DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure (London, England : 1993) 2012 imex curation Wang C., Chung BC., Yan H., Lee SY., Pitt GS. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Wang C., Chung BC., Yan H., Lee SY., Pitt GS. DIP original experiment: DIP-250478X Structure (London, England : 1993) 2012 IMEx Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure (London, England : 1993) 2012 imex curation Wang C., Chung BC., Yan H., Lee SY., Pitt GS. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Wang C., Chung BC., Yan H., Lee SY., Pitt GS. DIP original experiment: DIP-250477X Structure (London, England : 1993) 2012 IMEx Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure (London, England : 1993) 2012 imex curation Wang C., Chung BC., Yan H., Lee SY., Pitt GS. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Wang C., Chung BC., Yan H., Lee SY., Pitt GS. DIP original experiment: DIP-250475X Structure (London, England : 1993) 2012 IMEx Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure (London, England : 1993) 2012 imex curation Wang C., Chung BC., Yan H., Lee SY., Pitt GS. Only protein-protein interactions ecolx Escherichia coli pull down pull down weight by staining molecular weight estimation by staining weight by staining Wang C., Chung BC., Yan H., Lee SY., Pitt GS. DIP original experiment: DIP-250482X Structure (London, England : 1993) 2012 IMEx Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure (London, England : 1993) 2012 imex curation Wang C., Chung BC., Yan H., Lee SY., Pitt GS. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Wang C., Chung BC., Yan H., Lee SY., Pitt GS. DIP original experiment: DIP-250476X Structure (London, England : 1993) 2012 IMEx Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure (London, England : 1993) 2012 imex curation Wang C., Chung BC., Yan H., Lee SY., Pitt GS. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Wang C., Chung BC., Yan H., Lee SY., Pitt GS. DIP original experiment: DIP-250480X Structure (London, England : 1993) 2012 IMEx Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure (London, England : 1993) 2012 imex curation Wang C., Chung BC., Yan H., Lee SY., Pitt GS. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Wang C., Chung BC., Yan H., Lee SY., Pitt GS. DIP original experiment: DIP-250479X Structure (London, England : 1993) 2012 IMEx Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure (London, England : 1993) 2012 imex curation Wang C., Chung BC., Yan H., Lee SY., Pitt GS. Only protein-protein interactions ecolx Escherichia coli pull down pull down weight by staining molecular weight estimation by staining weight by staining Wang C., Chung BC., Yan H., Lee SY., Pitt GS. DIP original experiment: DIP-250481X Structure (London, England : 1993) 2012 IMEx Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. p61328-2 Fibroblast growth factor 12 FGF12 FGF12B FHF1 Fibroblast growth factor homologous factor 1 Myocyte-activating factor FGF-12B protein protein human Homo sapiens Human MESKEPQLKGIVTRLFSQQGYFLQMHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQQESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVCMYREPSLHEIGEKQGRSRKSSGTPTMNGGKVVNQDST DIP protein P61328-2 original sequence version: 87 E150D8758875C8B7 scn5a_human Sodium channel protein type 5 subunit alpha Sodium channel protein type V subunit alpha Voltage-gated sodium channel subunit alpha Nav1.5 Sodium channel protein cardiac muscle subunit alpha SCN5A hH1 protein protein human Homo sapiens Human MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQGTPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQQESQPVSGGPEAPPDSRTWSQVSATASSEAEASASQADWRQQWKAEPQAPGCGETPEDSCSEGSTADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYHIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRSLKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSVTRATSDNLQVRGSDYSHSEDLADFPPSPDRDRESIV DIP protein Q14524 original sequence version: 163 DIP protein Q14524 original sequence version: 119 DIP protein Q14524 original sequence version: 138 This sequence has been withdrawn from Uniprot. 841E3A365931190B p35498-1 Sodium channel protein type 1 subunit alpha SCN1A NAC1 SCN1 Sodium channel protein brain I subunit alpha Sodium channel protein type I subunit alpha Voltage-gated sodium channel subunit alpha Nav1.1 protein protein human Homo sapiens Human MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCIQWPPTNASLEEHSIEKNITVNYNGTLINETVFEFDWKSYIQDSRYHYFLEGFLDALLCGNSSDAGQCPEGYMCVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMIEQLKKQQEAAQQAATATASEHSREPSAAGRLSDSSSEASKLSSKSAKERRNRRKKRKQKEQSGGEEKDEDEFQKSESEDSIRRKGFRFSIEGNRLTYEKRYSSPHQSLLSIRGSLFSPRRNSRTSLFSFRGRAKDVGSENDFADDEHSTFEDNESRRDSLFVPRRHGERRNSNLSQTSRSSRMLAVFPANGKMHSTVDCNGVVSLVGGPSVPTSPVGQLLPEVIIDKPATDDNGTTTETEMRKRRSSSFHVSMDFLEDPSQRQRAMSIASILTNTVEELEESRQKCPPCWYKFSNIFLIWDCSPYWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTDHFNNVLTVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVTLSLVELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKDCVCKIASDCQLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLTVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDNEMNNLQIAVDRMHKGVAYVKRKIYEFIQQSFIRKQKILDEIKPLDDLNNKKDSCMSNHTAEIGKDLDYLKDVNGTTSGIGTGSSVEKYIIDESDYMSFINNPSLTVTVPIAVGESDFENLNTEDFSSESDLEESKEKLNESSSSSEGSTVDIGAPVEEQPVVEPEETLEPEACFTEGCVQRFKCCQINVEEGRGKQWWNLRRTCFRIVEHNWFETFIVFMILLSSGALAFEDIYIDQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGYQTYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINTTTGDRFDIEDVNNHTDCLKLIERNETARWKNVKVNFDNVGFGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEESLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSEYVTTILSRINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPNKVNPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFMEFEKLSQFAAALEPPLNLPQPNKLQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYQPITTTLKRKQEEVSAVIIQRAYRRHLLKRTVKQASFTYNKNKIKGGANLLIKEDMIIDRINENSITEKTDLTMSTAACPPSYDRVTKPIVEKHEQEGKDEKAKGK