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:13836 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,836 | train | mutant | 4,906,156 | 225 | 4,912,744 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271E | Q271E | 1 | 1 | 0 | 0 | 271 | Q | E | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,411 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.053369 | 0.072407 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183504,"numValue":0.0533693297220615,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183505,"numValue":0.0724073400146565,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13838 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,838 | train | mutant | 4,906,158 | 225 | 4,912,746 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271G | Q271G | 1 | 1 | 0 | 0 | 271 | Q | G | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,413 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.00996 | 0.046365 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183508,"numValue":0.00995965440834673,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183509,"numValue":0.0463645425354366,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13839 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,839 | train | mutant | 4,906,159 | 225 | 4,912,747 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271H | Q271H | 1 | 1 | 0 | 0 | 271 | Q | H | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,414 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.013463 | 0.066529 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183510,"numValue":-0.0134630784204863,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183511,"numValue":0.0665285022222215,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13840 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,840 | train | mutant | 4,906,160 | 225 | 4,912,748 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271I | Q271I | 1 | 1 | 0 | 0 | 271 | Q | I | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,415 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.128283 | 0.070558 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183512,"numValue":-0.128282767677757,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183513,"numValue":0.0705579888624297,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13841 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,841 | train | mutant | 4,906,161 | 225 | 4,912,749 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271K | Q271K | 1 | 1 | 0 | 0 | 271 | Q | K | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,416 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.117475 | 0.068859 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183514,"numValue":0.117474907501311,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183515,"numValue":0.0688585775741246,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13842 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,842 | train | mutant | 4,906,162 | 225 | 4,912,750 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271L | Q271L | 1 | 1 | 0 | 0 | 271 | Q | L | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,417 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.114789 | 0.053404 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183516,"numValue":-0.11478945302914,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183517,"numValue":0.0534036000995774,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13843 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,843 | train | mutant | 4,906,163 | 225 | 4,912,751 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271M | Q271M | 1 | 1 | 0 | 0 | 271 | Q | M | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,418 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.070368 | 0.076153 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183518,"numValue":-0.0703676597632465,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183519,"numValue":0.0761530437400499,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13844 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,844 | train | mutant | 4,906,164 | 225 | 4,912,752 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271N | Q271N | 1 | 1 | 0 | 0 | 271 | Q | N | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,419 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.065906 | 0.067847 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183520,"numValue":0.065906224733479,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183521,"numValue":0.0678470006912917,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13845 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,845 | train | mutant | 4,906,165 | 225 | 4,912,753 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271P | Q271P | 1 | 1 | 0 | 0 | 271 | Q | P | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,420 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.28325 | 0.061712 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183522,"numValue":-0.283249802371438,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183523,"numValue":0.0617119029085433,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13846 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,846 | train | mutant | 4,906,186 | 225 | 4,912,774 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271R | Q271R | 1 | 1 | 0 | 0 | 271 | Q | R | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,441 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.138788 | 0.047813 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183564,"numValue":-0.138788265572892,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183565,"numValue":0.047813311406339,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13847 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,847 | train | mutant | 4,906,187 | 225 | 4,912,775 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271S | Q271S | 1 | 1 | 0 | 0 | 271 | Q | S | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,442 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.038414 | 0.050307 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183566,"numValue":-0.0384135364601547,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183567,"numValue":0.0503073864682448,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13849 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,849 | train | mutant | 4,906,189 | 225 | 4,912,777 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271V | Q271V | 1 | 1 | 0 | 0 | 271 | Q | V | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,444 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.066933 | 0.049647 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183570,"numValue":-0.0669334607997229,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183571,"numValue":0.0496473932633596,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13850 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,850 | train | mutant | 4,906,190 | 225 | 4,912,778 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271W | Q271W | 1 | 1 | 0 | 0 | 271 | Q | W | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,445 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.240132 | 0.061568 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183572,"numValue":-0.240132145366252,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183573,"numValue":0.0615681137299756,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13851 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,851 | train | mutant | 4,906,191 | 225 | 4,912,779 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q271Y | Q271Y | 1 | 1 | 0 | 0 | 271 | Q | Y | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,446 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.0577 | 0.070154 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183574,"numValue":-0.0577002715567368,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183575,"numValue":0.0701543272599771,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16935,"numValue":8.0,"position":271,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13852 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,852 | train | mutant | 4,906,166 | 225 | 4,912,754 | 504 | 503 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | delR272 | delR272 | 1 | 0 | 1 | 0 | 272 | R | - | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,421 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.188525 | 0.443633 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183524,"numValue":-1.18852524161899,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183525,"numValue":0.44363262293753,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13854 