numValue":92.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53524,"numValue":null,"references":[... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,731 | train | mutant | 6,717 | 183 | 7,359 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|K95G | K91R|K95G | 2 | 2 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|95 | A | B|S | false | false | 108.286048 | 19.812778 | 15,056 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:K91R 2RN2_A:K95G | null | null | null | -1.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55303,"numValue":-1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55304,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9733 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,733 | train | mutant | 6,842 | 183 | 7,484 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|D94E|K95G | K91R|D94E|K95G | 3 | 3 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|94|95 | A | B|T|S | false | false | 105.692882 | 21.429352 | 14,669 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K91R 2RN2_A:D94E 2RN2_A:K95G | 53.8 | 4 | null | null | null | null | 104.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K91R 2RN2_A:D94... | [{"datasets":[],"id":54245,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54246,"numValue":4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54247,"numValue":104.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54248,"numValue":null,"references":... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,734 | train | mutant | 6,842 | 183 | 7,484 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|D94E|K95G | K91R|D94E|K95G | 3 | 3 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|94|95 | A | B|T|S | false | false | 105.692882 | 21.429352 | 14,670 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K91R 2RN2_A:D94E 2RN2_A:K95G | 57.6 | 5.6 | null | null | null | null | 86.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K91R 2RN2_A:D94... | [{"datasets":[],"id":54249,"numValue":57.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54250,"numValue":5.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54251,"numValue":86.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54252,"numValue":null,"references":[... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9735 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,735 | train | mutant | 6,842 | 183 | 7,484 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|D94E|K95G | K91R|D94E|K95G | 3 | 3 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|94|95 | A | B|T|S | false | false | 105.692882 | 21.429352 | 14,998 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | 52 | 2RN2_A:K91R 2RN2_A:D94E 2RN2_A:K95G | null | null | null | -1.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.0,"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":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55178,"numValue":-1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55179,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,736 | train | mutant | 6,842 | 183 | 7,484 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|D94E|K95G | K91R|D94E|K95G | 3 | 3 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|94|95 | A | B|T|S | false | false | 105.692882 | 21.429352 | 15,059 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:K91R 2RN2_A:D94E 2RN2_A:K95G | null | null | null | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55309,"numValue":-1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55310,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9737 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,737 | train | mutant | 6,842 | 183 | 7,484 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K91R|D94E|K95G | K91R|D94E|K95G | 3 | 3 | 0 | 0 | 91 | K | R | 5 | CONSERVATION | 2RN2 | 76 | null | 91|94|95 | A | B|T|S | false | false | 105.692882 | 21.429352 | 15,293 | ProTherm | 5.5 | CD | GdnHCl | glycine-HCl | 10 mM | 25 | 2RN2_A:K91R 2RN2_A:D94E 2RN2_A:K95G | null | null | 9.14 | 0.01 | null | null | null | 2.1 | 4.36 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_... | [{"datasets":[],"id":56101,"numValue":9.14,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56102,"numValue":0.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56103,"numValue":4.36,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56104,"numValue":2.1,"references":[],"... | [{"id":16600,"numValue":5.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9738 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,738 | train | mutant | 156 | 183 | 184 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D94E | D94E | 1 | 1 | 0 | 0 | 94 | D | E | 3 | CONSERVATION | 2RN2 | 76 | null | 94 | A | T | false | false | 100.50655 | 24.6625 | 290 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:D94E | 52 | -1.6 | null | null | null | null | 92.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D94E","type"... | [{"datasets":[],"id":1182,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1183,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1184,"numValue":92.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9739 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,739 | train | mutant | 156 | 183 | 184 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D94E | D94E | 1 | 1 | 0 | 0 | 94 | D | E | 3 | CONSERVATION | 2RN2 | 76 | null | 94 | A | T | false | false | 100.50655 | 24.6625 | 3,762 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D94E | 49.8 | -1.2 | null | null | null | null | 95.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D94E","type":"_... | [{"datasets":[],"id":13892,"numValue":49.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":13893,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13894,"numValue":95.9,"references":[],"str... | [{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9741 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,741 | train | mutant | 156 | 183 | 184 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D94E | D94E | 1 | 1 | 0 | 0 | 94 | D | E | 3 | CONSERVATION | 2RN2 | 76 | null | 94 | A | T | false | false | 100.50655 | 24.6625 | 7,719 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 49.8 | 2RN2_A:D94E | null | null | null | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26547,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26548,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9742 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,742 | train | mutant | 6,716 | 183 | 7,358 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D94R|K95G | D94R|K95G | 2 | 2 | 0 | 0 | 94 | D | R | 3 | CONSERVATION | 2RN2 | 76 | null | 94|95 | A | T|S | false | false | 118.439072 | 23.324583 | 14,473 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D94R 2RN2_A:K95G | 53.4 | 3.6 | null | null | null | null | 126.7 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D94R 2RN2_A:K95... | [{"datasets":[],"id":53509,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53510,"numValue":3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53511,"numValue":126.