SPIKE_SARS2
ID SPIKE_SARS2 Reviewed; 1273 AA.
AC P0DTC2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=2;
OS Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=2697049;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=32015508; DOI=10.1038/s41586-020-2008-3;
RA Wu F., Zhao S., Yu B., Chen Y.-M., Wang W., Song Z.-G., Hu Y., Tao Z.-W.,
RA Tian J.-H., Pei Y.-Y., Yuan M.-L., Zhang Y.-L., Dai F.-H., Liu Y.,
RA Wang Q.-M., Zheng J.-J., Xu L., Holmes E.C., Zhang Y.-Z.;
RT "A new coronavirus associated with human respiratory disease in China.";
RL Nature 579:265-269(2020).
RN [2]
RP FUNCTION (SPIKE PROTEIN S1), AND CLEAVAGE BETWEEN S2 AND S2' BY HOST
RP TMPRSS2.
RX PubMed=32142651; DOI=10.1016/j.cell.2020.02.052;
RA Hoffmann M., Kleine-Weber H., Schroeder S., Krueger N., Herrler T.,
RA Erichsen S., Schiergens T.S., Herrler G., Wu N.H., Nitsche A.,
RA Mueller M.A., Drosten C., Poehlmann S.;
RT "SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a
RT clinically proven protease inhibitor.";
RL Cell 181:1-10(2020).
RN [3]
RP CLEAVAGE BETWEEN S1 AND S2 BY HOST FURIN, FUNCTION, AND MUTAGENESIS OF
RP 681-PRO--ALA-684.
RX PubMed=32362314; DOI=10.1016/j.molcel.2020.04.022;
RA Hoffmann M., Kleine-Weber H., Poehlmann S.;
RT "A multibasic cleavage site in the Spike protein of SARS-CoV-2 is essential
RT for infection of human lung cells.";
RL Mol. Cell 78:779-784(2020).
RN [4]
RP GLYCOSYLATION AT ASN-17; ASN-61; ASN-74; ASN-122; ASN-149; ASN-165;
RP ASN-234; ASN-282; ASN-331; ASN-343; ASN-603; ASN-616; ASN-657; ASN-709;
RP ASN-717; ASN-801; ASN-1074; ASN-1098; ASN-1134; ASN-1158; ASN-1173 AND
RP ASN-1194, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=32366695; DOI=10.1126/science.abb9983;
RA Watanabe Y., Allen J.D., Wrapp D., McLellan J.S., Crispin M.;
RT "Site-specific glycan analysis of the SARS-CoV-2 spike.";
RL Science 369:330-333(2020).
RN [5]
RP GLYCOSYLATION AT ASN-61; ASN-74; ASN-122; ASN-149; ASN-165; ASN-234;
RP ASN-282; THR-323; SER-325; ASN-331; ASN-343; ASN-616; ASN-657; ASN-709;
RP ASN-717; ASN-801; ASN-1074; ASN-1098 AND ASN-1194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=32363391; DOI=10.1093/glycob/cwaa042;
RA Shajahan A., Supekar N.T., Gleinich A.S., Azadi P.;
RT "Deducing the N- and O- glycosylation profile of the spike protein of novel
RT coronavirus SARS-CoV-2.";
RL Glycobiology 30:981-988(2020).
RN [6]
RP VARIANT GLY-614.
RX PubMed=32820179; DOI=10.1038/s41598-020-70827-z;
RA Isabel S., Grana-Miraglia L., Gutierrez J.M., Bundalovic-Torma C.,
RA Groves H.E., Isabel M.R., Eshaghi A., Patel S.N., Gubbay J.B., Poutanen T.,
RA Guttman D.S., Poutanen S.M.;
RT "Evolutionary and structural analyses of SARS-CoV-2 D614G spike protein
RT mutation now documented worldwide.";
RL Sci. Rep. 10:14031-14031(2020).
RN [7]
RP VARIANT GLY-614, AND MUTAGENESIS OF ASP-614.
RX PubMed=32697968; DOI=10.1016/j.cell.2020.06.043;
RG Sheffield COVID-19 Genomics Group;
RA Korber B., Fischer W.M., Gnanakaran S., Yoon H., Theiler J., Abfalterer W.,
RA Hengartner N., Giorgi E.E., Bhattacharya T., Foley B., Hastie K.M.,
RA Parker M.D., Partridge D.G., Evans C.M., Freeman T.M., de Silva T.I.,
RA McDanal C., Perez L.G., Tang H., Moon-Walker A., Whelan S.P.,
RA LaBranche C.C., Saphire E.O., Montefiori D.C.;
RT "Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases
RT Infectivity of the COVID-19 Virus.";
RL Cell 182:812-827(2020).
RN [8]
RP FUNCTION.
RX PubMed=32817270; DOI=10.1126/science.abd5223;
RA Turonova B., Sikora M., Schuermann C., Hagen W.J.H., Welsch S.,
RA Blanc F.E.C., von Buelow S., Gecht M., Bagola K., Hoerner C.,
RA van Zandbergen G., Landry J., de Azevedo N.T.D., Mosalaganti S.,
RA Schwarz A., Covino R., Muehlebach M.D., Hummer G., Krijnse Locker J.,
RA Beck M.;
RT "In situ structural analysis of SARS-CoV-2 spike reveals flexibility
RT mediated by three hinges.";
RL Science 370:203-208(2020).
RN [9]
RP GLYCOSYLATION.
RX PubMed=32929138; DOI=10.1038/s41598-020-71748-7;
RA Grant O.C., Montgomery D., Ito K., Woods R.J.;
RT "Analysis of the SARS-CoV-2 spike protein glycan shield reveals
RT implications for immune recognition.";
RL Sci. Rep. 10:14991-14991(2020).
RN [10]
RP GLYCOSYLATION AT ASN-17; ASN-61; ASN-74; ASN-122; ASN-149; ASN-165;
RP ASN-234; ASN-282; ASN-331; ASN-343; ASN-603; ASN-616; ASN-657; ASN-709;
RP ASN-717; ASN-801; ASN-1074; ASN-1098; ASN-1134; ASN-1158; ASN-1173 AND
RP ASN-1194, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=32979942; DOI=10.1016/j.cell.2020.09.018;
RA Yao H., Song Y., Chen Y., Wu N., Xu J., Sun C., Zhang J., Weng T.,
RA Zhang Z., Wu Z., Cheng L., Shi D., Lu X., Lei J., Crispin M., Shi Y.,
RA Li L., Li S.;
RT "Molecular Architecture of the SARS-CoV-2 Virus.";
RL Cell 183:730-738(2020).
RN [11]
RP VARIANT GLY-614, AND MUTAGENESIS OF ASP-614.
RX PubMed=33106671; DOI=10.1038/s41586-020-2895-3;
RA Plante J.A., Liu Y., Liu J., Xia H., Johnson B.A., Lokugamage K.G.,
RA Zhang X., Muruato A.E., Zou J., Fontes-Garfias C.R., Mirchandani D.,
RA Scharton D., Bilello J.P., Ku Z., An Z., Kalveram B., Freiberg A.N.,
RA Menachery V.D., Xie X., Plante K.S., Weaver S.C., Shi P.Y.;
RT "Spike mutation D614G alters SARS-CoV-2 fitness.";
RL Nature 592:116-121(2020).
RN [12]
RP FUNCTION, AND INTERACTION WITH HUMAN NRP1 AND NRP2.
