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:8585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,585 | train | mutant | 931 | 158 | 1,053 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | N98A | N98A | 1 | 1 | 0 | 0 | 98 | N | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 98 | A | T|S | true | true | 29.704468 | 6.544375 | 1,685 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:N97A | 55.15 | -0.7 | null | null | 48.7 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6284,"numValue":55.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6285,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6286,"numValue":48.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6287,"numValue":3.0,"references":[],"st... | [{"id":9478,"numValue":7.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,586 | train | mutant | 931 | 158 | 1,053 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | N98A | N98A | 1 | 1 | 0 | 0 | 98 | N | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 98 | A | T|S | true | true | 29.704468 | 6.544375 | 7,930 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:N97A | null | null | null | 0.22 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27096,"numValue":0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27097,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27098,"numValue":null,"references":[],"strValue":"yes","... | [{"id":9478,"numValue":7.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,588 | train | mutant | 931 | 158 | 1,053 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | N98A | N98A | 1 | 1 | 0 | 0 | 98 | N | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 98 | A | T|S | true | true | 29.704468 | 6.544375 | 9,326 | ProTherm | 7 | CD | Urea | MOPS | 50 mM | 25 | NaCl | 15 mM | 1FTG_A:N97A | null | null | null | 0.83 | null | null | null | 1.86 | 2.27 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":31830,"numValue":0.83,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31831,"numValue":2.27,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31832,"numValue":1.86,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31833,"numValue":null,"references":[],... | [{"id":9478,"numValue":7.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,589 | train | mutant | 932 | 158 | 1,054 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q100A | Q100A | 1 | 1 | 0 | 0 | 100 | Q | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 100 | A | T | true | true | 0.614469 | 5.396111 | 1,668 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:Q99A | 49.35 | 5.2 | null | null | null | null | 52.7 | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6199,"numValue":49.35,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6200,"numValue":5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6201,"numValue":52.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":6202,"numValue":3.0,"references":[],"s... | [{"id":9480,"numValue":7.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,590 | train | mutant | 932 | 158 | 1,054 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q100A | Q100A | 1 | 1 | 0 | 0 | 100 | Q | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 100 | A | T | true | true | 0.614469 | 5.396111 | 1,686 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:Q99A | 58.15 | 2.3 | null | null | 56.2 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6289,"numValue":58.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6290,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6291,"numValue":56.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6292,"numValue":3.0,"references":[],"str... | [{"id":9480,"numValue":7.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,591 | train | mutant | 932 | 158 | 1,054 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q100A | Q100A | 1 | 1 | 0 | 0 | 100 | Q | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 100 | A | T | true | true | 0.614469 | 5.396111 | 1,992 | ProTherm | 7 | Fluorescence, CD | Thermal | Mops | 50 mM | null | NaCl | 0.5 M | 1FTG_A:Q99A | 51.75 | 8.5 | null | null | null | null | 17.8 | null | null | null | null | null | null | null | null | null | Yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|PON-TStab_dataset.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence, CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"I... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7410,"numValue":51.... | [{"id":9480,"numValue":7.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,592 | train | mutant | 932 | 158 | 1,054 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q100A | Q100A | 1 | 1 | 0 | 0 | 100 | Q | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 100 | A | T | true | true | 0.614469 | 5.396111 | 7,931 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:Q99A | null | null | null | -0.85 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":[],"id":27099,"numValue":-0.85,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27100,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27101,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9480,"numValue":7.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,593 | train | mutant | 932 | 158 | 1,054 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q100A | Q100A | 1 | 1 | 0 | 0 | 100 | Q | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 100 | A | T | true | true | 0.614469 | 5.396111 | 7,949 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:Q99A | null | null | null | -0.49 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":27153,"numValue":-0.49,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27154,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27155,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9480,"numValue":7.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,594 | train | mutant | 932 | 158 | 1,054 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q100A | Q100A | 1 | 1 | 0 | 0 | 100 | Q | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 100 | A | T | true | true | 0.614469 | 5.396111 | 8,003 | ProTherm | 7 | Fluorescence, CD | Thermal | Mops | 50 mM | 43.4 | NaCl | 0.5 M | 1FTG_A:Q99A | null | null | null | -0.43 | null | 0.34 | null | null | null | null | null | null | null | null | null | null | Yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":43.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence, CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":27312,"numValue":0.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv"],"id":27313,"numValue":-0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27314,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9480,"numValue":7.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,595 | train | mutant | 932 | 158 | 1,054 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q100A | Q100A | 1 | 1 | 0 | 0 | 100 | Q | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 100 | A | T | true | true | 0.614469 | 5.396111 | 8,488 | ProTherm | 7 | Fluorescence | Urea | Mops | 50 mM | 25.2 | NaCl | 0.5 M | 1FTG_A:Q99A | null | null | null | -0.24 | null | null | null | 1 | null | null | null | null | null | null | null | null | Yes | DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.2,"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":"50 mM","type":"BUFFER... | [{"datasets":[],"id":28869,"numValue":-0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28870,"numValue":1.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28871,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9480,"numValue":7.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,596 | train | mutant | 932 | 158 | 1,054 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q100A | Q100A | 1 | 1 | 0 | 0 | 100 | Q | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 100 | A | T | true | true | 0.614469 | 5.396111 | 9,327 | ProTherm | 7 | CD | Urea | MOPS | 50 mM | 25 | NaCl | 15 mM | 1FTG_A:Q99A | null | null | null | -1.72 | null | null | null | 2.33 | 2.9 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":31834,"numValue":-1.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31835,"numValue":2.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31836,"numValue":2.33,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31837,"numValue":null,"references":[],... | [{"id":9480,"numValue":7.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,597 | train | mutant | 1,111 | 158 | 1,252 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102V | A102V | 1 | 1 | 0 | 0 | 102 | A | V | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 1,993 | ProTherm | 7 | Fluorescence, CD | Thermal | Mops | 50 mM | null | NaCl | 0.5 M | 1FTG_A:A101V | 48.65 | 5.4 | null | null | null | null | 10.5 | null | null | null | null | null | null | null | null | null | Yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|EASE-MM_S1676.csv|M47andM8_S1810.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence, CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"I... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv"],"id":7414,"numValue":48.65,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.c... | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,598 | train | mutant | 1,111 | 158 | 1,252 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102V | A102V | 1 | 1 | 0 | 0 | 102 | A | V | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 2,366 | ProTherm | 7 | Abs, CD, Fluorescence | Thermal | Mops | 5-50 mM | null | NaCl | 15 mM | 1FLV_A:A101V | 53.05 | null | null | null | null | null | 43.6 | null | null | null | null | null | null | null | null | null | Yes | 2.0 | TM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 222 | ARTICLE | Filling small, empty protein cavities: structural and energetic consequences. | 2,006 | 10.1016/j.jmb.2006.02.060 | 16563433 | J Mol Biol;358;701-12 | 4 | Sancho Javier|Bueno Marta|Cremades Nunilo|Neira Jos? Luis | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Abs, CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"5-50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","t... | [{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_... | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,599 | train | mutant | 1,111 | 158 | 1,252 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102V | A102V | 1 | 1 | 0 | 0 | 102 | A | V | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 7,969 | ProTherm | 7 | Abs, CD, Fluorescence | Thermal | Mops | 5-50 mM | 44.3 | NaCl | 15 mM | 1FLV_A:A101V | null | null | null | 0.69 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 222 | ARTICLE | Filling small, empty protein cavities: structural and energetic consequences. | 2,006 | 10.1016/j.jmb.2006.02.060 | 16563433 | J Mol Biol;358;701-12 | 4 | Sancho Javier|Bueno Marta|Cremades Nunilo|Neira Jos? Luis | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Abs, CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"5-50 mM",... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":27210,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27211,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27212,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,600 | train | mutant | 1,111 | 158 | 1,252 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102V | A102V | 1 | 1 | 0 | 0 | 102 | A | V | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 8,004 | ProTherm | 7 | Fluorescence, CD | Thermal | Mops | 50 mM | 43.4 | NaCl | 0.5 M | 1FTG_A:A101V | null | null | null | -0.16 | null | 0.34 | null | null | null | null | null | null | null | null | null | null | Yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":43.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence, CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":27315,"numValue":0.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27316,"numValue":-0.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27317,"numValue":null,"references":[],"strValue":"Yes","... | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,601 | train | mutant | 1,111 | 158 | 1,252 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102V | A102V | 1 | 1 | 0 | 0 | 102 | A | V | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 8,489 | ProTherm | 7 | Fluorescence | Urea | Mops | 50 mM | 25.2 | NaCl | 0.5 M | 1FTG_A:A101V | null | null | null | -0.22 | null | null | null | 0.97 | null | null | null | null | null | null | null | null | Yes | DDG|CM|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.2,"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":"50 mM","type":"BUFFER... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":28872,"numValue":-0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28873,"numValue":0.97,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28874,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,602 | train | mutant | 1,111 | 158 | 1,252 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102V | A102V | 1 | 1 | 0 | 0 | 102 | A | V | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 9,932 | ProTherm | 7 | Fluorescence | Urea | Mops | 50 mM | 25 | 1FLV_A:A101V | null | null | null | 0.32 | null | null | null | 1.95 | 2.43 | null | null | null | null | null | null | null | Yes | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 222 | ARTICLE | Filling small, empty protein cavities: structural and energetic consequences. | 2,006 | 10.1016/j.jmb.2006.02.060 | 16563433 | J Mol Biol;358;701-12 | 4 | Sancho Javier|Bueno Marta|Cremades Nunilo|Neira Jos? Luis | [{"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":"50 mM","type":"BUFFER... | [{"datasets":["SAAFEC_S1262.csv"],"id":34129,"numValue":0.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34130,"numValue":2.43,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34131,"numValue":1.95,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":34132,"numValue":nul... | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,603 | train | mutant | 1,204 | 158 | 1,350 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102L | A102L | 1 | 1 | 0 | 0 | 102 | A | L | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 2,367 | ProTherm | 7 | Abs, CD, Fluorescence | Thermal | Mops | 5-50 mM | null | NaCl | 15 mM | 1FLV_A:A101L | 56.35 | null | null | null | null | null | 36.4 | null | null | null | null | null | null | null | null | null | Yes | 2.0 | TM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|Saraboji_S2204.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 222 | ARTICLE | Filling small, empty protein cavities: structural and energetic consequences. | 2,006 | 10.1016/j.jmb.2006.02.060 | 16563433 | J Mol Biol;358;701-12 | 4 | Sancho Javier|Bueno Marta|Cremades Nunilo|Neira Jos? Luis | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Abs, CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"5-50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","t... | [{"datasets":["AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","Saraboji_S2204.csv"],"id":8664,"numValue":56.35,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M4... | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,604 | train | mutant | 1,204 | 158 | 1,350 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102L | A102L | 1 | 1 | 0 | 0 | 102 | A | L | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 7,970 | ProTherm | 7 | Abs, CD, Fluorescence | Thermal | Mops | 5-50 mM | 44.3 | NaCl | 15 mM | 1FLV_A:A101L | null | null | null | 0.53 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 222 | ARTICLE | Filling small, empty protein cavities: structural and energetic consequences. | 2,006 | 10.1016/j.jmb.2006.02.060 | 16563433 | J Mol Biol;358;701-12 | 4 | Sancho Javier|Bueno Marta|Cremades Nunilo|Neira Jos? Luis | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Abs, CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"5-50 mM",... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27213,"numValue":0.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27214,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27215,"numValue":null,"references":[],"strValue":"Yes","... | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,605 | train | mutant | 1,204 | 158 | 1,350 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | A102L | A102L | 1 | 1 | 0 | 0 | 102 | A | L | 8 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 102 | A | H | true | true | 1.519057 | 4.163 | 9,933 | ProTherm | 7 | Fluorescence | Urea | Mops | 50 mM | 25 | 1FLV_A:A101L | null | null | null | -0.08 | null | null | null | 2.12 | 2.42 | null | null | null | null | null | null | null | Yes | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 222 | ARTICLE | Filling small, empty protein cavities: structural and energetic consequences. | 2,006 | 10.1016/j.jmb.2006.02.060 | 16563433 | J Mol Biol;358;701-12 | 4 | Sancho Javier|Bueno Marta|Cremades Nunilo|Neira Jos? Luis | [{"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":"50 mM","type":"BUFFER... | [{"datasets":["SAAFEC_S1262.csv"],"id":34133,"numValue":-0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34134,"numValue":2.42,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34135,"numValue":2.12,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":34136,"numValue":nu... | [{"id":9482,"numValue":8.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,606 | train | mutant | 933 | 158 | 1,055 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I105V | I105V | 1 | 1 | 0 | 0 | 105 | I | V | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 105 | A | H | true | true | 43.639084 | 6.178125 | 1,669 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:I104V | 40.15 | -4 | null | null | null | null | 29.5 | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6204,"numValue":40.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6205,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6206,"numValue":29.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":6207,"numValue":3.0,"references":[],"... | [{"id":9485,"numValue":4.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,607 | train | mutant | 933 | 158 | 1,055 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I105V | I105V | 1 | 1 | 0 | 0 | 105 | I | V | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 105 | A | H | true | true | 43.639084 | 6.178125 | 1,687 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:I104V | 54.75 | -1.1 | null | null | 54.5 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6294,"numValue":54.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6295,"numValue":-1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6296,"numValue":54.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6297,"numValue":3.0,"references":[],"st... | [{"id":9485,"numValue":4.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,608 | train | mutant | 933 | 158 | 1,055 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I105V | I105V | 1 | 1 | 0 | 0 | 105 | I | V | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 105 | A | H | true | true | 43.639084 | 6.178125 | 7,932 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:I104V | null | null | null | 0.38 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":[],"id":27102,"numValue":0.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27103,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27104,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9485,"numValue":4.