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53512,"numValue":null,"references":... | [{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9743 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,743 | train | mutant | 6,716 | 183 | 7,358 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D94R|K95G | D94R|K95G | 2 | 2 | 0 | 0 | 94 | D | R | 3 | CONSERVATION | 2RN2 | 76 | null | 94|95 | A | T|S | false | false | 118.439072 | 23.324583 | 14,474 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D94R 2RN2_A:K95G | 57.5 | 5.5 | null | null | null | null | 102.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D94R 2RN2_A:K95... | [{"datasets":[],"id":53513,"numValue":57.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53514,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53515,"numValue":102.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53516,"numValue":null,"references":... | [{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9744 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,744 | train | mutant | 6,716 | 183 | 7,358 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D94R|K95G | D94R|K95G | 2 | 2 | 0 | 0 | 94 | D | R | 3 | CONSERVATION | 2RN2 | 76 | null | 94|95 | A | T|S | false | false | 118.439072 | 23.324583 | 15,054 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:D94R 2RN2_A:K95G | null | null | null | -1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55299,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55300,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9745 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,745 | train | mutant | 6,716 | 183 | 7,358 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D94R|K95G | D94R|K95G | 2 | 2 | 0 | 0 | 94 | D | R | 3 | CONSERVATION | 2RN2 | 76 | null | 94|95 | A | T|S | false | false | 118.439072 | 23.324583 | 15,055 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:D94R 2RN2_A:K95G | null | null | null | -1.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55301,"numValue":-1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55302,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16603,"numValue":3.0,"position":94,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:9746 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,746 | train | mutant | 157 | 183 | 185 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95G | K95G | 1 | 1 | 0 | 0 | 95 | K | G | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 291 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K95G | 49.8 | 5.7 | null | null | null | null | 102.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K95G","type":"_... | [{"datasets":[],"id":1186,"numValue":49.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1187,"numValue":5.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1188,"numValue":102.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9747 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,747 | train | mutant | 157 | 183 | 185 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95G | K95G | 1 | 1 | 0 | 0 | 95 | K | G | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 292 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:K95G | 52 | 6.8 | null | null | null | null | 90.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K95G","type"... | [{"datasets":[],"id":1190,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1191,"numValue":6.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1192,"numValue":90.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9749 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,749 | train | mutant | 157 | 183 | 185 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95G | K95G | 1 | 1 | 0 | 0 | 95 | K | G | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 7,721 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 49.8 | 2RN2_A:K95G | null | null | null | -1.9 | 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|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26551,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26552,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9751 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,751 | train | mutant | 158 | 183 | 186 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95A | K95A | 1 | 1 | 0 | 0 | 95 | K | A | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 294 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:K95A | 52 | 0.4 | null | null | null | null | 96.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K95A","type"... | [{"datasets":[],"id":1198,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1199,"numValue":0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1200,"numValue":96.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9752 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,752 | train | mutant | 158 | 183 | 186 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95A | K95A | 1 | 1 | 0 | 0 | 95 | K | A | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 7,722 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:K95A | null | null | null | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26553,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26554,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9753 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,753 | train | mutant | 158 | 183 | 186 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95A | K95A | 1 | 1 | 0 | 0 | 95 | K | A | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 7,723 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 49.8 | 2RN2_A:K95A | null | null | null | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26555,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26556,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9754 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,754 | train | mutant | 159 | 183 | 187 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95N | K95N | 1 | 1 | 0 | 0 | 95 | K | N | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 295 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:K95N | 49.8 | 2.9 | null | null | null | null | 108.7 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K95N","type":"_... | [{"datasets":[],"id":1202,"numValue":49.