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:13950 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,950 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,485 | ProTherm | 5.5 | Fluorescence | GdnHCl | sodium acetate | 30 | NaCl | 100 mM | null | null | 4.1 | null | null | null | null | null | 2 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1799 | ARTICLE | Design, expression, and stability of a diverse protein library based on the human fibronectin type III domain. | 2,007 | 10.1110/ps.062498407 | 17322532 | Protein Sci;16;476-84 | 2 | Olson C Anders|Roberts Richard W | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":30.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","ty... | [{"datasets":[],"id":89626,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89627,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":89628,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:13951 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,951 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,489 | ProTherm | 6 | Fluorescence | GdnSCN | Sodium citrate | 20mM | 30 | NaCl | 100mM | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1800 | ARTICLE | High-throughput analysis of the protein sequence-stability landscape using a quantitative yeast surface two-hybrid system and fragment reconstitution. | 2,008 | 10.1016/j.jmb.2008.07.036 | 18674545 | J Mol Biol;382;721-33 | 3 | Koide Akiko|Koide Shohei|Dutta Sanjib | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":30.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnSCN","type":"METHOD"},{"numValue":null,"strValue":"Sodium citrate","type":"BUFFER"},{"numValue":null,"strValue":"20mM","ty... | [{"datasets":[],"id":89643,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | ||||||||||||||||||||||||
fireprotdb:13952 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,952 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,657 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | null | null | 7.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | DG|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 779 | ARTICLE | Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. | 2,008 | 10.1016/j.jmb.2007.10.056 | 18035373 | J Mol Biol;375;560-71 | 4 | Rutherford Trevor J|Clarke Jane|Best Robert B|Billings Kate S | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":93530,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93531,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | ||||||||||||||||||||||||||
fireprotdb:13953 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,953 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,681 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 6.1 | null | null | null | null | 5.7 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93613,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93614,"numValue":null,"references":[],"strValue":"?1.06","type":"M"},{"datasets":[],"id":93615,"numValue":5.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93616,"numValue":2.0,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:13954 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,954 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,682 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 5.9 | null | null | null | null | 5.6 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93618,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93619,"numValue":null,"references":[],"strValue":"?1.05","type":"M"},{"datasets":[],"id":93620,"numValue":5.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93621,"numValue":2.0,"references":[],"... | |||||||||||||||||||||||
fireprotdb:13955 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,955 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,683 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 4.7 | null | null | null | null | 5.8 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93623,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93624,"numValue":null,"references":[],"strValue":"?0.81","type":"M"},{"datasets":[],"id":93625,"numValue":5.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93626,"numValue":2.0,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:13956 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,956 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,684 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 3.4 | null | null | null | null | 2.5 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93628,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93629,"numValue":null,"references":[],"strValue":"?1.39","type":"M"},{"datasets":[],"id":93630,"numValue":2.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93631,"numValue":2.0,"references":[],"... | |||||||||||||||||||||||
fireprotdb:13957 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,957 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,685 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 3.3 | null | null | null | null | 2.8 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93633,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93634,"numValue":null,"references":[],"strValue":"?1.16","type":"M"},{"datasets":[],"id":93635,"numValue":2.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93636,"numValue":2.0,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:13958 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,958 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,686 | ProTherm | 7.2 | Trp (SVD) | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 3.8 | null | null | null | null | 3.4 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp (SVD)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,NaH2PO4",... | [{"datasets":[],"id":93638,"numValue":3.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93639,"numValue":null,"references":[],"strValue":"?1.15","type":"M"},{"datasets":[],"id":93640,"numValue":3.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93641,"numValue":2.0,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:13959 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,959 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,687 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 5.6 | null | null | null | null | 5.4 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93643,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93644,"numValue":null,"references":[],"strValue":"?1.03","type":"M"},{"datasets":[],"id":93645,"numValue":5.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93646,"numValue":2.0,"references":[],"... | |||||||||||||||||||||||
fireprotdb:13960 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,960 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,688 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 3.4 | null | null | null | null | 6.7 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93648,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93649,"numValue":null,"references":[],"strValue":"?0.51","type":"M"},{"datasets":[],"id":93650,"numValue":6.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93651,"numValue":2.0,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:13961 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,961 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,689 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 5.9 | null | null | null | null | 4.6 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93653,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93654,"numValue":null,"references":[],"strValue":"?1.3","type":"M"},{"datasets":[],"id":93655,"numValue":4.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93656,"numValue":2.0,"references":[],"s... | |||||||||||||||||||||||
fireprotdb:13962 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,962 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,690 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 3.7 | null | null | null | null | 3.6 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93658,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93659,"numValue":null,"references":[],"strValue":"?1.0","type":"M"},{"datasets":[],"id":93660,"numValue":3.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93661,"numValue":2.0,"references":[],"s... | |||||||||||||||||||||||
fireprotdb:13963 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,963 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,691 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 3 | null | null | null | null | 3.4 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93663,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93664,"numValue":null,"references":[],"strValue":"?0.87","type":"M"},{"datasets":[],"id":93665,"numValue":3.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93666,"numValue":2.0,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:13964 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,964 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,692 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 8.2 | null | null | null | null | 8.8 | -0.93 | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93668,"numValue":8.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93669,"numValue":-0.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":93670,"numValue":8.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93671,"numValue":2.0,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:13965 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,965 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,693 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 10.6 | null | null | null | null | 8.8 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93673,"numValue":10.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93674,"numValue":null,"references":[],"strValue":"?1.21","type":"M"},{"datasets":[],"id":93675,"numValue":8.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93676,"numValue":2.0,"references":[],... | ||||||||||||||||||||||||