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,854 | train | mutant | 4,906,168 | 225 | 4,912,756 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272C | R272C | 1 | 1 | 0 | 0 | 272 | R | C | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,423 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.343085 | 0.078379 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183528,"numValue":-0.343084910772274,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183529,"numValue":0.0783790428119648,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13855 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,855 | train | mutant | 4,906,169 | 225 | 4,912,757 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272D | R272D | 1 | 1 | 0 | 0 | 272 | R | D | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,424 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.082666 | 0.083654 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183530,"numValue":0.082665847710471,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183531,"numValue":0.0836544132323155,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13856 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,856 | train | mutant | 4,906,170 | 225 | 4,912,758 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272E | R272E | 1 | 1 | 0 | 0 | 272 | R | E | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,425 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.082976 | 1.393667 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183532,"numValue":-0.0829761668939217,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183533,"numValue":1.39366652789431,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13857 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,857 | train | mutant | 4,906,171 | 225 | 4,912,759 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272F | R272F | 1 | 1 | 0 | 0 | 272 | R | F | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,426 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.085275 | 0.107296 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183534,"numValue":-0.0852749159221006,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183535,"numValue":0.107296040439014,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13859 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,859 | train | mutant | 4,906,173 | 225 | 4,912,761 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272H | R272H | 1 | 1 | 0 | 0 | 272 | R | H | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,428 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.152146 | 0.11111 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183538,"numValue":-0.152145517194919,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183539,"numValue":0.111110022341668,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13860 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,860 | train | mutant | 4,906,174 | 225 | 4,912,762 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272I | R272I | 1 | 1 | 0 | 0 | 272 | R | I | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,429 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.060204 | 0.122408 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183540,"numValue":0.0602035129699076,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183541,"numValue":0.122407709413838,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13861 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,861 | train | mutant | 4,906,175 | 225 | 4,912,763 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272K | R272K | 1 | 1 | 0 | 0 | 272 | R | K | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,430 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.262947 | 0.144239 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183542,"numValue":-0.262946970871607,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183543,"numValue":0.144239459659825,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13863 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,863 | train | mutant | 4,906,177 | 225 | 4,912,765 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272M | R272M | 1 | 1 | 0 | 0 | 272 | R | M | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,432 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.17764 | 0.10268 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183546,"numValue":-0.177640227340948,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183547,"numValue":0.102679843662628,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13864 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,864 | train | mutant | 4,906,178 | 225 | 4,912,766 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272N | R272N | 1 | 1 | 0 | 0 | 272 | R | N | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,433 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.019658 | 0.073728 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183548,"numValue":0.0196575267362953,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183549,"numValue":0.0737275173900782,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13865 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,865 | train | mutant | 4,906,179 | 225 | 4,912,767 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272P | R272P | 1 | 1 | 0 | 0 | 272 | R | P | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,434 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.311144 | 0.082629 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183550,"numValue":-0.311143518512606,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183551,"numValue":0.0826285298394353,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13866 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,866 | train | mutant | 4,906,180 | 225 | 4,912,768 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272Q | R272Q | 1 | 1 | 0 | 0 | 272 | R | Q | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,435 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.336274 | 0.259644 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183552,"numValue":-0.336273802540633,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183553,"numValue":0.25964350381024,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13867 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,867 | train | mutant | 4,906,181 | 225 | 4,912,769 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272S | R272S | 1 | 1 | 0 | 0 | 272 | R | S | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,436 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.102123 | 0.07069 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183554,"numValue":-0.102122860512844,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183555,"numValue":0.0706900734379498,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13868 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,868 | train | mutant | 4,906,182 | 225 | 4,912,770 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272T | R272T | 1 | 1 | 0 | 0 | 272 | R | T | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,437 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.053723 | 0.068479 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183556,"numValue":-0.0537234118672811,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183557,"numValue":0.0684793516181433,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13869 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,869 | train | mutant | 4,906,183 | 225 | 4,912,771 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272V | R272V | 1 | 1 | 0 | 0 | 272 | R | V | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,438 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.177055 | 0.083028 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183558,"numValue":-0.177055395033675,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183559,"numValue":0.0830283641719586,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13870 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,870 | train | mutant | 4,906,184 | 225 | 4,912,772 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272W | R272W | 1 | 1 | 0 | 0 | 272 | R | W | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,439 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.211075 | 0.111293 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183560,"numValue":-0.21107513013225,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183561,"numValue":0.11129287195284,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13871 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,871 | train | mutant | 4,906,185 | 225 | 4,912,773 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | R272Y | R272Y | 1 | 1 | 0 | 0 | 272 | R | Y | 4 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,095,440 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.093355 | 0.070018 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12183562,"numValue":-0.0933551500450341,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12183563,"numValue":0.0700183835869192,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16936,"numValue":4.0,"position":272,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:13872 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,872 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,092 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 43.7 | null | null | null | 238 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":70444,"numValue":43.