eF-site ID 6h04-ABCDEFGHIJKLMNOPQRSTUVWX PDB Code 6h04 Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X Title Closed conformation of the Membrane Attack Complex Classification IMMUNE SYSTEM Compound Complement component C9 Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  YVISAPKIFRVGASENIVIQVYGYTAFDATISIKSYPDKK FSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVY LEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKV RVYSLNDDLKPAKRETVLTFIDPEGEVDMVEEIDIGIISF PDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLP HFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADV YITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSET AVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGI KYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGG VPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLP SGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSLSQSYLY IDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSK GKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIV TGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQ TVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQF LEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQRSY FPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTG ICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNY RTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKV EGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLR VVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLV PKTEIKRILSVKGLLVGEILSAVLSQEGINILTHAEAELM SVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGM LSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYV EQNQNSICNSLLWLVENYQLDNGSFKENSQLPVEARENSL YLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPA QSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNP PIYRFWKDNLQHGTARMVETTAYALLTSLNLKDINYVNPV IKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLS MDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVST GFGSGLATVHVTTVVHKTS B:  FCDHYAWTQWTSCSKTCNSGTQSRHQIVVDKYYQENFCEQ ICSKQETRECNWQRCPINCLLGDFGPWSDCDPCIEKQSKV RSCTAPLVAFQPCIPSKLCKIEEADCKNKFRCDSGRCIAR KLECNGENDCGDNSDERDCGRTKAVCTRKYNPIPSVQLMG NGFHFLAGEPRGEVLDNSFTGGICKTVKSSRTSNPYRVPA NLENVGFEVQTATDFYKDLTSLGHNENQQGSFSSQGGSSF SVPIFYSSKRSENINHNSAFKQAIQASHKKDSSFIRIHKV MKVLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFD DFGTHYFTSGSLGGVYDLLYQFSSEELKNSGLTEEEAKHC VRIETKKRVLFAKKTKVEHRCTTNKLSEKHEGSFIQGAEK SISLIRSEYGAALAWEKGSSGLEEKTFSEWLESVKENPAV IDFELAPIVDLVRNIPCAVTKRNNLRKALQEYAAKFDPCQ CAPCPNNGRPTLSGTECLCVCQSGTYGENCGQWGCWSSWS TCDATYKRSRTRECNCEGEKRQEEDCTFSIMENNGQPCIN DDEEMKEGCPQPVPPENGFIRNEKQLYLVGEDVEISCLTG FETVGYQYFRCLPDGTWRQGDVECQRTECIKPVVQEVLTI TPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGNSWTPPI SNSLTCEK C:  PIDCELSSWSSWTTCDPCQKKRYRYAYLLQPSQFHGEPCN FSDKEVEDCVTNRPCRSQVRCEGFVCAQTGRCVNRRLLCN GDNDCGDQSDEANCRRIYKKCQHEMDQYWGIGSLASGINL FTNSFEGPVLDHRYYCSPHYILNTRFRKPYNVESYTPQTQ GKYEFILKEYESYSDFERNVTEKMASKSGFSFGFKIPGIF ELGISSQSDRGKHYIRRTKRFSHTKSVFLHARSDLEVAHY KLKPRSLMLHYEFLQRVKRLPLEYSYGEYRDLFRDFGTHY ITEAVLGGIYEYTLVMNKEAMERGDYTLNNVHACAKNDFK IGGAIEEVYVSLGVSVGKCRGILNEIKDRNKRDTMVEDLV VLVRGGASEHITTLAYQELPTADLMQEWGDAVQYNPAIIK VKVEPLYELVTATDFAYSSTVRQNMKQALEEFQKEVSSCH CAPCQGNGVPVLKGSRCDCICPVGSQGLACEVSYRKNTPI DGKWNCWSNWSSCSGRRKTRQRQSGPASETLDC D:  SSPVNCQWDFYAPWSECNGCTKTQTRRRSVAVYGQYGGQP CVGNAFETQSCEPTRGCPTEEGCGERFRCFSGQCISKSLV CNGDSDCDEDSADEDRCEDSERRPSCDIDKPPPNIELTGN GYNELTGQFRNRVINTKSFGGQCRKVFSGDGKDFYRLSGN VLSYTFQVKINNDFNYEFYNSTWSYVKHTSTEHTSSSRKR SFFRSSSSSSRSYTSHTNEIHKGKSYQLLVVENTVEVAQF INNNPEFLQLAEPFWKELSHLPSLYDYSAYRRLIDQYGTH YLQSGSLGGEYRVLFYVDSEKLKQNDFNSVEEKKCKSSGW HFVVKFSSHGCKELENALKAASGTQNNVLRGEPFIRGAGF ISGLSYLELDNPAGNKRRYSAWAESVTNLPQVIKQKLTPL YELVKEVPCASVKKLYLKWALEEYLDEFDPCHCRPCQNGG LATVEGTHCLCHCKPYTFGAACEQGVLVGNQAGGVDGGWS CWSSWSPCVQGKKTRSRECNNPPPSGGGRSCVGETTESTQ CEDEELEHLRLLEPHCFCPSPPALKDGFVQDEGTMFPVGK NVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHCQKIACVL PVLMDGIQSHPQKPFYTVGEKVTVSCSGGMSLEGPSAFLC GSSLKWSPEMKNARCVQKEN E:  ISTIQPKANFDAQQFAGTWLLVAVGSACRFLQEQGHRAEA TTLHVAPQGTAMAVSTFRKLDGICWQVRQLYGDTGVLGRF LLQARGAVHVVVAETDYQSFAVLYLERAGQLSVKLYARSL PVSDSVLSGFEQRVQEAHLTEDQIFYFPKYGFCEAADQFH VLDEV F:  CQLSNWSEWTDCFPCQDKKYRHRSLLQPNKFGGTICSGDI WDQASCSSSTTCCGQDFQCKETGRCLKRHLVCNGDQDCLD GSDEDDCEDVRAIDEDCSQYEPIPGSQKAALGYNILTQED AQSVYDASYYGGQCETVYNGEWRELRYDSTCERLYYGDDE KYFRKPYNFLKYHFEALADTGISSEFYDNANDLLSKVKKD KSDSFGVTIGIGPAGSPLLVGVGVSHSQDTSFLNELNKYN EKKFIFTRIFTKVQTAHFKMRKDDIMLDEGMLQSLMELPD QYNYGMYAKFINDYGTHYITSGSMGGIYEYILVIDKAKME SLGITSRDITTCFGGSLGIQYEDKINVGGGLSGDHCKKFG GGKTERARKAMAVEDIISRVRGGSSGWSGGLAQNRSTITY RSWGRSLKYNPVVIDFEMQPIHEVLRHTSLGPLEAKRQNL RRALDQYLMEFNACRCGPCVPILEGTSCRCQCRLGSLGAA CEADGSWSCWSSWSQERRRECCPGRKVQTQ G:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP H:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP I:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP J:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP K:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP L:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP M:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP N:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP O:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP P:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP Q:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP R:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP S:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP T:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP U:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP V:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP W:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP X:  SHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRC TDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLR CNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGY GINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWN VASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAA ISLKFTPSLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFL HVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEY FAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELK DIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVN ITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDF VNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLE RAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFE GIACEISKQKISEGLPALEFP Description (1)  