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1203,"numValue":2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1204,"numValue":108.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9755 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,755 | train | mutant | 159 | 183 | 187 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95N | K95N | 1 | 1 | 0 | 0 | 95 | K | N | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 296 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:K95N | 52 | 3.2 | null | null | null | null | 90 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:K95N","type"... | [{"datasets":[],"id":1206,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1207,"numValue":3.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1208,"numValue":90.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9757 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,757 | train | mutant | 159 | 183 | 187 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95N | K95N | 1 | 1 | 0 | 0 | 95 | K | N | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 4,104 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:K95N | 53 | 2.9 | null | null | null | null | 108.7 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":15164,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15165,"numValue":2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15166,"numValue":108.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9758 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,758 | train | mutant | 159 | 183 | 187 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95N | K95N | 1 | 1 | 0 | 0 | 95 | K | N | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 7,428 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52.7 | NaCl | 0.1 M | 2RN2_A:K95N | null | null | null | -0.88 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.7,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25825,"numValue":-0.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25826,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9759 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,759 | train | mutant | 159 | 183 | 187 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95N | K95N | 1 | 1 | 0 | 0 | 95 | K | N | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 7,665 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:K95N | null | null | null | -0.88 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26395,"numValue":-0.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26396,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9760 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,760 | train | mutant | 159 | 183 | 187 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95N | K95N | 1 | 1 | 0 | 0 | 95 | K | N | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 7,724 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:K95N | null | null | null | -0.9 | 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|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26557,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26558,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9761 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,761 | train | mutant | 159 | 183 | 187 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K95N | K95N | 1 | 1 | 0 | 0 | 95 | K | N | 5 | CONSERVATION | 2RN2 | 76 | null | 95 | A | S | false | false | 136.371595 | 21.986667 | 7,725 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 49.8 | 2RN2_A:K95N | null | null | null | -0.9 | 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|_PDB_CHAIN_MUTATION | 32 | ARTICLE | Thermostabilization of Escherichia coli ribonuclease HI by replacing left-handed helical Lys95 with Gly or Asn. | 1,992 | 1331044 | J Biol Chem;267;22014-7 | 3 | Kanaya S|Nakamura H|Kimura S | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26559,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26560,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16604,"numValue":5.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9762 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,762 | train | mutant | 2,042 | 183 | 2,281 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q105G | Q105G | 1 | 1 | 0 | 0 | 105 | Q | G | 4 | CONSERVATION | 2RN2 | 76 | null | 105 | A | H | false | false | 81.486761 | 11.977778 | 3,961 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 2 mM | null | KF | 5 mM | 2RN2_A:Q105G | 38.2 | -9.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 369 | ARTICLE | Confirmation of the hierarchical folding of RNase H: a protein engineering study. | 1,999 | 10.1038/12277 | 10467093 | Nat Struct Biol;6;825-31 | 3 | Kho J|Marqusee S|Raschke T M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"2 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KF","type":"ION... | [{"datasets":[],"id":14586,"numValue":38.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14587,"numValue":-9.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14588,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16614,"numValue":4.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9763 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,763 | train | mutant | 2,042 | 183 | 2,281 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q105G | Q105G | 1 | 1 | 0 | 0 | 105 | Q | G | 4 | CONSERVATION | 2RN2 | 76 | null | 105 | A | H | false | false | 81.486761 | 11.977778 | 11,061 | ProTherm | 5.5 | CD | Urea | Potassium phosphate | 2 mM | 25 | KF | 5 mM | 2RN2_A:Q105G | null | null | 7.5 | 2.2 | null | null | null | null | 2.1 | null | null | null | null | null | null | null | yes | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 369 | ARTICLE | Confirmation of the hierarchical folding of RNase H: a protein engineering study. | 1,999 | 10.1038/12277 | 10467093 | Nat Struct Biol;6;825-31 | 3 | Kho J|Marqusee S|Raschke T M | [{"numValue":5.5,"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":"2 mM","type":"BU... | [{"datasets":[],"id":38075,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":38076,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38077,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38078,"numValue":null,"... | [{"id":16614,"numValue":4.