task_type stringclasses 1
value | subtask stringclasses 5
values | protein_id stringlengths 6 10 | pdb_id stringlengths 4 4 | sequence_length int32 138 780 | sequence stringlengths 138 780 | instruction stringlengths 1.78k 3.85k | metadata stringlengths 778 21.5k | ground_truth stringlengths 719 21.4k |
|---|---|---|---|---|---|---|---|---|
editing | solubility_editing | Q9AQQ8 | 2ZK9 | 320 | MKNLFLSMMAFVTVLTFNSCADSNGNQEINGKEKLSVNDSKLKDFGKTVPVGIDEENGMIKVSFMLTAQFYEIKPTKENEQYIGMLRQAVKNESPVHIFLKPNSNEIGKVESASPEDVRYFKTILTKEVKGQTNKLASVIPDVATLNSLFNQIKNQSCGTSTASSPCITFRYPVDGCYARAHKMRQILMNNGYDCEKQFVYGNLKASTGTCCVAWSYHVAILVSYKNASGVTEKRIIDPSLFSSGPVTDTAWRNACVNTSCGSASVSSYANTAGNVYYRSPSNSYLYDNNLINTNCVLTKFSLLSGCSPSPAPDVSSCGF | This protein would have poor aqueous solubility, potentially driven by aggregation-prone surface chemistry. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MKNLFLSMMAFVTVLTFNSCADSNGNQEINGKEKLSVNDSKLKDFGKTVPVGIDEENGMIKVSFMLTAQFYEIKPTKENEQ... | {"protein_id": "Q9AQQ8", "chain_id": "X", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 303, "wt_aa": "L", "suggested_aa": "N", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 228, "wt_aa": "A", "suggested_aa"... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 303, "wt_aa": "L", "suggested_aa": "N", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 228, "wt_aa": "A", "suggested_aa": "S", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "... |
editing | solubility_editing | G3XAP7 | 3ZUD | 228 | HGFVQNIVIDGKNYGGYLVNQYPYMSNPPEVIAWSTTATDLGFVDGTGYQTPDIICHRGAKPGALTAPVSPGGTVELQWTPWPDSHHGPVINYLAPCNGDCSTVDKTQLEFFKIAESGLINDDNPPGIWASDNLIAANNSWTVTIPTTIAPGNYVLRHEIIALHSAQNQDGAQNYPQCINLQVTGGGSDNPAGTLGTALYHDTDPGILINIYQKLSSYIIPGPPLYTG | This protein would have poor aqueous solubility, potentially driven by aggregation-prone surface chemistry. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: HGFVQNIVIDGKNYGGYLVNQYPYMSNPPEVIAWSTTATDLGFVDGTGYQTPDIICHRGAKPGALTAPVSPGGTVELQWTP... | {"protein_id": "G3XAP7", "chain_id": "A", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 219, "wt_aa": "I", "suggested_aa": "T", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 192, "wt_aa": "A", "suggested_aa"... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 219, "wt_aa": "I", "suggested_aa": "T", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 192, "wt_aa": "A", "suggested_aa": "S", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "... |
editing | solubility_editing | A0A0H3KNC4 | 4DLF | 296 | MGALRIDSHQHFWRYRAADYPWIGAGMGVLARDYLPDALHPLMHAQALGASIAVQARAGRDETAFLLELACDEARIAAVVGWEDLRAPQLAERVAEWRGTKLRGFRHQLQDEADVRAFVDDADFARGVAWLQANDYVYDVLVFERQLPDVQAFCARHDAHWLVLDHAGKPALAEFDRDDTALARWRAALRELAALPHVVCKLSGLVTEADWRRGLRASDLRHIEQCLDAALDAFGPQRLMFGSDWPVCLLAASYDEVASLVERWAESRLSAAERSALWGGTAARCYALPEPADARL | This protein would have poor aqueous solubility, potentially driven by aggregation-prone surface chemistry. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MGALRIDSHQHFWRYRAADYPWIGAGMGVLARDYLPDALHPLMHAQALGASIAVQARAGRDETAFLLELACDEARIAAVVG... | {"protein_id": "A0A0H3KNC4", "chain_id": "A", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 113, "wt_aa": "A", "suggested_aa": "E", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 71, "wt_aa": "C", "suggested_... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 113, "wt_aa": "A", "suggested_aa": "E", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 71, "wt_aa": "C", "suggested_aa": "S", "acceptable_aas": ["S"], "acceptable_class": "serin... |
editing | solubility_editing | P0DXA4 | 7N34 | 208 | MKSHEYIVICGLNRSKVGRYIAIVASFLSFISIFLALTALEWLKNYHINSHIPASVFSLISAGGIYMGLYAWFDKNLWQNSYLGKFLCVPNLEGRWHVDGHTRSEGGNTWEGELKIVQTWDKVRIHLKTKASHSDSVTASIIYDKGIGYQLLYNYRNQPKTGEEHLTSHVGFAEFRFDADLKSAEGHYFNGQGRATYGTMTITRIEHA | This protein is likely to have poor aqueous solubility that may arise from aggregation-prone surface chemistry. The design should address these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MKSHEYIVICGLNRSKVGRYIAIVASFLSFISIFLALTALEWLKNYHINSHIPASVFSLISAGGIYMGLYAWFDKN... | {"protein_id": "P0DXA4", "chain_id": "A", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 205, "wt_aa": "I", "suggested_aa": "K", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 170, "wt_aa": "V", "suggested_aa"... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 205, "wt_aa": "I", "suggested_aa": "K", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 170, "wt_aa": "V", "suggested_aa": "R", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "... |
editing | solubility_editing | P0DX98 | 7X4P | 299 | MSKFSESTLSGWTKPASVTEEDRIENTISMIKSAIKNDNNFDNLVYEVFVQGSYGNNTNVRTNSDIDVNIMLTSTFYSKYPEGKTNSDYGFTDGTITYNEYKNLILTALTNKFGTGNVTVGNKSIKITSNSYRVEADCIPSLLYRNYEYENSSSPNNYIEGIKYFASDNTSVVNYPKVHINNGIEKNNQTHKNYKRLVRVIKRLRNKMTAENHFTNENITSFLIECLIWNVPNNYINDYDTWDETIKQTLIFIKSSINDNSYKNWTEVSGMFYLFHNNRKWTSDDVSSFVNSLWSFMEY | This protein is likely to have poor aqueous solubility that may arise from aggregation-prone surface chemistry. The design should address these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MSKFSESTLSGWTKPASVTEEDRIENTISMIKSAIKNDNNFDNLVYEVFVQGSYGNNTNVRTNSDIDVNIMLTSTF... | {"protein_id": "P0DX98", "chain_id": "A", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 18, "wt_aa": "V", "suggested_aa": "D", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 210, "wt_aa": "A", "suggested_aa":... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 18, "wt_aa": "V", "suggested_aa": "D", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 210, "wt_aa": "A", "suggested_aa": "D", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R... |
editing | solubility_editing | C0HLV2 | 7ZVA | 380 | MQAKFFTFVILSSVFYFNYPLAEARSIQARLANKPKGTIKTIKGDDGEVVDCVDIYKQPAFDHPLLKNHTLQMQPSSYASKVGEYNKLEQPWHKNGECPKGSIPIRRQVITGLPVVKKQFPNLKFAPPSANTNHQYAVIAYFYGNASLQGANATINIWEPNLKNPNGDFSLTQIWISAGSGSSLNTIEAGWQVYPGRTGDSQPRFFIYWTADGYTSTGCYDLTCPGFVQTNNYYAIGMALQPSVYGGQQYELNESIQRDPATGNWWLYLWGTVVGYWPASIYNSITNGADTVEWGGEIYDSSGTGGFHTTTQMGSGHFPT... | This protein would have poor aqueous solubility, potentially driven by aggregation-prone surface chemistry. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MQAKFFTFVILSSVFYFNYPLAEARSIQARLANKPKGTIKTIKGDDGEVVDCVDIYKQPAFDHPLLKNHTLQMQPSSYASK... | {"protein_id": "C0HLV2", "chain_id": "A", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 29, "wt_aa": "A", "suggested_aa": "R", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 261, "wt_aa": "A", "suggested_aa":... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 29, "wt_aa": "A", "suggested_aa": "R", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 261, "wt_aa": "A", "suggested_aa": "K", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R... |