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70445,"numValue":238.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70446,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:13873 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,873 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,104 | ProTherm | 5.7 | DSC | Thermal | MES | 30 mM | null | NaCl | 50 mM | 30.6 | null | null | null | 138 | null | 135 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":70491,"numValue":30.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70492,"numValue":138.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70493,"numValue":135.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":70494,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13874 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,874 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,105 | ProTherm | 5.8 | DSC | Thermal | MES | 30 mM | null | NaCl | 50 mM | 32 | null | null | null | 139 | null | 145 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":70495,"numValue":32.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70496,"numValue":139.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70497,"numValue":145.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":70498,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13875 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,875 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,106 | ProTherm | 5.9 | DSC | Thermal | MES | 30 mM | null | NaCl | 50 mM | 34.4 | null | null | null | 166 | null | 175 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":5.9,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":70499,"numValue":34.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70500,"numValue":166.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70501,"numValue":175.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":70502,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13876 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,876 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,107 | ProTherm | 6 | DSC | Thermal | MES | 30 mM | null | NaCl | 50 mM | 34.7 | null | null | null | 159 | null | 166 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":70503,"numValue":34.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70504,"numValue":159.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70505,"numValue":166.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":70506,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13877 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,877 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,108 | ProTherm | 6.1 | DSC | Thermal | MES | 30 mM | null | NaCl | 50 mM | 37.3 | null | null | null | 179 | null | 188 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":6.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":70507,"numValue":37.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70508,"numValue":179.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70509,"numValue":188.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":70510,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13878 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,878 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,109 | ProTherm | 6.2 | DSC | Thermal | MES | 30 mM | null | NaCl | 50 mM | 37.9 | null | null | null | 195 | null | 210 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":6.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":70511,"numValue":37.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70512,"numValue":195.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70513,"numValue":210.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":70514,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13880 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,880 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,111 | ProTherm | 6.4 | DSC | Thermal | MES | 30 mM | null | NaCl | 50 mM | 40.7 | null | null | null | 223 | null | 231 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValu... | [{"datasets":[],"id":70519,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70520,"numValue":223.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70521,"numValue":231.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":70522,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13881 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,881 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,112 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 43.7 | null | null | null | 238 | null | 224 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1215 | ARTICLE | Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. | 1,999 | 10.1021/bi982650+ | 10194383 | Biochemistry;38;4613-9 | 3 | Gerday C|Feller G|d'Amico D | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":70523,"numValue":43.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70524,"numValue":238.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70525,"numValue":224.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":70526,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13882 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,882 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,244 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 44 | null | null | null | 214 | null | 203 | null | null | null | null | null | null | null | null | null | yes(100 %) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":80415,"numValue":44.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80416,"numValue":214.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":80417,"numValue":203.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":80418,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:13883 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,883 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,801 | ProTherm | 7.2 | DSC | Thermal | Mops | 30 mM | null | NaCl | 50 mM | 44 | null | null | null | 214 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 944 | ARTICLE | Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase. | 2,003 | 10.1016/j.jmb.2003.07.014 | 14499602 | J Mol Biol;332;981-8 | 3 | D'Amico Salvino|Gerday Charles|Feller Georges | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":82102,"numValue":44.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":82103,"numValue":214.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":82104,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:13885 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,885 | train | sequence | 246 | 246 | -1 | 669 | -1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 27,085 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | 20 | NaCl | 50 mM | null | null | 8.33 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 948 | ARTICLE | Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase. | 2,002 | 10.1074/jbc.M207253200 | 12324460 | J Biol Chem;277;46110-5 | 3 | D'Amico Salvino|Gerday Charles|Feller Georges | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":95070,"numValue":8.33,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":95071,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:13886 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,886 | train | mutant | 226 | 246 | 256 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | N36R | N36R | 1 | 1 | 0 | 0 | 36 | N | R | 6 | CONSERVATION | 1AQH | 402 | null | 36 | A | L | true | false | 48.345563 | 15.581818 | 411 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:N12R | 43.3 | null | null | null | 193 | null | 231 | null | null | null | null | null | null | null | null | null | yes(25 %) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1695,"numValue":43.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1696,"numValue":193.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1697,"numValue":231.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1698,"numValue":null,"references":[],... | [{"id":17204,"numValue":6.0,"position":36,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:13887 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,887 | train | mutant | 7,409 | 246 | 8,092 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | Q82C|A123C | Q82C|A123C | 2 | 2 | 0 | 0 | 82 | Q | C | 4 | CONSERVATION | 1AQH | 402 | null | 82|123 | A | L|T | false | false | 52.575186 | 23.71125 | 15,803 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:Q58C 1AQH_A:A99C | 40 | -4 | null | null | 78 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 948 | ARTICLE | Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase. | 2,002 | 10.1074/jbc.M207253200 | 12324460 | J Biol Chem;277;46110-5 | 3 | D'Amico Salvino|Gerday Charles|Feller Georges | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":58037,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58038,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58039,"numValue":78.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":58040,"numValue":null,"references":[]... | [{"id":17250,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":17291,"numValue":6.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:13889 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,889 | train | mutant | 7,409 | 246 | 8,092 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | Q82C|A123C | Q82C|A123C | 2 | 2 | 0 | 0 | 82 | Q | C | 4 | CONSERVATION | 1AQH | 402 | null | 82|123 | A | L|T | false | false | 52.575186 | 23.71125 | 17,300 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | 20 | NaCl | 50 mM | 1AQH_A:Q58C 1AQH_A:A99C | null | null | 3.19 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 948 | ARTICLE | Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase. | 2,002 | 10.1074/jbc.M207253200 | 12324460 | J Biol Chem;277;46110-5 | 3 | D'Amico Salvino|Gerday Charles|Feller Georges | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":63897,"numValue":3.19,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63898,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":63899,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":17250,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":17291,"numValue":6.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13890 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,890 | train | mutant | 7,409 | 246 | 8,092 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | Q82C|A123C | Q82C|A123C | 2 | 2 | 0 | 0 | 82 | Q | C | 4 | CONSERVATION | 1AQH | 402 | null | 82|123 | A | L|T | false | false | 52.575186 | 23.71125 | 17,301 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | 20 | NaCl | 50 mM | 1AQH_A:Q58C 1AQH_A:A99C | null | null | 7.01 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 948 | ARTICLE | Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase. | 2,002 | 10.1074/jbc.M207253200 | 12324460 | J Biol Chem;277;46110-5 | 3 | D'Amico Salvino|Gerday Charles|Feller Georges | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":63900,"numValue":7.01,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63901,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":63902,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":17250,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":17291,"numValue":6.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13891 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,891 | train | mutant | 7,409 | 246 | 8,092 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | Q82C|A123C | Q82C|A123C | 2 | 2 | 0 | 0 | 82 | Q | C | 4 | CONSERVATION | 1AQH | 402 | null | 82|123 | A | L|T | false | false | 52.575186 | 23.71125 | 17,302 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | 20 | NaCl | 50 mM | 1AQH_A:Q58C 1AQH_A:A99C | null | null | 10.2 | -1.87 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 948 | ARTICLE | Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase. | 2,002 | 10.1074/jbc.M207253200 | 12324460 | J Biol Chem;277;46110-5 | 3 | D'Amico Salvino|Gerday Charles|Feller Georges | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":63903,"numValue":10.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63904,"numValue":-1.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63905,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":63906,"numValue":null,"references"... | [{"id":17250,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":17291,"numValue":6.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13892 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,892 | train | mutant | 224 | 246 | 254 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | R88E | R88E | 1 | 1 | 0 | 0 | 88 | R | E | 6 | CONSERVATION | 1AQH | 402 | null | 88 | A | H | false | false | 118.520005 | 20.915294 | 409 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:R64E | 42.6 | null | null | null | 236 | null | 112 | null | null | null | null | null | null | null | null | null | yes(96 %) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1687,"numValue":42.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1688,"numValue":236.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1689,"numValue":112.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1690,"numValue":null,"references":[],... | [{"id":17256,"numValue":6.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:13893 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,893 | train | mutant | 218 | 246 | 248 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | N174D | N174D | 1 | 1 | 0 | 0 | 174 | N | D | 2 | CONSERVATION | 1AQH | 402 | null | 174 | A | H | false | false | 96.844633 | 12.984546 | 399 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:N150D | 44.8 | null | null | null | 271 | null | 240 | null | null | null | null | null | null | null | null | null | yes(97 %) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1639,"numValue":44.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1640,"numValue":271.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1641,"numValue":240.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1642,"numValue":null,"references":[],... | [{"id":17342,"numValue":2.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:13894 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,894 | train | mutant | 7,305 | 246 | 7,975 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | N174D|V220F | N174D|V220F | 2 | 2 | 0 | 0 | 174 | N | D | 2 | CONSERVATION | 1AQH | 402 | null | 174|220 | A | H|E | false | false | 78.08335 | 16.297898 | 15,664 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:N150D 1AQH_A:V196F | 46.4 | null | null | null | 272 | null | 271 | null | null | null | null | null | null | null | null | null | yes(91 %) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57487,"numValue":46.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57488,"numValue":272.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":57489,"numValue":271.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":57490,"numValue":null,"references"... | [{"id":17342,"numValue":2.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":17388,"numValue":7.0,"position":220,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:13896 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,896 | train | mutant | 7,369 | 246 | 8,039 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | K324R|N174D|V220F|Q188I|T256V | K324R|N174D|V220F|Q188I|T256V | 5 | 5 | 0 | 0 | 324 | K | R | 2 | BINDING_SITE|CONSERVATION | 1AQH | 402 | null | 174|188|220|256|324 | A | H|E | true | false | 41.830473 | 14.702155 | 15,757 | ProTherm | 7.2 | DSC | Thermal | Mops | 30 mM | null | NaCl | 50 mM | 1AQH_A:N150D 1AQH_A:Q164I 1AQH_A:V196F 1AQH_A:T232V 1AQH_A:K300R | 51.8 | 7.8 | null | null | 277 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 944 | ARTICLE | Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase. | 2,003 | 10.1016/j.jmb.2003.07.014 | 14499602 | J Mol Biol;332;981-8 | 3 | D'Amico Salvino|Gerday Charles|Feller Georges | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mops","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57853,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57854,"numValue":7.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57855,"numValue":277.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":57856,"numValue":null,"references":[]... | [{"id":99,"numValue":null,"position":324,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":17342,"numValue":2.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":17356,"numValue":6.0,"position":188,"positionArray":null,"positionRan... | |||||||||||