fireprotdb:13966 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,966 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,694 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 0.78 | null | null | null | null | 0.48 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93678,"numValue":0.78,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93679,"numValue":null,"references":[],"strValue":"?1.64","type":"M"},{"datasets":[],"id":93680,"numValue":0.48,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93681,"numValue":2.0,"references":[]... | |||||||||||||||||||||||
fireprotdb:13967 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,967 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,695 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 1.6 | null | null | null | null | 0.88 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93683,"numValue":1.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93684,"numValue":null,"references":[],"strValue":"?1.79","type":"M"},{"datasets":[],"id":93685,"numValue":0.88,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93686,"numValue":2.0,"references":[],... | ||||||||||||||||||||||||
fireprotdb:13968 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,968 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,696 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 4.3 | null | null | null | null | 2.96 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93688,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93689,"numValue":null,"references":[],"strValue":"?1.45","type":"M"},{"datasets":[],"id":93690,"numValue":2.96,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93691,"numValue":2.0,"references":[],... | |||||||||||||||||||||||
fireprotdb:13969 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,969 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,697 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 5.4 | null | null | null | null | 3.7 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93693,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93694,"numValue":null,"references":[],"strValue":"?1.47","type":"M"},{"datasets":[],"id":93695,"numValue":3.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93696,"numValue":2.0,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:13970 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,970 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,698 | ProTherm | 7.5 | SX (thiol exchange) | Urea | Phosphate buffer | 50mM | 25 | KH2PO4,K2HPO4 | 14mM, 37.3mM | null | null | 4.1 | null | null | null | null | 2.9 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SX (thiol exchange)","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50... | [{"datasets":[],"id":93698,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93699,"numValue":null,"references":[],"strValue":"?1.42","type":"M"},{"datasets":[],"id":93700,"numValue":2.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93701,"numValue":2.0,"references":[],"... | |||||||||||||||||||||||
fireprotdb:13973 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,973 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,701 | ProTherm | 7.2 | Trp Fluorescence | Urea | PBS | 25 | KH2PO4,NaCl,KCl,NaH2PO4 | 1.4mM, 0.14M, 2.5mM, 5mM | null | null | 2.5 | null | null | null | null | 3.9 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 1865 | ARTICLE | Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING. | 2,017 | 10.1074/jbc.M116.760371 | 27909052 | J Biol Chem;292;955-966 | 4 | Oas Terrence G|Shah Riddhi|Ohashi Tomoo|Erickson Harold P | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Trp Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"},{"numValue":null,"strValue":"KH2PO4,NaCl,KCl,Na... | [{"datasets":[],"id":93713,"numValue":2.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93714,"numValue":null,"references":[],"strValue":"?0.65","type":"M"},{"datasets":[],"id":93715,"numValue":3.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93716,"numValue":2.0,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:13974 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,974 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,839 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 1 mM | 24 | null | null | 10.5 | null | null | null | null | null | 4.8 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUF... | [{"datasets":[],"id":94280,"numValue":10.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94281,"numValue":4.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94282,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94283,"numValue":null,"references":[],... | |||||||||||||||||||||||||
fireprotdb:13975 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,975 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,840 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 1 mM | 24 | null | null | 9.9 | null | null | null | null | null | 3.6 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUF... | [{"datasets":[],"id":94284,"numValue":9.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94285,"numValue":3.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94286,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94287,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:13976 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,976 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,841 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 10 mM | 24 | null | null | 10.6 | null | null | null | null | null | 4.4 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":94288,"numValue":10.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94289,"numValue":4.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94290,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94291,"numValue":null,"references":[],... | |||||||||||||||||||||||||
fireprotdb:13977 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,977 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,842 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 10 mM | 24 | NaCl | 30 mM | null | null | 10.8 | null | null | null | null | null | 5 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":94292,"numValue":10.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94293,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94294,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94295,"numValue":null,"references":[],... | |||||||||||||||||||||||
fireprotdb:13978 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,978 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,843 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 10 mM | 24 | NaCl | 150 mM | null | null | 10.7 | null | null | null | null | null | 5.1 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":94296,"numValue":10.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94297,"numValue":5.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94298,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94299,"numValue":null,"references":[],... | |||||||||||||||||||||||
fireprotdb:13979 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,979 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,844 | ProTherm | 7.4 | Fluorescence | Urea | 24 | null | null | 8.6 | null | null | null | null | null | 1.8 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"}] | [{"datasets":[],"id":94300,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94301,"numValue":1.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94302,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94303,"numValue":null,"references":[],"... | |||||||||||||||||||||||||||
fireprotdb:13980 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,980 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,845 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 1 mM | 24 | null | null | 6.6 | null | null | null | null | null | 1.2 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUF... | [{"datasets":[],"id":94304,"numValue":6.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94305,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94306,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94307,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:13981 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,981 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,846 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 10 mM | 24 | null | null | 4.5 | null | null | null | null | null | 1 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":94308,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94309,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94310,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94311,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:13982 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,982 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,847 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 10 mM | 24 | NaCl | 30 mM | null | null | 4.2 | null | null | null | null | null | 1 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":94312,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94313,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94314,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94315,"numValue":null,"references":[],"... | |||||||||||||||||||||||