RC STRAIN=SARS-CoV-2/human/Liverpool/REMRQ001/2020;
RX PubMed=33082294; DOI=10.1126/science.abd3072;
RA Daly J.L., Simonetti B., Klein K., Chen K.E., Williamson M.K.,
RA Anton-Plagaro C., Shoemark D.K., Simon-Gracia L., Bauer M., Hollandi R.,
RA Greber U.F., Horvath P., Sessions R.B., Helenius A., Hiscox J.A.,
RA Teesalu T., Matthews D.A., Davidson A.D., Collins B.M., Cullen P.J.,
RA Yamauchi Y.;
RT "Neuropilin-1 is a host factor for SARS-CoV-2 infection.";
RL Science 370:861-865(2020).
RN [13]
RP FUNCTION, AND INTERACTION WITH HUMAN NRP1 AND NRP2.
RC STRAIN=SARS-CoV-2/human/Finland/1/2020;
RX PubMed=33082293; DOI=10.1126/science.abd2985;
RA Cantuti-Castelvetri L., Ojha R., Pedro L.D., Djannatian M., Franz J.,
RA Kuivanen S., van der Meer F., Kallio K., Kaya T., Anastasina M., Smura T.,
RA Levanov L., Szirovicza L., Tobi A., Kallio-Kokko H., Oesterlund P.,
RA Joensuu M., Meunier F.A., Butcher S.J., Winkler M.S., Mollenhauer B.,
RA Helenius A., Gokce O., Teesalu T., Hepojoki J., Vapalahti O.,
RA Stadelmann C., Balistreri G., Simons M.;
RT "Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.";
RL Science 370:856-860(2020).
RN [14]
RP INTERACTION WITH HUMAN ITGA5 AND ITGB1.
RX PubMed=33102950; DOI=10.1016/j.jacbts.2020.10.003;
RA Beddingfield B.J., Iwanaga N., Chapagain P.P., Zheng W., Roy C.J., Hu T.Y.,
RA Kolls J.K., Bix G.J.;
RT "The Integrin Binding Peptide, ATN-161, as a Novel Therapy for SARS-CoV-2
RT Infection.";
RL JACC Basic Transl. Sci. 6:1-8(2021).
RN [15]
RP VARIANT GLY-614.
RX PubMed=33184236; DOI=10.1126/science.abe8499;
RA Hou Y.J., Chiba S., Halfmann P., Ehre C., Kuroda M., Dinnon K.H. III,
RA Leist S.R., Schaefer A., Nakajima N., Takahashi K., Lee R.E.,
RA Mascenik T.M., Graham R., Edwards C.E., Tse L.V., Okuda K., Markmann A.J.,
RA Bartelt L., de Silva A., Margolis D.M., Boucher R.C., Randell S.H.,
RA Suzuki T., Gralinski L.E., Kawaoka Y., Baric R.S.;
RT "SARS-CoV-2 D614G variant exhibits efficient replication ex vivo and
RT transmission in vivo.";
RL Science 370:1464-1468(2020).
RN [16]
RP VARIANT GLY-614.
RX PubMed=33417835; DOI=10.1016/j.celrep.2020.108630;
RA Gobeil S.M., Janowska K., McDowell S., Mansouri K., Parks R., Manne K.,
RA Stalls V., Kopp M.F., Henderson R., Edwards R.J., Haynes B.F., Acharya P.;
RT "D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease
RT Cleavage at the S1/S2 Junction.";
RL Cell Rep. 34:108630-108630(2021).
RN [17]
RP VARIANTS 69-VAL--PHE-70 DEL; LYS-144 DEL; TYR-501; ASP-570; GLY-614;
RP HIS-681; ILE-716; ALA-982 AND HIS-1118.
RC STRAIN=20I/501Y.V1, Alpha, B.1.1.7, VOC-202012/01, and VUI-202012/01;
RX PubMed=33413740; DOI=10.2807/1560-7917.es.2020.26.1.2002106;
RA Leung K., Shum M.H., Leung G.M., Lam T.T., Wu J.T.;
RT "Early transmissibility assessment of the N501Y mutant strains of SARS-CoV-
RT 2 in the United Kingdom, October to November 2020.";
RL Eurosurveillance 26:0-0(2021).
RN [18]
RP VARIANT TYR-501.
RX PubMed=32732280; DOI=10.1126/science.abc4730;
RA Gu H., Chen Q., Yang G., He L., Fan H., Deng Y.Q., Wang Y., Teng Y.,
RA Zhao Z., Cui Y., Li Y., Li X.F., Li J., Zhang N.N., Yang X., Chen S.,
RA Guo Y., Zhao G., Wang X., Luo D.Y., Wang H., Yang X., Li Y., Han G., He Y.,
RA Zhou X., Geng S., Sheng X., Jiang S., Sun S., Qin C.F., Zhou Y.;
RT "Adaptation of SARS-CoV-2 in BALB/c mice for testing vaccine efficacy.";
RL Science 369:1603-1607(2020).
RN [19]
RP VARIANT GLY-614, AND MUTAGENESIS OF GLY-614.
RX PubMed=33636719; DOI=10.1038/s41586-021-03361-1;
RA Zhou B., Thi Nhu Thao T., Hoffmann D., Taddeo A., Ebert N., Labroussaa F.,
RA Pohlmann A., King J., Steiner S., Kelly J.N., Portmann J., Halwe N.J.,
RA Ulrich L., Trueeb B.S., Fan X., Hoffmann B., Wang L., Thomann L., Lin X.,
RA Stalder H., Pozzi B., de Brot S., Jiang N., Cui D., Hossain J., Wilson M.,
RA Keller M., Stark T.J., Barnes J.R., Dijkman R., Jores J., Benarafa C.,
RA Wentworth D.E., Thiel V., Beer M.;
RT "SARS-CoV-2 spike D614G change enhances replication and transmission.";
RL Nature 5920:122-127(2021).
RN [20]
RP MUTAGENESIS OF ASN-165; ASN-234; ASN-331; ASN-343; LEU-452; ALA-475;
RP VAL-483; PHE-490 AND HIS-519.
RX PubMed=32730807; DOI=10.1016/j.cell.2020.07.012;
RA Li Q., Wu J., Nie J., Zhang L., Hao H., Liu S., Zhao C., Zhang Q., Liu H.,
RA Nie L., Qin H., Wang M., Lu Q., Li X., Sun Q., Liu J., Zhang L., Li X.,
RA Huang W., Wang Y.;
RT "The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and
RT Antigenicity.";
RL Cell 182:1284-1294(2020).
RN [21]
RP FUNCTION, CLEAVAGE BETWEEN S1 AND S2 BY HOST CTSL, AND INTERACTION WITH
RP HUMAN ACE2.
RX PubMed=32221306; DOI=10.1038/s41467-020-15562-9;
RA Ou X., Liu Y., Lei X., Li P., Mi D., Ren L., Guo L., Guo R., Chen T.,
RA Hu J., Xiang Z., Mu Z., Chen X., Chen J., Hu K., Jin Q., Wang J., Qian Z.;
RT "Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and
RT its immune cross-reactivity with SARS-CoV.";
RL Nat. Commun. 11:1620-1620(2020).
RN [22]
RP INTERACTION WITH HUMAN ACE2.
RX PubMed=33607086; DOI=10.1016/j.bpj.2021.02.007;
RA Cao W., Dong C., Kim S., Hou D., Tai W., Du L., Im W., Zhang X.F.;
RT "Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2
RT protein-protein interaction.";
RL Biophys. J. 120:1011-1019(2021).
RN [23]
RP FUNCTION, AND CLEAVAGE BETWEEN S1 AND S2 BY HOST TMPRSS2.
RX PubMed=33465165; DOI=10.1371/journal.ppat.1009212;
RA Ou T., Mou H., Zhang L., Ojha A., Choe H., Farzan M.;
RT "Hydroxychloroquine-mediated inhibition of SARS-CoV-2 entry is attenuated
RT by TMPRSS2.";
RL PLoS Pathog. 17:e1009212-e1009212(2021).