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9764 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,764 | train | mutant | 1,525 | 183 | 1,717 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q113P | Q113P | 1 | 1 | 0 | 0 | 113 | Q | P | 3 | CONSERVATION | 2RN2 | 76 | null | 113 | A | T | true | false | 97.944428 | 25.154445 | 2,886 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:Q113P | 49.2 | -0.6 | null | null | null | null | 100.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:Q113P","type":"... | [{"datasets":[],"id":10485,"numValue":49.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":10486,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10487,"numValue":100.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[... | [{"id":16622,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9765 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,765 | train | mutant | 1,525 | 183 | 1,717 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q113P | Q113P | 1 | 1 | 0 | 0 | 113 | Q | P | 3 | CONSERVATION | 2RN2 | 76 | null | 113 | A | T | true | false | 97.944428 | 25.154445 | 2,888 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:Q113P | 49.9 | -2.1 | null | null | null | null | 81 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:Q113P","type... | [{"datasets":[],"id":10493,"numValue":49.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":10494,"numValue":-2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10495,"numValue":81.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16622,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9766 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,766 | train | mutant | 1,525 | 183 | 1,717 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q113P | Q113P | 1 | 1 | 0 | 0 | 113 | Q | P | 3 | CONSERVATION | 2RN2 | 76 | null | 113 | A | T | true | false | 97.944428 | 25.154445 | 7,465 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52 | 2RN2_A:Q113P | null | null | null | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25926,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25927,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16622,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9767 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,767 | train | mutant | 1,525 | 183 | 1,717 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Q113P | Q113P | 1 | 1 | 0 | 0 | 113 | Q | P | 3 | CONSERVATION | 2RN2 | 76 | null | 113 | A | T | true | false | 97.944428 | 25.154445 | 7,733 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:Q113P | null | null | null | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26575,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26576,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16622,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9769 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,769 | train | mutant | 2,046 | 183 | 2,285 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H114A | H114A | 1 | 1 | 0 | 0 | 114 | H | A | 8 | CONSERVATION | 2RN2 | 76 | null | 114 | A | S | true | false | 25.295648 | 12.804 | 3,973 | ProTherm | 7.8 | CD | Thermal | Sodium phosphate | 20 mM | null | 2RN2_A:H114A | 42.5 | -7.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H114A","ty... | [{"datasets":[],"id":14622,"numValue":42.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14623,"numValue":-7.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14624,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16623,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9770 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,770 | train | mutant | 2,046 | 183 | 2,285 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H114A | H114A | 1 | 1 | 0 | 0 | 114 | H | A | 8 | CONSERVATION | 2RN2 | 76 | null | 114 | A | S | true | false | 25.295648 | 12.804 | 10,729 | ProTherm | 5.5 | Fluorescence | GdnHCl | Sodium acetate | 20 mM | 25 | NaCl | 0.1 M | 2RN2_A:H114A | null | null | 6.63 | 2.63 | null | null | null | 1.57 | 4.23 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 701 | ARTICLE | Effect of mutagenesis at each of five histidine residues on enzymatic activity and stability of ribonuclease H from Escherichia coli. | 1,991 | 10.1111/j.1432-1033.1991.tb16033.x | 1645658 | Eur J Biochem;198;437-40 | 5 | Kanaya S|Katayanagi K|Morikawa K|Inoue H|Ohtsuka E | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","t... | [{"datasets":[],"id":36879,"numValue":6.63,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":36880,"numValue":2.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36881,"numValue":4.23,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36882,"numValue":1.5... | [{"id":16623,"numValue":8.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9772 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,772 | train | mutant | 2,076 | 183 | 2,317 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K117R | K117R | 1 | 1 | 0 | 0 | 117 | K | R | 1 | CONSERVATION | 2RN2 | 76 | null | 117 | A | E | true | false | 112.810596 | 23.851111 | 4,101 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:K117R | 49.9 | -0.2 | null | null | null | null | 97.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":15152,"numValue":49.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15153,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15154,"numValue":97.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16626,"numValue":1.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9773 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,773 | train | mutant | 2,076 | 183 | 2,317 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K117R | K117R | 1 | 1 | 0 | 0 | 117 | K | R | 1 | CONSERVATION | 2RN2 | 76 | null | 117 | A | E | true | false | 112.810596 | 23.851111 | 7,425 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52.7 | NaCl | 0.1 M | 2RN2_A:K117R | null | null | null | -0.03 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.7,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25819,"numValue":-0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25820,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16626,"numValue":1.