fireprotdb:13985 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,985 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,850 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 1 mM | 24 | null | null | 13.7 | null | null | null | null | null | 1.8 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUF... | [{"datasets":[],"id":94324,"numValue":13.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94325,"numValue":1.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94326,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94327,"numValue":null,"references":[],... | |||||||||||||||||||||||||
fireprotdb:13986 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,986 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,851 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 10 mM | 24 | null | null | 7.4 | null | null | null | null | null | 1.2 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":94328,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94329,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94330,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94331,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:13987 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,987 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,852 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 10 mM | 24 | NaCl | 30 mM | null | null | 7.4 | null | null | null | null | null | 1.1 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":94332,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94333,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94334,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94335,"numValue":null,"references":[],"... | |||||||||||||||||||||||
fireprotdb:13988 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,988 | train | sequence | 270 | 270 | -1 | 2,477 | -1 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,853 | ProTherm | 7.4 | Fluorescence | Urea | Tris-HCl | 10 mM | 24 | NaCl | 150 mM | null | null | 7.3 | null | null | null | null | null | 1.1 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1875 | ARTICLE | Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. | 2,004 | 10.1021/bi0347104 | 14769050 | Biochemistry;43;1724-35 | 4 | Patel Salima|Chaffotte Alain F|Goubard Fabrice|Pauthe Emmanuel | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":24.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":94336,"numValue":7.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94337,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":94338,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":94339,"numValue":null,"references":[],"... | |||||||||||||||||||||||
fireprotdb:13989 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,989 | train | mutant | 4,736 | 270 | 5,275 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | P1542A | P1542A | 1 | 1 | 0 | 0 | 1,542 | P | A | 8 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1542 | A|B | S|L | true | false | 12.806774 | 25.194762 | 11,156 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:P5A | null | null | null | -0.11 | null | null | null | 1.49 | 6.4 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38366,"numValue":-0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38367,"numValue":6.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38368,"numValue":1.49,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38... | [{"id":19379,"numValue":8.0,"position":1542,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:13990 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,990 | train | mutant | 4,736 | 270 | 5,275 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | P1542A | P1542A | 1 | 1 | 0 | 0 | 1,542 | P | A | 8 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1542 | A|B | S|L | true | false | 12.806774 | 25.194762 | 12,463 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 2CK2_A:P5A | null | null | null | -0.21 | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | DDG|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 779 | ARTICLE | Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. | 2,008 | 10.1016/j.jmb.2007.10.056 | 18035373 | J Mol Biol;375;560-71 | 4 | Rutherford Trevor J|Clarke Jane|Best Robert B|Billings Kate S | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":45212,"numValue":-0.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45213,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | [{"id":19379,"numValue":8.0,"position":1542,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:13992 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,992 | train | mutant | 240 | 270 | 271 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | D1544N | D1544N | 1 | 1 | 0 | 0 | 1,544 | D | N | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1544 | A|B | L|E | true | false | 87.141238 | 32.384213 | 429 | ProTherm | 2.4 | CD | Thermal | glycine hydrochloride | 20 mM | null | NaCl | 1 M | 1TTG_A:D7N | 82 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 45 | ARTICLE | Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. | 2,001 | 10.1021/bi010916y | 11513611 | Biochemistry;40;10326-33 | 5 | Koide A|Batori V|Koide S|Jordan M R|Horner S R | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":1763,"numValue":82.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1764,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":19381,"numValue":9.0,"position":1544,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:13993 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,993 | train | mutant | 240 | 270 | 271 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | D1544N | D1544N | 1 | 1 | 0 | 0 | 1,544 | D | N | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1544 | A|B | L|E | true | false | 87.141238 | 32.384213 | 431 | ProTherm | 7 | CD | Thermal | sodium phosphate | 20 mM | null | NaCl | 0.1 M | 1TTG_A:D7N | 69 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 45 | ARTICLE | Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. | 2,001 | 10.1021/bi010916y | 11513611 | Biochemistry;40;10326-33 | 5 | Koide A|Batori V|Koide S|Jordan M R|Horner S R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1767,"numValue":69.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1768,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":19381,"numValue":9.0,"position":1544,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:13994 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,994 | train | mutant | 240 | 270 | 271 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | D1544N | D1544N | 1 | 1 | 0 | 0 | 1,544 | D | N | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1544 | A|B | L|E | true | false | 87.141238 | 32.384213 | 433 | ProTherm | 7 | CD | Thermal | sodium phosphate | 20 mM | null | NaCl | 1 M | 1TTG_A:D7N | 80 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 45 | ARTICLE | Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. | 2,001 | 10.1021/bi010916y | 11513611 | Biochemistry;40;10326-33 | 5 | Koide A|Batori V|Koide S|Jordan M R|Horner S R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1771,"numValue":80.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1772,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":19381,"numValue":9.0,"position":1544,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:13995 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,995 | train | mutant | 241 | 270 | 272 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | D1544K | D1544K | 1 | 1 | 0 | 0 | 1,544 | D | K | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1544 | A|B | L|E | true | false | 87.141238 | 32.384213 | 428 | ProTherm | 2.4 | CD | Thermal | glycine hydrochloride | 20 mM | null | NaCl | 0.1 M | 1TTG_A:D7K | 69 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 45 | ARTICLE | Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. | 2,001 | 10.1021/bi010916y | 11513611 | Biochemistry;40;10326-33 | 5 | Koide A|Batori V|Koide S|Jordan M R|Horner S R | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":1761,"numValue":69.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1762,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":19381,"numValue":9.0,"position":1544,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:13996 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,996 | train | mutant | 241 | 270 | 272 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | D1544K | D1544K | 1 | 1 | 0 | 0 | 1,544 | D | K | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1544 | A|B | L|E | true | false | 87.141238 | 32.384213 | 430 | ProTherm | 2.4 | CD | Thermal | glycine hydrochloride | 20 mM | null | NaCl | 1 M | 1TTG_A:D7K | 77 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 45 | ARTICLE | Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. | 2,001 | 10.1021/bi010916y | 11513611 | Biochemistry;40;10326-33 | 5 | Koide A|Batori V|Koide S|Jordan M R|Horner S R | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":1765,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1766,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":19381,"numValue":9.0,"position":1544,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:13997 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,997 | train | mutant | 241 | 270 | 272 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | D1544K | D1544K | 1 | 1 | 0 | 0 | 1,544 | D | K | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1544 | A|B | L|E | true | false | 87.141238 | 32.384213 | 432 | ProTherm | 7 | CD | Thermal | sodium phosphate | 20 mM | null | NaCl | 0.1 M | 1TTG_A:D7K | 70 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 45 | ARTICLE | Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. | 2,001 | 10.1021/bi010916y | 11513611 | Biochemistry;40;10326-33 | 5 | Koide A|Batori V|Koide S|Jordan M R|Horner S R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1769,"numValue":70.