DIP protein P35498-1 original sequence version: 135 q92913-2 Fibroblast growth factor 13 FGF13 FHF2 hFHF-2(1U) Fibroblast growth factor homologous factor 2 1B FGF13B FGF13U protein protein human Homo sapiens Human MALLRKSYSEPQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSELFTPECKFKESVFENYYVTYSSMIYRQQQSGRGWYLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSHNEST DIP protein Q92913-2 original sequence version: 110 calm_human Calmodulin CALM1 CALM CAM CAM1 CALM2 CAMB CALM3 CAM3 CAMC CAMIII CAM2 CALML2 protein protein human Homo sapiens Human MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK DIP protein P62158 original sequence version: 97 DIP protein P62158 original sequence version: 144 DIP protein P62158 original sequence version: 146 DIP protein P62158 original sequence version: 73 DIP protein P62158 original sequence version: 102 DIP protein P62158 original sequence version: 98 DIP protein P62158 original sequence version: 96 DIP protein P62158 original sequence version: 111 DIP protein P62158 original sequence version: 131 DIP protein P62158 original sequence version: 136 DIP protein P62158 original sequence version: 145 DIP protein P62158 original sequence version: 154 DIP protein P62158 original sequence version: 148 DIP protein P62158 original sequence version: 116 DIP protein P62158 original sequence version: 120 DIP protein P62158 original sequence version: 130 6B4BC3FCDE10727B scn5a-calm1-1 3 12 unspecified role unspecified role prey prey ecolx Escherichia coli 13 unspecified role unspecified role prey prey ecolx Escherichia coli 10 unspecified role unspecified role bait bait Region 1773-1940 Region 1773-1940 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli association association calm1-fgf13-1 2 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role Region 1773-1940 Region 1773-1940 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction scn5a-fgf12-1 8 9 unspecified role unspecified role prey prey ecolx Escherichia coli 10 unspecified role unspecified role bait bait Q14524:p.Glu1890Lys E1890K mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E1890K'. Wed May 02 15:09:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu1890lys' Tue Jun 30 15:39:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu1890Lys' His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 1773-1940 Region 1773-1940 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association fgf12-scn1a-1 7 11 unspecified role unspecified role unspecified role unspecified role Region 1789-1948 Region 1789-1948 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P35498-1:p.Gln1904Glu Q1904E mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Q E This feature has been corrected as a result of our quality control procedures. The original label was 'Q1904E'. Wed May 02 16:37:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln1904glu' Tue Jun 30 16:34:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln1904Glu' ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction calm1-fgf13-2 5 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role Region 1773-1940 Region 1773-1940 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association fgf12-scn5a-1 1 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role Region 1773-1940 Region 1773-1940 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q14524:p.Glu1890Lys E1890K mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E1890K'. Wed May 02 19:24:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu1890lys' Tue Jun 30 18:25:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu1890Lys' ecolx Escherichia coli direct interaction direct interaction scn5a-fgf12-2 4 9 unspecified role unspecified role prey prey P61328-2:p.Lys9Glu K9E mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K9E'. Wed May 02 14:51:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys9glu' Tue Jun 30 19:24:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys9Glu' ecolx Escherichia coli 10 unspecified role unspecified role bait bait Region 1773-1940 Region 1773-1940 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association fgf12-scn5a-2 6 9 unspecified role unspecified role unspecified role unspecified role P61328-2:p.Lys9Glu K9E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K9E'. Wed May 02 19:35:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys9glu' Tue Jun 30 17:43:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys9Glu' ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role Region 1773-1940 Region 1773-1940 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction