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:1225 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,225 | train | mutant | 1,885 | 30 | 2,114 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102N | D102N | 1 | 1 | 0 | 0 | 102 | D | N | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 13,539 | ProTherm | 7 | DSC | Urea | MOPS | 30 mM | 20 | 1RN1_A:D76N | null | null | 3.53 | 3.19 | null | null | null | 2.39 | 1.48 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":50038,"numValue":3.53,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":50039,"numValue":3.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50040,"numValue":1.48,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50041,"numValue":2.39,"references":[],... | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1228 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,228 | train | mutant | 1,885 | 30 | 2,114 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102N | D102N | 1 | 1 | 0 | 0 | 102 | D | N | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 13,882 | ProTherm | 7 | DSC | Urea | MOPS | 30 mM | 15 | 1RN1_A:D76N | null | null | 4.25 | 3.09 | null | null | null | 3.01 | 1.41 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":15.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":51364,"numValue":4.25,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":51365,"numValue":3.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":51366,"numValue":1.41,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":51367,"numValue":3.0... | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1229 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,229 | train | mutant | 1,885 | 30 | 2,114 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102N | D102N | 1 | 1 | 0 | 0 | 102 | D | N | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 14,087 | ProTherm | 7 | DSC | Urea | MOPS | 30 mM | 10 | 1RN1_A:D76N | null | null | 5 | 2.87 | null | null | null | 3.3 | 1.52 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":52109,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":52110,"numValue":2.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":52111,"numValue":1.52,"references":[],"strValue":null,"type":"M"},{"d... | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1230 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,230 | train | mutant | 1,885 | 30 | 2,114 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102N | D102N | 1 | 1 | 0 | 0 | 102 | D | N | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 14,217 | ProTherm | 7 | DSC | Urea | MOPS | 30 mM | 5 | 1RN1_A:D76N | null | null | 5.55 | 2.77 | null | null | null | 3.63 | 1.53 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":5.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":52625,"numValue":5.55,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":52626,"numValue":2.77,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":52627,"numValue":1.53,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":52628,"numValue":3.63,"references":[],... | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1231 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,231 | train | mutant | 1,886 | 30 | 2,115 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102S | D102S | 1 | 1 | 0 | 0 | 102 | D | S | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 3,634 | ProTherm | 7 | DSC | Thermal | MOPS | 30 mM | null | 1RN1_A:D76S | 37.2 | -13.6 | null | null | 77.6 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:D76S","type":"_PDB_CH... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13351,"numValue":37.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13352,"numValue":-13.6,"references":[],"strValue":nu... | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1232 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,232 | train | mutant | 1,886 | 30 | 2,115 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102S | D102S | 1 | 1 | 0 | 0 | 102 | D | S | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 13,751 | ProTherm | 7 | DSC | Thermal | MOPS | 30 mM | 15 | 1RN1_A:D76S | null | null | null | 3.1 | null | 1.39 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":15.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":50755,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":50756,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50757,"numValue":null,"reference... | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1234 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,234 | train | mutant | 1,887 | 30 | 2,116 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102A | D102A | 1 | 1 | 0 | 0 | 102 | D | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 3,635 | ProTherm | 7 | DSC | Thermal | MOPS | 30 mM | null | 1RN1_A:D76A | 35.6 | -15.2 | null | null | 71.1 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Broom_S605.csv|Saraboji_S1791.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:D76A","type":"_PDB_CH... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13355,"numValue":35.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13356,"numValue":-15.2,"references":[],"strValue":nul... | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1235 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,235 | train | mutant | 1,887 | 30 | 2,116 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102A | D102A | 1 | 1 | 0 | 0 | 102 | D | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 13,752 | ProTherm | 7 | DSC | Thermal | MOPS | 30 mM | 15 | 1RN1_A:D76A | null | null | null | 3.8 | null | 1.39 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":15.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":50758,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":50759,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50760,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1236 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,236 | train | mutant | 1,887 | 30 | 2,116 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | D102A | D102A | 1 | 1 | 0 | 0 | 102 | D | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 102 | A | L|E | false | false | 10.063041 | 9.579375 | 13,881 | ProTherm | 7 | DSC | Urea | MOPS | 30 mM | 15 | 1RN1_A:D76A | null | null | null | 3.7 | null | null | null | 2.57 | 1.42 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 342 | ARTICLE | Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. | 1,999 | 10.1021/bi991422s | 10529213 | Biochemistry;38;13379-84 | 2 | Giletto A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":15.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":51360,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":51361,"numValue":1.42,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":51362,"numVa... | [{"id":6549,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1237 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,237 | train | mutant | 246 | 30 | 277 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104A | V104A | 1 | 1 | 0 | 0 | 104 | V | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 439 | ProTherm | 7 | CD | Thermal | MOPS | 30 mM | null | 1RN1_A:V78A | 43.3 | -7.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:V78A","type":"_PDB_CHA... | [{"datasets":[],"id":1787,"numValue":43.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1788,"numValue":-7.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1789,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1238 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,238 | train | mutant | 246 | 30 | 277 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104A | V104A | 1 | 1 | 0 | 0 | 104 | V | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 8,741 | ProTherm | 7 | CD | Urea | MOPS | 30 mM | 25 | 1RN1_A:V78A | null | null | null | 4.08 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":["SAAFEC_S1262.csv"],"id":29538,"numValue":4.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29539,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1239 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,239 | train | mutant | 246 | 30 | 277 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104A | V104A | 1 | 1 | 0 | 0 | 104 | V | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 12,520 | ProTherm | 7 | Fluorescence | Urea | MOPS | 30mM | 25 | 9RNT_A:V78A | null | null | 2.6 | 3.8 | null | null | null | 2.05 | 1.23 | null | null | null | null | null | null | null | yes | 2.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 519 | ARTICLE | Contribution of hydrophobic interactions to protein stability. | 2,011 | 10.1016/j.jmb.2011.02.053 | 21377472 | J Mol Biol;408;514-28 | 11 | Scholtz J Martin|Pace C Nick|Trevino Saul R|Fu Hailong|Landua John|Gajiwala Ketan|Shirley Bret A|Grimsley Gerald R|Fryar Katrina Lee|Hendricks Marsha McNutt|Iimura Satoshi | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30mM","type":"BUFFER_... | [{"datasets":[],"id":45397,"numValue":2.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45398,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45399,"numValue":1.23,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45400,"numValue":2.05,"references":[],"s... | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1240 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,240 | train | mutant | 246 | 30 | 277 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104A | V104A | 1 | 1 | 0 | 0 | 104 | V | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 12,523 | ProTherm | 5 | Fluorescence | Urea | Acetate | 30mM | 25 | 9RNT_A:V78A | null | null | 5 | 4.5 | null | null | null | 3.78 | 1.34 | null | null | null | null | null | null | null | yes | 2.