C9, Complement C5,Complement C5, Complement component C8 beta chain, Complement component C7, Complement component C8 gamma chain, Complement component C8 alpha chain, Complement component C6 Functional site 1) chain L residue 507-518 type prosite sequence CACPFKFEGIAC description EGF_1 EGF-like domain signature 1. CaCpfKfeGIaC source prosite : PS00022 2) chain C residue 469-480 type prosite sequence CICPVGSQGLAC description EGF_1 EGF-like domain signature 1. CaCpfKfeGIaC source prosite : PS00022 3) chain B residue 541-552 type prosite sequence CVCQSGTYGENC description EGF_1 EGF-like domain signature 1. CaCpfKfeGIaC source prosite : PS00022 4) chain F residue 487-498 type prosite sequence CQCRLGSLGAAC description EGF_1 EGF-like domain signature 1. CaCpfKfeGIaC source prosite : PS00022 5) chain D residue 475-486 type prosite sequence CHCKPYTFGAAC description EGF_1 EGF-like domain signature 1. CaCpfKfeGIaC source prosite : PS00022 6) chain L residue 91-113 type prosite sequence CIKMRLRCNGDNDCGDFSDEDDC description LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIkmrlr.CNgdnDCgdfsDEDd....C source prosite : PS01209 7) chain C residue 79-101 type prosite sequence CVNRRLLCNGDNDCGDQSDEANC description LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIkmrlr.CNgdnDCgdfsDEDd....C source prosite : PS01209 8) chain B residue 151-173 type prosite sequence CIARKLECNGENDCGDNSDERDC description LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIkmrlr.CNgdnDCgdfsDEDd....C source prosite : PS01209 9) chain F residue 78-100 type prosite sequence CLKRHLVCNGDQDCLDGSDEDDC description LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIkmrlr.CNgdnDCgdfsDEDd....C source prosite : PS01209 10) chain D residue 96-119 type prosite sequence CISKSLVCNGDSDCDEDSADEDRC description LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIkmrlr.CNgdnDCgdfsDEDd....C source prosite : PS01209 11) chain B residue 29 type CARBOHYD sequence W description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 12) chain Q residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 13) chain R residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 14) chain R residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 15) chain S residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 16) chain S residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 17) chain T residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 18) chain T residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 19) chain U residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 20) chain U residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 21) chain V residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 22) chain L residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 23) chain V residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 24) chain W residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 25) chain W residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 26) chain X residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 27) chain X residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 28) chain P residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 29) chain P residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 30) chain H residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 31) chain H residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 32) chain I residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 33) chain M residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 34) chain I residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 35) chain J residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 36) chain J residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 37) chain K residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 38) chain K residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 39) chain G residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 40) chain G residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 41) chain M residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 42) chain N residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 43) chain N residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 44) chain O residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 45) chain O residue 314-333 type CARBOHYD sequence YFAFLETYGTHYSSSGSLGG description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 46) chain Q residue 293-309 type CARBOHYD sequence VLTTTFVDDIKALPTTY description C-linked (Man) tryptophan => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 32 type CARBOHYD sequence W description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 48) chain V residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 49) chain W residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 50) chain X residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 51) chain P residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 52) chain H residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 53) chain I residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 54) chain J residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 55) chain K residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 56) chain G residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 90 type CARBOHYD sequence W description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 568 type CARBOHYD sequence W description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 59) chain B residue 571 type CARBOHYD sequence W description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 60) chain B residue 574 type CARBOHYD sequence W description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 61) chain R residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 62) chain S residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 63) chain T residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 64) chain U residue 244 type CARBOHYD sequence H description C-linked (Man) tryptophan; partial => ECO:0000269|PubMed:10551839 source Swiss-Prot : SWS_FT_FI2 65) chain E residue 21-34 type prosite sequence NFDAQQFAGTWLLV description LIPOCALIN Lipocalin signature. NFDaqQFAGTWLLV source prosite : PS00213 66) chain B residue 38 type CARBOHYD sequence T