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1770,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":19381,"numValue":9.0,"position":1544,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:13998 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,998 | train | mutant | 241 | 270 | 272 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | D1544K | D1544K | 1 | 1 | 0 | 0 | 1,544 | D | K | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1544 | A|B | L|E | true | false | 87.141238 | 32.384213 | 434 | ProTherm | 7 | CD | Thermal | sodium phosphate | 20 mM | null | NaCl | 1 M | 1TTG_A:D7K | 78 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 45 | ARTICLE | Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. | 2,001 | 10.1021/bi010916y | 11513611 | Biochemistry;40;10326-33 | 5 | Koide A|Batori V|Koide S|Jordan M R|Horner S R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1773,"numValue":78.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1774,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":19381,"numValue":9.0,"position":1544,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:13999 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,999 | train | mutant | 4,737 | 270 | 5,276 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | L1545A | L1545A | 1 | 1 | 0 | 0 | 1,545 | L | A | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1545 | A|B | L|E | true | true | 26.19402 | 24.264028 | 11,157 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:L8A | null | null | null | 1.64 | null | null | null | 1.22 | 6.2 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38370,"numValue":1.64,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38371,"numValue":6.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38372,"numValue":1.22,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38373,"numValue":null... | [{"id":19382,"numValue":9.0,"position":1545,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14000 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,000 | train | mutant | 4,738 | 270 | 5,277 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | V1547A | V1547A | 1 | 1 | 0 | 0 | 1,547 | V | A | 8 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1547 | A|B | E | true | true | 31.548143 | 21.290714 | 11,158 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:V10A | null | null | null | 1.38 | null | null | null | 1.26 | 6.8 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38374,"numValue":1.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38375,"numValue":6.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38376,"numValue":1.26,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38377,"numValue":null... | [{"id":19384,"numValue":8.0,"position":1547,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14001 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,001 | train | mutant | 4,739 | 270 | 5,278 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | A1550G | A1550G | 1 | 1 | 0 | 0 | 1,550 | A | G | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1550 | A|B | E | true | true | 52.26626 | 32.132619 | 11,159 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:A13G | null | null | null | 0.93 | null | null | null | 1.33 | 6.1 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38378,"numValue":0.93,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38379,"numValue":6.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38380,"numValue":1.33,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38381,"numValue":null... | [{"id":19387,"numValue":5.0,"position":1550,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14002 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,002 | train | mutant | 4,740 | 270 | 5,279 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | L1555A | L1555A | 1 | 1 | 0 | 0 | 1,555 | L | A | 6 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1555 | A|B | E | true | true | 7.574966 | 22.989333 | 11,160 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:L18A | null | null | null | 0.87 | null | null | null | 1.34 | 6.3 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38382,"numValue":0.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38383,"numValue":6.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38384,"numValue":1.34,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38385,"numValue":null... | [{"id":19392,"numValue":6.0,"position":1555,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14004 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,004 | train | mutant | 4,741 | 270 | 5,280 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1557A | I1557A | 1 | 1 | 0 | 0 | 1,557 | I | A | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1557 | A|B | E | true | true | 8.60869 | 17.61963 | 12,465 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 2CK2_A:I20A | null | null | null | -3.74 | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | DDG|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 779 | ARTICLE | Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. | 2,008 | 10.1016/j.jmb.2007.10.056 | 18035373 | J Mol Biol;375;560-71 | 4 | Rutherford Trevor J|Clarke Jane|Best Robert B|Billings Kate S | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":45216,"numValue":-3.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45217,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | [{"id":19394,"numValue":5.0,"position":1557,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14008 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,008 | train | mutant | 4,744 | 270 | 5,283 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | P1562A | P1562A | 1 | 1 | 0 | 0 | 1,562 | P | A | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1562 | A|B | L | true | false | 17.103209 | 26.180476 | 11,164 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:P25A | null | null | null | 0.48 | null | null | null | 1.4 | 6.5 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38398,"numValue":0.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38399,"numValue":6.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38400,"numValue":1.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":3840... | [{"id":19399,"numValue":9.0,"position":1562,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14010 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,010 | train | mutant | 4,745 | 270 | 5,284 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | V1566A | V1566A | 1 | 1 | 0 | 0 | 1,566 | V | A | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1566 | A|B | L | true | false | 20.985747 | 24.168333 | 11,165 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:V29A | null | null | null | 1.45 | null | null | null | 1.25 | 6.6 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38402,"numValue":1.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38403,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38404,"numValue":1.25,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38405,"numValue":null... | [{"id":19403,"numValue":9.0,"position":1566,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14011 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,011 | train | mutant | 4,746 | 270 | 5,285 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1569F | Y1569F | 1 | 1 | 0 | 0 | 1,569 | Y | F | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1569 | A|B | E | true | false | 1.247481 | 17.85619 | 11,166 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y32F | null | null | null | 0.41 | null | null | null | 1.41 | 6.3 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38406,"numValue":0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38407,"numValue":6.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38408,"numValue":1.41,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":384... | [{"id":19406,"numValue":9.0,"position":1569,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14012 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,012 | train | mutant | 4,747 | 270 | 5,286 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1569L | Y1569L | 1 | 1 | 0 | 0 | 1,569 | Y | L | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1569 | A|B | E | true | false | 1.247481 | 17.85619 | 11,167 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y32L | null | null | null | 2.81 | null | null | null | 1.04 | 6.6 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":38410,"numValue":2.81,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38411,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38412,"numValue":1.04,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38413,"numValue":null,"references":[],"... | [{"id":19406,"numValue":9.0,"position":1569,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14013 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,013 | train | mutant | 4,747 | 270 | 5,286 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1569L | Y1569L | 1 | 1 | 0 | 0 | 1,569 | Y | L | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1569 | A|B | E | true | false | 1.247481 | 17.85619 | 11,170 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y32L | null | null | null | 2.