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 519 | ARTICLE | Contribution of hydrophobic interactions to protein stability. | 2,011 | 10.1016/j.jmb.2011.02.053 | 21377472 | J Mol Biol;408;514-28 | 11 | Scholtz J Martin|Pace C Nick|Trevino Saul R|Fu Hailong|Landua John|Gajiwala Ketan|Shirley Bret A|Grimsley Gerald R|Fryar Katrina Lee|Hendricks Marsha McNutt|Iimura Satoshi | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Acetate","type":"BUFFER"},{"numValue":null,"strValue":"30mM","type":"BUFF... | [{"datasets":[],"id":45415,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45416,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45417,"numValue":1.34,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45418,"numValue":3.78,"references":[],"s... | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1241 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,241 | train | mutant | 247 | 30 | 278 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104S | V104S | 1 | 1 | 0 | 0 | 104 | V | S | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 440 | ProTherm | 7 | CD | Thermal | MOPS | 30 mM | null | 1RN1_A:V78S | 34.6 | -16.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:V78S","type":"_PDB_CHA... | [{"datasets":[],"id":1790,"numValue":34.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1791,"numValue":-16.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1792,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1243 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,243 | train | mutant | 248 | 30 | 279 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104T | V104T | 1 | 1 | 0 | 0 | 104 | V | T | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 441 | ProTherm | 7 | CD | Thermal | MOPS | 30 mM | null | 1RN1_A:V78T | 41.4 | -9.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(0.98) | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:V78T","type":"_PDB_CHA... | [{"datasets":[],"id":1793,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1794,"numValue":-9.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1795,"numValue":null,"references":[],"strValue":"yes(0.98)","type":"REVERSIBILITY"}] | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1244 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,244 | train | mutant | 248 | 30 | 279 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104T | V104T | 1 | 1 | 0 | 0 | 104 | V | T | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 449 | ProTherm | 7 | DSC | Thermal | MOPS | 30 mM | null | 1RN1_A:V78T | 40.2 | -11.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(0.98) | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:V78T","type":"_PDB_CH... | [{"datasets":[],"id":1817,"numValue":40.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1818,"numValue":-11.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1819,"numValue":null,"references":[],"strValue":"yes(0.98)","type":"REVERSIBILITY"}] | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1245 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,245 | train | mutant | 248 | 30 | 279 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104T | V104T | 1 | 1 | 0 | 0 | 104 | V | T | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 8,743 | ProTherm | 7 | CD | Urea | MOPS | 30 mM | 25 | 1RN1_A:V78T | null | null | null | 4.08 | null | null | null | null | null | null | null | null | null | null | null | null | yes(0.98) | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":["SAAFEC_S1262.csv"],"id":29542,"numValue":4.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29543,"numValue":null,"references":[],"strValue":"yes(0.98)","type":"REVERSIBILITY"}] | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1246 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,246 | train | mutant | 248 | 30 | 279 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104T | V104T | 1 | 1 | 0 | 0 | 104 | V | T | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 8,752 | ProTherm | 7 | DSC | Thermal | MOPS | 30 mM | 25 | 1RN1_A:V78T | null | null | null | 3.1 | null | 1.29 | null | null | null | null | null | null | null | null | null | null | yes(0.98) | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":29564,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv"],"id":29565,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29566,"numValue":null,"references":[],"strValue":"yes(0.98)","type":"REVERSIBILITY"}] | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1247 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,247 | train | mutant | 3,836 | 30 | 4,310 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V104C | V104C | 1 | 1 | 0 | 0 | 104 | V | C | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 104 | A | E | false | false | 0 | 12.185 | 8,744 | ProTherm | 7 | CD | Urea | MOPS | 30 mM | 25 | 1RN1_A:V78C | null | null | null | 3.67 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":["SAAFEC_S1262.csv"],"id":29544,"numValue":3.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29545,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6551,"numValue":9.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1248 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,248 | train | mutant | 653 | 30 | 706 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | N107A | N107A | 1 | 1 | 0 | 0 | 107 | N | A | 6 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 107 | A | L|E | false | false | 0.948539 | 13.37125 | 1,070 | ProTherm | 7 | Fluorescence | Thermal | MOPS | 30 mM | null | 1RN1_A:N81A | 42.3 | -8.6 | null | null | null | null | 91 | 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 | 110 | ARTICLE | Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. | 1,992 | 10.1021/bi00118a013 | 1731929 | Biochemistry;31;725-32 | 4 | Stanssens P|Hahn U|Shirley B A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:N81A","type"... | [{"datasets":[],"id":4000,"numValue":42.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4001,"numValue":-8.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4002,"numValue":91.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6554,"numValue":6.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1249 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,249 | train | mutant | 653 | 30 | 706 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | N107A | N107A | 1 | 1 | 0 | 0 | 107 | N | A | 6 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 107 | A | L|E | false | false | 0.948539 | 13.37125 | 7,634 | ProTherm | 7 | Fluorescence | Thermal | MOPS | 30 mM | 50.9 | 1RN1_A:N81A | null | null | null | 2.91 | 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 | 110 | ARTICLE | Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. | 1,992 | 10.1021/bi00118a013 | 1731929 | Biochemistry;31;725-32 | 4 | Stanssens P|Hahn U|Shirley B A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":50.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":26333,"numValue":2.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26334,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6554,"numValue":6.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1250 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,250 | train | mutant | 653 | 30 | 706 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | N107A | N107A | 1 | 1 | 0 | 0 | 107 | N | A | 6 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 107 | A | L|E | false | false | 0.948539 | 13.37125 | 8,904 | ProTherm | 7 | Fluorescence | Urea | MOPS | 30 mM | 25 | 1RN1_A:N81A | null | null | null | 2.87 | null | null | null | 2.92 | 1.44 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 110 | ARTICLE | Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. | 1,992 | 10.1021/bi00118a013 | 1731929 | Biochemistry;31;725-32 | 4 | Stanssens P|Hahn U|Shirley B A|Pace C N | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":30184,"numValue":2.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30185,"numValue":1.44,"references":[],"strValue":null,"type":"M"},{"data... | [{"id":6554,"numValue":6.0,"position":107,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1251 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,251 | train | mutant | 5,802 | 30 | 6,358 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | L112A | L112A | 1 | 1 | 0 | 0 | 112 | L | A | 4 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 112 | A | E | false | false | 47.905728 | 14.3375 | 12,521 | ProTherm | 7 | Fluorescence | Urea | MOPS | 30mM | 25 | 9RNT_A:L86A | null | null | 2.1 | 4.3 | null | null | null | 1.7 | 1.23 | null | null | null | null | null | null | null | yes | 2.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 519 | ARTICLE | Contribution of hydrophobic interactions to protein stability. | 2,011 | 10.1016/j.jmb.2011.02.053 | 21377472 | J Mol Biol;408;514-28 | 11 | Scholtz J Martin|Pace C Nick|Trevino Saul R|Fu Hailong|Landua John|Gajiwala Ketan|Shirley Bret A|Grimsley Gerald R|Fryar Katrina Lee|Hendricks Marsha McNutt|Iimura Satoshi | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30mM","type":"BUFFER_... | [{"datasets":[],"id":45403,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45404,"numValue":4.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45405,"numValue":1.23,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45406,"numValue":1.7,"references":[],"st... | [{"id":6559,"numValue":4.