RN [24]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH S PROTEIN.
RX PubMed=33229438; DOI=10.1074/jbc.ra120.016175;
RA Boson B., Legros V., Zhou B., Siret E., Mathieu C., Cosset F.L.,
RA Lavillette D., Denolly S.;
RT "The SARS-CoV-2 Envelope and Membrane proteins modulate maturation and
RT retention of the Spike protein, allowing assembly of virus-like
RT particles.";
RL J. Biol. Chem. 296:100111-100111(2020).
RN [25]
RP CLEAVAGE BETWEEN S1 AND S2 BY HOST FURIN, CLEAVAGE BETWEEN S2 AND S2' BY
RP HOST TMPRSS2, MUTAGENESIS OF ALA-684, AND FUNCTION (SPIKE PROTEIN S2').
RX PubMed=32703818; DOI=10.26508/lsa.202000786;
RA Bestle D., Heindl M.R., Limburg H., Van Lam van T., Pilgram O., Moulton H.,
RA Stein D.A., Hardes K., Eickmann M., Dolnik O., Rohde C., Klenk H.D.,
RA Garten W., Steinmetzer T., Boettcher-Friebertshaeuser E.;
RT "TMPRSS2 and furin are both essential for proteolytic activation of SARS-
RT CoV-2 in human airway cells.";
RL Life. Sci Alliance 3:1-14(2020).
RN [26]
RP CLEAVAGE BETWEEN S1 AND S2 BY HOST FURIN, CLEAVAGE BETWEEN S2 AND S2' BY
RP HOST TMPRSS2, CLEAVAGE BETWEEN S2 AND S2' BY HOST CSTL, AND FUNCTION (SPIKE
RP PROTEIN S2').
RX PubMed=34159616; DOI=10.15252/embj.2021107821;
RA Koch J., Uckeley Z.M., Doldan P., Stanifer M., Boulant S., Lozach P.Y.;
RT "TMPRSS2 expression dictates the entry route used by SARS-CoV-2 to infect
RT host cells.";
RL EMBO J. 40:1-20(2021).
RN [27]
RP VARIANTS PHE-18; ALA-80; GLY-215; ASN-417; LYS-484; TYR-501; GLY-614 AND
RP VAL-701.
RC STRAIN=20H/501Y.V2, B.1.351, and Beta;
RX PubMed=33690265; DOI=10.1038/s41586-021-03402-9;
RA Tegally H., Wilkinson E., Giovanetti M., Iranzadeh A., Fonseca V.,
RA Giandhari J., Doolabh D., Pillay S., San E.J., Msomi N., Mlisana K.,
RA von Gottberg A., Walaza S., Allam M., Ismail A., Mohale T., Glass A.J.,
RA Engelbrecht S., Van Zyl G., Preiser W., Petruccione F., Sigal A.,
RA Hardie D., Marais G., Hsiao M., Korsman S., Davies M.A., Tyers L.,
RA Mudau I., York D., Maslo C., Goedhals D., Abrahams S., Laguda-Akingba O.,
RA Alisoltani-Dehkordi A., Godzik A., Wibmer C.K., Sewell B.T., Lourenco J.,
RA Alcantara L.C.J., Kosakovsky Pond S.L., Weaver S., Martin D.,
RA Lessells R.J., Bhiman J.N., Williamson C., de Oliveira T.;
RT "Emergence of a SARS-CoV-2 variant of concern with mutations in spike
RT glycoprotein.";
RL Nature 592:438-443(2021).
RN [28]
RP POLYMORPHISM.
RX PubMed=34142653; DOI=10.2807/1560-7917.es.2021.26.24.2100509;
RA Campbell F., Archer B., Laurenson-Schafer H., Jinnai Y., Konings F.,
RA Batra N., Pavlin B., Vandemaele K., Van Kerkhove M.D., Jombart T.,
RA Morgan O., le Polain de Waroux O.;
RT "Increased transmissibility and global spread of SARS-CoV-2 variants of
RT concern as at June 2021.";
RL Eurosurveillance 26:0-0(2021).
RN [29]
RP VARIANTS ARG-452 AND PHE-453, AND MUTAGENESIS OF LEU-452; TYR-453 AND
RP ASN-501.
RX PubMed=34171266; DOI=10.1016/j.chom.2021.06.006;
RG Genotype to Phenotype Japan (G2P-Japan) Consortium;
RA Motozono C., Toyoda M., Zahradnik J., Saito A., Nasser H., Tan T.S.,
RA Ngare I., Kimura I., Uriu K., Kosugi Y., Yue Y., Shimizu R., Ito J.,
RA Torii S., Yonekawa A., Shimono N., Nagasaki Y., Minami R., Toya T.,
RA Sekiya N., Fukuhara T., Matsuura Y., Schreiber G., Ikeda T., Nakagawa S.,
RA Ueno T., Sato K.;
RT "SARS-CoV-2 spike L452R variant evades cellular immunity and increases
RT infectivity.";
RL Cell Host Microbe 0:0-0(2021).
RN [30]
RP VARIANT 69-VAL--PHE-70 DEL, AND MUTAGENESIS OF 69-HIS-VAL-70.
RX PubMed=34166617; DOI=10.1016/j.celrep.2021.109292;
RG COVID-19 Genomics UK (COG-UK) Consortium;
RA Meng B., Kemp S.A., Papa G., Datir R., Ferreira I.A.T.M., Marelli S.,
RA Harvey W.T., Lytras S., Mohamed A., Gallo G., Thakur N., Collier D.A.,
RA Mlcochova P., Duncan L.M., Carabelli A.M., Kenyon J.C., Lever A.M.,
RA De Marco A., Saliba C., Culap K., Cameroni E., Matheson N.J., Piccoli L.,
RA Corti D., James L.C., Robertson D.L., Bailey D., Gupta R.K.;
RT "Recurrent emergence of SARS-CoV-2 spike deletion H69/V70 and its role in
RT the Alpha variant B.1.1.7.";
RL Cell Rep. 35:109292-109292(2021).
RN [31]
RP VARIANTS ILE-13 AND CYS-152, POLYMORPHISM, AND MASS SPECTROMETRY (SIGNAL).
RX PubMed=34210893; DOI=10.1126/science.abi7994;
RA McCallum M., Bassi J., De Marco A., Chen A., Walls A.C., Di Iulio J.,
RA Tortorici M.A., Navarro M.J., Silacci-Fregni C., Saliba C., Sprouse K.R.,
RA Agostini M., Pinto D., Culap K., Bianchi S., Jaconi S., Cameroni E.,
RA Bowen J.E., Tilles S.W., Pizzuto M.S., Guastalla S.B., Bona G.,
RA Pellanda A.F., Garzoni C., Van Voorhis W.C., Rosen L.E., Snell G.,
RA Telenti A., Virgin H.W., Piccoli L., Corti D., Veesler D.;
RT "SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern.";
RL Science 373:648-654(2021).
RN [32]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-1269 AND HIS-1271.
RX PubMed=34504087; DOI=10.1038/s41467-021-25589-1;
RA Cattin-Ortola J., Welch L.G., Maslen S.L., Papa G., James L.C., Munro S.;
RT "Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate
RT expression at the cell surface and syncytia formation.";
RL Nat. Commun. 12:5333-5333(2021).
RN [33]
RP PALMITOYLATION AT CYS-1235; CYS-1236; CYS-1240; CYS-1241; CYS-1243;
RP CYS-1247; CYS-1248; CYS-1250; CYS-1253 AND CYS-1254.