editing | solubility_editing | A0A7H0DN96 | 8JED | 287 | MDEIVKNIREGTHVLLPFYETLPELNLSLGKSPLPSLEYGANYFLQISRVNDLNRMPTDMLKLFTHDIMLPESDLDKVYEILKINSVKYYGRSTRADAVVADLSARNKLFKRERDAIKSNNHLTENNLYISDYKMLTFDVFRPLFDFVNEKYCIIKLPTLFGRGVIDTMRIYCSLFKNVRLLKCVSDSWLKDSAIMVASDVYKKNLDLFMSHVKSVTKSSSWKDVNTVQFSILNDPVDTEFINKFLEFSNRVYEALYYVHSLLYSSMTSDSKSIENKHQRRLVKLLL | This protein would have poor aqueous solubility, potentially driven by aggregation-prone surface chemistry. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MDEIVKNIREGTHVLLPFYETLPELNLSLGKSPLPSLEYGANYFLQISRVNDLNRMPTDMLKLFTHDIMLPESDLDKVYEI... | {"protein_id": "A0A7H0DN96", "chain_id": "B", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 225, "wt_aa": "V", "suggested_aa": "S", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 208, "wt_aa": "L", "suggested... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 225, "wt_aa": "V", "suggested_aa": "S", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 208, "wt_aa": "L", "suggested_aa": "K", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "... |
editing | solubility_editing | B2HG54 | 8SWL | 414 | MSDTLASPSPETASGIPDYPMSRSAGCPFAPPPGVMALAAAKPLTRVRIWDGSTPWLITGYEQVRELFSDSRVSVDDRLPGFPHWNAGMLSTVHKRPRSVFTADGEEHTRFRRMLSKPFTFKRVEALRPTIQQITDEHIDAMLAGPQPADLVAKLALPVPSLVISQLLGVPYEDAEMFQHHANVGLARYATGADTVKGAMSLHKYLAELVEAKMANPAEDAVSDLAERVKAGELSVKEAAQLGTGLLIAGHETTANMIGLGVLALLVNPDQAGILRDAQDPKIVANAVEELLRYLSIIQNGQRRVAHEDIHIGGETIRAG... | This protein is likely to have poor aqueous solubility that may arise from aggregation-prone surface chemistry. The design should address these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MSDTLASPSPETASGIPDYPMSRSAGCPFAPPPGVMALAAAKPLTRVRIWDGSTPWLITGYEQVRELFSDSRVSVD... | {"protein_id": "B2HG54", "chain_id": "A", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 348, "wt_aa": "A", "suggested_aa": "R", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 144, "wt_aa": "A", "suggested_aa"... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 348, "wt_aa": "A", "suggested_aa": "R", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 144, "wt_aa": "A", "suggested_aa": "E", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "... |
editing | solubility_editing | B2Z3V8 | 9V14 | 240 | MQLTDFKALTFDCYGTLIDWETGIVNALQPLAKRTGKTFTSDELLEVFGRNESPQQTETPGALYQDILRAVYDRIAKEWGLEPDAAEREEFGTSVKNWPAFPDTVEALQYLKKHYKLVILSNIDRNEFKLSNAKLGVEFDHIITAQDVGSYKPNPNNFTYMIDALAKAGIEKKDILHTAESLYHDHIPANDAGLVSAWIYRRHGKEGYGATHVPSRMPNVDFRFNSMGEMAEAHKQALKG | This protein is likely to have poor aqueous solubility that may arise from aggregation-prone surface chemistry. The design should address these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MQLTDFKALTFDCYGTLIDWETGIVNALQPLAKRTGKTFTSDELLEVFGRNESPQQTETPGALYQDILRAVYDRIA... | {"protein_id": "B2Z3V8", "chain_id": "A", "gold_answer": {"task_type": "solubility_editing", "gt_mutations": [{"position": 213, "wt_aa": "V", "suggested_aa": "E", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 133, "wt_aa": "A", "suggested_aa"... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 213, "wt_aa": "V", "suggested_aa": "E", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 133, "wt_aa": "A", "suggested_aa": "R", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "... |
editing | solubility_editing | Q9WY48 | 1GM5 | 780 | MLCSRYFTSSLFLWGEALPTLLEEFLNEVEKMLKNQVNTRRIHQLLKELDDPLLENKDLEEKLQAFLDYVKEIPNLPEARKRYRIQKSLEMIEKLRSWFLIDYLECSGEEVDLSTDIQYAKGVGPNRKKKLKKLGIETLRDLLEFFPRDYEDRRKIFKLNDLLPGEKVTTQGKIVSVETKKFQNMNILTAVLSDGLVHVPLKWFNQDYLQTYLKQLTGKEVFVTGTVKSNAYTGQYEIHNAEVTPKEGEYVRRILPIYRLTSGISQKQMRKIFEENIPSLCCSLKETLPERILEKRKLLGVKDAYYGMHFPKTFYHLEKA... | This protein is likely to have poor aqueous solubility that may arise from aggregation-prone surface chemistry. The design should address these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MLCSRYFTSSLFLWGEALPTLLEEFLNEVEKMLKNQVNTRRIHQLLKELDDPLLENKDLEEKLQAFLDYVKEIPNL... | {"chain_id": "A", "gold_answer": {"extras": {}, "gt_mutations": [{"acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar", "position": 196, "suggested_aa": "T", "wt_aa": "L"}, {"acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": ... | {"task_type": "solubility_editing", "gt_mutations": [{"position": 196, "wt_aa": "L", "suggested_aa": "T", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "R", "S", "T", "Y"], "acceptable_class": "charged_or_polar"}, {"position": 587, "wt_aa": "L", "suggested_aa": "R", "acceptable_aas": ["D", "E", "H", "K", "N", "Q", "... |
editing | stability_type1_editing | Q1HRL7 | 6OG0 | 138 | MKVFIAVFALIAVAAAEFTVSTTEDLQRYRTECVSSLNIPADYVEKFKKWEFPEDDTTMCYIKCVFNKMQLFDDTEGPLVDNLVHQLAHGRDAEEVRTEVLKCVDKNTDNNACHWAFRGFKCFQKNNLSLIKASIKKD | This protein appears to have reduced fold stability, potentially due to local structural or evolutionary signals. The design should improve this property while preserving functional and structurally constrained residues.
WT protein sequence: MKVFIAVFALIAVAAAEFTVSTTEDLQRYRTECVSSLNIPADYVEKFKKWEFPEDDTTMCYIKCVFNKMQLFDDTEG... | {"protein_id": "Q1HRL7", "chain_id": "A", "gold_answer": {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 61, "wt_aa": "Y", "suggested_aa": "F", "acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydr... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 61, "wt_aa": "Y", "suggested_aa": "F", "acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 86, "wt_aa": "Q", "sugge... |
editing | stability_type1_editing | Q9KN86 | 6U2A | 430 | MISKSIILRFSELSMRKKATLVGLPLLAVAAISSSLNSPTRQQRIELSLPESPLVQFSSAEHTVEVVKVGHPDYEYEIKPGDNLSTIFNQLGFAYTELMKVMETDLNYLALDTLRPGNVLRFWKGSDNTLAKMELEFSLVDRAVYTRLNDGSYEFEERKIPGTWKVEPLIGEVDGSFSLSANRAGLGAADVDQIVTLLKDKINFGRDLRRGDRFEVVLSRQLVGEKLTGNSEIQAIKIFNRGKEITAYLHQDGQYYDKNGDSLQRAFQRYPVDSKWRISSNFDPRRLHPVTKRVAPHNGTDFAMPIGTPVYTSGDGVVVM... | This protein appears to have reduced fold stability, potentially due to local structural or evolutionary signals. The design should improve this property while preserving functional and structurally constrained residues.
WT protein sequence: MISKSIILRFSELSMRKKATLVGLPLLAVAAISSSLNSPTRQQRIELSLPESPLVQFSSAEHTVEVVKVGHPDYEYE... | {"protein_id": "Q9KN86", "chain_id": "A", "gold_answer": {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 300, "wt_aa": "T", "suggested_aa": "V", "acceptable_aas": ["V", "I"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hyd... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 300, "wt_aa": "T", "suggested_aa": "V", "acceptable_aas": ["V", "I"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 246, "wt_aa": "T", "sug... |
editing | stability_type1_editing | A0A3B6UEU3 | 6XOJ | 296 | MQIDEQPGNAIGAAVEGFDHATASDADIDALKSTIYTKKIAVLKGQDLSPQQFLALGKRLGRPEAYYEPMYQHPEVTEIFVSSNVPENGKQIGVPKTGKFWHADYQFMPDPFGITLIYPQVIPEKNRGTYFIDMGRAYDRLPEDLKKEISGTYCRHSVRKYFKIRPHDVYRPISEIIEEVERKTPAVVQPTTFTHPMTGETVLYISEGFTVGIEDQDGKPLDEELLKRLFDATGQLDESFEHDNIHLQSFEQGDLLVWDNRSLIHRARHTTTPEPTVSYRVTVHDERKLHDGIQAA | This protein appears to have reduced fold stability, potentially due to local structural or evolutionary signals. The design should improve this property while preserving functional and structurally constrained residues.