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1252 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,252 | train | mutant | 2,137 | 30 | 2,422 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | G114R | G114R | 1 | 1 | 0 | 0 | 114 | G | R | 7 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 114 | A | E | true | false | 9.316385 | 12.19375 | 4,212 | ProTherm | 6 | DSC | Thermal | phosphate | null | 1RTB_A:G88R | 64 | 0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 399 | ARTICLE | Conformational stability is a determinant of ribonuclease A cytotoxicity. | 2,000 | 10.1074/jbc.M001132200 | 10747991 | J Biol Chem;275;17463-7 | 2 | Klink T A|Raines R T | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1RTB_A:G88R","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":15612,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15613,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15614,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}... | [{"id":6561,"numValue":7.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1253 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,253 | train | mutant | 249 | 30 | 280 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V115S | V115S | 1 | 1 | 0 | 0 | 115 | V | S | 5 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 115 | A | E | true | false | 2.256627 | 10.763571 | 442 | ProTherm | 7 | CD | Thermal | MOPS | 30 mM | null | 1RN1_A:V89S | 29.6 | -21.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:V89S","type":"_PDB_CHA... | [{"datasets":[],"id":1796,"numValue":29.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1797,"numValue":-21.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1798,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6562,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1254 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,254 | train | mutant | 249 | 30 | 280 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V115S | V115S | 1 | 1 | 0 | 0 | 115 | V | S | 5 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 115 | A | E | true | false | 2.256627 | 10.763571 | 8,745 | ProTherm | 7 | CD | Urea | MOPS | 30 mM | 25 | 1RN1_A:V89S | null | null | null | 4.87 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":["SAAFEC_S1262.csv"],"id":29546,"numValue":4.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29547,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6562,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1255 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,255 | train | mutant | 250 | 30 | 281 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V115T | V115T | 1 | 1 | 0 | 0 | 115 | V | T | 5 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 115 | A | E | true | false | 2.256627 | 10.763571 | 443 | ProTherm | 7 | CD | Thermal | MOPS | 30 mM | null | 1RN1_A:V89T | 38 | -13.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:V89T","type":"_PDB_CHA... | [{"datasets":[],"id":1799,"numValue":38.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1800,"numValue":-13.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1801,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6562,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1256 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,256 | train | mutant | 250 | 30 | 281 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V115T | V115T | 1 | 1 | 0 | 0 | 115 | V | T | 5 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 115 | A | E | true | false | 2.256627 | 10.763571 | 8,746 | ProTherm | 7 | CD | Urea | MOPS | 30 mM | 25 | 1RN1_A:V89T | null | null | null | 3.07 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":["SAAFEC_S1262.csv"],"id":29548,"numValue":3.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29549,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6562,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1257 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,257 | train | mutant | 251 | 30 | 282 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V115C | V115C | 1 | 1 | 0 | 0 | 115 | V | C | 5 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 115 | A | E | true | false | 2.256627 | 10.763571 | 444 | ProTherm | 7 | CD | Thermal | MOPS | 30 mM | null | 1RN1_A:V89C | 46.3 | -4.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RN1_A:V89C","type":"_PDB_CHA... | [{"datasets":[],"id":1802,"numValue":46.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1803,"numValue":-4.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1804,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6562,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1258 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,258 | train | mutant | 251 | 30 | 282 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | V115C | V115C | 1 | 1 | 0 | 0 | 115 | V | C | 5 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 115 | A | E | true | false | 2.256627 | 10.763571 | 8,747 | ProTherm | 7 | CD | Urea | MOPS | 30 mM | 25 | 1RN1_A:V89C | null | null | null | 3.54 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 46 | ARTICLE | Hydrophobic core manipulations in ribonuclease T1. | 2,001 | 10.1021/bi010565n | 11513591 | Biochemistry;40;10140-9 | 5 | Backmann J|De Vos S|Steyaert J|Loris R|Pr?vost M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":["SAAFEC_S1262.csv"],"id":29550,"numValue":3.54,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29551,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6562,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1259 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,259 | train | mutant | 5,803 | 30 | 6,359 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | I116V | I116V | 1 | 1 | 0 | 0 | 116 | I | V | 8 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 116 | A | E | true | true | 0.04479 | 10.4225 | 12,522 | ProTherm | 7 | Fluorescence | Urea | MOPS | 30mM | 25 | 9RNT_A:I90V | null | null | 5.2 | 1.2 | null | null | null | 4.49 | 1.23 | null | null | null | null | null | null | null | yes | 2.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 519 | ARTICLE | Contribution of hydrophobic interactions to protein stability. | 2,011 | 10.1016/j.jmb.2011.02.053 | 21377472 | J Mol Biol;408;514-28 | 11 | Scholtz J Martin|Pace C Nick|Trevino Saul R|Fu Hailong|Landua John|Gajiwala Ketan|Shirley Bret A|Grimsley Gerald R|Fryar Katrina Lee|Hendricks Marsha McNutt|Iimura Satoshi | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30mM","type":"BUFFER_... | [{"datasets":[],"id":45409,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45410,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45411,"numValue":1.23,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45412,"numValue":4.49,"references":[],"s... | [{"id":6563,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1260 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,260 | train | mutant | 2,308 | 30 | 2,636 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117A | T117A | 1 | 1 | 0 | 0 | 117 | T | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117 | A | L|E | false | false | 2.269345 | 9.869286 | 4,597 | ProTherm | 7 | DSC | Thermal | MOPS | 30000.0 | null | 1YGW_A:T91A | 41.9 | -10.6 | null | 3.2 | 98 | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91A","type":"_PDB_CH... | [{"datasets":[],"id":17024,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":17025,"numValue":-10.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17026,"numValue":98.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":17027,"numValue":3.2,"references":[]... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1261 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,261 | train | mutant | 2,308 | 30 | 2,636 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117A | T117A | 1 | 1 | 0 | 0 | 117 | T | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117 | A | L|E | false | false | 2.269345 | 9.869286 | 11,510 | ProTherm | 7 | Urea | MOPS | 30000.0 | 25 | 1YGW_A:T91A | null | null | 2.9 | null | null | null | null | 2.32 | 1.25 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91A","type":"_PD... | [{"datasets":[],"id":39727,"numValue":2.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39728,"numValue":1.25,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":39729,"numValue":2.32,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":39730,"numValue":2.0,"references":[],"st... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1262 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,262 | train | mutant | 2,309 | 30 | 2,637 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117V | T117V | 1 | 1 | 0 | 0 | 117 | T | V | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117 | A | L|E | false | false | 2.269345 | 9.869286 | 4,598 | ProTherm | 7 | DSC | Thermal | MOPS | 30000.0 | null | 1YGW_A:T91V | 40.7 | -11.8 | null | 3.6 | 95 | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91V","type":"_PDB_CH... | [{"datasets":[],"id":17030,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":17031,"numValue":-11.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17032,"numValue":95.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":17033,"numValue":3.6,"references":[]... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1263 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,263 | train | mutant | 2,309 | 30 | 2,637 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117V | T117V | 1 | 1 | 0 | 0 | 117 | T | V | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117 | A | L|E | false | false | 2.269345 | 9.869286 | 11,511 | ProTherm | 7 | Urea | MOPS | 30000.0 | 25 | 1YGW_A:T91V | null | null | 2.6 | null | null | null | null | 2.07 | 1.24 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91V","type":"_PD... | [{"datasets":[],"id":39732,"numValue":2.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39733,"numValue":1.24,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":39734,"numValue":2.07,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":39735,"numValue":2.0,"references":[],"st... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1264 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,264 | train | mutant | 7,690 | 30 | 8,393 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117A|T119A | T117A|T119A | 2 | 2 | 0 | 0 | 117 | T | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117|119 | A | L|T|E | false | false | 35.653038 | 10.478571 | 16,306 | ProTherm | 7 | DSC | Thermal | MOPS | 30000.0 | null | 1YGW_A:T91A 1YGW_A:T93A | 40.5 | -12 | null | 3.7 | 96 | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91A 1YGW_A:T93A","ty... | [{"datasets":[],"id":59768,"numValue":40.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":59769,"numValue":-12.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":59770,"numValue":96.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":59771,"numValue":3.7,"references":[]... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1265 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,265 | train | mutant | 7,690 | 30 | 8,393 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117A|T119A | T117A|T119A | 2 | 2 | 0 | 0 | 117 | T | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117|119 | A | L|T|E | false | false | 35.653038 | 10.478571 | 17,092 | ProTherm | 7 | Urea | MOPS | 30000.0 | 25 | 1YGW_A:T91A 1YGW_A:T93A | null | null | 2.3 | null | null | null | null | 1.9 | 1.21 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91A 1YGW_A:T93A"... | [{"datasets":[],"id":62915,"numValue":2.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62916,"numValue":1.21,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62917,"numValue":1.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":62918,"numValue":2.0,"references":[],"str... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1266 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,266 | train | mutant | 7,691 | 30 | 8,394 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117A|T119V | T117A|T119V | 2 | 2 | 0 | 0 | 117 | T | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117|119 | A | L|T|E | false | false | 35.653038 | 10.478571 | 16,307 | ProTherm | 7 | DSC | Thermal | MOPS | 30000.0 | null | 1YGW_A:T91A 1YGW_A:T93V | 41.4 | -11 | null | 3.4 | 90 | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91A 1YGW_A:T93V","ty... | [{"datasets":[],"id":59774,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":59775,"numValue":-11.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":59776,"numValue":90.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":59777,"numValue":3.4,"references":[]... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1267 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,267 | train | mutant | 7,691 | 30 | 8,394 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117A|T119V | T117A|T119V | 2 | 2 | 0 | 0 | 117 | T | A | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117|119 | A | L|T|E | false | false | 35.653038 | 10.478571 | 17,093 | ProTherm | 7 | Urea | MOPS | 30000.0 | 25 | 1YGW_A:T91A 1YGW_A:T93V | null | null | 2.9 | null | null | null | null | 2.35 | 1.21 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91A 1YGW_A:T93V"... | [{"datasets":[],"id":62920,"numValue":2.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62921,"numValue":1.21,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62922,"numValue":2.35,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":62923,"numValue":2.0,"references":[],"st... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1268 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,268 | train | mutant | 7,692 | 30 | 8,395 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117V|T119A | T117V|T119A | 2 | 2 | 0 | 0 | 117 | T | V | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117|119 | A | L|T|E | false | false | 35.653038 | 10.478571 | 16,308 | ProTherm | 7 | DSC | Thermal | MOPS | 30000.0 | null | 1YGW_A:T91V 1YGW_A:T93A | 38.5 | -14 | null | 4.3 | 92 | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91V 1YGW_A:T93A","ty... | [{"datasets":[],"id":59780,"numValue":38.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":59781,"numValue":-14.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":59782,"numValue":92.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":59783,"numValue":4.3,"references":[]... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1269 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,269 | train | mutant | 7,692 | 30 | 8,395 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117V|T119A | T117V|T119A | 2 | 2 | 0 | 0 | 117 | T | V | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117|119 | A | L|T|E | false | false | 35.653038 | 10.478571 | 17,094 | ProTherm | 7 | Urea | MOPS | 30000.0 | 25 | 1YGW_A:T91V 1YGW_A:T93A | null | null | 2.5 | null | null | null | null | 1.9 | 1.33 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91V 1YGW_A:T93A"... | [{"datasets":[],"id":62925,"numValue":2.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62926,"numValue":1.33,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62927,"numValue":1.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":62928,"numValue":2.0,"references":[],"str... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1271 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,271 | train | mutant | 7,693 | 30 | 8,396 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T117V|T119V | T117V|T119V | 2 | 2 | 0 | 0 | 117 | T | V | 9 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 117|119 | A | L|T|E | false | false | 35.653038 | 10.478571 | 17,095 | ProTherm | 7 | Urea | MOPS | 30000.0 | 25 | 1YGW_A:T91V 1YGW_A:T93V | null | null | 2.9 | null | null | null | null | 2.19 | 1.32 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T91V 1YGW_A:T93V"... | [{"datasets":[],"id":62930,"numValue":2.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62931,"numValue":1.32,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62932,"numValue":2.19,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":62933,"numValue":2.0,"references":[],"st... | [{"id":6564,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1273 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,273 | train | mutant | 34 | 30 | 36 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | H118A | H118A | 1 | 1 | 0 | 0 | 118 | H | A | 9 | ACTIVE_SITE|CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 118 | A | L|S | false | true | 46.181261 | 12.403 | 8,553 | ProTherm | 6 | DSC | Thermal | sodium acetate, calcium acetate | 20 mM, 2 mM | 25 | Mops | 50 mM | 1RN1_A:H92A | null | null | null | 0.62 | null | 0.98 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_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 | 3 | ARTICLE | X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1. | 1,994 | 10.1111/j.1432-1033.1994.tb18652.x | 8125111 | Eur J Biochem;220;527-34 | 4 | Schluckebier G|Backmann J|Granzin J|Schubert W D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate, calcium acetate","type":"BUFFER"},{"numValue":null,"strValue":"... | [{"datasets":[],"id":29025,"numValue":0.98,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":29026,"numValue":0.62,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29027,... | [{"id":5,"numValue":null,"position":118,"positionArray":null,"positionRange":null,"strValue":"Proton donor","type":"ACTIVE_SITE"},{"id":6565,"numValue":9.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1274 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,274 | train | mutant | 34 | 30 | 36 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | H118A | H118A | 1 | 1 | 0 | 0 | 118 | H | A | 9 | ACTIVE_SITE|CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 118 | A | L|S | false | true | 46.181261 | 12.403 | 8,559 | ProTherm | 6 | DSC | Thermal | sodium acetate, calcium acetate | 20 mM, 2 mM | 25 | Mops | 50 mM | 1RN1_A:H92A | null | null | 7.19 | null | null | 0.98 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 3 | ARTICLE | X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1. | 1,994 | 10.1111/j.1432-1033.1994.tb18652.x | 8125111 | Eur J Biochem;220;527-34 | 4 | Schluckebier G|Backmann J|Granzin J|Schubert W D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate, calcium acetate","type":"BUFFER"},{"numValue":null,"strValue":"... | [{"datasets":[],"id":29043,"numValue":0.98,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29044,"numValue":7.19,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29045,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":5,"numValue":null,"position":118,"positionArray":null,"positionRange":null,"strValue":"Proton donor","type":"ACTIVE_SITE"},{"id":6565,"numValue":9.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1275 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,275 | train | mutant | 2,310 | 30 | 2,638 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T119A | T119A | 1 | 1 | 0 | 0 | 119 | T | A | 8 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 119 | A | T | false | false | 69.036731 | 11.087857 | 4,599 | ProTherm | 7 | DSC | Thermal | MOPS | 30000.0 | null | 1YGW_A:T93A | 50.2 | -2.3 | null | 0.7 | 104 | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T93A","type":"_PDB_CH... | [{"datasets":[],"id":17036,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":17037,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17038,"numValue":104.