RX PubMed=34599882; DOI=10.1016/j.devcel.2021.09.016;
RA Mesquita F.S., Abrami L., Sergeeva O., Turelli P., Qing E., Kunz B.,
RA Raclot C., Paz Montoya J., Abriata L.A., Gallagher T., Dal Peraro M.,
RA Trono D., D'Angelo G., van der Goot F.G.;
RT "S-acylation controls SARS-CoV-2 membrane lipid organization and enhances
RT infectivity.";
RL Dev. Cell 56:1-18(2021).
RN [34] {ECO:0007744|PDB:6M17}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP S1), DOMAIN, AND INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN S1).
RX PubMed=32132184; DOI=10.1126/science.abb2762;
RA Yan R., Zhang Y., Li Y., Xia L., Guo Y., Zhou Q.;
RT "Structural basis for the recognition of the SARS-CoV-2 by full-length
RT human ACE2.";
RL Science 367:1444-1448(2020).
RN [35]
RP SUPERANTIGEN, AND DOMAIN.
RX PubMed=32989130; DOI=10.1073/pnas.2010722117;
RA Cheng M.H., Zhang S., Porritt R.A., Noval Rivas M., Paschold L.,
RA Willscher E., Binder M., Arditi M., Bahar I.;
RT "Superantigenic character of an insert unique to SARS-CoV-2 spike supported
RT by skewed TCR repertoire in patients with hyperinflammation.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:25254-25262(2020).
RN [36]
RP INTERACTION WITH HUMAN BILIRUBIN, INTERACTION WITH HUMAN BILIVERDIN, AND
RP MUTAGENESIS OF ASN-121 AND ARG-190.
RX PubMed=33888467; DOI=10.1126/sciadv.abg7607;
RA Rosa A., Pye V.E., Graham C., Muir L., Seow J., Ng K.W., Cook N.J.,
RA Rees-Spear C., Parker E., Dos Santos M.S., Rosadas C., Susana A., Rhys H.,
RA Nans A., Masino L., Roustan C., Christodoulou E., Ulferts R., Wrobel A.G.,
RA Short C.E., Fertleman M., Sanders R.W., Heaney J., Spyer M., Kjaer S.,
RA Riddell A., Malim M.H., Beale R., MacRae J.I., Taylor G.P., Nastouli E.,
RA van Gils M.J., Rosenthal P.B., Pizzato M., McClure M.O., Tedder R.S.,
RA Kassiotis G., McCoy L.E., Doores K.J., Cherepanov P.;
RT "SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity.";
RL Sci. Adv. 7:0-0(2021).
RN [37]
RP BIOTECHNOLOGY, AND MUTAGENESIS OF 682-ARG--ARG-685 AND 986-LYS-VAL-987.
RX PubMed=34322129; DOI=10.3389/fimmu.2021.701501;
RA Martinez-Flores D., Zepeda-Cervantes J., Cruz-Resendiz A.,
RA Aguirre-Sampieri S., Sampieri A., Vaca L.;
RT "SARS-CoV-2 Vaccines Based on the Spike Glycoprotein and Implications of
RT New Viral Variants.";
RL Front. Immunol. 12:701501-701501(2021).
RN [38]
RP GLYCOSYLATION AT THR-676 AND THR-678 BY HOST GALNT1, AND MUTAGENESIS OF
RP SER-673; THR-676; THR-678; SER-680 AND PRO-681.
RX PubMed=34732583; DOI=10.1073/pnas.2109905118;
RA Zhang L., Mann M., Syed Z.A., Reynolds H.M., Tian E., Samara N.L.,
RA Zeldin D.C., Tabak L.A., Ten Hagen K.G.;
RT "Furin cleavage of the SARS-CoV-2 spike is modulated by O-glycosylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [39]
RP REVIEW, PROTEOLITIC PROCESSING, FUNCTION (SPIKE PROTEIN S2), AND FUNCTION
RP (SPIKE PROTEIN S2').
RX PubMed=34561887; DOI=10.1111/1348-0421.12945;
RA Takeda M.;
RT "Proteolytic activation of SARS-CoV-2 spike protein.";
RL Microbiol. Immunol. 66:15-23(2022).
RN [40]
RP INTERACTION WITH HOST MBL2.
RX PubMed=35102342; DOI=10.1038/s41590-021-01114-w;
RA Stravalaci M., Pagani I., Paraboschi E.M., Pedotti M., Doni A.,
RA Scavello F., Mapelli S.N., Sironi M., Perucchini C., Varani L.,
RA Matkovic M., Cavalli A., Cesana D., Gallina P., Pedemonte N., Capurro V.,
RA Clementi N., Mancini N., Invernizzi P., Bayarri-Olmos R., Garred P.,
RA Rappuoli R., Duga S., Bottazzi B., Uguccioni M., Asselta R., Vicenzi E.,
RA Mantovani A., Garlanda C.;
RT "Recognition and inhibition of SARS-CoV-2 by humoral innate immunity
RT pattern recognition molecules.";
RL Nat. Immunol. 23:275-286(2022).
RN [41]
RP FUNCTION (SPIKE PROTEIN S1), AND INTERACTION WITH HOST INTEGRIN (SPIKE
RP PROTEIN S1).
RX PubMed=35150743; DOI=10.1016/j.jbc.2022.101710;
RA Liu J., Lu F., Chen Y., Plow E., Qin J.;
RT "Integrin mediates cell entry of the SARS-CoV-2 virus independent of
RT cellular receptor ACE2.";
RL J. Biol. Chem. 1:101710-101710(2022).
RN [42] {ECO:0007744|PDB:6VSB}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.46 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP S1), INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN S1), SUBUNIT, AND
RP GLYCOSYLATION.
RX PubMed=32075877; DOI=10.1126/science.abb2507;
RA Wrapp D., Wang N., Corbett K.S., Goldsmith J.A., Hsieh C.L., Abiona O.,
RA Graham B.S., McLellan J.S.;
RT "Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.";
RL Science 367:1260-1263(2020).
RN [43] {ECO:0007744|PDB:6VXX, ECO:0007744|PDB:6VYB}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP S1), SUBUNIT (SPIKE PROTEIN S1), INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN
RP S1), MUTAGENESIS OF 679-GLN--ALA-684, GLYCOSYLATION AT ASN-61; ASN-122;
RP ASN-61; ASN-165; ASN-234; ASN-282; ASN-331; ASN-343; ASN-603; ASN-616;
RP ASN-657; ASN-709; ASN-717; ASN-801; ASN-1074; ASN-1098 AND ASN-1134, AND
RP DISULFIDE BOND.
RX PubMed=32155444; DOI=10.1016/j.cell.2020.02.058;
RA Walls A.C., Park Y.J., Tortorici M.A., Wall A., McGuire A.T., Veesler D.;
RT "Structure, function, and antigenicity of the SARS-CoV-2 spike
RT glycoprotein.";
RL Cell 180:1-12(2020).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF SPIKE PROTEIN S1 AND IN COMPLEX
RP WITH HOST ACE2.
RX PubMed=32225176; DOI=10.1038/s41586-020-2180-5;
RA Lan J., Ge J., Yu J., Shan S., Zhou H., Fan S., Zhang Q., Shi X., Wang Q.,
RA Zhang L., Wang X.;
RT "Structure of the SARS-CoV-2 spike receptor-binding domain bound to the
RT ACE2 receptor.";
RL Nature 581:215-220(2020).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF SPIKE PROTEIN S1 AND IN COMPLEX
RP WITH HOST ACE2, INTERACTION WITH HOST ACE2, AND MUTAGENESIS OF GLN-493 AND
RP ASN-501.