WT protein sequence: MQIDEQPGNAIGAAVEGFDHATASDADIDALKSTIYTKKIAVLKGQDLSPQQFLALGKRLGRPEAYYEPMYQHPEVT... | {"protein_id": "A0A3B6UEU3", "chain_id": "A", "gold_answer": {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 130, "wt_aa": "Y", "suggested_aa": "F", "acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u219... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 130, "wt_aa": "Y", "suggested_aa": "F", "acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 38, "wt_aa": "K", "sugg... |
editing | stability_type1_editing | P0DY63 | 8ZAD | 442 | MQEVITQTLIDDRFVQLSQQTKNETSKGPGIDDKRWAQEQPNRAKSSDQAAAVTMKAAAPIKEHRDTWYYPPDIASDLQSVNLPAELKGEIFACAWEYTRCVIPNYTNWNRYVAFMRTIIIGVIAEFRGEMVDVTASTSILGYDLDGVLAALFEGTPGHKEMAREYKTFLLITADKASERRDGELFRRYVNALAQSPRHWFRMRDCDALARFTIASALACNDLDDIWYTEEQFEILTEIGDTLYDAVAFYKHRAEGETNSTFAYMPEDLRIKAYSECREILWALDAAWARNPKLVNVINFLRFFGGPIHMMMRRYRFVEE... | This protein is likely to have reduced fold stability, potentially driven by local structural or evolutionary signals. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MQEVITQTLIDDRFVQLSQQTKNETSKGPGIDDKRWAQEQPNRAKSSDQAAAVTMKAAAPIKEHRDTWYY... | {"protein_id": "P0DY63", "chain_id": "A", "gold_answer": {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 296, "wt_aa": "N", "suggested_aa": "L", "acceptable_aas": ["L", "V", "I"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u21... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 296, "wt_aa": "N", "suggested_aa": "L", "acceptable_aas": ["L", "V", "I"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 168, "wt_aa": "T",... |
editing | stability_type1_editing | Q8DPI6 | 1JYK | 229 | MKAIILAAGLGTRLRPMTENTPKALVQVNQKPLIEYQIEFLKEKGINDIIIIVGYLKEQFDYLKEKYGVRLVFNDKYADYNNFYSLYLVKEELANSYVIDADNYLFKNMFRNDLTRSTYFSVYREDCTNEWFLVYGDDYKVQDIIVDSKAGRILSGVSFWDAPTAEKIVSFIDKAYASGEFVDLYWDNMVKDNIKELDVYVEELEGNSIYEIDSVQDYRKLEEILKNEN | This protein appears to have reduced fold stability, potentially due to local structural or evolutionary signals. The design should improve this property while preserving functional and structurally constrained residues.
WT protein sequence: MKAIILAAGLGTRLRPMTENTPKALVQVNQKPLIEYQIEFLKEKGINDIIIIVGYLKEQFDYLKEKYGVRLVFNDKY... | {"chain_id": "A", "gold_answer": {"extras": {}, "gt_mutations": [{"acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "fix_direction": "polar\u2192hydrophobic isostere", "pattern_name": "P2_buried_unsatisfied_polar", "position": 104, "suggested_aa": "F", "wt_aa": "Y"}, {"acceptable_aas": ["L", "V"... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 104, "wt_aa": "Y", "suggested_aa": "F", "acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 103, "wt_aa": "N", "sug... |
editing | stability_type1_editing | Q8GB88 | 1SN7 | 553 | MSDMEKPWKEGEEARAVLQGHARAQAPQAVDKGPVAGDERMAVTVVLRRQRAGELAAHVERQAAIAPHAREHLKREAFAASHGASLDDFAELRRFADAHGLALDRANVAAGTAVLSGPVDAINRAFGVELRHFDHPDGSYRSYLGEVTVPASIAPMIEAVLGLDTRPVARPHFRMQRRAEGGFEARSQAAAPTAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDEASLAQYFASLGVPAPQVVSVSVDGASNQPTGDPSGPDGEVELDIEVAGALAPGAKFAVYFAPNTDAGFLDAITTAIHDPTLKPSVVSISWGG... | This protein appears to have reduced fold stability, potentially due to local structural or evolutionary signals. The design should improve this property while preserving functional and structurally constrained residues.
WT protein sequence: MSDMEKPWKEGEEARAVLQGHARAQAPQAVDKGPVAGDERMAVTVVLRRQRAGELAAHVERQAAIAPHAREHLKREA... | {"chain_id": "A", "gold_answer": {"extras": {}, "gt_mutations": [{"acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "fix_direction": "polar\u2192hydrophobic isostere", "pattern_name": "P2_buried_unsatisfied_polar", "position": 195, "suggested_aa": "F", "wt_aa": "Y"}, {"acceptable_aas": ["A", "V"... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 195, "wt_aa": "Y", "suggested_aa": "F", "acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 216, "wt_aa": "C", "sug... |
editing | stability_type1_editing | Q8RR56 | 1T1E | 552 | MSDMEKPWKEEEKREVLAGHARRQAPQAVDKGPVTGDQRISVTVVLRRQRGDELEAHVERQAALAPHARVHLEREAFAASHGASLDDFAEIRKFAEAHGLTLDRAHVAAGTAVLSGPVDAVNQAFGVELRHFDHPDGSYRSYVGDVRVPASIAPLIEAVFGLDTRPVARPHFRLRRRAEGEFEARSQSAAPTAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDETSLAQYFASLGVSAPQVVSVSVDGATNQPTGDPNGPDGEVELDIEVAGALAPGAKIAVYFAPNTDAGFLNAITTAVHDPTHKPSIVSISWGGP... | This protein is likely to have reduced fold stability, potentially driven by local structural or evolutionary signals. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MSDMEKPWKEEEKREVLAGHARRQAPQAVDKGPVTGDQRISVTVVLRRQRGDELEAHVERQAALAPHARV... | {"chain_id": "A", "gold_answer": {"extras": {}, "gt_mutations": [{"acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "fix_direction": "polar\u2192hydrophobic isostere", "pattern_name": "P2_buried_unsatisfied_polar", "position": 139, "suggested_aa": "F", "wt_aa": "Y"}, {"acceptable_aas": ["F", "L"... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 139, "wt_aa": "Y", "suggested_aa": "F", "acceptable_aas": ["F", "L"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 194, "wt_aa": "Y", "sug... |
editing | stability_type1_editing | Q8U3D2 | 1U04 | 770 | MKAKVVINLVKINKKIIPDKIYVYRLFNDPEEELQKEGYSIYRLAYENVGIVIDPENLIIATTKELEYEGEFIPEGEISFSELRNDYQSKLVLRLLKENGIGEYELSKLLRKFRKPKTFGDYKVIPSVEMSVIKHDEDFYLVIHIIHQIQSMKTLWELVNKDPKELEEFLMTHKENLMLKDIASPLKTVYKPCFEEYTKKPKLDHNQEIVKYWYNYHIERYWNTPEAKLEFYRKFGQVDLKQPAILAKFASKIKKNKNYKIYLLPQLVVPTYNAEQLESDVAKEILEYTKLMPEERKELLENILAEVDSDIIDKSLSEIE... | This protein is likely to have reduced fold stability, potentially driven by local structural or evolutionary signals. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MKAKVVINLVKINKKIIPDKIYVYRLFNDPEEELQKEGYSIYRLAYENVGIVIDPENLIIATTKELEYEG... | {"chain_id": "A", "gold_answer": {"extras": {}, "gt_mutations": [{"acceptable_aas": ["V", "I"], "acceptable_class": "hydrophobic_isostere", "fix_direction": "polar\u2192hydrophobic isostere", "pattern_name": "P2_buried_unsatisfied_polar", "position": 289, "suggested_aa": "V", "wt_aa": "T"}, {"acceptable_aas": ["A", "V"... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 289, "wt_aa": "T", "suggested_aa": "V", "acceptable_aas": ["V", "I"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 89, "wt_aa": "S", "sugg... |
editing | stability_type1_editing | Q9KUL5 | 2GU1 | 426 | MGQFRFLALIVAVLCFSVALFLPTADEPDQDSYSVPLNQSVNTSQPPSSEMVPSDIRLTPLPQPKRIHYMVKVGDTLSGIFAQLGVPYSILQKILSVDLDHLQLDMIQPGEELELMMDDMGQLSRLIYHMSIVEKAIYTRENDGSFSYDFQEISGEWREILFSGEINGSFSVSARRVGLTSSQVANITQVMKDKIDFSRSLRAGDRFDILVKQQYLGEHNTGNSEIKAISFKLAKGDVSAFLAEDGRFYDRAGNSLERAFNRYPVDKAYRQITSGFNPKRKHPVTGRVVPHNGTDFATPIGAPVYSTGDGKVIVVRKHPY... | This protein is likely to have reduced fold stability, potentially driven by local structural or evolutionary signals. The design should repair these weaknesses while preserving functional and structurally constrained residues.
WT protein sequence: MGQFRFLALIVAVLCFSVALFLPTADEPDQDSYSVPLNQSVNTSQPPSSEMVPSDIRLTPLPQPKRIHYM... | {"chain_id": "A", "gold_answer": {"extras": {}, "gt_mutations": [{"acceptable_aas": ["L", "M", "F"], "acceptable_class": "hydrophobic_isostere", "fix_direction": "polar\u2192hydrophobic isostere", "pattern_name": "P2_buried_unsatisfied_polar", "position": 318, "suggested_aa": "L", "wt_aa": "H"}, {"acceptable_aas": ["V"... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 318, "wt_aa": "H", "suggested_aa": "L", "acceptable_aas": ["L", "M", "F"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 294, "wt_aa": "T",... |
editing | stability_type1_editing | P9WEM3 | 2LHS | 197 | MNKTSRTLLSLGLLSAAMFGVSQQANAHGYVESPASRAYQCKLQLNTQCGSVQYEPQSVEGLKGFPQAGPADGHIASADKSTFFELDQQTPTRWNKLNLKTGPNSFTWKLTARHSTTSWRYFITKPNWDASQPLTRASFDLTPFCQFNDGGAIPAAQVTHQCNIPADRSGSHVILAVWDIADTANAFYQAIDVNLSK | This protein appears to have reduced fold stability, potentially due to local structural or evolutionary signals. The design should improve this property while preserving functional and structurally constrained residues.
WT protein sequence: MNKTSRTLLSLGLLSAAMFGVSQQANAHGYVESPASRAYQCKLQLNTQCGSVQYEPQSVEGLKGFPQAGPADGHIAS... | {"chain_id": "A", "gold_answer": {"extras": {}, "gt_mutations": [{"acceptable_aas": ["A", "V"], "acceptable_class": "hydrophobic_isostere", "fix_direction": "polar\u2192hydrophobic isostere", "pattern_name": "P2_buried_unsatisfied_polar", "position": 138, "suggested_aa": "A", "wt_aa": "S"}, {"acceptable_aas": ["L", "M"... | {"task_type": "fold_stability_editing", "gt_mutations": [{"position": 138, "wt_aa": "S", "suggested_aa": "A", "acceptable_aas": ["A", "V"], "acceptable_class": "hydrophobic_isostere", "pattern_name": "P2_buried_unsatisfied_polar", "fix_direction": "polar\u2192hydrophobic isostere"}, {"position": 189, "wt_aa": "Q", "sug... |
editing | stability_type2_editing | P0C1V0 | 4FAK | 159 | MKITILAVGKLKEKYWKQAIAEYEKRLGPYTKIDIIEVPDEKAPENMSDKEIEQVKEKEGQRILAKIKPQSTVITLEIQGKMLSSEGLAQELNQRMTQGQSDFVFVIGGSNGLHKDVLQRSNYALSFSKMTFPHQMMRVVLIEQVYRAFKIMRGEAYHK | You are given a mesophilic target protein with ortholog context from a
thermophilic sequence. Group-level analysis of mesophilic and thermophilic
orthologs found amino-acid preferences that differ systematically by growth
temperature. These positions provide candidate thermostability-editing sites.
[TASK]
Inspect the ... | {"protein_id": "P0C1V0", "gold_answer": {"task_type": "thermostability_editing", "gt_mutations": [{"position": 88, "wt_aa": "L", "suggested_aa": "F", "acceptable_aas": ["F"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"F": 0.399623, "L": 0.600377}, "thermophile_group_freqs": {"F": 0.8352, "L"... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 88, "wt_aa": "L", "suggested_aa": "F", "acceptable_aas": ["F"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"F": 0.399623, "L": 0.600377}, "thermophile_group_freqs": {"F": 0.8352, "L": 0.100602, "Y": 0.064198}}], "protected... |
editing | stability_type2_editing | P00456 | 1CP2 | 273 | MRQVAIYGKGGIGKSTTTQNLTSGLHAMGKTIMVVGCDPKADSTRLLLGGLAQKSVLDTLREEGEDVELDSILKEGYGGIRCVESGGPEPGVGCAGRGIITSINMLEQLGAYTDDLDYVFYDVLGDVVCGGFAMPIREGKAQEIYIVASGEMMALYAANNISKGIQKYAKSGGVRLGGIICNSRKVANEYELLDAFAKELGSQLIHFVPRSPMVTKAEINKQTVIEYDPTCEQAEEYRELARKVDANELFVIPKPMTQERLEEILMQYGLMDL | You are given a mesophilic target protein with ortholog context from a
thermophilic sequence. Group-level analysis of mesophilic and thermophilic
orthologs found amino-acid preferences that differ systematically by growth
temperature. These positions provide candidate thermostability-editing sites.
[TASK]
Inspect the ... | {"protein_id": "P00456", "gold_answer": {"task_type": "thermostability_editing", "gt_mutations": [{"position": 195, "wt_aa": "A", "suggested_aa": "E", "acceptable_aas": ["E"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"A": 0.487686, "E": 0.108897, "K": 0.086183, "N": 0.10084, "R": 0.216395},... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 195, "wt_aa": "A", "suggested_aa": "E", "acceptable_aas": ["E"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"A": 0.487686, "E": 0.108897, "K": 0.086183, "N": 0.10084, "R": 0.216395}, "thermophile_group_freqs": {"D": 0.1819... |
editing | stability_type2_editing | Q81LW0 | 1XUQ | 203 | MAKHELPNLPYAYDALEPHFDKETMNIHHTKHHNTYITNLNAALEGHAELADKSVEELVANLNEVPEAIRTAVRNNGGGHANHTFFWTILSPNGGGQPVGELATAIEAKFGSFDAFKEEFAKAGATRFGSGWAWLVVNNGELEVTSTPNQDSPLTEGKTPVIGLDVWEHAYYLNYQNRRPDYIGAFWNVVDWNAAEKRYQEAK | You are given a mesophilic target protein with ortholog context from a
thermophilic sequence. Group-level analysis of mesophilic and thermophilic
orthologs found amino-acid preferences that differ systematically by growth
temperature. These positions provide candidate thermostability-editing sites.
[TASK]
Inspect the ... | {"protein_id": "Q81LW0", "gold_answer": {"task_type": "thermostability_editing", "gt_mutations": [{"position": 82, "wt_aa": "N", "suggested_aa": "L", "acceptable_aas": ["L"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"C": 0.100397, "N": 0.899603}, "thermophile_group_freqs": {"L": 0.616845, "... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 82, "wt_aa": "N", "suggested_aa": "L", "acceptable_aas": ["L"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"C": 0.100397, "N": 0.899603}, "thermophile_group_freqs": {"L": 0.616845, "M": 0.13434, "N": 0.248815}}, {"position... |
editing | stability_type2_editing | O82827 | 1F75 | 249 | MFPIKKRKAIKNNNINAAQIPKHIAIIMDGNGRWAKQKKMPRIKGHYEGMQTVKKITRYASDLGVKYLTLYAFSTENWSRPKDEVNYLMKLPGDFLNTFLPELIEKNVKVETIGFIDDLPDHTKKAVLEAKEKTKHNTGLTLVFALNYGGRKEIISAVQLIAERYKSGEISLDEISETHFNEYLFTANMPDPELLIRTSGEERLSNFLIWQCSYSEFVFIDEFWPDFNEESLAQCISIYQNRHRRFGGL | You are given a mesophilic target protein with ortholog context from a
thermophilic sequence. Group-level analysis of mesophilic and thermophilic
orthologs found amino-acid preferences that differ systematically by growth
temperature. These positions provide candidate thermostability-editing sites.
[TASK]
Review the t... | {"protein_id": "O82827", "gold_answer": {"task_type": "thermostability_editing", "gt_mutations": [{"position": 65, "wt_aa": "V", "suggested_aa": "I", "acceptable_aas": ["I"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"I": 0.201625, "L": 0.084334, "V": 0.714042}, "thermophile_group_freqs": {"... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 65, "wt_aa": "V", "suggested_aa": "I", "acceptable_aas": ["I"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"I": 0.201625, "L": 0.084334, "V": 0.714042}, "thermophile_group_freqs": {"I": 0.864475, "V": 0.135525}}, {"positio... |
editing | stability_type2_editing | P39669 | 3BRK | 420 | MSEKRVQPLARDAMAYVLAGGRGSRLKELTDRRAKPAVYFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWDFFRPERNESFDILPASQRVSETQWYEGTADAVYQNIDIIEPYAPEYMVILAGDHIYKMDYEYMLQQHVDSGADVTIGCLEVPRMEATGFGVMHVNEKDEIIDFIEKPADPPGIPGNEGFALASMGIYVFHTKFLMEAVRRDAADPTSSRDFGKDIIPYIVEHGKAVAHRFADSCVRSDFEHEPYWRDVGTIDAYWQANIDLTDVVPDLDIYDKSWPIWTYAEITPPAKFVHDDEDRRG... | You are given a mesophilic protein sequence and its aligned thermophilic ortholog.