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":17039,"numValue":0.7,"references":[]... | [{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1276 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,276 | train | mutant | 2,310 | 30 | 2,638 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T119A | T119A | 1 | 1 | 0 | 0 | 119 | T | A | 8 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 119 | A | T | false | false | 69.036731 | 11.087857 | 11,512 | ProTherm | 7 | Urea | MOPS | 30000.0 | 25 | 1YGW_A:T93A | null | null | 4.1 | null | null | null | null | 4.46 | 0.91 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T93A","type":"_PD... | [{"datasets":[],"id":39737,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39738,"numValue":0.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":39739,"numValue":4.46,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":39740,"numValue":2.0,"references":[],"st... | [{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1277 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,277 | train | mutant | 2,311 | 30 | 2,639 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T119V | T119V | 1 | 1 | 0 | 0 | 119 | T | V | 8 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 119 | A | T | false | false | 69.036731 | 11.087857 | 4,600 | ProTherm | 7 | DSC | Thermal | MOPS | 30000.0 | null | 1YGW_A:T93V | 49.3 | -3.2 | null | 1 | 97 | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T93V","type":"_PDB_CH... | [{"datasets":[],"id":17042,"numValue":49.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":17043,"numValue":-3.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17044,"numValue":97.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":17045,"numValue":1.0,"references":[],... | [{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1278 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,278 | train | mutant | 2,311 | 30 | 2,639 | 130 | 130 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | T119V | T119V | 1 | 1 | 0 | 0 | 119 | T | V | 8 | CONSERVATION | 1YGW|1RN1|9RNT | 135|350|420 | null | 119 | A | T | false | false | 69.036731 | 11.087857 | 11,513 | ProTherm | 7 | Urea | MOPS | 30000.0 | 25 | 1YGW_A:T93V | null | null | 5 | null | null | null | null | 4.16 | 1.2 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 447 | ARTICLE | Contribution of hydrogen bonds to protein stability. | 2,014 | 10.1002/pro.2449 | 24591301 | Protein Sci;23;652-61 | 17 | Takano Kazufumi|Scholtz J Martin|Pace C Nick|Trevino Saul R|Thurlkill Richard L|Fu Hailong|Lee Fryar Katrina|Landua John|Schell David|Imura Satoshi|Gajiwala Ketan|Sevcik Jozef|Urbanikova Lubica|Myers Jeffery K|Hebert Eric J|Shirley Bret A|Grimsley Gerald R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":30000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"1YGW_A:T93V","type":"_PD... | [{"datasets":[],"id":39742,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39743,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":39744,"numValue":4.16,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":39745,"numValue":2.0,"references":[],"str... | [{"id":6566,"numValue":8.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1279 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,279 | train | sequence | 37 | 37 | -1 | 214 | -1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,433 | ProTherm | 7.2 | DSC | Thermal | HEPES | 0.05 mM | null | 51.8 | null | null | null | 95 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 4 | ARTICLE | Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase. | 1,991 | 1748642 | J Biol Chem;266;23654-9 | 5 | Reinstein J|Rose T|Glaser P|Surewicz W K|Mantsch H H | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64351,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64352,"numValue":95.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64353,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:1280 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,280 | train | sequence | 37 | 37 | -1 | 214 | -1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,368 | ProTherm | 7.4 | DSC | Thermal | HEPES | 50 mM | null | 51.8 | null | null | null | 95 | null | 158 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 287 | ARTICLE | Structural and catalytic role of arginine 88 in Escherichia coli adenylate kinase as evidenced by chemical modification and site-directed mutagenesis. | 1,989 | 2542263 | J Biol Chem;264;8107-12 | 5 | Reinstein J|Rose T|Wittinghofer A|Saint Girons I|Gilles A M | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67779,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67780,"numValue":95.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67781,"numValue":158.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67782,"numValue":null,"references":... | ||||||||||||||||||||||||||
fireprotdb:1281 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,281 | train | sequence | 37 | 37 | -1 | 214 | -1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,967 | ProTherm | 7.5 | Intensity | Thermal | HEPES | 20mM | null | 42.55 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1776 | ARTICLE | Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability. | 2,017 | 10.1126/science.aai7825 | 28232526 | Science;355; | 8 | Leuenberger Pascal|Ganscha Stefan|Kahraman Abdullah|Cappelletti Valentina|Boersema Paul J|von Mering Christian|Claassen Manfred|Picotti Paola | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Intensity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"20mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":88129,"numValue":42.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88130,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":88131,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1282 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,282 | train | mutant | 37 | 37 | 40 | 214 | 214 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | D84H | D84H | 1 | 1 | 0 | 0 | 84 | D | H | 9 | CONSERVATION | 1ANK | 295 | null | 84 | A | E | true | true | 13.345868 | 7.222222 | 37 | ProTherm | 7.2 | DSC | Thermal | HEPES | 0.05 mM | null | 1ANK_A:D84H | 44.6 | -7.2 | null | null | 63 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 4 | ARTICLE | Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase. | 1,991 | 1748642 | J Biol Chem;266;23654-9 | 5 | Reinstein J|Rose T|Glaser P|Surewicz W K|Mantsch H H | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1ANK_A:D84H","type":"_PDB... | [{"datasets":[],"id":117,"numValue":44.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":118,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":119,"numValue":63.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12... | [{"id":6661,"numValue":9.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1283 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,283 | train | mutant | 37 | 37 | 40 | 214 | 214 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | D84H | D84H | 1 | 1 | 0 | 0 | 84 | D | H | 9 | CONSERVATION | 1ANK | 295 | null | 84 | A | E | true | true | 13.345868 | 7.222222 | 7,496 | ProTherm | 7.2 | DSC | Thermal | HEPES | 0.05 mM | 51.8 | 1ANK_A:D84H | null | null | null | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 4 | ARTICLE | Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase. | 1,991 | 1748642 | J Biol Chem;266;23654-9 | 5 | Reinstein J|Rose T|Glaser P|Surewicz W K|Mantsch H H | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":51.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CO... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25988,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25989,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6661,"numValue":9.0,"position":84,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1284 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,284 | train | mutant | 35 | 37 | 38 | 214 | 214 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | G85V | G85V | 1 | 1 | 0 | 0 | 85 | G | V | 9 | BINDING_SITE|CONSERVATION | 1ANK | 295 | null | 85 | A | S | true | true | 7.650576 | 3.84 | 35 | ProTherm | 7.2 | DSC | Thermal | HEPES | 0.05 mM | null | 1ANK_A:G85V | 40.7 | -11.1 | null | null | 70 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 4 | ARTICLE | Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase. | 1,991 | 1748642 | J Biol Chem;266;23654-9 | 5 | Reinstein J|Rose T|Glaser P|Surewicz W K|Mantsch H H | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1ANK_A:G85V","type":"_PDB... | [{"datasets":[],"id":109,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":110,"numValue":-11.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":111,"numValue":70.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1... | [{"id":10,"numValue":null,"position":null,"positionArray":null,"positionRange":[85,88],"strValue":null,"type":"BINDING_SITE"},{"id":6662,"numValue":9.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1285 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,285 | train | mutant | 35 | 37 | 38 | 214 | 214 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | G85V | G85V | 1 | 1 | 0 | 0 | 85 | G | V | 9 | BINDING_SITE|CONSERVATION | 1ANK | 295 | null | 85 | A | S | true | true | 7.650576 | 3.84 | 7,497 | ProTherm | 7.2 | DSC | Thermal | HEPES | 0.05 mM | 51.8 | 1ANK_A:G85V | null | null | null | 2.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 4 | ARTICLE | Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase. | 1,991 | 1748642 | J Biol Chem;266;23654-9 | 5 | Reinstein J|Rose T|Glaser P|Surewicz W K|Mantsch H H | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":51.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CO... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25990,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25991,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":10,"numValue":null,"position":null,"positionArray":null,"positionRange":[85,88],"strValue":null,"type":"BINDING_SITE"},{"id":6662,"numValue":9.