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,609 | train | mutant | 933 | 158 | 1,055 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I105V | I105V | 1 | 1 | 0 | 0 | 105 | I | V | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 105 | A | H | true | true | 43.639084 | 6.178125 | 7,950 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:I104V | null | null | null | 0.11 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":27156,"numValue":0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27157,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27158,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9485,"numValue":4.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,610 | train | mutant | 933 | 158 | 1,055 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I105V | I105V | 1 | 1 | 0 | 0 | 105 | I | V | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 105 | A | H | true | true | 43.639084 | 6.178125 | 9,328 | ProTherm | 7 | CD | Urea | MOPS | 50 mM | 25 | NaCl | 15 mM | 1FTG_A:I104V | null | null | null | 0.67 | null | null | null | 1.82 | 2.41 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":31838,"numValue":0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31839,"numValue":2.41,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31840,"numValue":1.82,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31841,"numValue":null,"references":[],... | [{"id":9485,"numValue":4.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,611 | train | mutant | 1,112 | 158 | 1,253 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | E108A | E108A | 1 | 1 | 0 | 0 | 108 | E | A | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 108 | A | H | true | false | 111.105305 | 16.658889 | 1,994 | ProTherm | 7 | Fluorescence, CD | Thermal | Mops | 50 mM | null | NaCl | 0.5 M | 1FTG_A:E107A | 45.95 | 2.7 | null | null | null | null | 17.5 | null | null | null | null | null | null | null | null | null | Yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|HotMuSiC_S1626.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence, CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"I... | [{"datasets":[],"id":7418,"numValue":45.95,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":7419,"numValue":2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv"... | [{"id":9488,"numValue":4.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,613 | train | mutant | 1,112 | 158 | 1,253 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | E108A | E108A | 1 | 1 | 0 | 0 | 108 | E | A | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 108 | A | H | true | false | 111.105305 | 16.658889 | 8,490 | ProTherm | 7 | Fluorescence | Urea | Mops | 50 mM | 25.2 | NaCl | 0.5 M | 1FTG_A:E107A | null | null | null | -0.23 | null | null | null | 0.98 | null | null | null | null | null | null | null | null | Yes | DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.2,"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":"50 mM","type":"BUFFER... | [{"datasets":[],"id":28875,"numValue":-0.23,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28876,"numValue":0.98,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28877,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9488,"numValue":4.0,"position":108,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,615 | train | mutant | 934 | 158 | 1,056 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | S111A | S111A | 1 | 1 | 0 | 0 | 111 | S | A | 1 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 111 | A | H | false | false | 36.774236 | 13.311667 | 1,688 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:S110A | 55.55 | -0.3 | null | null | 44.3 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6299,"numValue":55.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6300,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6301,"numValue":44.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6302,"numValue":3.0,"references":[],"st... | [{"id":9491,"numValue":1.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,616 | train | mutant | 934 | 158 | 1,056 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | S111A | S111A | 1 | 1 | 0 | 0 | 111 | S | A | 1 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 111 | A | H | false | false | 36.774236 | 13.311667 | 7,933 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:S110A | null | null | null | 0.18 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27105,"numValue":0.18,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27106,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27107,"numValue":null,"references":[],"strValue":"yes","... | [{"id":9491,"numValue":1.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,617 | train | mutant | 934 | 158 | 1,056 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | S111A | S111A | 1 | 1 | 0 | 0 | 111 | S | A | 1 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 111 | A | H | false | false | 36.774236 | 13.311667 | 7,951 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:S110A | null | null | null | 0.34 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":27159,"numValue":0.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27160,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27161,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9491,"numValue":1.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,618 | train | mutant | 934 | 158 | 1,056 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | S111A | S111A | 1 | 1 | 0 | 0 | 111 | S | A | 1 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 111 | A | H | false | false | 36.774236 | 13.311667 | 9,329 | ProTherm | 7 | CD | Urea | MOPS | 50 mM | 25 | NaCl | 15 mM | 1FTG_A:S110A | null | null | null | 1.03 | null | null | null | 1.79 | 2.25 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":31842,"numValue":1.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31843,"numValue":2.25,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31844,"numValue":1.79,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31845,"numValue":null,"references":[],... | [{"id":9491,"numValue":1.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,619 | train | mutant | 1,113 | 158 | 1,254 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q112G | Q112G | 1 | 1 | 0 | 0 | 112 | Q | G | 1 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 112 | A | H | true | false | 120.743707 | 20.878889 | 1,995 | ProTherm | 7 | Fluorescence, CD | Thermal | Mops | 50 mM | null | NaCl | 0.5 M | 1FTG_A:Q111G | 46.95 | 3.7 | null | null | null | null | 19.8 | null | null | null | null | null | null | null | null | null | Yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence, CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"I... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7422,"numValue":46.95,"references":[],... | [{"id":9492,"numValue":1.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,620 | train | mutant | 1,113 | 158 | 1,254 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q112G | Q112G | 1 | 1 | 0 | 0 | 112 | Q | G | 1 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 112 | A | H | true | false | 120.743707 | 20.878889 | 8,006 | ProTherm | 7 | Fluorescence, CD | Thermal | Mops | 50 mM | 43.4 | NaCl | 0.5 M | 1FTG_A:Q111G | null | null | null | -0.22 | null | 0.34 | null | null | null | null | null | null | null | null | null | null | Yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":43.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence, CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":27321,"numValue":0.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27322,"numValue":-0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27323,"numValue":null,"references":[],"strValue":"Yes","... | [{"id":9492,"numValue":1.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,621 | train | mutant | 1,113 | 158 | 1,254 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | Q112G | Q112G | 1 | 1 | 0 | 0 | 112 | Q | G | 1 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 112 | A | H | true | false | 120.743707 | 20.878889 | 8,491 | ProTherm | 7 | Fluorescence | Urea | Mops | 50 mM | 25.2 | NaCl | 0.5 M | 1FTG_A:Q111G | null | null | null | -0.1 | null | null | null | 0.79 | null | null | null | null | null | null | null | null | Yes | DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 210 | ARTICLE | Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment. | 2,006 | 10.1016/j.jmb.2005.10.086 | 16364364 | J Mol Biol;356;354-66 | 4 | Bueno M|Sancho J|L?pez-Llano J|Campos L A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.2,"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":"50 mM","type":"BUFFER... | [{"datasets":[],"id":28878,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28879,"numValue":0.79,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":28880,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9492,"numValue":1.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,622 | train | mutant | 935 | 158 | 1,057 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 118 | A | L | true | false | 18.274448 | 9.061428 | 1,671 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:V117A | 36.15 | -8 | null | null | null | null | 36.9 | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6214,"numValue":36.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6215,"numValue":-8.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6216,"numValue":36.