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":38420,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38421,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":19406,"numValue":9.0,"position":1569,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14014 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,014 | train | mutant | 4,748 | 270 | 5,287 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1569A | Y1569A | 1 | 1 | 0 | 0 | 1,569 | Y | A | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1569 | A|B | E | true | false | 1.247481 | 17.85619 | 11,168 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y32A | null | null | null | 4.37 | null | null | null | 0.8 | 6.8 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":38414,"numValue":4.37,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38415,"numValue":6.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38416,"numValue":0.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38417,"numValue":null,"references":[],"s... | [{"id":19406,"numValue":9.0,"position":1569,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14015 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,015 | train | mutant | 4,748 | 270 | 5,287 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1569A | Y1569A | 1 | 1 | 0 | 0 | 1,569 | Y | A | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1569 | A|B | E | true | false | 1.247481 | 17.85619 | 11,169 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y32A | null | null | null | 3.96 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":38418,"numValue":3.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38419,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":19406,"numValue":9.0,"position":1569,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14016 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,016 | train | mutant | 4,749 | 270 | 5,288 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1571A | I1571A | 1 | 1 | 0 | 0 | 1,571 | I | A | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1571 | A|B | E | true | false | 1.585577 | 17.413981 | 11,171 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I34A | null | null | null | 5.02 | null | null | null | 0.7 | 6.9 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38422,"numValue":5.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38423,"numValue":6.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38424,"numValue":0.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38425,"numValue":null,... | [{"id":19408,"numValue":9.0,"position":1571,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14017 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,017 | train | mutant | 4,750 | 270 | 5,289 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1571V | I1571V | 1 | 1 | 0 | 0 | 1,571 | I | V | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1571 | A|B | E | true | false | 1.585577 | 17.413981 | 11,172 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I34V | null | null | null | 0.41 | null | null | null | 1.41 | 6.9 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38426,"numValue":0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38427,"numValue":6.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38428,"numValue":1.41,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":384... | [{"id":19408,"numValue":9.0,"position":1571,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14018 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,018 | train | mutant | 4,751 | 270 | 5,290 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1573A | Y1573A | 1 | 1 | 0 | 0 | 1,573 | Y | A | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1573 | A|B | E | true | true | 27.146676 | 20.629365 | 11,173 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y36A | null | null | null | 2.29 | null | null | null | 1.12 | 7.9 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38430,"numValue":2.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38431,"numValue":7.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38432,"numValue":1.12,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38433,"numValue":null... | [{"id":19410,"numValue":5.0,"position":1573,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14019 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,019 | train | mutant | 4,751 | 270 | 5,290 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1573A | Y1573A | 1 | 1 | 0 | 0 | 1,573 | Y | A | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1573 | A|B | E | true | true | 27.146676 | 20.629365 | 12,468 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 2CK2_A:Y36A | null | null | null | -2.65 | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | DDG|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 779 | ARTICLE | Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. | 2,008 | 10.1016/j.jmb.2007.10.056 | 18035373 | J Mol Biol;375;560-71 | 4 | Rutherford Trevor J|Clarke Jane|Best Robert B|Billings Kate S | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":45222,"numValue":-2.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45223,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | [{"id":19410,"numValue":5.0,"position":1573,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14020 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,020 | train | mutant | 5,772 | 270 | 6,326 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1573F | Y1573F | 1 | 1 | 0 | 0 | 1,573 | Y | F | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1573 | A|B | E | true | true | 27.146676 | 20.629365 | 12,467 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 2CK2_A:Y36F | null | null | null | -0.27 | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | DDG|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 779 | ARTICLE | Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. | 2,008 | 10.1016/j.jmb.2007.10.056 | 18035373 | J Mol Biol;375;560-71 | 4 | Rutherford Trevor J|Clarke Jane|Best Robert B|Billings Kate S | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":45220,"numValue":-0.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45221,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | [{"id":19410,"numValue":5.0,"position":1573,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14021 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,021 | train | mutant | 5,773 | 270 | 6,327 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | E1575A | E1575A | 1 | 1 | 0 | 0 | 1,575 | E | A | 6 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1575 | A|B | E | true | false | 69.626747 | 28.367926 | 12,469 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 2CK2_A:E38A | null | null | null | -0.57 | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | DDG|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 779 | ARTICLE | Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. | 2,008 | 10.1016/j.jmb.2007.10.056 | 18035373 | J Mol Biol;375;560-71 | 4 | Rutherford Trevor J|Clarke Jane|Best Robert B|Billings Kate S | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":45224,"numValue":-0.57,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45225,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | [{"id":19412,"numValue":6.0,"position":1575,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14022 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,022 | train | mutant | 4,752 | 270 | 5,291 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | F1585A | F1585A | 1 | 1 | 0 | 0 | 1,585 | F | A | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1585 | A|B | E | true | false | 56.948526 | 23.698611 | 11,174 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:F48A | null | null | null | 2.16 | null | null | null | 1.14 | 6.8 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38434,"numValue":2.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38435,"numValue":6.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38436,"numValue":1.14,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38437,"numValue":null... | [{"id":19422,"numValue":5.0,"position":1585,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14023 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,023 | train | mutant | 4,753 | 270 | 5,292 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | V1587A | V1587A | 1 | 1 | 0 | 0 | 1,587 | V | A | 7 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1587 | A|B | E | true | false | 19.608121 | 21.379583 | 11,175 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:V50A | null | null | null | 2.42 | null | null | null | 1.1 | 5.7 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38438,"numValue":2.42,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38439,"numValue":5.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38440,"numValue":1.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38441,"numValue":null,... | [{"id":19424,"numValue":7.0,"position":1587,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14024 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,024 | train | mutant | 4,754 | 270 | 5,293 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | A1594G | A1594G | 1 | 1 | 0 | 0 | 1,594 | A | G | 7 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1594 | A|B | E | true | false | 27.840759 | 22.329444 | 11,176 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:A57G | null | null | null | 2.81 | null | null | null | 1.04 | 7.1 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38442,"numValue":2.81,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38443,"numValue":7.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38444,"numValue":1.04,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38445,"numValue":null... | [{"id":19431,"numValue":7.0,"position":1594,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14025 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,025 | train | mutant | 4,755 | 270 | 5,294 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1596A | I1596A | 1 | 1 | 0 | 0 | 1,596 | I | A | 8 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1596 | A|B | E | true | true | 9.241166 | 23.49199 | 11,177 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I59A | null | null | null | 3.66 | null | null | null | 0.91 | 7.2 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38446,"numValue":3.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38447,"numValue":7.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38448,"numValue":0.91,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38449,"numValue":null... | [{"id":19433,"numValue":8.0,"position":1596,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14026 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,026 | train | mutant | 4,755 | 270 | 5,294 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1596A | I1596A | 1 | 1 | 0 | 0 | 1,596 | I | A | 8 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1596 | A|B | E | true | true | 9.241166 | 23.49199 | 12,470 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 2CK2_A:I59A | null | null | null | -2.9 | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | DDG|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 779 | ARTICLE | Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. | 2,008 | 10.1016/j.jmb.2007.10.056 | 18035373 | J Mol Biol;375;560-71 | 4 | Rutherford Trevor J|Clarke Jane|Best Robert B|Billings Kate S | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":45226,"numValue":-2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45227,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | [{"id":19433,"numValue":8.0,"position":1596,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14027 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,027 | train | mutant | 4,756 | 270 | 5,295 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1596V | I1596V | 1 | 1 | 0 | 0 | 1,596 | I | V | 8 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1596 | A|B | E | true | true | 9.241166 | 23.49199 | 11,178 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I59V | null | null | null | 1.12 | null | null | null | 1.3 | 7.1 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38450,"numValue":1.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38451,"numValue":7.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38452,"numValue":1.3,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38453,"numValue":null,... | [{"id":19433,"numValue":8.0,"position":1596,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14028 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,028 | train | mutant | 4,757 | 270 | 5,296 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | L1599A | L1599A | 1 | 1 | 0 | 0 | 1,599 | L | A | 8 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1599 | A|B | L | true | true | 20.347687 | 29.278333 | 11,179 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:L62A | null | null | null | 2.94 | null | null | null | 1.02 | 6.6 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38454,"numValue":2.94,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38455,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38456,"numValue":1.02,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38457,"numValue":null... | [{"id":19436,"numValue":8.0,"position":1599,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14030 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,030 | train | mutant | 4,758 | 270 | 5,297 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | P1601A | P1601A | 1 | 1 | 0 | 0 | 1,601 | P | A | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1601 | A|B | S|T | true | false | 84.970799 | 33.178095 | 11,180 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:P64A | null | null | null | 0.41 | null | null | null | 1.41 | 6.6 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38458,"numValue":0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38459,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38460,"numValue":1.41,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":384... | [{"id":19438,"numValue":9.0,"position":1601,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14031 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,031 | train | mutant | 4,759 | 270 | 5,298 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | V1603A | V1603A | 1 | 1 | 0 | 0 | 1,603 | V | A | 6 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1603 | A|B | S|L | true | false | 28.823425 | 29.03881 | 11,181 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:V66A | null | null | null | 0.67 | null | null | null | 1.37 | 6.12 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38462,"numValue":0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38463,"numValue":6.12,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38464,"numValue":1.37,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38... | [{"id":19440,"numValue":6.0,"position":1603,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14032 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,032 | train | mutant | 4,678 | 270 | 5,214 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1605F | Y1605F | 1 | 1 | 0 | 0 | 1,605 | Y | F | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1605 | A|B | E | true | true | 16.715744 | 25.115992 | 11,020 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 50 mM | 25 | 1TTG_A:Y68F | null | null | null | -2.03 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 737 | ARTICLE | Conservation of folding and stability within a protein family: the tyrosine corner as an evolutionary cul-de-sac. | 2,000 | 10.1006/jmbi.1999.3360 | 10623553 | J Mol Biol;295;641-9 | 4 | Cota E|Chothia C|Clarke J|Hamill S J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","typ... | [{"datasets":[],"id":37933,"numValue":-2.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37934,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":19442,"numValue":9.0,"position":1605,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14033 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,033 | train | mutant | 4,678 | 270 | 5,214 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1605F | Y1605F | 1 | 1 | 0 | 0 | 1,605 | Y | F | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1605 | A|B | E | true | true | 16.715744 | 25.115992 | 11,182 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y68F | null | null | null | 2.03 | null | null | null | 1.16 | 6.2 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":38466,"numValue":2.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38467,"numValue":6.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38468,"numValue":1.16,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38469,"numValue":null,"references":[],"... | [{"id":19442,"numValue":9.0,"position":1605,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14034 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,034 | train | mutant | 4,678 | 270 | 5,214 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1605F | Y1605F | 1 | 1 | 0 | 0 | 1,605 | Y | F | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1605 | A|B | E | true | true | 16.715744 | 25.115992 | 12,472 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 2CK2_A:Y68F | null | null | null | -2.87 | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | DDG|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 779 | ARTICLE | Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. | 2,008 | 10.1016/j.jmb.2007.10.056 | 18035373 | J Mol Biol;375;560-71 | 4 | Rutherford Trevor J|Clarke Jane|Best Robert B|Billings Kate S | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":45230,"numValue":-2.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45231,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | [{"id":19442,"numValue":9.0,"position":1605,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14035 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,035 | train | mutant | 4,760 | 270 | 5,299 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1607A | I1607A | 1 | 1 | 0 | 0 | 1,607 | I | A | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1607 | A|B | E | true | true | 14.83811 | 18.561481 | 11,183 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I70A | null | null | null | 3.72 | null | null | null | 0.9 | 5.6 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38470,"numValue":3.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38471,"numValue":5.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38472,"numValue":0.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38473,"numValue":null,... | [{"id":19444,"numValue":5.0,"position":1607,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14038 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,038 | train | mutant | 4,763 | 270 | 5,302 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | A1611G | A1611G | 1 | 1 | 0 | 0 | 1,611 | A | G | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1611 | A|B | E | true | false | 2.410945 | 18.977222 | 11,186 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:A74G | null | null | null | 1.38 | null | null | null | 1.26 | 6.2 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38482,"numValue":1.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38483,"numValue":6.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38484,"numValue":1.26,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38485,"numValue":null... | [{"id":19448,"numValue":9.0,"position":1611,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14039 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,039 | train | mutant | 3,867 | 270 | 4,358 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | P1619A | P1619A | 1 | 1 | 0 | 0 | 1,619 | P | A | 9 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1619 | A|B | L|T | true | false | 80.588097 | 38.593334 | 8,968 | ProTherm | 5 | CD | Urea | sodium acetate | 50 mM | 25 | 1TTG_A:P82A | null | null | null | 0.42 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 609 | ARTICLE | Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily. | 2,002 | 10.1016/S0022-2836(02)00184-5 | 12054791 | J Mol Biol;318;935-40 | 3 | Steward Annette|Adhya Sima|Clarke Jane | [{"numValue":5.0,"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":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":30471,"numValue":0.42,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30472,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":19456,"numValue":9.0,"position":1619,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14040 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,040 | train | mutant | 4,764 | 270 | 5,303 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | S1622A | S1622A | 1 | 1 | 0 | 0 | 1,622 | S | A | 8 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1622 | A|B | L | true | false | 21.086101 | 20.375972 | 11,187 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:S85A | null | null | null | -0.11 | null | null | null | 1.49 | 6.5 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38486,"numValue":-0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38487,"numValue":6.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38488,"numValue":1.49,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38... | [{"id":19459,"numValue":8.0,"position":1622,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14041 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,041 | train | mutant | 3,868 | 270 | 4,359 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | P1624A | P1624A | 1 | 1 | 0 | 0 | 1,624 | P | A | 6 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1624 | A|B | L | true | false | 69.504506 | 26.878572 | 8,969 | ProTherm | 5 | CD | Urea | sodium acetate | 50 mM | 25 | 1TTG_A:P87A | null | null | null | 0.21 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 609 | ARTICLE | Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily. | 2,002 | 10.1016/S0022-2836(02)00184-5 | 12054791 | J Mol Biol;318;935-40 | 3 | Steward Annette|Adhya Sima|Clarke Jane | [{"numValue":5.0,"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":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":30473,"numValue":0.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30474,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":19461,"numValue":6.0,"position":1624,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14042 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,042 | train | mutant | 4,765 | 270 | 5,304 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1625A | I1625A | 1 | 1 | 0 | 0 | 1,625 | I | A | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1625 | A|B | E | true | false | 43.276396 | 20.541185 | 11,188 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I88A | null | null | null | 0.35 | null | null | null | 1.42 | 6.03 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38490,"numValue":0.35,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38491,"numValue":6.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38492,"numValue":1.42,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38... | [{"id":19462,"numValue":5.0,"position":1625,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14043 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,043 | train | mutant | 4,766 | 270 | 5,305 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1625V | I1625V | 1 | 1 | 0 | 0 | 1,625 | I | V | 5 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1625 | A|B | E | true | false | 43.276396 | 20.541185 | 11,189 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I88V | null | null | null | 0.35 | null | null | null | 1.42 | 6.5 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38494,"numValue":0.35,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38495,"numValue":6.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38496,"numValue":1.42,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":384... | [{"id":19462,"numValue":5.0,"position":1625,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14044 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,044 | train | mutant | 4,767 | 270 | 5,306 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1627A | I1627A | 1 | 1 | 0 | 0 | 1,627 | I | A | 6 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1627 | A|B | E | true | true | 40.985429 | 25.854583 | 11,190 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I90A | null | null | null | 0.35 | null | null | null | 1.42 | 6 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38498,"numValue":0.35,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38499,"numValue":6.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38500,"numValue":1.42,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":385... | [{"id":19464,"numValue":6.0,"position":1627,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14045 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,045 | train | mutant | 4,767 | 270 | 5,306 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1627A | I1627A | 1 | 1 | 0 | 0 | 1,627 | I | A | 6 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1627 | A|B | E | true | true | 40.985429 | 25.854583 | 11,229 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 1FNF_A:I1505A | null | null | 5.74 | 3.66 | null | null | null | 1.04 | 7.2 | null | null | null | null | null | null | null | 2.0 | DG|DDG|M|CM|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":38649,"numValue":5.74,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38650,"numValue":3.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38651,"numValue":7.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38652,"numValue":1.04,"references":[],"... | [{"id":19464,"numValue":6.0,"position":1627,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14046 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,046 | train | mutant | 4,768 | 270 | 5,307 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1627V | I1627V | 1 | 1 | 0 | 0 | 1,627 | I | V | 6 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1627 | A|B | E | true | true | 40.985429 | 25.854583 | 11,191 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:I90V | null | null | null | 0.28 | null | null | null | 1.43 | 6.3 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38502,"numValue":0.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38503,"numValue":6.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38504,"numValue":1.43,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":385... | [{"id":19464,"numValue":6.0,"position":1627,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14047 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,047 | train | mutant | 4,768 | 270 | 5,307 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | I1627V | I1627V | 1 | 1 | 0 | 0 | 1,627 | I | V | 6 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1627 | A|B | E | true | true | 40.985429 | 25.854583 | 11,230 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | 1FNF_A:I1505V | null | null | 8.28 | 1.12 | null | null | null | 0.91 | 7.1 | null | null | null | null | null | null | null | 2.0 | DG|DDG|M|CM|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50mM","ty... | [{"datasets":[],"id":38654,"numValue":8.28,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38655,"numValue":1.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38656,"numValue":7.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38657,"numValue":0.91,"references":[],"... | [{"id":19464,"numValue":6.0,"position":1627,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14048 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,048 | train | mutant | 4,769 | 270 | 5,308 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1629F | Y1629F | 1 | 1 | 0 | 0 | 1,629 | Y | F | 7 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1629 | A|B | E | true | true | 54.325537 | 29.766451 | 11,192 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y92F | null | null | null | -0.11 | null | null | null | 1.49 | 6.5 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38506,"numValue":-0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38507,"numValue":6.