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1286 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,286 | train | mutant | 36 | 37 | 39 | 214 | 214 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | F86L | F86L | 1 | 1 | 0 | 0 | 86 | F | L | 8 | BINDING_SITE|CONSERVATION | 1ANK | 295 | null | 86 | A | L | true | true | 4.115483 | 3.041667 | 36 | ProTherm | 7.2 | DSC | Thermal | HEPES | 0.05 mM | null | 1ANK_A:F86L | 49.2 | -2.6 | null | null | 97 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 4 | ARTICLE | Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase. | 1,991 | 1748642 | J Biol Chem;266;23654-9 | 5 | Reinstein J|Rose T|Glaser P|Surewicz W K|Mantsch H H | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1ANK_A:F86L","type":"_PDB... | [{"datasets":[],"id":113,"numValue":49.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":114,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":115,"numValue":97.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11... | [{"id":10,"numValue":null,"position":null,"positionArray":null,"positionRange":[85,88],"strValue":null,"type":"BINDING_SITE"},{"id":6663,"numValue":8.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1287 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,287 | train | mutant | 36 | 37 | 39 | 214 | 214 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | F86L | F86L | 1 | 1 | 0 | 0 | 86 | F | L | 8 | BINDING_SITE|CONSERVATION | 1ANK | 295 | null | 86 | A | L | true | true | 4.115483 | 3.041667 | 7,498 | ProTherm | 7.2 | DSC | Thermal | HEPES | 0.05 mM | 51.8 | 1ANK_A:F86L | null | null | null | 0.8 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 4 | ARTICLE | Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase. | 1,991 | 1748642 | J Biol Chem;266;23654-9 | 5 | Reinstein J|Rose T|Glaser P|Surewicz W K|Mantsch H H | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":51.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CO... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25992,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25993,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":10,"numValue":null,"position":null,"positionArray":null,"positionRange":[85,88],"strValue":null,"type":"BINDING_SITE"},{"id":6663,"numValue":8.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1288 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,288 | train | mutant | 1,665 | 37 | 1,874 | 214 | 214 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | R88G | R88G | 1 | 1 | 0 | 0 | 88 | R | G | 9 | BINDING_SITE|CONSERVATION | 1ANK | 295 | null | 88 | A | L | true | true | 74.834544 | 3.523529 | 3,114 | ProTherm | 7.4 | DSC | Thermal | HEPES | 50 mM | null | 1ANK_A:R88G | 51 | -0.8 | null | null | 75 | null | 161 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S2204.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1791.csv|STRUM_Q3421.csv|Bro... | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 287 | ARTICLE | Structural and catalytic role of arginine 88 in Escherichia coli adenylate kinase as evidenced by chemical modification and site-directed mutagenesis. | 1,989 | 2542263 | J Biol Chem;264;8107-12 | 5 | Reinstein J|Rose T|Wittinghofer A|Saint Girons I|Gilles A M | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1ANK_A:R88G","type":"_PDB_C... | [{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S2204.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":11338,"numValue":51.0,"references":[],... | [{"id":10,"numValue":null,"position":null,"positionArray":null,"positionRange":[85,88],"strValue":null,"type":"BINDING_SITE"},{"id":6665,"numValue":9.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1289 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,289 | train | mutant | 1,665 | 37 | 1,874 | 214 | 214 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | 3 | Adenylate kinase | Escherichia coli (strain K12) | 1 | P69441 | IPR006259|IPR000850|IPR033690|IPR007862|IPR027417 | 2.7.4.3 | R88G | R88G | 1 | 1 | 0 | 0 | 88 | R | G | 9 | BINDING_SITE|CONSERVATION | 1ANK | 295 | null | 88 | A | L | true | true | 74.834544 | 3.523529 | 7,505 | ProTherm | 7.4 | DSC | Thermal | HEPES | 50 mM | 51.8 | 1ANK_A:R88G | null | null | null | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 287 | ARTICLE | Structural and catalytic role of arginine 88 in Escherichia coli adenylate kinase as evidenced by chemical modification and site-directed mutagenesis. | 1,989 | 2542263 | J Biol Chem;264;8107-12 | 5 | Reinstein J|Rose T|Wittinghofer A|Saint Girons I|Gilles A M | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":51.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26012,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26013,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":10,"numValue":null,"position":null,"positionArray":null,"positionRange":[85,88],"strValue":null,"type":"BINDING_SITE"},{"id":6665,"numValue":9.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,290 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,466 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | null | KCl | 0.025 M | 51.8 | null | null | null | null | 2.5 | 118.8 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.020 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type"... | [{"datasets":[],"id":64453,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64454,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64455,"numValue":118.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":64456,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1291 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,291 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,473 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 50.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":64471,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64472,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1292 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,292 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,474 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 66.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":64473,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64474,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1293 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,293 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,511 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 51.65 | null | null | null | null | null | 118 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":64588,"numValue":51.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64589,"numValue":118.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":64590,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,294 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,512 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | null | KCl | 0.15 M | 62.2 | null | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64591,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64592,"numValue":127.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":64593,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1295 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,295 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,590 | ProTherm | 1.6 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 32.92 | null | null | null | 78.5 | 3.38 | 86.35 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":1.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64866,"numValue":32.92,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64867,"numValue":78.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64868,"numValue":3.38,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64869,"numValue":86.35,"references":... | |||||||||||||||||||||||
fireprotdb:1296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,296 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,591 | ProTherm | 1.8 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 35.51 | null | null | null | 83 | 2.38 | 83.83 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":1.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64871,"numValue":35.51,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64872,"numValue":83.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64873,"numValue":2.38,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64874,"numValue":83.83,"references":... | |||||||||||||||||||||||
fireprotdb:1297 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,297 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,592 | ProTherm | 1.8 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 35.61 | null | null | null | 87.7 | 2.47 | 88.58 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":1.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64876,"numValue":35.61,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64877,"numValue":87.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64878,"numValue":2.47,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64879,"numValue":88.58,"references":... | |||||||||||||||||||||||
fireprotdb:1298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,298 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,593 | ProTherm | 1.8 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 35.5 | null | null | null | 87.5 | 2.8 | 88.38 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":1.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64881,"numValue":35.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64882,"numValue":87.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64883,"numValue":2.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64884,"numValue":88.38,"references":[]... | |||||||||||||||||||||||