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":6217,"numValue":3.0,"references":[],"... | [{"id":9498,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,623 | train | mutant | 935 | 158 | 1,057 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 118 | A | L | true | false | 18.274448 | 9.061428 | 1,689 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:V117A | 49.45 | -6.4 | null | null | 33.7 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6304,"numValue":49.45,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6305,"numValue":-6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6306,"numValue":33.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6307,"numValue":3.0,"references":[],"st... | [{"id":9498,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,624 | train | mutant | 935 | 158 | 1,057 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 118 | A | L | true | false | 18.274448 | 9.061428 | 7,934 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:V117A | null | null | null | 0.95 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":27108,"numValue":0.95,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27109,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27110,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9498,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,625 | train | mutant | 935 | 158 | 1,057 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 118 | A | L | true | false | 18.274448 | 9.061428 | 7,952 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:V117A | null | null | null | 1.32 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":[],"id":27162,"numValue":1.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27163,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27164,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9498,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,626 | train | mutant | 935 | 158 | 1,057 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 118 | A | L | true | false | 18.274448 | 9.061428 | 9,330 | ProTherm | 7 | CD | Urea | MOPS | 50 mM | 25 | NaCl | 15 mM | 1FTG_A:V117A | null | null | null | 2.05 | null | null | null | 1.3 | 2.3 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":31846,"numValue":2.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31847,"numValue":2.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31848,"numValue":1.3,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31849,"numValue":null,"references":[],"s... | [{"id":9498,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,627 | train | mutant | 936 | 158 | 1,058 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | T123S | T123S | 1 | 1 | 0 | 0 | 123 | T | S | 6 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 123 | A | L | false | false | 33.707468 | 6.377143 | 1,672 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:T122S | 50.05 | 5.9 | null | null | null | null | 35.5 | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6219,"numValue":50.05,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6220,"numValue":5.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6221,"numValue":35.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":6222,"numValue":3.0,"references":[],"s... | [{"id":9503,"numValue":6.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,628 | train | mutant | 936 | 158 | 1,058 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | T123S | T123S | 1 | 1 | 0 | 0 | 123 | T | S | 6 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 123 | A | L | false | false | 33.707468 | 6.377143 | 1,690 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:T122S | 57.15 | 1.3 | null | null | 50.7 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6309,"numValue":57.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6310,"numValue":1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6311,"numValue":50.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6312,"numValue":3.0,"references":[],"str... | [{"id":9503,"numValue":6.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,630 | train | mutant | 936 | 158 | 1,058 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | T123S | T123S | 1 | 1 | 0 | 0 | 123 | T | S | 6 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 123 | A | L | false | false | 33.707468 | 6.377143 | 7,953 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:T122S | null | null | null | -0.11 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":27165,"numValue":-0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27166,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27167,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9503,"numValue":6.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,631 | train | mutant | 936 | 158 | 1,058 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | T123S | T123S | 1 | 1 | 0 | 0 | 123 | T | S | 6 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 123 | A | L | false | false | 33.707468 | 6.377143 | 9,331 | ProTherm | 7 | CD | Urea | MOPS | 50 mM | 25 | NaCl | 15 mM | 1FTG_A:T122S | null | null | null | 0.37 | null | null | null | 1.93 | 2.42 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":31850,"numValue":0.37,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31851,"numValue":2.42,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31852,"numValue":1.93,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":3185... | [{"id":9503,"numValue":6.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8633 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,633 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 1,638 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | 1FTG_A:D126K | 48.75 | 4.6 | null | null | null | null | 40.6 | null | null | null | null | null | null | null | null | null | Yes | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1FTG_A:D126K","type":"_PDB_CH... | [{"datasets":[],"id":6049,"numValue":48.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6050,"numValue":4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6051,"numValue":40.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":6052,"numValue":3.0,"references":[],"s... | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8634 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,634 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 1,646 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | 1FTG_A:D126K | 57.65 | 1.8 | null | null | null | null | 45.1 | null | null | null | null | null | null | null | null | null | Yes | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1FTG_A:D126K","type":"_PDB_CH... | [{"datasets":[],"id":6089,"numValue":57.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6090,"numValue":1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6091,"numValue":45.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":6092,"numValue":3.0,"references":[],"s... | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8635 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,635 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 1,657 | ProTherm | 7 | DSC | Thermal | MOPS | 50 mM | null | 1FTG_A:D126K | 54.35 | 1.5 | null | null | 39.7 | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1FTG_A:D126K","type":"_PDB_C... | [{"datasets":[],"id":6144,"numValue":54.35,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6145,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6146,"numValue":39.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6147,"numValue":3.0,"references":[],"str... | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8636 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,636 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 7,886 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D126K | null | null | null | 0.58 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":26964,"numValue":0.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26965,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":26966,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8637 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,637 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 7,894 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D126K | null | null | null | -0.03 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":26988,"numValue":-0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26989,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":26990,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,638 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 7,902 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D126K | null | null | null | 0.55 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":27012,"numValue":0.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27013,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27014,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,639 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 7,908 | ProTherm | 7 | DSC | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D126K | null | null | null | 0.71 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"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":"50 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":27030,"numValue":0.71,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27031,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27032,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,640 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 7,914 | ProTherm | 7 | DSC | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D126K | null | null | null | 0.28 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"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":"50 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":27048,"numValue":0.