fireprotdb:13897 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,897 | train | mutant | 220 | 246 | 250 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | Q188I | Q188I | 1 | 1 | 0 | 0 | 188 | Q | I | 6 | CONSERVATION | 1AQH | 402 | null | 188 | A | H | false | false | 44.347583 | 14.589167 | 401 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:Q164I | 42.7 | null | null | null | 87 | null | 117 | null | null | null | null | null | null | null | null | null | yes(64 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1647,"numValue":42.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1648,"numValue":87.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1649,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1650,"numValue":3.0,"references":[],"s... | [{"id":17356,"numValue":6.0,"position":188,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13898 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,898 | train | mutant | 220 | 246 | 250 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | Q188I | Q188I | 1 | 1 | 0 | 0 | 188 | Q | I | 6 | CONSERVATION | 1AQH | 402 | null | 188 | A | H | false | false | 44.347583 | 14.589167 | 402 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:Q164I | 45.2 | null | null | null | 117 | null | 240 | null | null | null | null | null | null | null | null | null | yes(64 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1652,"numValue":45.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1653,"numValue":117.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1654,"numValue":240.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1655,"numValue":3.0,"references":[],"... | [{"id":17356,"numValue":6.0,"position":188,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13899 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,899 | train | mutant | 7,306 | 246 | 7,976 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | Q188I|V220F | Q188I|V220F | 2 | 2 | 0 | 0 | 188 | Q | I | 6 | CONSERVATION | 1AQH | 402 | null | 188|220 | A | H|E | false | false | 51.834825 | 17.100209 | 15,665 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:Q164I 1AQH_A:V196F | 44.7 | null | null | null | 83 | null | 121 | null | null | null | null | null | null | null | null | null | yes(51 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57491,"numValue":44.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57492,"numValue":83.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":57493,"numValue":121.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":57494,"numValue":3.0,"references":[... | [{"id":17356,"numValue":6.0,"position":188,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":17388,"numValue":7.0,"position":220,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13901 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,901 | train | mutant | 219 | 246 | 249 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | V220F | V220F | 1 | 1 | 0 | 0 | 220 | V | F | 7 | CONSERVATION | 1AQH | 402 | null | 220 | A | E | false | false | 59.322068 | 19.61125 | 400 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:V196F | 45.4 | null | null | null | 234 | null | 296 | null | null | null | null | null | null | null | null | null | yes(60 %) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1643,"numValue":45.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1644,"numValue":234.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1645,"numValue":296.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1646,"numValue":null,"references":[],... | [{"id":17388,"numValue":7.0,"position":220,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:13902 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,902 | train | mutant | 225 | 246 | 255 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | L243R | L243R | 1 | 1 | 0 | 0 | 243 | L | R | 6 | CONSERVATION | 1AQH | 402 | null | 243 | A | E | false | false | 40.848767 | 15.766667 | 410 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:L219R | 42.5 | null | null | null | 217 | null | 187 | null | null | null | null | null | null | null | null | null | yes(81 %) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1691,"numValue":42.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1692,"numValue":217.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1693,"numValue":187.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1694,"numValue":null,"references":[],... | [{"id":17411,"numValue":6.0,"position":243,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:13903 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,903 | train | mutant | 221 | 246 | 251 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | T256V | T256V | 1 | 1 | 0 | 0 | 256 | T | V | 5 | CONSERVATION | 1AQH | 402 | null | 256 | A | H | false | false | 2.830271 | 14.098889 | 403 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:T232V | 42.7 | null | null | null | 102 | null | 114 | null | null | null | null | null | null | null | null | null | yes(85 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1657,"numValue":42.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1658,"numValue":102.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1659,"numValue":114.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1660,"numValue":3.0,"references":[],"... | [{"id":17424,"numValue":5.0,"position":256,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13904 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,904 | train | mutant | 221 | 246 | 251 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | T256V | T256V | 1 | 1 | 0 | 0 | 256 | T | V | 5 | CONSERVATION | 1AQH | 402 | null | 256 | A | H | false | false | 2.830271 | 14.098889 | 404 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:T232V | 45.7 | null | null | null | 104 | null | 202 | null | null | null | null | null | null | null | null | null | yes(85 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1662,"numValue":45.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1663,"numValue":104.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1664,"numValue":202.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1665,"numValue":3.0,"references":[],"... | [{"id":17424,"numValue":5.0,"position":256,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13905 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,905 | train | mutant | 227 | 246 | 257 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | E303W | E303W | 1 | 1 | 0 | 0 | 303 | E | W | 5 | CONSERVATION | 1AQH | 402 | null | 303 | A | G | false | false | 121.588994 | 25.873 | 412 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:E279W | 41.4 | null | null | null | 186 | null | 234 | null | null | null | null | null | null | null | null | null | yes(76 %) | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1699,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1700,"numValue":186.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1701,"numValue":234.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1702,"numValue":null,"references":[],... | [{"id":17471,"numValue":5.0,"position":303,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:13906 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,906 | train | mutant | 222 | 246 | 252 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | N312V | N312V | 1 | 1 | 0 | 0 | 312 | N | V | 5 | CONSERVATION | 1AQH | 402 | null | 312 | A | H | true | false | 1.083724 | 9.051818 | 405 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:N288V | 38.1 | null | null | null | 88 | null | 133 | null | null | null | null | null | null | null | null | null | yes(30 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1667,"numValue":38.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1668,"numValue":88.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1669,"numValue":133.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1670,"numValue":3.0,"references":[],"s... | [{"id":17480,"numValue":5.0,"position":312,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13907 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,907 | train | mutant | 222 | 246 | 252 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | N312V | N312V | 1 | 1 | 0 | 0 | 312 | N | V | 5 | CONSERVATION | 1AQH | 402 | null | 312 | A | H | true | false | 1.083724 | 9.051818 | 406 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:N288V | 45.9 | null | null | null | 59 | null | 114 | null | null | null | null | null | null | null | null | null | yes(30 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1672,"numValue":45.