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9774 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,774 | train | mutant | 2,076 | 183 | 2,317 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | K117R | K117R | 1 | 1 | 0 | 0 | 117 | K | R | 1 | CONSERVATION | 2RN2 | 76 | null | 117 | A | E | true | false | 112.810596 | 23.851111 | 7,662 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:K117R | null | null | null | 0.06 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26389,"numValue":0.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26390,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16626,"numValue":1.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9775 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,775 | train | mutant | 2,077 | 183 | 2,318 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E119V | E119V | 1 | 1 | 0 | 0 | 119 | E | V | 3 | CONSERVATION | 2RN2 | 76 | null | 119 | A | E | true | false | 55.669997 | 22.426667 | 4,089 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:E119V | 55.4 | 2.7 | null | null | null | null | 94.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":15104,"numValue":55.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15105,"numValue":2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15106,"numValue":94.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9777 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,777 | train | mutant | 2,077 | 183 | 2,318 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E119V | E119V | 1 | 1 | 0 | 0 | 119 | E | V | 3 | CONSERVATION | 2RN2 | 76 | null | 119 | A | E | true | false | 55.669997 | 22.426667 | 7,426 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52.7 | NaCl | 0.1 M | 2RN2_A:E119V | null | null | null | -0.74 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.7,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25821,"numValue":-0.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25822,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9778 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,778 | train | mutant | 2,077 | 183 | 2,318 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E119V | E119V | 1 | 1 | 0 | 0 | 119 | E | V | 3 | CONSERVATION | 2RN2 | 76 | null | 119 | A | E | true | false | 55.669997 | 22.426667 | 7,663 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:E119V | null | null | null | -0.09 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26391,"numValue":-0.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26392,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9779 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,779 | train | mutant | 2,047 | 183 | 2,286 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A | H124A | 1 | 1 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124 | A | T | true | true | 158.609385 | 25.726 | 3,967 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:H124A | 51.1 | 1.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H124A","type":"... | [{"datasets":[],"id":14604,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14605,"numValue":1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14606,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9780 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,780 | train | mutant | 2,047 | 183 | 2,286 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A | H124A | 1 | 1 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124 | A | T | true | true | 158.609385 | 25.726 | 3,970 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:H124A | 52.7 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H124A","type... | [{"datasets":[],"id":14613,"numValue":52.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14614,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14615,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9781 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,781 | train | mutant | 2,047 | 183 | 2,286 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A | H124A | 1 | 1 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124 | A | T | true | true | 158.609385 | 25.726 | 3,974 | ProTherm | 7.8 | CD | Thermal | Sodium phosphate | 20 mM | null | 2RN2_A:H124A | 50.3 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H124A","ty... | [{"datasets":[],"id":14625,"numValue":50.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14626,"numValue":0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14627,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9782 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,782 | train | mutant | 2,047 | 183 | 2,286 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A | H124A | 1 | 1 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124 | A | T | true | true | 158.609385 | 25.726 | 10,730 | ProTherm | 5.5 | Fluorescence | GdnHCl | Sodium acetate | 20 mM | 25 | NaCl | 0.1 M | 2RN2_A:H124A | null | null | 9.74 | -0.48 | null | null | null | 1.82 | 5.36 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 701 | ARTICLE | Effect of mutagenesis at each of five histidine residues on enzymatic activity and stability of ribonuclease H from Escherichia coli. | 1,991 | 10.1111/j.1432-1033.1991.tb16033.x | 1645658 | Eur J Biochem;198;437-40 | 5 | Kanaya S|Katayanagi K|Morikawa K|Inoue H|Ohtsuka E | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","t... | [{"datasets":[],"id":36884,"numValue":9.74,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36885,"numValue":-0.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36886,"numValue":5.36,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36887,"numValue":1.82,"references":[]... | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9783 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,783 | train | mutant | 2,047 | 183 | 2,286 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A | H124A | 1 | 1 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124 | A | T | true | true | 158.609385 | 25.726 | 11,066 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 25 | 2RN2_A:H124A | null | null | 9.38 | -0.17 | null | null | null | 1.82 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":38095,"numValue":9.38,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38096,"numValue":-0.