RX PubMed=32225175; DOI=10.1038/s41586-020-2179-y;
RA Shang J., Ye G., Shi K., Wan Y., Luo C., Aihara H., Geng Q., Auerbach A.,
RA Li F.;
RT "Structural basis of receptor recognition by SARS-CoV-2.";
RL Nature 581:221-224(2020).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF SPIKE PROTEIN S1 AND IN COMPLEX
RP WITH HUMAN ANTIBODY CR3022, AND DISULFIDE BOND.
RX PubMed=32245784; DOI=10.1126/science.abb7269;
RA Yuan M., Wu N.C., Zhu X., Lee C.D., So R.T.Y., Lv H., Mok C.K.P.,
RA Wilson I.A.;
RT "A highly conserved cryptic epitope in the receptor-binding domains of
RT SARS-CoV-2 and SARS-CoV.";
RL Science 368:630-633(2020).
CC -!- FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane
CC by interacting with host receptor, initiating the infection. The major
CC receptor is host ACE2 (PubMed:32142651, PubMed:33607086,
CC PubMed:32155444). When S2/S2' has been cleaved, binding to the receptor
CC triggers direct fusion at the cell membrane (PubMed:34561887). When
CC S2/s2' has not been cleaved, binding to the receptor results in
CC internalization of the virus by endocytosis leading to fusion of the
CC virion membrane with the host endosomal membrane (PubMed:32221306,
CC PubMed:32075877). Alternatively, may use NRP1/NRP2 (PubMed:33082294,
CC PubMed:33082293) and integrin as entry receptors (PubMed:35150743). The
CC use of NRP1/NRP2 receptors may explain the tropism of the virus in
CC human olfactory epithelial cells, which express these molecules at high
CC levels but ACE2 at low levels (PubMed:33082293). The stalk domain of S
CC contains three hinges, giving the head unexpected orientational freedom
CC (PubMed:32817270). {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:32075877, ECO:0000269|PubMed:32142651,
CC ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32221306,
CC ECO:0000269|PubMed:32817270, ECO:0000269|PubMed:33082293,
CC ECO:0000269|PubMed:33082294, ECO:0000269|PubMed:35150743,
CC ECO:0000303|PubMed:33082293, ECO:0000305|PubMed:34561887}.
CC -!- FUNCTION: [Spike protein S2]: Precursor of the fusion protein processed
CC in the biosynthesis of the S protein and the formation of virus
CC particle. Mediates fusion of the virion and cellular membranes by
CC functioning as a class I viral fusion protein. Contains two viral
CC fusion peptides that are unmasked after cleavage. The S2/S2' cleavage
CC occurs during virus entry at the cell membrane by host TMPRSS2
CC (PubMed:32142651) or during endocytosis by host CSTL (PubMed:32703818,
CC PubMed:34159616). In either case, this triggers an extensive and
CC irreversible conformational change leading to fusion of the viral
CC envelope with the cellular cytoplasmic membrane, releasing viral
CC genomic RNA into the host cell cytoplasm (PubMed:34561887). Under the
CC current model, the protein has at least three conformational states:
CC pre-fusion native state, pre-hairpin intermediate state, and post-
CC fusion hairpin state. During fusion of the viral and target cell
CC membranes, the coiled coil regions (heptad repeats) adopt a trimer-of-
CC hairpins structure and position the fusion peptide in close proximity
CC to the C-terminal region of the ectodomain. Formation of this structure
CC appears to promote apposition and subsequent fusion of viral and target
CC cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616,
CC ECO:0000305|PubMed:34561887}.
CC -!- FUNCTION: [Spike protein S2']: Subunit of the fusion protein that is
CC processed upon entry into the host cell. Mediates fusion of the virion
CC and cellular membranes by functioning as a class I viral fusion
CC protein. Contains a viral fusion peptide that is unmasked after S2
CC cleavage. This cleavage can occur at the cell membrane by host TMPRSS2
CC or during endocytosis by host CSTL (PubMed:32703818, PubMed:34159616).
CC In either case, this triggers an extensive and irreversible
CC conformational change that leads to fusion of the viral envelope with
CC the cellular cytoplasmic membrane, releasing viral genomic RNA into the
CC host cell cytoplasm (PubMed:34561887). Under the current model, the
CC protein has at least three conformational states: pre-fusion native
CC state, pre-hairpin intermediate state, and post-fusion hairpin state.
CC During fusion of the viral and target cell membranes, the coiled coil
CC regions (heptad repeats) adopt a trimer-of-hairpins structure and
CC position the fusion peptide in close proximity to the C-terminal region
CC of the ectodomain. Formation of this structure appears to promote
CC apposition and subsequent fusion of viral and target cell membranes.
CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32703818,
CC ECO:0000269|PubMed:34159616, ECO:0000305|PubMed:34561887}.
CC -!- SUBUNIT: [Spike glycoprotein]: Homotrimer; each monomer consists of a
CC S1 and a S2 subunit (PubMed:32075877, PubMed:32155444,
CC PubMed:32245784). The resulting peplomers protrude from the virus
CC surface as spikes (PubMed:32979942). Interacts with ORF3a protein and
CC ORF7a protein (By similarity) (PubMed:32075877, PubMed:32155444,
CC PubMed:32245784, PubMed:32979942). There are an average of 26 +/-15
CC spike trimers at the surface of virion particles (PubMed:32979942).
CC Binds to host MBL2 (PubMed:35102342). This binding occurs via glycans
CC and inhibits viral infectivity. Inhibition is effective against alpha,
CC beta, gamma, and delta variants (PubMed:35102342). {ECO:0000255|HAMAP-
CC Rule:MF_04099, ECO:0000269|PubMed:32075877,
CC ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32245784,
CC ECO:0000269|PubMed:32979942, ECO:0000269|PubMed:35102342}.
CC -!- SUBUNIT: [Spike protein S1]: Binds to host ACE2 (PubMed:32221306,
CC PubMed:33607086, PubMed:32075877, PubMed:32132184, PubMed:32155444,
CC PubMed:32225175, PubMed:32225176). RBD also interacts with the N-linked
CC glycan on 'Asn-90' of ACE2 (PubMed:33607086). Cleavage of S generates a
CC polybasic C-terminal sequence on S1 that binds to host Neuropilin-1
CC (NRP1) and Neuropilin-2 (NRP2) receptors (PubMed:33082294,
CC PubMed:33082293). Interacts with host integrin alpha-5/beta-1
CC (ITGA5:ITGB1) and with ACE2 in complex with integrin alpha-5/beta-1
CC (ITGA5:ITGB1) (PubMed:33102950). May interact via cytoplasmic c-
CC terminus with M protein (PubMed:33229438). May interact (via N-
CC terminus) with host bilirubin and biliverdin, thereby preventing
CC antibody binding to the SARS-CoV-2 spike NTD via an allosteric
CC mechanism (PubMed:33888467). {ECO:0000269|PubMed:32075877,
CC ECO:0000269|PubMed:32132184, ECO:0000269|PubMed:32155444,
CC ECO:0000269|PubMed:32221306, ECO:0000269|PubMed:32225175,
CC ECO:0000269|PubMed:32225176, ECO:0000269|PubMed:33082293,
CC ECO:0000269|PubMed:33082294, ECO:0000269|PubMed:33102950,
CC ECO:0000269|PubMed:33229438, ECO:0000269|PubMed:33607086,
CC ECO:0000269|PubMed:33888467}.