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27049,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27050,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,641 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 7,920 | ProTherm | 7 | DSC | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D126K | null | null | null | 0.99 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"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":"50 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":27066,"numValue":0.99,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27067,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27068,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8642 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,642 | train | mutant | 139 | 158 | 159 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D127K | D127K | 1 | 1 | 0 | 0 | 127 | D | K | 3 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 127 | A | L | false | false | 104.969096 | 15.816875 | 9,309 | ProTherm | 7 | Fluorescence | Urea | MOPS | 50 mM | 25 | 1FTG_A:D126K | null | null | null | -1.01 | null | null | null | 2.35 | 2.58 | null | null | null | null | null | null | null | Yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"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":"50 mM","type":"BUFFER... | [{"datasets":[],"id":31762,"numValue":-1.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31763,"numValue":2.58,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31764,"numValue":2.35,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31765,"numValue":null,"references":[]... | [{"id":9507,"numValue":3.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:8645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,645 | train | mutant | 937 | 158 | 1,059 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V140A | V140A | 1 | 1 | 0 | 0 | 140 | V | A | 6 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 140 | A | S | false | false | 0.403113 | 7.12 | 7,936 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:V139A | null | null | null | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":[],"id":27114,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27115,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27116,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9520,"numValue":6.0,"position":140,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8646 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,646 | train | mutant | 937 | 158 | 1,059 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V140A | V140A | 1 | 1 | 0 | 0 | 140 | V | A | 6 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 140 | A | S | false | false | 0.403113 | 7.12 | 7,954 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:V139A | null | null | null | 0.29 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":27168,"numValue":0.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27169,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27170,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9520,"numValue":6.0,"position":140,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,647 | train | mutant | 937 | 158 | 1,059 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V140A | V140A | 1 | 1 | 0 | 0 | 140 | V | A | 6 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 140 | A | S | false | false | 0.403113 | 7.12 | 9,332 | ProTherm | 7 | CD | Urea | MOPS | 50 mM | 25 | NaCl | 15 mM | 1FTG_A:V139A | null | null | null | 1.51 | null | null | null | 1.68 | 2.1 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":31854,"numValue":1.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31855,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31856,"numValue":1.68,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31857,"numValue":null,"references":[],"... | [{"id":9520,"numValue":6.0,"position":140,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,648 | train | mutant | 938 | 158 | 1,060 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | L144A | L144A | 1 | 1 | 0 | 0 | 144 | L | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 144 | A | E | true | false | 0 | 5.618125 | 1,674 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:L143A | 42.65 | -1.5 | null | null | null | null | 33.3 | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6229,"numValue":42.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6230,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6231,"numValue":33.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":6232,"numValue":3.0,"references":[],"... | [{"id":9524,"numValue":7.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8649 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,649 | train | mutant | 938 | 158 | 1,060 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | L144A | L144A | 1 | 1 | 0 | 0 | 144 | L | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 144 | A | E | true | false | 0 | 5.618125 | 1,692 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:L143A | 55.75 | -0.1 | null | null | 50 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6319,"numValue":55.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6320,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6321,"numValue":50.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6322,"numValue":3.0,"references":[],"st... | [{"id":9524,"numValue":7.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8650 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,650 | train | mutant | 938 | 158 | 1,060 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | L144A | L144A | 1 | 1 | 0 | 0 | 144 | L | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 144 | A | E | true | false | 0 | 5.618125 | 7,937 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:L143A | null | null | null | 0.15 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":27117,"numValue":0.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27118,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27119,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9524,"numValue":7.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8651 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,651 | train | mutant | 938 | 158 | 1,060 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | L144A | L144A | 1 | 1 | 0 | 0 | 144 | L | A | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 144 | A | E | true | false | 0 | 5.618125 | 7,955 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:L143A | null | null | null | 0.11 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27171,"numValue":0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27172,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27173,"numValue":null,"references":[],"strValue":"yes","... | [{"id":9524,"numValue":7.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8653 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,653 | train | mutant | 922 | 158 | 1,044 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D151K | D151K | 1 | 1 | 0 | 0 | 151 | D | K | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 151 | A | T|H | false | false | 120.2072 | 7.409375 | 1,639 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | 1FTG_A:D150K | 44.05 | -0.1 | null | null | null | null | 30.4 | null | null | null | null | null | null | null | null | null | Yes | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1FTG_A:D150K","type":"_PDB_CH... | [{"datasets":[],"id":6054,"numValue":44.05,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6055,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6056,"numValue":30.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":6057,"numValue":3.0,"references":[],"... | [{"id":9531,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8656 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,656 | train | mutant | 922 | 158 | 1,044 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D151K | D151K | 1 | 1 | 0 | 0 | 151 | D | K | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 151 | A | T|H | false | false | 120.2072 | 7.409375 | 1,658 | ProTherm | 7 | DSC | Thermal | MOPS | 50 mM | null | 1FTG_A:D150K | 53.75 | 0.9 | null | null | 48 | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1FTG_A:D150K","type":"_PDB_C... | [{"datasets":[],"id":6149,"numValue":53.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6150,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6151,"numValue":48.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6152,"numValue":3.0,"references":[],"str... | [{"id":9531,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8657 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,657 | train | mutant | 922 | 158 | 1,044 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D151K | D151K | 1 | 1 | 0 | 0 | 151 | D | K | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 151 | A | T|H | false | false | 120.2072 | 7.409375 | 7,887 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D150K | null | null | null | -0.01 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":26967,"numValue":-0.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26968,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":26969,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9531,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8658 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,658 | train | mutant | 922 | 158 | 1,044 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D151K | D151K | 1 | 1 | 0 | 0 | 151 | D | K | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 151 | A | T|H | false | false | 120.2072 | 7.409375 | 7,895 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D150K | null | null | null | -0.21 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":26991,"numValue":-0.