A comparison across multiple mesophilic and thermophilic orthologs identified
positions where the two temperature groups consistently prefer different amino
acids. These temperature-correlated sites are potential targets for
thermostabil... | {"protein_id": "P39669", "gold_answer": {"task_type": "thermostability_editing", "gt_mutations": [{"position": 97, "wt_aa": "A", "suggested_aa": "P", "acceptable_aas": ["P"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"A": 0.7446, "P": 0.2554}, "thermophile_group_freqs": {"A": 0.227518, "P": ... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 97, "wt_aa": "A", "suggested_aa": "P", "acceptable_aas": ["P"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"A": 0.7446, "P": 0.2554}, "thermophile_group_freqs": {"A": 0.227518, "P": 0.772482}}, {"position": 282, "wt_aa": "... |
editing | stability_type2_editing | P61431 | 1HSK | 307 | MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES | You are given a mesophilic protein sequence and its aligned thermophilic ortholog.
A comparison across multiple mesophilic and thermophilic orthologs identified
positions where the two temperature groups consistently prefer different amino
acids. These temperature-correlated sites are potential targets for
thermostabil... | {"protein_id": "P61431", "gold_answer": {"task_type": "thermostability_editing", "gt_mutations": [{"position": 255, "wt_aa": "V", "suggested_aa": "I", "acceptable_aas": ["I"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"F": 0.070839, "I": 0.301385, "V": 0.627776}, "thermophile_group_freqs": {... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 255, "wt_aa": "V", "suggested_aa": "I", "acceptable_aas": ["I"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"F": 0.070839, "I": 0.301385, "V": 0.627776}, "thermophile_group_freqs": {"F": 0.128137, "I": 0.66897, "V": 0.2028... |
editing | stability_type2_editing | Q818Z9 | 3TWZ | 394 | MNKYKRIFLVVMDSVGIGEAPDAEQFGDLGSDTIGHIAEHMNGLQMPNMVKLGLGNIREMKGISKVEKPLGYYTKMQEKSTGKDTMTGHWEIMGLYIDTPFQVFPEGFPKELLDELEEKTGRKIIGNKPASGTEILDELGQEQMETGSLIVYTSADSVLQIAAHEEVVPLDELYKICKIARELTLDEKYMVGRVIARPFVGEPGNFTRTPNRHDYALKPFGRTVMNELKDSDYDVIAIGKISDIYDGEGVTESLRTKSNMDGMDKLVDTLNMDFTGLSFLNLVDFDALFGHRRDPQGYGEALQEYDARLPEVFAKLKEDD... | You are given a mesophilic target protein with ortholog context from a
thermophilic sequence. Group-level analysis of mesophilic and thermophilic
orthologs found amino-acid preferences that differ systematically by growth
temperature. These positions provide candidate thermostability-editing sites.
[TASK]
Inspect the ... | {"protein_id": "Q818Z9", "gold_answer": {"task_type": "thermostability_editing", "gt_mutations": [{"position": 26, "wt_aa": "F", "suggested_aa": "Y", "acceptable_aas": ["Y"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"F": 0.888284, "Y": 0.111716}, "thermophile_group_freqs": {"Y": 1.0}}, {"po... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 26, "wt_aa": "F", "suggested_aa": "Y", "acceptable_aas": ["Y"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"F": 0.888284, "Y": 0.111716}, "thermophile_group_freqs": {"Y": 1.0}}, {"position": 136, "wt_aa": "L", "suggested_a... |
editing | stability_type2_editing | Q81LV1 | 1XP3 | 298 | MLKIGSHVSMSGKKMLLAASEEAVSYGATTFMIYTGAPQNTRRKPIEELNIEAGRKHMEQNGIEEIIVHAPYIINVGNTTKPETFQLGVDFLRMEIERTSALGVAKQIVLHPGAHVGAGADAGIQQIIKGLNEVLTPDQTVNIALETMAGKGTECGRSFEEIAKIIDGVKYNEKLSVCFDTCHTHDAGYDIVNNFDGVLNEFDKIVGIDRLQVLHINDSKNVRGAGKDRHENIGFGHIGYKALHHIVHHPQLTHVPKILETPYVGEDKKDKKPPYKLEIEMLKNGTFDEGLLEKIKAQ | You are given a mesophilic target protein with ortholog context from a
thermophilic sequence. Group-level analysis of mesophilic and thermophilic
orthologs found amino-acid preferences that differ systematically by growth
temperature. These positions provide candidate thermostability-editing sites.
[TASK]
Review the t... | {"protein_id": "Q81LV1", "gold_answer": {"task_type": "thermostability_editing", "gt_mutations": [{"position": 153, "wt_aa": "T", "suggested_aa": "G", "acceptable_aas": ["G", "S"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"N": 0.196124, "S": 0.223543, "T": 0.580332}, "thermophile_group_freq... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 153, "wt_aa": "T", "suggested_aa": "G", "acceptable_aas": ["G", "S"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"N": 0.196124, "S": 0.223543, "T": 0.580332}, "thermophile_group_freqs": {"G": 0.742568, "S": 0.257432}}, {"p... |
editing | stability_type2_editing | Q9Z462 | 1IOK | 545 | MAAKEVKFNSDARDRMLKGVNILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELSDKFENMGAQMVREVASRTNDEAGDGTTTATVLAQAIVREGLKAVAAGMNPMDLKRGIDVATAKVVEAIKSAARPVNDSSEVAQVGTISANGESFIGQQIAEAMQRVGNEGVITVEENKGMETEVEVVEGMQFDRGYLSPYFVTNADKMIAELEDAYILLHEKKLSSLQPMVPLLESVIQSQKPLLIVAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLQDIAILTGGQVISEDLGMKLENVTIDMLGRA... | You are given a mesophilic protein sequence and its aligned thermophilic ortholog.
A comparison across multiple mesophilic and thermophilic orthologs identified
positions where the two temperature groups consistently prefer different amino
acids. These temperature-correlated sites are potential targets for
thermostabil... | {"gold_answer": {"extras": {"candidate_temperature_correlated_positions": [222, 346, 334, 436, 17], "scored_temperature_correlated_positions": [222, 346], "temperature_correlated_positions": [222, 346]}, "gt_mutations": [{"acceptable_aas": ["I"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"I"... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 222, "wt_aa": "L", "suggested_aa": "I", "acceptable_aas": ["I"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"I": 0.326033, "L": 0.593908, "M": 0.027191, "V": 0.052868}, "thermophile_group_freqs": {"I": 1.0}}, {"position": ... |
editing | stability_type2_editing | Q8PYJ6 | 6X94 | 422 | MLELKFVRNNPDIVGRALISRNMGTELIDSLLEYDAAWRECLIEGDDLKHKRNVVTREIAQLKKENKDAASRINEMQGINSRIKELDDKIRDYKSKINEIMLSIPNIPSETTPVGKDENDNPVVRVVGEPREFTFTPKPHWEIGESLDILDFERAAKISGQGFAVYKGMGAKLERALINFMLDVHTRQGYLEVFPPVLINEKAMTGTGQLPKFKDDMYGCTDGFYLAPTAEVPVTNLFMDEYMENLPVFLTAYTACFRREAGKHGQDTRGIIRNHQFNKVELVKFVMPETSYEELEKLTLDAEEILKLLKLPYRVVSLCT... | You are given a mesophilic target protein with ortholog context from a
thermophilic sequence. Group-level analysis of mesophilic and thermophilic
orthologs found amino-acid preferences that differ systematically by growth
temperature. These positions provide candidate thermostability-editing sites.
[TASK]
Review the t... | {"gold_answer": {"extras": {"candidate_temperature_correlated_positions": [200, 236, 165], "scored_temperature_correlated_positions": [200], "temperature_correlated_positions": [200]}, "gt_mutations": [{"acceptable_aas": ["K", "R"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"G": 0.026003, "K... | {"task_type": "thermostability_editing", "gt_mutations": [{"position": 200, "wt_aa": "N", "suggested_aa": "R", "acceptable_aas": ["K", "R"], "acceptable_class": "thermophile_dominant", "mesophile_group_freqs": {"G": 0.026003, "K": 0.140811, "N": 0.623063, "Q": 0.014144, "R": 0.19598}, "thermophile_group_freqs": {"A": 0... |
editing | activity_type2_editing | Q8I3X4 | 2BSX | 245 | MDNLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVECHYKGQKFLCVSHGVGSAGCAVCFEELCQNGAKVIIRAGSCGSLQPDLIKRGDICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNGISVSSDMYYPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGILIVDGCPFKWDEGDFDNNLVPHQLENMIKIALGACAKLATKYA | This enzyme has substrate-binding pocket contacts that could restrict access for larger or alternative substrate analogs.