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38097,"numValue":1.82,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":... | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9784 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,784 | train | mutant | 2,047 | 183 | 2,286 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A | H124A | 1 | 1 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124 | A | T | true | true | 158.609385 | 25.726 | 11,070 | ProTherm | 8.2 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 2RN2_A:H124A | null | null | 8.54 | -0.05 | null | null | null | 1.66 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":8.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":38111,"numValue":8.54,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38112,"numValue":-0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38113,"numValue":1.66,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38114,"numValue":null,"references":[... | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9785 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,785 | train | mutant | 6,929 | 183 | 7,571 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A|H127A | H124A|H127A | 2 | 2 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124|127 | A | T|L | true | true | 115.2923 | 27.4075 | 14,778 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:H124A 2RN2_A:H127A | 53 | 3.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H124A 2RN2_A:H1... | [{"datasets":[],"id":54602,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54603,"numValue":3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54604,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16636,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9786 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,786 | train | mutant | 6,929 | 183 | 7,571 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A|H127A | H124A|H127A | 2 | 2 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124|127 | A | T|L | true | true | 115.2923 | 27.4075 | 14,780 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:H124A 2RN2_A:H127A | 52.1 | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H124A 2RN2_A... | [{"datasets":[],"id":54608,"numValue":52.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54609,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54610,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16636,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9787 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,787 | train | mutant | 6,929 | 183 | 7,571 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H124A|H127A | H124A|H127A | 2 | 2 | 0 | 0 | 124 | H | A | 9 | CONSERVATION | 2RN2 | 76 | null | 124|127 | A | T|L | true | true | 115.2923 | 27.4075 | 14,782 | ProTherm | 7.8 | CD | Thermal | Sodium phosphate | 20 mM | null | 2RN2_A:H124A 2RN2_A:H127A | 50.1 | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H124A 2RN2... | [{"datasets":[],"id":54614,"numValue":50.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54615,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54616,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16636,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9788 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,788 | train | mutant | 1,523 | 183 | 1,715 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A125T | A125T | 1 | 1 | 0 | 0 | 125 | A | T | 5 | CONSERVATION | 2RN2 | 76 | null | 125 | A | S | true | true | 65.919381 | 29.294 | 2,883 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A125T | 50.2 | 0.4 | null | null | null | null | 96.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|STRUM_Q306.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A125T","type":"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":10473,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv","STRUM_Q306.csv","STRUM_Q34... | [{"id":16634,"numValue":5.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9789 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,789 | train | mutant | 1,523 | 183 | 1,715 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A125T | A125T | 1 | 1 | 0 | 0 | 125 | A | T | 5 | CONSERVATION | 2RN2 | 76 | null | 125 | A | S | true | true | 65.919381 | 29.294 | 2,884 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A125T | 52 | 0 | null | null | null | null | 88.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|STRUM_Q306.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A125T","type":"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":10477,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv","STRUM_Q306.csv","STRUM_Q34... | [{"id":16634,"numValue":5.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9790 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,790 | train | mutant | 1,523 | 183 | 1,715 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A125T | A125T | 1 | 1 | 0 | 0 | 125 | A | T | 5 | CONSERVATION | 2RN2 | 76 | null | 125 | A | S | true | true | 65.919381 | 29.294 | 7,466 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | 52 | 2RN2_A:A125T | null | null | null | 0 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.0,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25928,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":25929,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":16634,"numValue":5.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9791 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,791 | train | mutant | 1,523 | 183 | 1,715 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A125T | A125T | 1 | 1 | 0 | 0 | 125 | A | T | 5 | CONSERVATION | 2RN2 | 76 | null | 125 | A | S | true | true | 65.919381 | 29.294 | 7,734 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:A125T | null | null | null | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26577,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26578,"numValue":null,"references":[],"strValue":"yes","type":... | [{"id":16634,"numValue":5.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9792 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,792 | train | mutant | 2,048 | 183 | 2,287 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H127A | H127A | 1 | 1 | 0 | 0 | 127 | H | A | 7 | CONSERVATION | 2RN2 | 76 | null | 127 | A | L | true | true | 71.975216 | 29.089 | 3,968 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:H127A | 50.3 | 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|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H127A","type":"... | [{"datasets":[],"id":14607,"numValue":50.