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26992,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":26993,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9531,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8659 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,659 | train | mutant | 922 | 158 | 1,044 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D151K | D151K | 1 | 1 | 0 | 0 | 151 | D | K | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 151 | A | T|H | false | false | 120.2072 | 7.409375 | 7,903 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D150K | null | null | null | -0.22 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":27015,"numValue":-0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27016,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27017,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9531,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8661 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,661 | train | mutant | 922 | 158 | 1,044 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D151K | D151K | 1 | 1 | 0 | 0 | 151 | D | K | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 151 | A | T|H | false | false | 120.2072 | 7.409375 | 7,915 | ProTherm | 7 | DSC | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D150K | null | null | null | 0.12 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"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":"50 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":27051,"numValue":0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27052,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27053,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9531,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8662 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,662 | train | mutant | 922 | 158 | 1,044 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D151K | D151K | 1 | 1 | 0 | 0 | 151 | D | K | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 151 | A | T|H | false | false | 120.2072 | 7.409375 | 7,921 | ProTherm | 7 | DSC | Thermal | MOPS | 50 mM | 44.3 | 1FTG_A:D150K | null | null | null | -0.48 | null | null | null | null | null | null | null | null | null | null | null | null | Yes | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"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":"50 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":27069,"numValue":-0.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27070,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27071,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | [{"id":9531,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8663 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,663 | train | mutant | 922 | 158 | 1,044 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | D151K | D151K | 1 | 1 | 0 | 0 | 151 | D | K | 4 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 151 | A | T|H | false | false | 120.2072 | 7.409375 | 9,310 | ProTherm | 7 | Fluorescence | Urea | MOPS | 50 mM | 25 | 1FTG_A:D150K | null | null | null | 0.28 | null | null | null | 2.12 | 2.25 | null | null | null | null | null | null | null | Yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 24 | ARTICLE | Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. | 2,004 | 10.1016/j.jmb.2004.09.047 | 15504413 | J Mol Biol;344;223-37 | 5 | Campos Luis A|Garcia-Mira Maria M|Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Sancho Javier | [{"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":"50 mM","type":"BUFFER... | [{"datasets":[],"id":31766,"numValue":0.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31767,"numValue":2.25,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31768,"numValue":2.12,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31769,"numValue":null,"references":[],... | [{"id":9531,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:8664 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,664 | train | mutant | 939 | 158 | 1,061 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I157V | I157V | 1 | 1 | 0 | 0 | 157 | I | V | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 157 | A | H | true | false | 1.074968 | 5.625625 | 1,675 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:I156V | 35.65 | -8.4 | null | null | 25.3 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6234,"numValue":35.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6235,"numValue":-8.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6236,"numValue":25.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6237,"numValue":3.0,"references":[],"st... | [{"id":9537,"numValue":7.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8665 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,665 | train | mutant | 939 | 158 | 1,061 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I157V | I157V | 1 | 1 | 0 | 0 | 157 | I | V | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 157 | A | H | true | false | 1.074968 | 5.625625 | 1,693 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:I156V | 47.15 | -8.7 | null | null | 29.9 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6324,"numValue":47.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6325,"numValue":-8.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6326,"numValue":29.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6327,"numValue":3.0,"references":[],"st... | [{"id":9537,"numValue":7.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8666 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,666 | train | mutant | 939 | 158 | 1,061 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I157V | I157V | 1 | 1 | 0 | 0 | 157 | I | V | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 157 | A | H | true | false | 1.074968 | 5.625625 | 7,938 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:I156V | null | null | null | 0.69 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":27120,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27121,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27122,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9537,"numValue":7.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8668 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,668 | train | mutant | 939 | 158 | 1,061 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | I157V | I157V | 1 | 1 | 0 | 0 | 157 | I | V | 7 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 157 | A | H | true | false | 1.074968 | 5.625625 | 9,334 | ProTherm | 7 | CD | Urea | MOPS | 50 mM | 25 | NaCl | 15 mM | 1FTG_A:I156V | null | null | null | 3.6 | null | null | null | 0.99 | 1.47 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":31862,"numValue":3.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31863,"numValue":1.47,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31864,"numValue":0.99,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":31865,"numValue":null,"references":[],"... | [{"id":9537,"numValue":7.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8669 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,669 | train | mutant | 940 | 158 | 1,062 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V161A | V161A | 1 | 1 | 0 | 0 | 161 | V | A | 5 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 161 | A | H | false | false | 1.814008 | 4.555 | 1,676 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:V160A | 35.95 | -8.2 | null | null | 27.7 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6239,"numValue":35.95,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6240,"numValue":-8.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6241,"numValue":27.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6242,"numValue":3.0,"references":[],"st... | [{"id":9541,"numValue":5.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8670 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,670 | train | mutant | 940 | 158 | 1,062 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V161A | V161A | 1 | 1 | 0 | 0 | 161 | V | A | 5 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 161 | A | H | false | false | 1.814008 | 4.555 | 1,694 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | null | NaCl | 15 mM | 1FTG_A:V160A | 49.25 | -6.6 | null | null | 49.2 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":6329,"numValue":49.25,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":6330,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":6331,"numValue":49.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":6332,"numValue":3.0,"references":[],"st... | [{"id":9541,"numValue":5.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,671 | train | mutant | 940 | 158 | 1,062 | 170 | 170 | 20 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) | 1 | 20|123 | Flavodoxin | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)|Nostoc sp. (strain ATCC 29151 / PCC 7119) | 1 | P0A3D9|P0A3E0 | IPR050619|IPR008254|IPR001226|IPR010086|IPR029039 | V161A | V161A | 1 | 1 | 0 | 0 | 161 | V | A | 5 | CONSERVATION | 1FTG|1FLV | 182|301 | null | 161 | A | H | false | false | 1.814008 | 4.555 | 7,939 | ProTherm | 7 | CD | Thermal | MOPS | 50 mM | 44.3 | NaCl | 15 mM | 1FTG_A:V160A | null | null | null | 0.73 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 178 | ARTICLE | Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. | 2,004 | 10.1016/j.jmb.2004.08.081 | 15504414 | J Mol Biol;344;239-55 | 5 | Campos Luis A|Sancho Javier|Bueno Marta|Lopez-Llano Jon|Jim?nez Mar?a Angeles | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":44.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":27123,"numValue":0.73,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27124,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27125,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":9541,"numValue":5.