WT protein sequence: MDNLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVECHYKGQKFLCVSHGVGSAGCAVCFEELCQNGAKVIIRAGSCGSLQPDLIKRGDICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNGISVSSDMYYPNKIIPSRLEDYSKA... | {"protein_id": "Q8I3X4", "chain_id": "A", "gold_answer": {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 212, "wt_aa": "W", "suggested_aa": "G", "acceptable_aas": ["G", "D", "E", "N", "S"], "acceptable_class": "smaller_than_wt", "wt_volume": 227.8, "max_acceptable_volume": 217.8}, {"position": 1... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 212, "wt_aa": "W", "suggested_aa": "G", "acceptable_aas": ["G", "D", "E", "N", "S"], "acceptable_class": "smaller_than_wt", "wt_volume": 227.8, "max_acceptable_volume": 217.8}, {"position": 181, "wt_aa": "V", "suggested_aa": "S", "acceptable_aas": ... |
editing | activity_type2_editing | Q381M1 | 2IKF | 333 | MPPSPAVVGRSLVNSFKQFVSKDLHTRHVDATYRLVLDCVAAVDPLMRLYTFGSTVVYGVHEKGSDVDFVVLNKTDVEDGKGGDAATQVAKGLQADILAKLARVIRQKHLSWNVEEVRRTRVPVVRVKGGGAVDFDITAYRRNGVRNSALLRAYFEQNPPCRWLSMSIKRWSKQTGLNASVIGGSITSYGFNLMVVYYLLQRNHLQFVPPSTIDVSRVEPLPPHLPLEEPADEGLELGTQVLDFLHFFLHEFDSDKQVISLNRPGITTKEELDWTKSAEDFARMNGEKVHYQWCIEDPYELNLNVGRNVTPLKRDFLRRH... | This enzyme has substrate-binding pocket contacts that could restrict access for larger or alternative substrate analogs.
WT protein sequence: MPPSPAVVGRSLVNSFKQFVSKDLHTRHVDATYRLVLDCVAAVDPLMRLYTFGSTVVYGVHEKGSDVDFVVLNKTDVEDGKGGDAATQVAKGLQADILAKLARVIRQKHLSWNVEEVRRTRVPVVRVKGGGAVDFDITAYRRNGVRNSALLRAYFEQNPPCRWLSMSIKRWSKQTG... | {"protein_id": "Q381M1", "chain_id": "A", "gold_answer": {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 58, "wt_aa": "Y", "suggested_aa": "M", "acceptable_aas": ["M", "L", "N", "S", "H"], "acceptable_class": "smaller_than_wt", "wt_volume": 193.6, "max_acceptable_volume": 183.6}, {"position": 57... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 58, "wt_aa": "Y", "suggested_aa": "M", "acceptable_aas": ["M", "L", "N", "S", "H"], "acceptable_class": "smaller_than_wt", "wt_volume": 193.6, "max_acceptable_volume": 183.6}, {"position": 57, "wt_aa": "V", "suggested_aa": "A", "acceptable_aas": ["... |
editing | activity_type2_editing | Q6FNA9 | 3G59 | 304 | MRLGDAAELCYNLTSSYLQIAAESDSIIAQTQRAINTTKSILINETFPKWSPLNGEISFSYNGGKDCQVLLLLYLSCLWEYYIVKLSQSQFDGKFHRFPLTKLPTVFIDHDDTFKTLENFIEETSLRYSLSLYESDRDKCETMAEAFETFLQVFPETKAIVIGIRHTDPFGEHLKPIQKTDANWPDFYRLQPLLHWNLANIWSFLLYSNEPICELYRYGFTSLGNVEETLPNPHLRKDKNSTPLKLNFEWEIENRYKHNEVTKAEPIPIADEDLVKIENLHEDYYPGWYLVDDKLERAGRIKKK | This enzyme contains pocket-lining residues that may limit accommodation of larger or alternative substrate analogs.
WT protein sequence: MRLGDAAELCYNLTSSYLQIAAESDSIIAQTQRAINTTKSILINETFPKWSPLNGEISFSYNGGKDCQVLLLLYLSCLWEYYIVKLSQSQFDGKFHRFPLTKLPTVFIDHDDTFKTLENFIEETSLRYSLSLYESDRDKCETMAEAFETFLQVFPETKAIVIGIRHTDPFGEHLKPIQKTD... | {"protein_id": "Q6FNA9", "chain_id": "A", "gold_answer": {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 147, "wt_aa": "F", "suggested_aa": "L", "acceptable_aas": ["L", "V", "I", "M", "C"], "acceptable_class": "smaller_than_wt", "wt_volume": 189.9, "max_acceptable_volume": 179.9}, {"position": 5... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 147, "wt_aa": "F", "suggested_aa": "L", "acceptable_aas": ["L", "V", "I", "M", "C"], "acceptable_class": "smaller_than_wt", "wt_volume": 189.9, "max_acceptable_volume": 179.9}, {"position": 59, "wt_aa": "F", "suggested_aa": "L", "acceptable_aas": [... |
editing | activity_type2_editing | P74535 | 6JV1 | 705 | MADDIRILMCPPDHYDVDYVINPWMEGNIHKSSQERAVEQWKKLHQTIKECAIVDLVKPAKGWPDMVFTANAGLVLGENVVLSRFYHKERQGEEPYFKAWFEENGFTVYELPQDLPFEGAGDALFDREGRWLWAGYGFRSELDSHPYIAKWLDTEVVSLRLIDERFYHLDTCFCPLSGGYLLYYPPAFDAYSNRVIEMRIPPEKRIIVEELDAVNFACNAVNVNDIIIMNLVSRTLKEKLAEAGFKVRETPLTEFLKAGGAAKCLTLRVTEPILPDVHATVSIESRVIRMEGHLLDAGILNQALDLVVENSGSFRVLNFN... | This enzyme has substrate-binding pocket contacts that could restrict access for larger or alternative substrate analogs.
WT protein sequence: MADDIRILMCPPDHYDVDYVINPWMEGNIHKSSQERAVEQWKKLHQTIKECAIVDLVKPAKGWPDMVFTANAGLVLGENVVLSRFYHKERQGEEPYFKAWFEENGFTVYELPQDLPFEGAGDALFDREGRWLWAGYGFRSELDSHPYIAKWLDTEVVSLRLIDERFYHLDTCFCPL... | {"protein_id": "P74535", "chain_id": "A", "gold_answer": {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 19, "wt_aa": "Y", "suggested_aa": "D", "acceptable_aas": ["D", "E", "G", "V", "A"], "acceptable_class": "smaller_than_wt", "wt_volume": 193.6, "max_acceptable_volume": 183.6}, {"position": 85... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 19, "wt_aa": "Y", "suggested_aa": "D", "acceptable_aas": ["D", "E", "G", "V", "A"], "acceptable_class": "smaller_than_wt", "wt_volume": 193.6, "max_acceptable_volume": 183.6}, {"position": 85, "wt_aa": "F", "suggested_aa": "M", "acceptable_aas": ["... |
editing | activity_type2_editing | A0A3B6UEU3 | 6XOJ | 296 | MQIDEQPGNAIGAAVEGFDHATASDADIDALKSTIYTKKIAVLKGQDLSPQQFLALGKRLGRPEAYYEPMYQHPEVTEIFVSSNVPENGKQIGVPKTGKFWHADYQFMPDPFGITLIYPQVIPEKNRGTYFIDMGRAYDRLPEDLKKEISGTYCRHSVRKYFKIRPHDVYRPISEIIEEVERKTPAVVQPTTFTHPMTGETVLYISEGFTVGIEDQDGKPLDEELLKRLFDATGQLDESFEHDNIHLQSFEQGDLLVWDNRSLIHRARHTTTPEPTVSYRVTVHDERKLHDGIQAA | This enzyme has substrate-binding pocket contacts that could restrict access for larger or alternative substrate analogs.
WT protein sequence: MQIDEQPGNAIGAAVEGFDHATASDADIDALKSTIYTKKIAVLKGQDLSPQQFLALGKRLGRPEAYYEPMYQHPEVTEIFVSSNVPENGKQIGVPKTGKFWHADYQFMPDPFGITLIYPQVIPEKNRGTYFIDMGRAYDRLPEDLKKEISGTYCRHSVRKYFKIRPHDVYRPISEI... | {"protein_id": "A0A3B6UEU3", "chain_id": "A", "gold_answer": {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 100, "wt_aa": "F", "suggested_aa": "G", "acceptable_aas": ["G", "D", "V", "L", "N"], "acceptable_class": "smaller_than_wt", "wt_volume": 189.9, "max_acceptable_volume": 179.9}, {"position... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 100, "wt_aa": "F", "suggested_aa": "G", "acceptable_aas": ["G", "D", "V", "L", "N"], "acceptable_class": "smaller_than_wt", "wt_volume": 189.9, "max_acceptable_volume": 179.9}, {"position": 80, "wt_aa": "F", "suggested_aa": "L", "acceptable_aas": [... |
editing | activity_type2_editing | Q8L3C7 | 7E0D | 701 | MTTDTARRHTGAERANEMTYEQLARELLLVGPAPTNEDLKLRYLDVLIDNGLNPPGPPKRILIVGAGIAGLVAGDLLTRAGHDVTILEANANRVGGRIKTFHAKKGEPSPFADPAQYAEAGAMRLPSFHPLTLALIDKLGLKRRLFFNVDIDPQTGNQDAPVPPVFYKSFKDGKTWTNGAPSPEFKEPDKRNHTWIRTNREQVRRAQYATDPSSINEGFHLTGCETRLTVSDMVNQALEPVRDYYSVKQDDGTRVNKPFKEWLAGWADVVRDFDGYSMGRFLREYAEFSDEAVEAIGTIENMTSRLHLAFFHSFLGRSDI... | This enzyme contains pocket-lining residues that may limit accommodation of larger or alternative substrate analogs.