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14608,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14609,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16636,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9793 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,793 | train | mutant | 2,048 | 183 | 2,287 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H127A | H127A | 1 | 1 | 0 | 0 | 127 | H | A | 7 | CONSERVATION | 2RN2 | 76 | null | 127 | A | L | true | true | 71.975216 | 29.089 | 10,731 | ProTherm | 5.5 | Fluorescence | GdnHCl | Sodium acetate | 20 mM | 25 | NaCl | 0.1 M | 2RN2_A:H127A | null | null | 8.68 | 0.58 | null | null | null | 1.74 | 4.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 701 | ARTICLE | Effect of mutagenesis at each of five histidine residues on enzymatic activity and stability of ribonuclease H from Escherichia coli. | 1,991 | 10.1111/j.1432-1033.1991.tb16033.x | 1645658 | Eur J Biochem;198;437-40 | 5 | Kanaya S|Katayanagi K|Morikawa K|Inoue H|Ohtsuka E | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","t... | [{"datasets":[],"id":36889,"numValue":8.68,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36890,"numValue":0.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36891,"numValue":4.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36892,"numValue":1.74,"references":[],... | [{"id":16636,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9794 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,794 | train | mutant | 2,048 | 183 | 2,287 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H127A | H127A | 1 | 1 | 0 | 0 | 127 | H | A | 7 | CONSERVATION | 2RN2 | 76 | null | 127 | A | L | true | true | 71.975216 | 29.089 | 11,067 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 25 | 2RN2_A:H127A | null | null | 8.97 | 0.24 | null | null | null | 1.74 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":38099,"numValue":8.97,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":38100,"numValue":0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38101,"numValue":1.74,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38102,"numValue":nul... | [{"id":16636,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9795 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,795 | train | mutant | 2,048 | 183 | 2,287 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H127A | H127A | 1 | 1 | 0 | 0 | 127 | H | A | 7 | CONSERVATION | 2RN2 | 76 | null | 127 | A | L | true | true | 71.975216 | 29.089 | 11,071 | ProTherm | 8.2 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 2RN2_A:H127A | null | null | 8.18 | 0.31 | null | null | null | 1.59 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":8.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":38115,"numValue":8.18,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38116,"numValue":0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38117,"numValue":1.59,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":3... | [{"id":16636,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9796 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,796 | train | mutant | 477 | 183 | 526 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134N | D134N | 1 | 1 | 0 | 0 | 134 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 770 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:D134N | 53.4 | 6.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D134N","type":... | [{"datasets":[],"id":2936,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2937,"numValue":6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2938,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9797 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,797 | train | mutant | 477 | 183 | 526 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134N | D134N | 1 | 1 | 0 | 0 | 134 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 783 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D134N | 49.7 | -0.3 | null | null | null | null | 110.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D134N","type":"... | [{"datasets":[],"id":2986,"numValue":49.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2987,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2988,"numValue":110.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9798 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,798 | train | mutant | 477 | 183 | 526 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134N | D134N | 1 | 1 | 0 | 0 | 134 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,935 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:D134N | 56.3 | 3.2 | null | null | null | null | 96.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":14485,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14486,"numValue":3.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14487,"numValue":96.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9799 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,799 | train | mutant | 477 | 183 | 526 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134N | D134N | 1 | 1 | 0 | 0 | 134 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,945 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134N | 49.7 | -0.3 | null | null | null | null | 110.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14525,"numValue":49.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14526,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14527,"numValue":110.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9801 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,801 | train | mutant | 477 | 183 | 526 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134N | D134N | 1 | 1 | 0 | 0 | 134 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,687 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D134N | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26445,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26446,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9802 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,802 | train | mutant | 477 | 183 | 526 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134N | D134N | 1 | 1 | 0 | 0 | 134 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,689 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134N | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26449,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26450,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9803 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,803 | train | mutant | 477 | 183 | 526 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134N | D134N | 1 | 1 | 0 | 0 | 134 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,809 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:D134N | null | null | null | -1.