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1673,"numValue":59.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1674,"numValue":114.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1675,"numValue":3.0,"references":[],"s... | [{"id":17480,"numValue":5.0,"position":312,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13909 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,909 | train | mutant | 223 | 246 | 253 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | M403V | M403V | 1 | 1 | 0 | 0 | 403 | M | V | 7 | CONSERVATION | 1AQH | 402 | null | 403 | A | E | true | false | 0.134371 | 12.292222 | 407 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:M379V | 42.6 | null | null | null | 127 | null | 96 | null | null | null | null | null | null | null | null | null | yes(95 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1677,"numValue":42.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1678,"numValue":127.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1679,"numValue":96.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1680,"numValue":3.0,"references":[],"s... | [{"id":17571,"numValue":7.0,"position":403,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13910 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,910 | train | mutant | 223 | 246 | 253 | 669 | 669 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | 30 | Alpha-amylase | Pseudoalteromonas haloplanktis | 1 | P29957 | IPR006048|IPR031319|IPR006046|IPR006047|IPR013780|IPR017853 | 3.2.1.1 | M403V | M403V | 1 | 1 | 0 | 0 | 403 | M | V | 7 | CONSERVATION | 1AQH | 402 | null | 403 | A | E | true | false | 0.134371 | 12.292222 | 408 | ProTherm | 7.2 | DSC | Thermal | MOPS | 30 mM | null | NaCl | 50 mM | 1AQH_A:M379V | 47.7 | null | null | null | 84 | null | 137 | null | null | null | null | null | null | null | null | null | yes(95 %) | 3.0 | TM|DH|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 42 | ARTICLE | Structural determinants of cold adaptation and stability in a large protein. | 2,001 | 10.1074/jbc.M102741200 | 11325973 | J Biol Chem;276;25791-6 | 3 | D'Amico S|Gerday C|Feller G | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":1682,"numValue":47.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1683,"numValue":84.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1684,"numValue":137.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1685,"numValue":3.0,"references":[],"s... | [{"id":17571,"numValue":7.0,"position":403,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:13911 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,911 | 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 | 19,394 | ProTherm | 9.5 | DSC | Thermal | Tris | 0.02 M | null | NaCl | 0.15 M | 60.9 | null | null | null | 112 | null | 81 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1240 | ARTICLE | Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded. | 1,991 | 10.1016/0022-2836(91)90758-x | 1994038 | J Mol Biol;217;563-75 | 4 | Medved L V|Strickland D K|Ingham K C|Litvinovich S V | [{"numValue":9.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":71395,"numValue":60.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71396,"numValue":112.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71397,"numValue":81.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71398,"numValue":null,"references":... | ||||||||||||||||||||||||
fireprotdb:13912 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,912 | 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 | 19,395 | ProTherm | 8 | DSC | Thermal | Tris | 0.02 M | null | NaCl | 0.15 M | 64.1 | null | null | null | 130 | null | 74 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1240 | ARTICLE | Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded. | 1,991 | 10.1016/0022-2836(91)90758-x | 1994038 | J Mol Biol;217;563-75 | 4 | Medved L V|Strickland D K|Ingham K C|Litvinovich S V | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":71399,"numValue":64.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71400,"numValue":130.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71401,"numValue":74.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71402,"numValue":null,"references":... | ||||||||||||||||||||||||
fireprotdb:13914 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,914 | 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 | 19,397 | ProTherm | 4.1 | DSC | Thermal | acetate | 0.01 M | null | NaCl | 0.15 M | 56 | null | null | null | 89 | null | 75 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1240 | ARTICLE | Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded. | 1,991 | 10.1016/0022-2836(91)90758-x | 1994038 | J Mol Biol;217;563-75 | 4 | Medved L V|Strickland D K|Ingham K C|Litvinovich S V | [{"numValue":4.1,"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":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":71407,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71408,"numValue":89.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71409,"numValue":75.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71410,"numValue":null,"references":[... | ||||||||||||||||||||||||
fireprotdb:13915 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,915 | 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 | 19,398 | ProTherm | 3.4 | DSC | Thermal | glycine | 0.05 M | null | 51.8 | null | null | null | 82 | null | 63 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1240 | ARTICLE | Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded. | 1,991 | 10.1016/0022-2836(91)90758-x | 1994038 | J Mol Biol;217;563-75 | 4 | Medved L V|Strickland D K|Ingham K C|Litvinovich S V | [{"numValue":3.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71411,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71412,"numValue":82.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71413,"numValue":63.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71414,"numValue":null,"references":[... | ||||||||||||||||||||||||||
fireprotdb:13916 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,916 | 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 | 19,399 | ProTherm | 2.5 | DSC | Thermal | glycine | 0.05 M | null | 37.5 | null | null | null | 69 | null | 53 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1240 | ARTICLE | Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded. | 1,991 | 10.1016/0022-2836(91)90758-x | 1994038 | J Mol Biol;217;563-75 | 4 | Medved L V|Strickland D K|Ingham K C|Litvinovich S V | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71415,"numValue":37.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71416,"numValue":69.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71417,"numValue":53.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71418,"numValue":null,"references":[... | ||||||||||||||||||||||||||
fireprotdb:13917 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,917 | 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 | 19,400 | ProTherm | 2.5 | DSC | Thermal | H3PO4 | 0.01 M | null | NaCl | 0.15 M | 37.3 | null | null | null | 62 | null | 50 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1240 | ARTICLE | Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded. | 1,991 | 10.1016/0022-2836(91)90758-x | 1994038 | J Mol Biol;217;563-75 | 4 | Medved L V|Strickland D K|Ingham K C|Litvinovich S V | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numV... | [{"datasets":[],"id":71419,"numValue":37.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71420,"numValue":62.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71421,"numValue":50.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71422,"numValue":null,"references":[... | ||||||||||||||||||||||||