WT protein sequence: MTTDTARRHTGAERANEMTYEQLARELLLVGPAPTNEDLKLRYLDVLIDNGLNPPGPPKRILIVGAGIAGLVAGDLLTRAGHDVTILEANANRVGGRIKTFHAKKGEPSPFADPAQYAEAGAMRLPSFHPLTLALIDKLGLKRRLFFNVDIDPQTGNQDAPVPPVFYKSFKDGKTWTNGAP... | {"protein_id": "Q8L3C7", "chain_id": "A", "gold_answer": {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 564, "wt_aa": "W", "suggested_aa": "L", "acceptable_aas": ["L", "C", "F", "V", "R"], "acceptable_class": "smaller_than_wt", "wt_volume": 227.8, "max_acceptable_volume": 217.8}, {"position": 6... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 564, "wt_aa": "W", "suggested_aa": "L", "acceptable_aas": ["L", "C", "F", "V", "R"], "acceptable_class": "smaller_than_wt", "wt_volume": 227.8, "max_acceptable_volume": 217.8}, {"position": 617, "wt_aa": "E", "suggested_aa": "A", "acceptable_aas": ... |
editing | activity_type2_editing | Q8BGL3 | 7EOV | 282 | MTDEFLWIEGIPFPTVYYSQEIIREVRDRFVVRDEDTIIVTYPKSGTHWLNEIVCLILTKGDPTWVQSTIANERTPWIEFENNYRILNSKEGPRLMASLLPIQLFPKSFFSSKAKVIYLIRNPRDVLVSGYHYFNALKQGKEQVPWKIYFENFLQGKSYFGSWFEHACGWISLRKRENILVLSYEQLKKDTRNTIKKICEFLGENLESGELELVLKNISFQIMKERMISQSCLSNIEKHEFIMRKGITGDWKNHFTVAQAEAFDKAFQEKAADFPQELFSWE | This enzyme has substrate-binding pocket contacts that could restrict access for larger or alternative substrate analogs.
WT protein sequence: MTDEFLWIEGIPFPTVYYSQEIIREVRDRFVVRDEDTIIVTYPKSGTHWLNEIVCLILTKGDPTWVQSTIANERTPWIEFENNYRILNSKEGPRLMASLLPIQLFPKSFFSSKAKVIYLIRNPRDVLVSGYHYFNALKQGKEQVPWKIYFENFLQGKSYFGSWFEHACGWISLRKR... | {"protein_id": "Q8BGL3", "chain_id": "A", "gold_answer": {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 65, "wt_aa": "W", "suggested_aa": "P", "acceptable_aas": ["P", "K", "E", "T", "G"], "acceptable_class": "smaller_than_wt", "wt_volume": 227.8, "max_acceptable_volume": 217.8}, {"position": 90... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 65, "wt_aa": "W", "suggested_aa": "P", "acceptable_aas": ["P", "K", "E", "T", "G"], "acceptable_class": "smaller_than_wt", "wt_volume": 227.8, "max_acceptable_volume": 217.8}, {"position": 90, "wt_aa": "K", "suggested_aa": "Q", "acceptable_aas": ["... |
editing | activity_type2_editing | Q8ZNC4 | 8D5R | 465 | MTDSIMQNYNQLREQVINGDRRFQHKDGHLCFEGVDLDALARQYPTPFYVFSEPEIIRNIHEIQQAFAAHKNTKTFFASKTCSVMGVLKAIRDAGICAEANSQYEVRKCLEIGFRGDQIVFNGVVKKPADLEYAIANDLYLINVDSLYELEHIDAISRKLKKVANVCVRVEPNVPSATHAELVTAFHAKSGLDLEQAEETCRRILAMPYVHLRGLHMHVGDQVPESEPFAKATKVLVDESRRLEEVLGIKFDLINVGGGIPVPYKYDDENGDPLKDNMYAGITAQDFADAVIREVHKWRTDVEICIEPGRKVTGSAAVLL... | This enzyme has substrate-binding pocket contacts that could restrict access for larger or alternative substrate analogs.
WT protein sequence: MTDSIMQNYNQLREQVINGDRRFQHKDGHLCFEGVDLDALARQYPTPFYVFSEPEIIRNIHEIQQAFAAHKNTKTFFASKTCSVMGVLKAIRDAGICAEANSQYEVRKCLEIGFRGDQIVFNGVVKKPADLEYAIANDLYLINVDSLYELEHIDAISRKLKKVANVCVRVEPNVPS... | {"protein_id": "Q8ZNC4", "chain_id": "A", "gold_answer": {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 217, "wt_aa": "M", "suggested_aa": "C", "acceptable_aas": ["C", "V", "A", "S", "T"], "acceptable_class": "smaller_than_wt", "wt_volume": 162.9, "max_acceptable_volume": 152.9}, {"position": 9... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 217, "wt_aa": "M", "suggested_aa": "C", "acceptable_aas": ["C", "V", "A", "S", "T"], "acceptable_class": "smaller_than_wt", "wt_volume": 162.9, "max_acceptable_volume": 152.9}, {"position": 99, "wt_aa": "E", "suggested_aa": "D", "acceptable_aas": [... |
editing | activity_type2_editing | Q0S4Q9 | 4AT2 | 490 | MVDATPIRPRSATTVTEWDYEADVVVAGYGIAGVAASIEAARAGADVLVLERTSGWGGAAALAGGFIYLGGGTPLQKACGFDDSPENMKTFMMAALGPGADEEKITDYCEGSVEHYNWLVDCGVPFKESFWGEPGWEPPFDDGLMYSGGENAAPFNEIATPAPRGHVPQMDGKRTGEKGGGYMLMKPLVETAEKLGVRAEYDMRVQTLVTDDTGRVVGIVAKQYGKEVAVRARRGVVLATGSFAYNDKMIEAHAPRLIGRPGAAIEEHDGRSILMAQALGADLAHMDATEVAFVCDPQLIVRGILVNGRGQRYVPEDTYS... | This enzyme has substrate-binding pocket contacts that could restrict access for larger or alternative substrate analogs.
WT protein sequence: MVDATPIRPRSATTVTEWDYEADVVVAGYGIAGVAASIEAARAGADVLVLERTSGWGGAAALAGGFIYLGGGTPLQKACGFDDSPENMKTFMMAALGPGADEEKITDYCEGSVEHYNWLVDCGVPFKESFWGEPGWEPPFDDGLMYSGGENAAPFNEIATPAPRGHVPQMDGKRTG... | {"chain_id": "A", "gold_answer": {"extras": {"chain_id": "A", "ligand_chain": "A", "ligand_coords": [[35.364, 19.375, 40.428], [34.959, 18.032, 41.062], [33.594, 17.379, 38.965], [32.279, 16.852, 38.34], [31.736, 15.675, 39.145], [31.573, 16.111, 40.6], [30.633, 15.076, 41.236], [29.589, 14.815, 40.137], [30.32, 15.259... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 136, "wt_aa": "W", "suggested_aa": "S", "acceptable_aas": ["S", "V", "I", "T", "G"], "acceptable_class": "smaller_than_wt", "wt_volume": 227.8, "max_acceptable_volume": 217.8}, {"position": 427, "wt_aa": "F", "suggested_aa": "L", "acceptable_aas": ... |
editing | activity_type2_editing | A0A286R7K5 | 5U92 | 357 | MVDQATLDKLEAGFKKLQDATDCKSLLKKYLNREVFDQCKSLKTALGATLLDCIQSGVENLDSGVGIYAPDAEAYTLFAPIFNPIIEDYHEGFKPTDKHPPTDFGDINTIVNVDPSGKYVVSTHVRCGRSLKGYPFNPCLTEANYKEMEDKVSAIFGTFEGELKGKYYPLTGMDKATQQQLIDDHFLFKEGDRFLQAANACRYWPTGRGIYHNDAKTFLVWVNEEDHLRIISMQKGGDLKTIFQRLVNAVNTIESKLPFSRDDRLGFLTFCPTNLGTTIRASVHIALPKLAKDKKQLEAIAAKFNLQVRGTRGEHTESEG... | This enzyme contains pocket-lining residues that may limit accommodation of larger or alternative substrate analogs.