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"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":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv"],"id":26753,"numValue":-1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26754,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9805 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,805 | train | mutant | 478 | 183 | 527 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134A | D134A | 1 | 1 | 0 | 0 | 134 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 784 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D134A | 52.9 | 2.9 | null | null | null | null | 104.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D134A","type":"... | [{"datasets":[],"id":2990,"numValue":52.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2991,"numValue":2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2992,"numValue":104.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9806 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,806 | train | mutant | 478 | 183 | 527 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134A | D134A | 1 | 1 | 0 | 0 | 134 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,944 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:D134A | 58.6 | 5.5 | null | null | null | null | 117.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":14521,"numValue":58.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14522,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14523,"numValue":117.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9808 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,808 | train | mutant | 478 | 183 | 527 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134A | D134A | 1 | 1 | 0 | 0 | 134 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,386 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 53.1 | NaCl | 0.1 M | 2RN2_A:D134A | null | null | null | -1.51 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":53.1,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25725,"numValue":-1.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25726,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9809 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,809 | train | mutant | 478 | 183 | 527 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134A | D134A | 1 | 1 | 0 | 0 | 134 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,688 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D134A | null | null | null | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26447,"numValue":-0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26448,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9810 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,810 | train | mutant | 478 | 183 | 527 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134A | D134A | 1 | 1 | 0 | 0 | 134 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,698 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134A | null | null | null | -0.89 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"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":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv"],"id":26467,"numValue":-0.89,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26468,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9811 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,811 | train | mutant | 478 | 183 | 527 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134A | D134A | 1 | 1 | 0 | 0 | 134 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,810 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:D134A | null | null | null | -2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"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":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv"],"id":26755,"numValue":-2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26756,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9812 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,812 | train | mutant | 2,027 | 183 | 2,263 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134H | D134H | 1 | 1 | 0 | 0 | 134 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,927 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134H | 53.6 | 1.7 | null | null | null | null | 106.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 362 | ARTICLE | High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. | 1,995 | 10.1021/bi00025a018 | 7794925 | Biochemistry;34;8115-22 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14457,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14458,"numValue":1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14459,"numValue":106.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9813 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,813 | train | mutant | 2,027 | 183 | 2,263 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134H | D134H | 1 | 1 | 0 | 0 | 134 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,931 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134H | 59.5 | 7 | null | null | null | null | 106.6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 362 | ARTICLE | High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. | 1,995 | 10.1021/bi00025a018 | 7794925 | Biochemistry;34;8115-22 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":5.5,"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":14473,"numValue":59.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14474,"numValue":7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14475,"numValue":106.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9815 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,815 | train | mutant | 2,027 | 183 | 2,263 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134H | D134H | 1 | 1 | 0 | 0 | 134 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,946 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134H | 51.7 | 1.7 | null | null | null | null | 106.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14529,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14530,"numValue":1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14531,"numValue":106.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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