CC -!- INTERACTION:
CC P0DTC2; P0DTC2: S; NbExp=54; IntAct=EBI-25474821, EBI-25474821;
CC P0DTC2; A0A1S3APE5: ACE2; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-26998936;
CC P0DTC2; E2DHI3: ACE2; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-26998885;
CC P0DTC2; Q58DD0: ACE2; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-26998567;
CC P0DTC2; Q5EGZ1: Ace2; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-25503774;
CC P0DTC2; Q8R0I0: Ace2; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-8365920;
CC P0DTC2; Q9BYF1: ACE2; Xeno; NbExp=224; IntAct=EBI-25474821, EBI-7730807;
CC P0DTC2; P30530: AXL; Xeno; NbExp=9; IntAct=EBI-25474821, EBI-2850927;
CC P0DTC2; P35613: BSG; Xeno; NbExp=7; IntAct=EBI-25474821, EBI-750709;
CC P0DTC2; PRO_0000018590 [Q07021]: C1QBP; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-14032968;
CC P0DTC2; Q9NNX6: CD209; Xeno; NbExp=12; IntAct=EBI-25474821, EBI-9257341;
CC P0DTC2; Q8IUN9: CLEC10A; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-2873246;
CC P0DTC2; Q8IUN9-2: CLEC10A; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-25776912;
CC P0DTC2; Q9H2X3: CLEC4M; Xeno; NbExp=12; IntAct=EBI-25474821, EBI-1391211;
CC P0DTC2; P35606: COPB2; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-1056534;
CC P0DTC2; P07711: CTSL; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-1220160;
CC P0DTC2; PRO_0000006773 [P59665]: DEFA1B; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-27090284;
CC P0DTC2; P00533: EGFR; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-297353;
CC P0DTC2; P08246: ELANE; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-986345;
CC P0DTC2; P09958: FURIN; Xeno; NbExp=5; IntAct=EBI-25474821, EBI-1056807;
CC P0DTC2; A5CKE2: GP1BA; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-28956381;
CC P0DTC2; Q14416: GRM2; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-10232876;
CC P0DTC2; Q96D42: HAVCR1; Xeno; NbExp=7; IntAct=EBI-25474821, EBI-953786;
CC P0DTC2; P11021: HSPA5; Xeno; NbExp=8; IntAct=EBI-25474821, EBI-354921;
CC P0DTC2; P01130: LDLR; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-988319;
CC P0DTC2; P17931: LGALS3; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-1170392;
CC P0DTC2; P47929: LGALS7B; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-357504;
CC P0DTC2; O00214: LGALS8; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-740058;
CC P0DTC2; Q61830: Mrc1; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-642509;
CC P0DTC2; P26038: MSN; Xeno; NbExp=20; IntAct=EBI-25474821, EBI-528768;
CC P0DTC2; P35579: MYH9; Xeno; NbExp=7; IntAct=EBI-25474821, EBI-350338;
CC P0DTC2; P46934-3: NEDD4; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-11980721;
CC P0DTC2; O14786: NRP1; Xeno; NbExp=9; IntAct=EBI-25474821, EBI-1187100;
CC P0DTC2; PRO_0000005068 [P02776]: PF4; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-11809981;
CC P0DTC2; P31431: SDC4; Xeno; NbExp=17; IntAct=EBI-25474821, EBI-3913237;
CC P0DTC2; Q15436: SEC23A; Xeno; NbExp=20; IntAct=EBI-25474821, EBI-81088;
CC P0DTC2; P35247: SFTPD; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-11316157;
CC P0DTC2; PRO_0000017465 [P35247]: SFTPD; Xeno; NbExp=11; IntAct=EBI-25474821, EBI-27021977;
CC P0DTC2; Q96LC7: SIGLEC10; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-8502656;
CC P0DTC2; Q96L92: SNX27; Xeno; NbExp=16; IntAct=EBI-25474821, EBI-2514865;
CC P0DTC2; Q15005: SPCS2; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-1043352;
CC P0DTC2; P42224: STAT1; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-1057697;
CC P0DTC2; Q5EA32: TRPV2; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-27029641;
CC P0DTC2; Q9Y5S1: TRPV2; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-11721896;
CC P0DTC2; Q5MNZ6: WDR45B; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-2819021;
CC PRO_0000449647; Q9BYF1: ACE2; Xeno; NbExp=2; IntAct=EBI-25490323, EBI-7730807;
CC PRO_0000449647; PRO_0000000092 [P05067]: APP; Xeno; NbExp=3; IntAct=EBI-25490323, EBI-821758;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:32979942}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:34504087}. Host
CC endoplasmic reticulum-Golgi intermediate compartment membrane
CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:34504087}; Single-
CC pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host
CC cell membrane {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:34504087}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic
CC reticulum-Golgi intermediate compartment, where it participates in
CC virus particle assembly. Some S oligomers are transported to the host
CC plasma membrane, where they may mediate cell-cell fusion
CC (PubMed:34504087). An average of 26 +/-15 S trimers are found randomly
CC distributed at the surface of the virion (PubMed:32979942).
CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32979942,
CC ECO:0000269|PubMed:34504087}.
CC -!- DOMAIN: Contains sequence and structural motifs very similar to those
CC of a bacterial superantigen and can directly bind and activate T-cell
CC receptors. Activation of a broad T-cell repertoire may be involved in
CC the hyperinflammatory syndrome in acute COVID disease.
CC {ECO:0000303|PubMed:32989130}.
CC -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval and binds
CC COPI in vitro. {ECO:0000250|UniProtKB:P59594}.
CC -!- DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function
CC cooperatively and have a membrane-ordering effect on lipid headgroups
CC and shallow hydrophobic regions of target bilayers. They are considered
CC as two domains of an extended, bipartite FP. The membrane-ordering
CC activity is calcium-dependent and also dependent on correct folding,
CC which is maintained by an internal disulfide bond in FP2.
CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000305|PubMed:34561887}.
CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Palmitoylated
CC spike proteins drive the formation of localized ordered cholesterol and
CC sphingo-lipid-rich lipid nanodomains in the early Golgi, where viral
CC budding occurs. {ECO:0000269|PubMed:34599882}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC precursor is processed into S1 and S2 by host furin or unknown
CC proteases to yield the mature S1 and S2 proteins (PubMed:32362314,
CC PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444).
CC Processing between S2 and S2' occurs either by host CTSL in endosomes
CC (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2
CC at the cell surface (PubMed:32142651). Both cleavages are necessary for
CC the protein to be fusion competent (PubMed:32703818, PubMed:34159616,
CC PubMed:34561887). Cell surface activation allows the virus to enter the
CC cell despite inhibition of the endosomal pathway by hydroxychloroquine
CC (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-
CC CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases
CC the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165).
CC D614G substitution would enhance furin cleavage at the S1/S2 junction
CC (PubMed:33417835). {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32155444,
CC ECO:0000269|PubMed:32221306, ECO:0000269|PubMed:32362314,
CC ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:33417835,
CC ECO:0000269|PubMed:33465165, ECO:0000269|PubMed:34159616,
CC ECO:0000305|PubMed:34561887}.
CC -!- PTM: Highly decorated by heterogeneous N-linked glycans protruding from
CC the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138).
CC Highly glycosylated by host both on S1 and S2 subunits, occluding many
CC regions across the surface of the protein (PubMed:32366695,
CC PubMed:32363391, PubMed:32929138). Approximately 40% of the protein
CC surface is shielded from antibody recognition by glycans, with the
CC notable exception of the ACE2 receptor binding domain
CC (PubMed:32929138). {ECO:0000269|PubMed:32075877,
CC ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
CC ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32929138}.
CC -!- PTM: O-glycosylated by host GALNT1 at the end of S1. This could reduce
CC the efficiency of S1/S2 cleavage. {ECO:0000269|PubMed:34732583}.