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:8674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,674 | train | sequence | 160 | 160 | -1 | 196 | -1 | 21 | Elongation factor Ts | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) | 1 | 21 | Elongation factor Ts | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) | 1 | P43895 | IPR036402|IPR001816|IPR014039|IPR018101|IPR009060 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,133 | ProTherm | 7 | CD | Thermal | Phosphate | 10 mM | null | 115 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 25 | ARTICLE | Irreversible thermal denaturation of elongation factor Ts from Thermus thermophilus effect of the residual structure and intermonomer disulfide bond. | 2,006 | 10.1016/j.bbapap.2006.04.011 | 16781902 | Biochim Biophys Acta;1764;1277-85 | 7 | Zold?k Gabriel|Sedl?k Erik|Valusov? Eva|Wolfrum Alexandra|Marek Jozef|Antal?k Mari?n|Sprinzl Mathias | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":80074,"numValue":115.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80075,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:8676 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,676 | train | mutant | 140 | 160 | 161 | 196 | 196 | 21 | Elongation factor Ts | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) | 1 | 21 | Elongation factor Ts | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) | 1 | P43895 | IPR036402|IPR001816|IPR014039|IPR018101|IPR009060 | C190A | C190A | 1 | 1 | 0 | 0 | 190 | C | A | 4 | CONSERVATION | 1TFE | 292 | null | 190 | A|B | E | false | false | 16.860277 | 18.728333 | 264 | ProTherm | 7 | CD | Thermal | Phosphate | 10 mM | null | 1TFE_A:C190A | 105 | -10 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 25 | ARTICLE | Irreversible thermal denaturation of elongation factor Ts from Thermus thermophilus effect of the residual structure and intermonomer disulfide bond. | 2,006 | 10.1016/j.bbapap.2006.04.011 | 16781902 | Biochim Biophys Acta;1764;1277-85 | 7 | Zold?k Gabriel|Sedl?k Erik|Valusov? Eva|Wolfrum Alexandra|Marek Jozef|Antal?k Mari?n|Sprinzl Mathias | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1TFE_A:C190A","type":"_P... | [{"datasets":[],"id":1085,"numValue":105.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1086,"numValue":-10.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1087,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":9740,"numValue":4.0,"position":190,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:8679 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,679 | train | mutant | 141 | 162 | 163 | 302 | 302 | 22 | Dermatophagoides pteronyssinus | 1 | 22 | Dermatophagoides pteronyssinus | 1 | Q3HWZ5 | IPR038765|IPR025661|IPR000169|IPR025660|IPR013128|IPR000668|IPR039417|IPR013201 | C114A | C114A | 1 | 1 | 0 | 0 | 114 | C | A | 9 | CONSERVATION | null | false | false | null | null | 265 | ProTherm | 7 | Fluorescence | Thermal | Polybuffer (mix of Tris, phosphate, citrate, acetate and KCl) | 50 mM | null | 5VPG_A:C34A | 61.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 26 | ARTICLE | Comparative study of mature and zymogen mite cysteine protease stability and pH unfolding. | 2,010 | 10.1016/j.bbagen.2010.05.011 | 20682463 | Biochim Biophys Acta;1800;937-45 | 6 | Chevign? Andy|Dumez Marie-Eve|Dumoulin Mireille|Matagne Andr?|Jacquet Alain|Galleni Moreno | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Polybuffer (mix of Tris, phosphate, citrate, acetate and KCl)","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":[],"id":1088,"numValue":61.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1089,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":9860,"numValue":9.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:8680 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,680 | train | sequence | 164 | 164 | -1 | 636 | -1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P38993 | IPR011707|IPR001117|IPR011706|IPR045087|IPR033138|IPR002355|IPR008972|IPR044130 | 1.16.3.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,223 | ProTherm | 7 | DSC | Thermal | Phosphate | 50 mM | null | 54.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | 3.0 | TM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 27 | ARTICLE | Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability. | 2,010 | 10.1002/pro.457 | 20662012 | Protein Sci;19;1739-50 | 4 | Ziegler Lynn|Terzulli Alaina|Sedlak Erik|Kosman Daniel J | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":80365,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80366,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":80367,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,681 | train | sequence | 164 | 164 | -1 | 636 | -1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P38993 | IPR011707|IPR001117|IPR011706|IPR045087|IPR033138|IPR002355|IPR008972|IPR044130 | 1.16.3.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,224 | ProTherm | 7 | DSC | Thermal | Phosphate | 50 mM | null | 67.6 | null | null | null | 353.73 | null | null | null | null | null | null | null | null | null | null | null | No | 3.0 | TM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 27 | ARTICLE | Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability. | 2,010 | 10.1002/pro.457 | 20662012 | Protein Sci;19;1739-50 | 4 | Ziegler Lynn|Terzulli Alaina|Sedlak Erik|Kosman Daniel J | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":80368,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80369,"numValue":353.73,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":80370,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":80371,"numValue":null,"references"... | ||||||||||||||||||||||||
fireprotdb:8682 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,682 | train | mutant | 142 | 164 | 165 | 636 | 636 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P38993 | IPR011707|IPR001117|IPR011706|IPR045087|IPR033138|IPR002355|IPR008972|IPR044130 | 1.16.3.1 | N77A | N77A | 1 | 1 | 0 | 0 | 77 | N | A | 5 | CONSERVATION | null | false | false | null | null | 266 | ProTherm | 7 | DSC | Thermal | Phosphate | 50 mM | null | 57 | null | null | null | 322.66 | null | null | null | null | null | null | null | null | null | null | null | No | 3.0 | TM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 27 | ARTICLE | Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability. | 2,010 | 10.1002/pro.457 | 20662012 | Protein Sci;19;1739-50 | 4 | Ziegler Lynn|Terzulli Alaina|Sedlak Erik|Kosman Daniel J | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":1090,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1091,"numValue":322.66,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1092,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":1093,"numValue":null,"references":[],... | [{"id":10125,"numValue":5.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8683 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,683 | train | mutant | 142 | 164 | 165 | 636 | 636 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P38993 | IPR011707|IPR001117|IPR011706|IPR045087|IPR033138|IPR002355|IPR008972|IPR044130 | 1.16.3.1 | N77A | N77A | 1 | 1 | 0 | 0 | 77 | N | A | 5 | CONSERVATION | null | false | false | null | null | 267 | ProTherm | 7 | DSC | Thermal | Phosphate | 50 mM | null | 73.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 27 | ARTICLE | Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability. | 2,010 | 10.1002/pro.457 | 20662012 | Protein Sci;19;1739-50 | 4 | Ziegler Lynn|Terzulli Alaina|Sedlak Erik|Kosman Daniel J | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":1094,"numValue":73.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1095,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":10125,"numValue":5.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||
fireprotdb:8684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,684 | train | mutant | 143 | 164 | 166 | 636 | 636 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P38993 | IPR011707|IPR001117|IPR011706|IPR045087|IPR033138|IPR002355|IPR008972|IPR044130 | 1.16.3.1 | N113A | N113A | 1 | 1 | 0 | 0 | 113 | N | A | 6 | CONSERVATION | null | false | false | null | null | 268 | ProTherm | 7 | DSC | Thermal | Phosphate | 50 mM | null | 52.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | 4.0 | TM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 27 | ARTICLE | Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability. | 2,010 | 10.1002/pro.457 | 20662012 | Protein Sci;19;1739-50 | 4 | Ziegler Lynn|Terzulli Alaina|Sedlak Erik|Kosman Daniel J | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":1096,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1097,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":1098,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":10161,"numValue":6.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8686 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,686 | train | mutant | 143 | 164 | 166 | 636 | 636 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P38993 | IPR011707|IPR001117|IPR011706|IPR045087|IPR033138|IPR002355|IPR008972|IPR044130 | 1.16.3.1 | N113A | N113A | 1 | 1 | 0 | 0 | 113 | N | A | 6 | CONSERVATION | null | false | false | null | null | 270 | ProTherm | 7 | DSC | Thermal | Phosphate | 50 mM | null | 65.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | 4.0 | TM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 27 | ARTICLE | Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability. | 2,010 | 10.1002/pro.457 | 20662012 | Protein Sci;19;1739-50 | 4 | Ziegler Lynn|Terzulli Alaina|Sedlak Erik|Kosman Daniel J | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":1103,"numValue":65.