description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 67) chain V residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 68) chain W residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 69) chain X residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 70) chain P residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 71) chain H residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 72) chain I residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 73) chain J residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 74) chain K residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 75) chain G residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 76) chain B residue 392 type CARBOHYD sequence T description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 77) chain D residue 509 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 78) chain O residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 79) chain Q residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 80) chain R residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 81) chain S residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 82) chain T residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 83) chain U residue 27 type CARBOHYD sequence W description O-linked (Fuc...) threonine => ECO:0000305|PubMed:22267737 source Swiss-Prot : SWS_FT_FI3 84) chain B residue 324 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 85) chain V residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 86) chain W residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 87) chain X residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 88) chain P residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 89) chain H residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 90) chain I residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 91) chain J residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 92) chain K residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 93) chain G residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 94) chain M residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 95) chain N residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 96) chain O residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 97) chain Q residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 98) chain R residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 99) chain S residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 100) chain T residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 101) chain U residue 30 type CARBOHYD sequence W description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22267737 source Swiss-Prot : SWS_FT_FI4 102) chain V residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 103) chain W residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 104) chain X residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 105) chain P residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 106) chain H residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 107) chain I residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 108) chain J residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 109) chain K residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 110) chain G residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 111) chain M residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 112) chain N residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 113) chain O residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 114) chain Q residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 115) chain R residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 116) chain S residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 117) chain T residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 118) chain U residue 256 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI5 119) chain L residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 120) chain V residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 121) chain W residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 122) chain X residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 123) chain P residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 124) chain H residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 125) chain I residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 126) chain J residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 127) chain K residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 128) chain G residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 129) chain M residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 130) chain N residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 131) chain O residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 132) chain Q residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 133) chain R residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 134) chain S residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 135) chain T residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 136) chain U residue 394 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:4055801 source Swiss-Prot : SWS_FT_FI6 137) chain L residue 314-325 type prosite sequence YFAFLETYGTHY description MACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YfafletYGTHY source prosite : PS00279 138) chain C residue 279-290 type prosite sequence YRDLFRDFGTHY description MACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YfafletYGTHY source prosite : PS00279 139) chain B residue 354-365 type prosite sequence YSRIFDDFGTHY description MACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YfafletYGTHY source prosite : PS00279 140) chain F residue 300-311 type prosite sequence YAKFINDYGTHY description MACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YfafletYGTHY source prosite : PS00279 141) chain D residue 292-303 type prosite sequence YRRLIDQYGTHY description MACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YfafletYGTHY source prosite : PS00279 142) chain L residue 505-518 type prosite sequence CLCACPFKFEGIAC description EGF_2 EGF-like domain signature 2. ClCacPFkfegia..C source prosite : PS01186

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