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38508,"numValue":1.49,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38... | [{"id":19466,"numValue":7.0,"position":1629,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14049 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,049 | train | mutant | 4,770 | 270 | 5,309 | 2,477 | 2,477 | 31 | Fibronectin | Homo sapiens | 1 | 31 | Fibronectin | Homo sapiens | 1 | P02751 | IPR050991|IPR000083|IPR003961|IPR036116|IPR000562|IPR036943|IPR013783|IPR013806 | Y1629A | Y1629A | 1 | 1 | 0 | 0 | 1,629 | Y | A | 7 | CONSERVATION | 1TTF|2CK2|1FNF|1TTG | 27|157|160|435 | null | 1629 | A|B | E | true | true | 54.325537 | 29.766451 | 11,193 | ProTherm | 5 | CD | GdnHCl | Sodium acetate | 50 mM | 25 | 1TTG_A:Y92A | null | null | null | 1.19 | null | null | null | 1.29 | 6.6 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 751 | ARTICLE | Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. | 2,000 | 10.1006/jmbi.2000.4053 | 10986129 | J Mol Biol;302;713-25 | 4 | Cota E|Clarke J|Hamill S J|Fowler S B | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["SAAFEC_S1262.csv"],"id":38510,"numValue":1.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38511,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38512,"numValue":1.29,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38513,"numValue":null... | [{"id":19466,"numValue":7.0,"position":1629,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14051 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,051 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,480 | ProTherm | 6.2 | DSC | Thermal | PIPES | 0.01 M | null | NaCl | 0.05 M | 54.8 | null | null | null | 128 | null | null | null | null | null | null | null | null | null | null | null | yes(54%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1008 | ARTICLE | Thermostability of the barnase-barstar complex. | 1,994 | 10.1016/0014-5793(94)01127-3 | 7957933 | FEBS Lett;354;251-4 | 4 | Protasevich I I|Lobachov V M|Kirpichnikov M P|Makarov A A | [{"numValue":6.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numV... | [{"datasets":[],"id":64489,"numValue":54.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64490,"numValue":128.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64491,"numValue":null,"references":[],"strValue":"yes(54%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14052 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,052 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,007 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 51.5 | null | null | null | 128.5 | null | 128.4 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08 mM,13.92 mM,","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66568,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66569,"numValue":128.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66570,"numValue":128.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66571,"numValue":null,"references"... | |||||||||||||||||||||||||
fireprotdb:14053 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,053 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,008 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 51.63 | null | null | null | 127.5 | null | 128.7 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08 mM,13.92 mM,","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66572,"numValue":51.63,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66573,"numValue":127.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66574,"numValue":128.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66575,"numValue":null,"references... | |||||||||||||||||||||||||
fireprotdb:14054 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,054 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,128 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | null | 53.9 | null | null | null | null | null | 125 | null | null | null | null | null | null | null | null | null | yes (>85%) | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66920,"numValue":53.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66921,"numValue":125.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66922,"numValue":null,"references":[],"strValue":"yes (>85%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14055 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,055 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,192 | ProTherm | 6.2 | DSC | Thermal | Na-acetate | 10 mM | null | NaCl | 0.05 M | 54.5 | null | null | null | 129 | null | 130 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 126 | ARTICLE | Key role of barstar Cys-40 residue in the mechanism of heat denaturation of bacterial ribonuclease complexes with barstar. | 1,999 | 10.1016/s0014-5793(99)00158-1 | 10094494 | FEBS Lett;445;384-8 | 6 | Protasevich I I|Schulga A A|Vasilieva L I|Polyakov K M|Lobachov V M|Hartley R W | [{"numValue":6.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Na-acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":67143,"numValue":54.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67144,"numValue":129.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67145,"numValue":130.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67146,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:14056 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,056 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,355 | ProTherm | 5.8 | DSC | Thermal | acetate | 10 mM | null | 54.3 | null | null | null | 125.6 | 1.37 | 124.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1096 | ARTICLE | Thermodynamics of barnase unfolding. | 1,994 | 10.1002/pro.5560030414 | 8003984 | Protein Sci;3;669-76 | 4 | Privalov P L|Hartley R W|Makhatadze G I|Griko Y V | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67741,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67742,"numValue":125.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67743,"numValue":1.37,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":67744,"numValue":124.2,"references":... | |||||||||||||||||||||||||
fireprotdb:14057 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,057 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,737 | ProTherm | 2 | DSC | Thermal | Potassium acetate | 50 mM | null | 24 | null | null | null | 82.5 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69061,"numValue":24.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69062,"numValue":82.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69063,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14058 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,058 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,738 | ProTherm | 2.5 | DSC | Thermal | Potassium acetate | 50 mM | null | 31.6 | null | null | null | 94.3 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69064,"numValue":31.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69065,"numValue":94.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69066,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14060 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,060 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,740 | ProTherm | 3.5 | DSC | Thermal | Potassium acetate | 50 mM | null | 46.7 | null | null | null | 118.9 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69070,"numValue":46.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69071,"numValue":118.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69072,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14061 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,061 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,741 | ProTherm | 4 | DSC | Thermal | Potassium acetate | 50 mM | null | 50.5 | null | null | null | 125.1 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69073,"numValue":50.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69074,"numValue":125.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69075,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14062 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,062 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,742 | ProTherm | 4.5 | DSC | Thermal | Potassium acetate | 50 mM | null | 53 | null | null | null | 129.2 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69076,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69077,"numValue":129.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69078,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14063 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,063 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,743 | ProTherm | 5 | DSC | Thermal | Potassium acetate | 50 mM | null | 53.9 | null | null | null | 130.6 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69079,"numValue":53.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69080,"numValue":130.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69081,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14064 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,064 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,903 | ProTherm | 7 | DSC | Thermal | PIPES | 50 mM | null | 54 | null | null | null | 131.6 | null | null | null | null | null | null | null | null | null | null | null | yes (~80%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 912 | ARTICLE | A calorimetric study of the thermal stability of barstar and its interaction with barnase. | 1,995 | 10.1021/bi00015a036 | 7711042 | Biochemistry;34;5224-33 | 5 | Schreiber G|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69750,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69751,"numValue":131.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69752,"numValue":null,"references":[],"strValue":"yes (~80%)","type":"REVERSIBILITY"}] |
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