CC -!- POLYMORPHISM: Variant Alpha/B.1.1.7 belongs to a lineage isolated first
CC in United Kingdom (December 2020). It is also called Variant of Concern
CC (VOC) 202012/01, Variant Under Investigation (VUI) 202012/01, 501Y.V1
CC or 20B/501Y.V1 (PubMed:33413740). It has an estimated 25% increase of
CC transmissibility (PubMed:34142653). {ECO:0000305|PubMed:33413740,
CC ECO:0000305|PubMed:34142653}.
CC -!- POLYMORPHISM: Variant Beta/B.1.351 belongs to a lineage first isolated
CC in South Africa (December 2020) and is also called 501Y.V2. It has an
CC estimated 25% increase of transmissibility.
CC {ECO:0000305|PubMed:34142653}.
CC -!- POLYMORPHISM: Variant Gamma/P.1 belongs to a lineage first isolated in
CC Brazil (November 2020) and is also called 20J (V3) and GR/501Y.V3. It
CC has an estimated 38% increase of transmissibility.
CC {ECO:0000305|PubMed:34142653}.
CC -!- POLYMORPHISM: Variant Delta/B.1.617.2 belongs to a lineage first
CC isolated in India (October 2020) and is also called G/478K.V1. It has
CC an estimated 97% increase of transmissibility.
CC {ECO:0000305|PubMed:34142653}.
CC -!- POLYMORPHISM: Variant Epsilon/B.1.427/B.1.429 belong to lineages first
CC isolated in USA (Sept 2020). Variant S13I shifts the signal peptide
CC cleavage site from S13-Q14 to C15-V16, thus removing Cys-15 which can
CC no longer establish disulfide bonds with Cys-136. The latter would make
CC a disulfid bond with Cys-152 (W152C variant), thereby changing the N-
CC terminus structure of the protein and its antigenicity.
CC {ECO:0000269|PubMed:34210893}.
CC -!- POLYMORPHISM: Variant Omicron/BA.1 belongs to a lineage first isolated
CC in South Africa (November 2021). {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Main component of the anti-COVID19 vaccines
CC BNT162b2/Pfizer-Biontech and mRNA-1273/Moderna; in which the mutations
CC of Lys-986 (K986P) and Val-987 (V987P) have been added to stabilize the
CC protein in the prefusion state. {ECO:0000305|PubMed:34322129}.
CC -!- BIOTECHNOLOGY: Main component of the anti-COVID19 vaccine
CC Ad26.COV2.S/Janssen Pharmaceutical; in which the mutations Arg-682
CC (R682S), Arg-685 (R685G), Lys-986 (K986P) and Val-987 (V987P) have been
CC added to stabilize the protein in the prefusion state.
CC {ECO:0000305|PubMed:34322129}.
CC -!- BIOTECHNOLOGY: Main component of the anti-COVID vaccine
CC Chadox1/AZD1222/AstraZeneca; in which the human tPA leader sequence is
CC added in N-terminus to enhance protein secretion.
CC {ECO:0000305|PubMed:34322129}.
CC -!- MISCELLANEOUS: Variant D614G has become the most prevalent circulating
CC sequence in the global pandemic since April 2020 (PubMed:32697968). The
CC mutation is associated with higher viral loads produced in cell culture
CC and animal models (PubMed:32697968, PubMed:33106671, PubMed:33184236).
CC It would not change pathogenicity nor neutralization properties vs
CC vaccination (PubMed:33184236). May be prevalent because the mutation
CC increases virus transmission in human population (PubMed:33106671).
CC {ECO:0000269|PubMed:32697968, ECO:0000269|PubMed:33106671,
CC ECO:0000269|PubMed:33184236}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- CAUTION: Asn-17, Asn-603, Asn-1134, Asn-1158, and Asn-1173 are not
CC glycosylated when S1 or S2 are expressed individually in HEK293 cells.
CC {ECO:0000269|PubMed:32363391}.
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DR EMBL; MN908947; QHD43416.1; -; Genomic_RNA.
DR RefSeq; YP_009724390.1; NC_045512.2.
DR PDB; 6LVN; X-ray; 2.47 A; A/B/C/D=1168-1203.
DR PDB; 6LXT; X-ray; 2.90 A; A/B/C/D/E/F=910-988, A/B/C/D/E/F=1162-1206.
DR PDB; 6LZG; X-ray; 2.50 A; B=319-527.
DR PDB; 6M0J; X-ray; 2.45 A; E=319-541.
DR PDB; 6M17; EM; 2.90 A; E/F=319-541.
DR PDB; 6M1V; X-ray; 1.50 A; A=917-966.
DR PDB; 6VSB; EM; 3.46 A; A/B/C=1-1208.
DR PDB; 6VW1; X-ray; 2.68 A; E/F=455-518.
DR PDB; 6VXX; EM; 2.80 A; A/B/C=14-1211.
DR PDB; 6VYB; EM; 3.20 A; A/B/C=14-1211.
DR PDB; 6W41; X-ray; 3.08 A; C=319-541.
DR PDB; 6WPS; EM; 3.10 A; A/B/E=11-1211.
DR PDB; 6WPT; EM; 3.70 A; A/B/C=11-1211.
DR PDB; 6X29; EM; 2.70 A; A/B/C=16-1208.
DR PDB; 6X2A; EM; 3.30 A; A/B/C=16-1208.
DR PDB; 6X2B; EM; 3.60 A; A/B/C=16-1208.
DR PDB; 6X2C; EM; 3.20 A; A/B/C=16-1208.
DR PDB; 6X45; X-ray; 2.20 A; A/B/C=912-966, D/E/F=1168-1203.
DR PDB; 6X6P; EM; 3.22 A; A/B/C=15-1208.
DR PDB; 6X79; EM; 2.90 A; A/B/C=14-1211.
DR PDB; 6XC2; X-ray; 3.11 A; A/Z=319-541.
DR PDB; 6XC3; X-ray; 2.70 A; C=319-541.
DR PDB; 6XC4; X-ray; 2.34 A; A/Z=319-541.
DR PDB; 6XC7; X-ray; 2.88 A; A=319-541.
DR PDB; 6XCM; EM; 3.42 A; A/B/C=1-1213.
DR PDB; 6XCN; EM; 3.66 A; A/C/E=1-1213.
DR PDB; 6XDG; EM; 3.90 A; E=319-541.
DR PDB; 6XE1; X-ray; 2.75 A; E=319-591.
DR PDB; 6XEY; EM; 3.25 A; A/B/C=1-1208.
DR PDB; 6XF5; EM; 3.45 A; A/B/C=14-1208.
DR PDB; 6XF6; EM; 4.00 A; A/B/C=14-1208.
DR PDB; 6XKL; EM; 3.21 A; A/B/C=1-1208.
DR PDB; 6XKP; X-ray; 2.72 A; A/B=319-541.
DR PDB; 6XKQ; X-ray; 2.55 A; A=319-541.
DR PDB; 6XLU; EM; 2.40 A; A/B/C=14-1208.
DR PDB; 6XM0; EM; 2.70 A; A/B/C=14-1208.
DR PDB; 6XM3; EM; 2.90 A; A/B/C=14-1208.
DR PDB; 6XM4; EM; 2.90 A; A/B/C=14-1208.
DR PDB; 6XM5; EM; 3.10 A; A/B/C=14-1208.
DR PDB; 6XR8; EM; 2.90 A; A/B/C=1-1273.
DR PDB; 6XRA; EM; 3.00 A; A/B/C=1-1273.
DR PDB; 6XS6; EM; 3.70 A; A/B/C=1-1213.
DR PDB; 6YLA; X-ray; 2.42 A; A/E=330-532.
DR PDB; 6YM0; X-ray; 4.36 A; E=330-532.
DR PDB; 6YOR; EM; 3.30 A; A/E=330-532.