fireprotdb:1299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,299 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,594 | ProTherm | 1.8 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 35.66 | null | null | null | 87.3 | 2.67 | 88.17 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":1.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64886,"numValue":35.66,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64887,"numValue":87.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64888,"numValue":2.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64889,"numValue":88.17,"references":... | |||||||||||||||||||||||
fireprotdb:1300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,300 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,595 | ProTherm | 1.8 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 35.72 | null | null | null | 87.9 | 3.03 | 88.78 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":1.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64891,"numValue":35.72,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64892,"numValue":87.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64893,"numValue":3.03,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64894,"numValue":88.78,"references":... | |||||||||||||||||||||||
fireprotdb:1301 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,301 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,596 | ProTherm | 2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 39.1 | null | null | null | 95.7 | 1.93 | 88.96 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64896,"numValue":39.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64897,"numValue":95.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64898,"numValue":1.93,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64899,"numValue":88.96,"references":[... | |||||||||||||||||||||||
fireprotdb:1302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,302 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,597 | ProTherm | 2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 38.35 | null | null | null | 98.5 | 2.84 | 89.64 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64901,"numValue":38.35,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64902,"numValue":98.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64903,"numValue":2.84,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64904,"numValue":89.64,"references":... | |||||||||||||||||||||||
fireprotdb:1303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,303 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,598 | ProTherm | 2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 39.17 | null | null | null | 98.5 | 1.99 | 89.64 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64906,"numValue":39.17,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64907,"numValue":98.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64908,"numValue":1.99,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64909,"numValue":89.64,"references":... | |||||||||||||||||||||||
fireprotdb:1304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,304 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,599 | ProTherm | 2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 37.89 | null | null | null | 93.1 | 2.9 | 87.51 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64911,"numValue":37.89,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64912,"numValue":93.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64913,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64914,"numValue":87.51,"references":[... | |||||||||||||||||||||||
fireprotdb:1305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,305 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,600 | ProTherm | 2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 38.71 | null | null | null | 99.7 | 1.95 | 90.73 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64916,"numValue":38.71,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64917,"numValue":99.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64918,"numValue":1.95,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64919,"numValue":90.73,"references":... | |||||||||||||||||||||||
fireprotdb:1306 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,306 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,601 | ProTherm | 2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 39.22 | null | null | null | 96.9 | 2.59 | 88.18 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64921,"numValue":39.22,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64922,"numValue":96.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64923,"numValue":2.59,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64924,"numValue":88.18,"references":... | |||||||||||||||||||||||
fireprotdb:1307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,307 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,602 | ProTherm | 2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 38.81 | null | null | null | 96.9 | 2.59 | 88.18 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64926,"numValue":38.81,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64927,"numValue":96.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64928,"numValue":2.59,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64929,"numValue":88.18,"references":... | |||||||||||||||||||||||
fireprotdb:1308 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,308 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,603 | ProTherm | 2.2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 40.55 | null | null | null | 101.9 | 2.27 | 90.69 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64931,"numValue":40.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64932,"numValue":101.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64933,"numValue":2.27,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64934,"numValue":90.69,"references"... | |||||||||||||||||||||||
fireprotdb:1309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,309 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,604 | ProTherm | 2.34 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 42.94 | null | null | null | 111.3 | 2.53 | 93.49 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.34,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":[],"id":64936,"numValue":42.94,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64937,"numValue":111.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64938,"numValue":2.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64939,"numValue":93.49,"references"... | |||||||||||||||||||||||
fireprotdb:1310 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,310 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,605 | ProTherm | 2.4 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 43.5 | null | null | null | 114.3 | 2.44 | 102.87 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64941,"numValue":43.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64942,"numValue":114.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64943,"numValue":2.44,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64944,"numValue":102.87,"references"... | |||||||||||||||||||||||
fireprotdb:1311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,311 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,606 | ProTherm | 2.4 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 43.67 | null | null | null | 114.1 | 2.59 | 98.13 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64946,"numValue":43.67,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64947,"numValue":114.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64948,"numValue":2.59,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64949,"numValue":98.13,"references"... | |||||||||||||||||||||||
fireprotdb:1312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,312 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,607 | ProTherm | 2.4 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 43.93 | null | null | null | 114.3 | 2.43 | 98.3 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64951,"numValue":43.93,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64952,"numValue":114.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64953,"numValue":2.43,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64954,"numValue":98.3,"references":... | |||||||||||||||||||||||
fireprotdb:1313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,313 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,608 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 44.18 | null | null | null | 114.3 | 2.56 | 100.58 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64956,"numValue":44.18,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64957,"numValue":114.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64958,"numValue":2.56,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64959,"numValue":100.58,"references... | |||||||||||||||||||||||
fireprotdb:1314 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,314 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,609 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 44.92 | null | null | null | 113.1 | 1.9 | 98.4 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64961,"numValue":44.92,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64962,"numValue":113.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64963,"numValue":1.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64964,"numValue":98.4,"references":[... | |||||||||||||||||||||||
fireprotdb:1315 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,315 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,610 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 45.22 | null | null | null | 118.4 | 1.78 | 97.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64966,"numValue":45.22,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64967,"numValue":118.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64968,"numValue":1.78,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64969,"numValue":97.09,"references"... | |||||||||||||||||||||||
fireprotdb:1316 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,316 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,611 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 45.16 | null | null | null | 113.7 | 2.43 | 90.96 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64971,"numValue":45.16,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64972,"numValue":113.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64973,"numValue":2.43,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64974,"numValue":90.96,"references"... | |||||||||||||||||||||||
fireprotdb:1317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,317 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,612 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 45.66 | null | null | null | 113.3 | 2.11 | 91.77 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64976,"numValue":45.66,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64977,"numValue":113.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64978,"numValue":2.11,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64979,"numValue":91.77,"references"... | |||||||||||||||||||||||
fireprotdb:1318 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,318 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,613 | ProTherm | 2.7 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 48.37 | null | null | null | 117.2 | 2.16 | 107.82 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64981,"numValue":48.37,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64982,"numValue":117.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64983,"numValue":2.16,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64984,"numValue":107.82,"references... | |||||||||||||||||||||||
fireprotdb:1319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,319 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,614 | ProTherm | 2.7 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 48.45 | null | null | null | 115.2 | 2.27 | 108.29 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64986,"numValue":48.45,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64987,"numValue":115.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64988,"numValue":2.27,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64989,"numValue":108.29,"references... | |||||||||||||||||||||||
fireprotdb:1320 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,320 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,615 | ProTherm | 2.7 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 48.65 | null | null | null | 116.7 | 2.52 | 101.53 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64991,"numValue":48.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64992,"numValue":116.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64993,"numValue":2.52,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64994,"numValue":101.53,"references... | |||||||||||||||||||||||
fireprotdb:1321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,321 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,616 | ProTherm | 2.7 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 48.75 | null | null | null | 113.9 | 2.23 | 100.23 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64996,"numValue":48.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64997,"numValue":113.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64998,"numValue":2.23,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64999,"numValue":100.23,"references... | |||||||||||||||||||||||
fireprotdb:1322 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,322 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,617 | ProTherm | 2.7 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 48.9 | null | null | null | 110.7 | 2.47 | 100.74 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":65001,"numValue":48.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65002,"numValue":110.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65003,"numValue":2.47,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65004,"numValue":100.74,"references"... | |||||||||||||||||||||||
fireprotdb:1323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,323 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,618 | ProTherm | 2.7 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 49.06 | null | null | null | 113.9 | 2.34 | 95.68 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":65006,"numValue":49.06,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65007,"numValue":113.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65008,"numValue":2.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65009,"numValue":95.68,"references"... | |||||||||||||||||||||||
fireprotdb:1324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,324 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,619 | ProTherm | 2.84 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 51.76 | null | null | null | 123.4 | 2.54 | 111.06 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.84,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":[],"id":65011,"numValue":51.76,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65012,"numValue":123.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65013,"numValue":2.54,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65014,"numValue":111.06,"references... | |||||||||||||||||||||||
fireprotdb:1325 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,325 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,620 | ProTherm | 2.84 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 51.59 | null | null | null | 123.8 | 2.46 | 102.75 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.84,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":[],"id":65016,"numValue":51.59,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65017,"numValue":123.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65018,"numValue":2.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65019,"numValue":102.75,"references... | |||||||||||||||||||||||
fireprotdb:1326 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,326 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,687 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 65.15 | null | null | null | null | 3.5 | 134 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":65351,"numValue":65.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65352,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65353,"numValue":134.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":65354,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:1327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,327 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,688 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 62.19 | null | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":[],"id":65355,"numValue":62.19,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65356,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65357,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1328 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,328 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,790 | ProTherm | 2 | CD | Thermal | Unknown | null | 46.85 | null | null | null | null | 2.1 | 122 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER | 22 | ARTICLE | Mutations and protein stability. | 1,981 | 10.1002/bip.1981.360200921 | 7306671 | Biopolymers;20;1989-99 | 4 | Lindorfer M|Hawkes R|Grutter M|Schellman J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"}] | [{"datasets":[],"id":65693,"numValue":46.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65694,"numValue":2.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65695,"numValue":122.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":65696,"numValue":null,"references"... | ||||||||||||||||||||||||||
fireprotdb:1329 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,329 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,791 | ProTherm | 3 | CD | Thermal | Unknown | null | 46.85 | null | null | null | null | 2.26 | 77.9 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER | 22 | ARTICLE | Mutations and protein stability. | 1,981 | 10.1002/bip.1981.360200921 | 7306671 | Biopolymers;20;1989-99 | 4 | Lindorfer M|Hawkes R|Grutter M|Schellman J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"}] | [{"datasets":[],"id":65697,"numValue":46.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65698,"numValue":2.26,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65699,"numValue":77.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":65700,"numValue":null,"references"... | ||||||||||||||||||||||||||
fireprotdb:1331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,331 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,793 | ProTherm | 3 | CD | Thermal | Unknown | null | 59 | null | null | null | null | 2.26 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER | 22 | ARTICLE | Mutations and protein stability. | 1,981 | 10.1002/bip.1981.360200921 | 7306671 | Biopolymers;20;1989-99 | 4 | Lindorfer M|Hawkes R|Grutter M|Schellman J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"}] | [{"datasets":[],"id":65704,"numValue":59.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65705,"numValue":2.26,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65706,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] |
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