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1104,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":1105,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":10161,"numValue":6.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8687 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,687 | train | mutant | 144 | 164 | 167 | 636 | 636 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P38993 | IPR011707|IPR001117|IPR011706|IPR045087|IPR033138|IPR002355|IPR008972|IPR044130 | 1.16.3.1 | N198A | N198A | 1 | 1 | 0 | 0 | 198 | N | A | 6 | CONSERVATION | null | false | false | null | null | 271 | ProTherm | 7 | DSC | Thermal | Phosphate | 50 mM | null | 56.1 | null | null | null | 293.98 | null | null | null | null | null | null | null | null | null | null | null | No | 3.0 | TM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 27 | ARTICLE | Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability. | 2,010 | 10.1002/pro.457 | 20662012 | Protein Sci;19;1739-50 | 4 | Ziegler Lynn|Terzulli Alaina|Sedlak Erik|Kosman Daniel J | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":1106,"numValue":56.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1107,"numValue":293.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1108,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":1109,"numValue":null,"references":[],... | [{"id":10246,"numValue":6.0,"position":198,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8688 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,688 | train | mutant | 144 | 164 | 167 | 636 | 636 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 23 | Iron transport multicopper oxidase FET3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P38993 | IPR011707|IPR001117|IPR011706|IPR045087|IPR033138|IPR002355|IPR008972|IPR044130 | 1.16.3.1 | N198A | N198A | 1 | 1 | 0 | 0 | 198 | N | A | 6 | CONSERVATION | null | false | false | null | null | 272 | ProTherm | 7 | DSC | Thermal | Phosphate | 50 mM | null | 66.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | 3.0 | TM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 27 | ARTICLE | Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability. | 2,010 | 10.1002/pro.457 | 20662012 | Protein Sci;19;1739-50 | 4 | Ziegler Lynn|Terzulli Alaina|Sedlak Erik|Kosman Daniel J | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":1110,"numValue":66.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1111,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":1112,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":10246,"numValue":6.0,"position":198,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,689 | train | sequence | 168 | 168 | -1 | 1,480 | -1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,225 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 57.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":80372,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80373,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,690 | train | sequence | 168 | 168 | -1 | 1,480 | -1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,226 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 51.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":80374,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80375,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,691 | train | sequence | 168 | 168 | -1 | 1,480 | -1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,227 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 58.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":80376,"numValue":58.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80377,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8692 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,692 | train | sequence | 168 | 168 | -1 | 1,480 | -1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,228 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 51.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":80378,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80379,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8693 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,693 | train | sequence | 168 | 168 | -1 | 1,480 | -1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,229 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 57.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":80380,"numValue":57.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80381,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8694 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,694 | train | sequence | 168 | 168 | -1 | 1,480 | -1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,230 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 57.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":80382,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80383,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,695 | train | mutant | 7,299 | 168 | 7,969 | 1,480 | 1,480 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | F494N|Q637R | F494N|Q637R | 2 | 2 | 0 | 0 | 494 | F | N | 7 | CONSERVATION | null | false | false | null | null | 15,656 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 59.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":57459,"numValue":59.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57460,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":11178,"numValue":7.0,"position":494,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":11321,"numValue":8.0,"position":637,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,696 | train | mutant | 7,299 | 168 | 7,969 | 1,480 | 1,480 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | F494N|Q637R | F494N|Q637R | 2 | 2 | 0 | 0 | 494 | F | N | 7 | CONSERVATION | null | false | false | null | null | 15,657 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 52.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":57461,"numValue":52.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57462,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":11178,"numValue":7.0,"position":494,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":11321,"numValue":8.0,"position":637,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,698 | train | mutant | 145 | 168 | 169 | 1,480 | 1,480 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | 24 | Cystic fibrosis transmembrane conductance regulator | Homo sapiens | 1 | P13569 | IPR003593|IPR011527|IPR036640|IPR003439|IPR017871|IPR050173|IPR009147|IPR047082|IPR025837|IPR027417 | V510D | V510D | 1 | 1 | 0 | 0 | 510 | V | D | 7 | CONSERVATION | null | false | false | null | null | 274 | ProTherm | 7.5 | DSC | Thermal | HEPES | 20 mM | null | NaCl | 150 mM | 53 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 28 | ARTICLE | Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. | 2,010 | 10.1002/pro.479 | 20687133 | Protein Sci;19;1917-31 | 9 | Protasevich Irina|Yang Zhengrong|Wang Chi|Atwell Shane|Zhao Xun|Emtage Spencer|Wetmore Diana|Hunt John F|Brouillette Christie G | [{"numValue":7.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":1115,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1116,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":11194,"numValue":7.0,"position":510,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,699 | train | sequence | 170 | 170 | -1 | 296 | -1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,894 | ProTherm | 7.7 | Fluorescence | GdnHCl | HEPES | 10 mM | 25 | null | null | 5.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 720 | ARTICLE | Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli. | 1,991 | 1904869 | J Biol Chem;266;11789-96 | 6 | Kim J|Park S|Song T|Park C|Teschke C M|Randall L L | [{"numValue":7.7,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":76265,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76266,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||||
fireprotdb:8700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,700 | train | sequence | 170 | 170 | -1 | 296 | -1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,231 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 62.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"Potassium chloride","ty... | [{"datasets":[],"id":80384,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80385,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,701 | train | sequence | 170 | 170 | -1 | 296 | -1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,503 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 57.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84092,"numValue":57.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84093,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:8702 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,702 | train | sequence | 170 | 170 | -1 | 296 | -1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,504 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 63.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84094,"numValue":63.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84095,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:8703 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,703 | train | sequence | 170 | 170 | -1 | 296 | -1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,057 | ProTherm | 7.6 | Quantitative cysteine reactivity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 62.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Quantitative cysteine reactivity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":... | [{"datasets":[],"id":85698,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85699,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] |
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