fireprotdb:13918 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,918 | 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 | 19,515 | ProTherm | 4 | DSC | Thermal | glycine | 50 mM | null | 74.8 | null | null | null | 58.56 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71830,"numValue":74.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71831,"numValue":58.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71832,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13919 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,919 | 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 | 19,516 | ProTherm | 4 | DSC | Thermal | glycine | 50 mM | null | 73.1 | null | null | null | 46.61 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71833,"numValue":73.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71834,"numValue":46.61,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71835,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13920 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,920 | 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 | 19,517 | ProTherm | 7.4 | DSC | Thermal | glycine | 50 mM | null | 64 | null | null | null | 41.83 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71836,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71837,"numValue":41.83,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71838,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13921 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,921 | 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 | 19,518 | ProTherm | 4 | DSC | Thermal | glycine | 50 mM | null | 60.7 | null | null | null | 83.65 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71839,"numValue":60.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71840,"numValue":83.65,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71841,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13922 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,922 | 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 | 19,519 | ProTherm | 8 | DSC | Thermal | glycine | 50 mM | null | 63 | null | null | null | 131.45 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71842,"numValue":63.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71843,"numValue":131.45,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71844,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13923 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,923 | 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 | 19,520 | ProTherm | 8 | DSC | Thermal | glycine | 50 mM | null | 86 | null | null | null | 71.7 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71845,"numValue":86.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71846,"numValue":71.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71847,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13924 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,924 | 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 | 19,521 | ProTherm | 8 | DSC | Thermal | glycine | 50 mM | null | 62 | null | null | null | 69.31 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71848,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71849,"numValue":69.31,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71850,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13925 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,925 | 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 | 19,522 | ProTherm | 8 | DSC | Thermal | glycine | 50 mM | null | 66 | null | null | null | 62.14 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71851,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71852,"numValue":62.14,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71853,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13926 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,926 | 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 | 19,523 | ProTherm | 4 | DSC | Thermal | glycine | 50 mM | null | 70 | null | null | null | 47.8 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71854,"numValue":70.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71855,"numValue":47.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71856,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13927 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,927 | 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 | 19,524 | ProTherm | 8 | DSC | Thermal | glycine | 50 mM | null | 56 | null | null | null | 74.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71857,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71858,"numValue":74.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71859,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13928 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,928 | 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 | 19,525 | ProTherm | 8 | DSC | Thermal | glycine | 50 mM | null | 60 | null | null | null | 88.43 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71860,"numValue":60.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71861,"numValue":88.43,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71862,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13929 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,929 | 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 | 19,526 | ProTherm | 8 | DSC | Thermal | glycine | 50 mM | null | 90 | null | null | null | 92.02 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1255 | ARTICLE | Co-operative domains in fibronectin. | 1,990 | 10.1016/0022-2836(90)90018-H | 2299666 | J Mol Biol;211;161-9 | 4 | Privalov P L|Filimonov V V|Tatunashvili L V|Metsis M L | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71863,"numValue":90.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71864,"numValue":92.02,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71865,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13930 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,930 | 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 | 19,858 | ProTherm | 5 | Fluorescence | Thermal | Sodium acetate | 50 mM | null | 55 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1296 | ARTICLE | Folding and stability of a fibronectin type III domain of human tenascin. | 1,997 | 10.1006/jmbi.1997.1147 | 9245604 | J Mol Biol;270;771-8 | 3 | Clarke J|Johnson C M|Hamill S J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72952,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72953,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13931 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,931 | 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 | 19,859 | ProTherm | 7 | CD | Thermal | Sodium phosphate | 50 mM | null | 44 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1296 | ARTICLE | Folding and stability of a fibronectin type III domain of human tenascin. | 1,997 | 10.1006/jmbi.1997.1147 | 9245604 | J Mol Biol;270;771-8 | 3 | Clarke J|Johnson C M|Hamill S J | [{"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72954,"numValue":44.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72955,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:13932 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,932 | 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 | 21,311 | ProTherm | 5 | CD | GdnSCN | Sodium acetate | 50 mM | 25 | null | null | 9.38 | null | null | null | null | 1.47 | 6.38 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1461 | ARTICLE | Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module. | 2,000 | 10.1110/ps.9.1.112 | 10739253 | Protein Sci;9;112-20 | 2 | Cota E|Clarke J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnSCN","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":77528,"numValue":9.38,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77529,"numValue":6.38,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77530,"numValue":1.47,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77531,"numValue":null,"references":[],"... | ||||||||||||||||||||||||||