WT protein sequence: MVDQATLDKLEAGFKKLQDATDCKSLLKKYLNREVFDQCKSLKTALGATLLDCIQSGVENLDSGVGIYAPDAEAYTLFAPIFNPIIEDYHEGFKPTDKHPPTDFGDINTIVNVDPSGKYVVSTHVRCGRSLKGYPFNPCLTEANYKEMEDKVSAIFGTFEGELKGKYYPLTGMDKATQQQL... | {"chain_id": "A", "gold_answer": {"extras": {"chain_id": "A", "ligand_chain": "A", "ligand_coords": [[55.926, -19.103, 79.014], [56.046, -18.68, 80.447], [55.001, -19.393, 81.288], [53.946, -19.703, 80.738], [55.847, -17.182, 80.583], [54.387, -16.809, 80.741], [54.175, -15.335, 80.643], [54.793, -14.769, 79.454], [55.... | {"task_type": "pocket_expansion_editing", "gt_mutations": [{"position": 68, "wt_aa": "Y", "suggested_aa": "V", "acceptable_aas": ["V", "T", "L", "H", "I"], "acceptable_class": "smaller_than_wt", "wt_volume": 193.6, "max_acceptable_volume": 183.6}, {"position": 194, "wt_aa": "F", "suggested_aa": "L", "acceptable_aas": [... |
editing | activity_type1_editing | O58212 | 1WU8 | 256 | MITLTTDFGLKGPYVGEMKVAMLRINPNAKIVDVTHSVTRHSILEGSFVMEQVVKYSPKGTVHVGVIDPGVGTERRAIVIEGDQYLVVPDNGLATLPLKHIKVKSVYEIIPDKIRKFTGWEISSTFHGRDIFGPAGALIEKGIHPEEFGREIPVDSIVKLNVEPRKEGDVWILKVIYIDDFGNVILNLENYEKPRTVELLDFNLRLPYLETYGLVEKGEMLALPGSHDYLEIAVNMGSAAERLNVKVGDELRVRLL | This enzyme-substrate complex contains substrate-contacting residues with potential chemical mismatches that may be optimized for target-substrate binding.
WT protein sequence: MITLTTDFGLKGPYVGEMKVAMLRINPNAKIVDVTHSVTRHSILEGSFVMEQVVKYSPKGTVHVGVIDPGVGTERRAIVIEGDQYLVVPDNGLATLPLKHIKVKSVYEIIPDKIRKFTGWEISSTFHGRDIFGPAGALIEKG... | {"protein_id": "O58212", "chain_id": "A", "gold_answer": {"task_type": "binding_affinity_editing", "gt_mutations": [{"position": 236, "wt_aa": "M", "suggested_aa": "Q", "acceptable_aas": ["C", "H", "N", "Q", "S", "T", "Y"], "acceptable_class": "polar", "ideal_character": "polar", "substrate_charge": "donor", "mismatch_... | {"task_type": "binding_affinity_editing", "gt_mutations": [{"position": 236, "wt_aa": "M", "suggested_aa": "Q", "acceptable_aas": ["C", "H", "N", "Q", "S", "T", "Y"], "acceptable_class": "polar", "ideal_character": "polar", "substrate_charge": "donor", "mismatch_type": "hydrophobic_near_polar"}, {"position": 233, "wt_a... |
editing | activity_type1_editing | Q0S4Q9 | 4AT2 | 490 | MVDATPIRPRSATTVTEWDYEADVVVAGYGIAGVAASIEAARAGADVLVLERTSGWGGAAALAGGFIYLGGGTPLQKACGFDDSPENMKTFMMAALGPGADEEKITDYCEGSVEHYNWLVDCGVPFKESFWGEPGWEPPFDDGLMYSGGENAAPFNEIATPAPRGHVPQMDGKRTGEKGGGYMLMKPLVETAEKLGVRAEYDMRVQTLVTDDTGRVVGIVAKQYGKEVAVRARRGVVLATGSFAYNDKMIEAHAPRLIGRPGAAIEEHDGRSILMAQALGADLAHMDATEVAFVCDPQLIVRGILVNGRGQRYVPEDTYS... | The following enzyme-substrate complex includes active-site contacts where residue chemistry appears potentially suboptimal for the nearby substrate atoms.
WT protein sequence: MVDATPIRPRSATTVTEWDYEADVVVAGYGIAGVAASIEAARAGADVLVLERTSGWGGAAALAGGFIYLGGGTPLQKACGFDDSPENMKTFMMAALGPGADEEKITDYCEGSVEHYNWLVDCGVPFKESFWGEPGWEPPFDD... | {"protein_id": "Q0S4Q9", "chain_id": "A", "gold_answer": {"task_type": "binding_affinity_editing", "gt_mutations": [{"position": 354, "wt_aa": "T", "suggested_aa": "G", "acceptable_aas": ["A", "F", "G", "I", "L", "M", "P", "V", "W"], "acceptable_class": "hydrophobic", "ideal_character": "hydrophobic", "substrate_charge... | {"task_type": "binding_affinity_editing", "gt_mutations": [{"position": 354, "wt_aa": "T", "suggested_aa": "G", "acceptable_aas": ["A", "F", "G", "I", "L", "M", "P", "V", "W"], "acceptable_class": "hydrophobic", "ideal_character": "hydrophobic", "substrate_charge": "aromatic", "mismatch_type": "polar_near_nonpolar"}, {... |
editing | activity_type1_editing | P74535 | 6JV1 | 705 | MADDIRILMCPPDHYDVDYVINPWMEGNIHKSSQERAVEQWKKLHQTIKECAIVDLVKPAKGWPDMVFTANAGLVLGENVVLSRFYHKERQGEEPYFKAWFEENGFTVYELPQDLPFEGAGDALFDREGRWLWAGYGFRSELDSHPYIAKWLDTEVVSLRLIDERFYHLDTCFCPLSGGYLLYYPPAFDAYSNRVIEMRIPPEKRIIVEELDAVNFACNAVNVNDIIIMNLVSRTLKEKLAEAGFKVRETPLTEFLKAGGAAKCLTLRVTEPILPDVHATVSIESRVIRMEGHLLDAGILNQALDLVVENSGSFRVLNFN... | This enzyme-substrate complex contains substrate-contacting residues with potential chemical mismatches that may be optimized for target-substrate binding.
WT protein sequence: MADDIRILMCPPDHYDVDYVINPWMEGNIHKSSQERAVEQWKKLHQTIKECAIVDLVKPAKGWPDMVFTANAGLVLGENVVLSRFYHKERQGEEPYFKAWFEENGFTVYELPQDLPFEGAGDALFDREGRWLWAGYGFRSEL... | {"protein_id": "P74535", "chain_id": "A", "gold_answer": {"task_type": "binding_affinity_editing", "gt_mutations": [{"position": 258, "wt_aa": "A", "suggested_aa": "S", "acceptable_aas": ["C", "H", "N", "Q", "S", "T", "Y"], "acceptable_class": "polar", "ideal_character": "polar", "substrate_charge": "donor", "mismatch_... | {"task_type": "binding_affinity_editing", "gt_mutations": [{"position": 258, "wt_aa": "A", "suggested_aa": "S", "acceptable_aas": ["C", "H", "N", "Q", "S", "T", "Y"], "acceptable_class": "polar", "ideal_character": "polar", "substrate_charge": "donor", "mismatch_type": "hydrophobic_near_polar"}, {"position": 21, "wt_aa... |
editing | activity_type1_editing | A0A286R7K5 | 5U92 | 357 | MVDQATLDKLEAGFKKLQDATDCKSLLKKYLNREVFDQCKSLKTALGATLLDCIQSGVENLDSGVGIYAPDAEAYTLFAPIFNPIIEDYHEGFKPTDKHPPTDFGDINTIVNVDPSGKYVVSTHVRCGRSLKGYPFNPCLTEANYKEMEDKVSAIFGTFEGELKGKYYPLTGMDKATQQQLIDDHFLFKEGDRFLQAANACRYWPTGRGIYHNDAKTFLVWVNEEDHLRIISMQKGGDLKTIFQRLVNAVNTIESKLPFSRDDRLGFLTFCPTNLGTTIRASVHIALPKLAKDKKQLEAIAAKFNLQVRGTRGEHTESEG... | This enzyme-substrate complex contains substrate-contacting residues with potential chemical mismatches that may be optimized for target-substrate binding.
WT protein sequence: MVDQATLDKLEAGFKKLQDATDCKSLLKKYLNREVFDQCKSLKTALGATLLDCIQSGVENLDSGVGIYAPDAEAYTLFAPIFNPIIEDYHEGFKPTDKHPPTDFGDINTIVNVDPSGKYVVSTHVRCGRSLKGYPFNPCLTE... | {"chain_id": "A", "gold_answer": {"extras": {"binding_site_center": [55.24250000000001, -16.723500000000005, 80.313], "box_size": [16.0, 18.637, 16.173999999999992], "chain_id": "A", "reference_structure_path": "/mnt/vast/trillion/hyunjin/filtered_data/editing/activity/5U92_A0A286R7K5.pdb", "substrate_atoms": [{"atom_i... | {"task_type": "binding_affinity_editing", "gt_mutations": [{"position": 65, "wt_aa": "V", "suggested_aa": "C", "acceptable_aas": ["C", "H", "N", "Q", "S", "T", "Y"], "acceptable_class": "polar", "ideal_character": "polar", "substrate_charge": "acceptor", "mismatch_type": "hydrophobic_near_polar"}, {"position": 273, "wt... |
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