fireprotdb:13933 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,933 | 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 | 21,319 | ProTherm | 5 | Fluorescence | GdnHCl | Sodium acetate | 50mM | 25 | null | null | 9.4 | null | null | null | null | 1.49 | 6.4 | null | null | null | null | null | null | null | 2.0 | DG|M|CM|STATE | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":77554,"numValue":9.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77555,"numValue":6.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77556,"numValue":1.49,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77557,"numValue":2.0,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:13934 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,934 | 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 | 21,803 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 50 mM | 20 | null | null | 4.3 | null | null | null | null | 3.9 | 1.1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1296 | ARTICLE | Folding and stability of a fibronectin type III domain of human tenascin. | 1,997 | 10.1006/jmbi.1997.1147 | 9245604 | J Mol Biol;270;771-8 | 3 | Clarke J|Johnson C M|Hamill S J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":20.0,"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":79077,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79078,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79079,"numValue":3.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79080,"numValue":null,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:13935 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,935 | 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 | 21,804 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 50 mM | 20 | null | null | 5.2 | null | null | null | null | 3.7 | 1.4 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1296 | ARTICLE | Folding and stability of a fibronectin type III domain of human tenascin. | 1,997 | 10.1006/jmbi.1997.1147 | 9245604 | J Mol Biol;270;771-8 | 3 | Clarke J|Johnson C M|Hamill S J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":20.0,"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":79081,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79082,"numValue":1.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79083,"numValue":3.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79084,"numValue":null,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:13936 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,936 | 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 | 21,805 | ProTherm | 7 | Fluorescence | Urea | Sodium phosphate | 50 mM | 20 | null | null | 2.8 | null | null | null | null | 2.5 | 1.1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1296 | ARTICLE | Folding and stability of a fibronectin type III domain of human tenascin. | 1,997 | 10.1006/jmbi.1997.1147 | 9245604 | J Mol Biol;270;771-8 | 3 | Clarke J|Johnson C M|Hamill S J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":79085,"numValue":2.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79086,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79087,"numValue":2.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79088,"numValue":null,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:13937 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,937 | 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 | 21,806 | ProTherm | 7 | Fluorescence | Urea | Sodium phosphate | 50 mM | 20 | null | null | 2.9 | null | null | null | null | 2.4 | 1.2 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1296 | ARTICLE | Folding and stability of a fibronectin type III domain of human tenascin. | 1,997 | 10.1006/jmbi.1997.1147 | 9245604 | J Mol Biol;270;771-8 | 3 | Clarke J|Johnson C M|Hamill S J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":79089,"numValue":2.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79090,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79091,"numValue":2.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79092,"numValue":null,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:13939 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,939 | 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 | 22,271 | ProTherm | 2.4 | CD | Thermal | glycine hydrochloride | 20 mM | null | NaCl | 0.1 M | 72 | 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 | 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":80507,"numValue":72.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80508,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:13940 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,940 | 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 | 22,272 | ProTherm | 2.4 | CD | Thermal | glycine hydrochloride | 20 mM | null | NaCl | 1 M | 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 | 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":80509,"numValue":82.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80510,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:13941 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,941 | 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 | 22,273 | ProTherm | 7 | CD | Thermal | sodium phosphate | 20 mM | null | NaCl | 0.1 M | 62 | 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 | 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":80511,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80512,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:13942 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,942 | 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 | 22,274 | ProTherm | 7 | CD | Thermal | sodium phosphate | 20 mM | null | NaCl | 1 M | 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 | 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":80513,"numValue":70.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80514,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:13943 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,943 | 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 | 24,623 | ProTherm | 7.4 | CD | Thermal | null | 82.5 | null | 9.38 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DG|STATE|REVERSIBILITY | PH|MEASURE|METHOD | 1758 | ARTICLE | Structural and dynamic properties that govern the stability of an engineered fibronectin type III domain. | 2,015 | 10.1093/protein/gzv002 | 25691761 | Protein Eng Des Sel;28;67-78 | 8 | Buckle Ashley M|Porebski Benjamin T|Nickson Adrian A|Hoke David E|Hunter Morag R|Zhu Liguang|McGowan Sheena|Webb Geoffrey I | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"}] | [{"datasets":[],"id":87224,"numValue":82.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":87225,"numValue":9.38,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":87226,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":87227,"numValue":null,"references":[... | |||||||||||||||||||||||||||
fireprotdb:13944 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,944 | 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 | 24,624 | ProTherm | 7.4 | CD | Thermal | null | 58 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|STATE|REVERSIBILITY | PH|MEASURE|METHOD | 1758 | ARTICLE | Structural and dynamic properties that govern the stability of an engineered fibronectin type III domain. | 2,015 | 10.1093/protein/gzv002 | 25691761 | Protein Eng Des Sel;28;67-78 | 8 | Buckle Ashley M|Porebski Benjamin T|Nickson Adrian A|Hoke David E|Hunter Morag R|Zhu Liguang|McGowan Sheena|Webb Geoffrey I | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"}] | [{"datasets":[],"id":87228,"numValue":58.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":87229,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":87230,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||||
fireprotdb:13945 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,945 | 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 | 25,480 | ProTherm | 5.5 | Fluorescence | GdnHCl | sodium acetate | 30 | NaCl | 100 mM | null | null | 7.7 | null | null | null | null | null | 2.4 | 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":89611,"numValue":7.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89612,"numValue":2.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":89613,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:13946 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,946 | 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 | 25,481 | ProTherm | 5.5 | Fluorescence | GdnHCl | sodium acetate | 30 | NaCl | 100 mM | null | null | 7.4 | null | null | null | null | null | 1.6 | 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":89614,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89615,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":89616,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:13947 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,947 | 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 | 25,482 | ProTherm | 5.5 | Fluorescence | GdnHCl | sodium acetate | 30 | NaCl | 100 mM | null | null | 7.2 | null | null | null | null | null | 1.6 | 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":89617,"numValue":7.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89618,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":89619,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:13949 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13,949 | 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 | 25,484 | ProTherm | 5.5 | Fluorescence | GdnHCl | sodium acetate | 30 | NaCl | 100 mM | null | null | 5.2 | null | null | null | null | null | 1.6 | 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":89623,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89624,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":89625,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] |
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