DR PDB; 6YZ5; X-ray; 1.80 A; E=330-532.
DR PDB; 6YZ7; X-ray; 3.30 A; AAA/EEE=330-532.
DR PDB; 6Z2M; X-ray; 2.71 A; A/E=332-528.
DR PDB; 6Z43; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 6Z97; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 6ZB4; EM; 3.03 A; A/B/C=1-1213.
DR PDB; 6ZB5; EM; 2.85 A; A/B/C=1-1213.
DR PDB; 6ZBP; X-ray; 1.85 A; EEE=330-532.
DR PDB; 6ZCZ; X-ray; 2.65 A; E=333-528.
DR PDB; 6ZDG; EM; 4.70 A; A/D/E=333-526.
DR PDB; 6ZDH; EM; 3.70 A; A/B/C=1-1208.
DR PDB; 6ZER; X-ray; 3.80 A; A/D/E=330-532.
DR PDB; 6ZFO; EM; 4.40 A; A/E=333-526.
DR PDB; 6ZGE; EM; 2.60 A; A/B/C=1-1208.
DR PDB; 6ZGG; EM; 3.80 A; A/B/C=1-1208.
DR PDB; 6ZGI; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 6ZH9; X-ray; 3.31 A; EEE=332-528.
DR PDB; 6ZHD; EM; 3.70 A; A/B/C=1-1208.
DR PDB; 6ZLR; X-ray; 3.10 A; AAA/DDD/EEE=319-541.
DR PDB; 6ZOW; EM; 3.00 A; A/B/C/a=1-1273.
DR PDB; 6ZOX; EM; 3.00 A; A/B/C=14-1211.
DR PDB; 6ZOY; EM; 3.10 A; A/B/C=14-1211.
DR PDB; 6ZOZ; EM; 3.50 A; A/B/C=14-1211.
DR PDB; 6ZP0; EM; 3.00 A; A/B/C=14-1211.
DR PDB; 6ZP1; EM; 3.30 A; A/B/C=14-1211.
DR PDB; 6ZP2; EM; 3.10 A; A/B/C=14-1211.
DR PDB; 6ZP5; EM; 3.10 A; A/B/C=1-1273.
DR PDB; 6ZP7; EM; 3.30 A; A/B/C=1-1273.
DR PDB; 6ZWV; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 6ZXN; EM; 2.93 A; A/B/C=1-1208.
DR PDB; 7A25; EM; 3.06 A; A/B/C=1-1146.
DR PDB; 7A29; EM; 2.94 A; A/B/C=1-1208.
DR PDB; 7A4N; EM; 2.75 A; A/B/C=1-1208.
DR PDB; 7A5R; EM; 3.70 A; A/B=1-1208.
DR PDB; 7A5S; EM; 3.90 A; A/B=1-1208.
DR PDB; 7A91; EM; 3.60 A; A=1-685.
DR PDB; 7A92; EM; 4.20 A; A=1-676.
DR PDB; 7A93; EM; 5.90 A; A/B/C=1-1208.
DR PDB; 7A94; EM; 3.90 A; A/B/C=1-1208.
DR PDB; 7A95; EM; 4.30 A; A/B/C=1-1208.
DR PDB; 7A96; EM; 4.80 A; A/B/C=1-1208.
DR PDB; 7A97; EM; 4.40 A; A/B/C=1-1208.
DR PDB; 7A98; EM; 5.40 A; A/B/C=1-1208.
DR PDB; 7AD1; EM; 2.92 A; A/B/C=1-1208.
DR PDB; 7AKD; EM; 4.00 A; A/B/C=1-1208.
DR PDB; 7B14; EM; 3.79 A; A=333-528.
DR PDB; 7B17; EM; 4.01 A; A=334-528.
DR PDB; 7B18; EM; 2.62 A; A/B/C=1-1208.
DR PDB; 7B3O; X-ray; 2.00 A; E=331-524.
DR PDB; 7B62; X-ray; 1.82 A; A=1-311.
DR PDB; 7BEH; X-ray; 2.30 A; E=333-528.
DR PDB; 7BEI; X-ray; 2.30 A; E=333-528.
DR PDB; 7BEJ; X-ray; 2.42 A; E=333-528.
DR PDB; 7BEK; X-ray; 2.04 A; E=333-528.
DR PDB; 7BEL; X-ray; 2.53 A; R/X=333-528.
DR PDB; 7BEM; X-ray; 2.52 A; E=333-528.
DR PDB; 7BEN; X-ray; 2.50 A; C/E=333-528.
DR PDB; 7BEO; X-ray; 3.19 A; R/X=333-528.
DR PDB; 7BEP; X-ray; 2.61 A; C/E=333-528.
DR PDB; 7BH9; EM; 2.90 A; E=333-528.
DR PDB; 7BNM; EM; 3.60 A; A/B/C=1-1146.
DR PDB; 7BNN; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7BNO; EM; 4.20 A; A/B/C=1-1146.
DR PDB; 7BWJ; X-ray; 2.85 A; E=319-529.
DR PDB; 7BYR; EM; 3.84 A; A/B/C=1-1208.
DR PDB; 7BZ5; X-ray; 1.84 A; A=319-541.
DR PDB; 7C01; X-ray; 2.88 A; A/B=319-541.
DR PDB; 7C2L; EM; 3.10 A; A/B/C=1-1273.
DR PDB; 7C53; X-ray; 2.28 A; A/B/C/D/E/F=910-975.
DR PDB; 7C8D; EM; 3.00 A; B=333-527.
DR PDB; 7C8J; X-ray; 3.18 A; B=333-527.
DR PDB; 7C8V; X-ray; 2.15 A; B=330-531.
DR PDB; 7C8W; X-ray; 2.77 A; B=330-531.
DR PDB; 7CAB; EM; 3.52 A; A/B/C=1-1208.
DR PDB; 7CAC; EM; 3.55 A; A/B/C=1-1208.
DR PDB; 7CAH; EM; 3.90 A; A=334-527.
DR PDB; 7CAI; EM; 3.49 A; A/B/C=1-1208.
DR PDB; 7CAK; EM; 3.58 A; A/B/C=1-1208.
DR PDB; 7CAN; X-ray; 2.94 A; B=330-531.
DR PDB; 7CDI; X-ray; 2.96 A; E=319-529.
DR PDB; 7CDJ; X-ray; 3.40 A; E=319-529.
DR PDB; 7CH4; X-ray; 3.15 A; R=319-541.
DR PDB; 7CH5; X-ray; 2.70 A; R=319-541.
DR PDB; 7CHB; X-ray; 2.40 A; R=319-541.
DR PDB; 7CHC; X-ray; 2.71 A; R=319-541.
DR PDB; 7CHE; X-ray; 3.42 A; R=319-541.
DR PDB; 7CHF; X-ray; 2.67 A; R=319-541.
DR PDB; 7CHH; EM; 3.49 A; A/B/C=1-1208.
DR PDB; 7CHO; X-ray; 2.56 A; A/E=319-529.
DR PDB; 7CHP; X-ray; 2.36 A; E=319-529.
DR PDB; 7CHS; X-ray; 2.40 A; E=319-529.
DR PDB; 7CJF; X-ray; 2.11 A; C=334-527.
DR PDB; 7CM4; X-ray; 2.71 A; A=319-536.
DR PDB; 7CN4; EM; 2.93 A; A/B/C=1-1213.
DR PDB; 7CN9; EM; 4.70 A; A/B/C=14-1140.
DR PDB; 7CT5; EM; 4.00 A; A/B/C=1-1273.
DR PDB; 7CWL; EM; 3.80 A; A/B/C=1-1273.
DR PDB; 7CWM; EM; 3.60 A; A/B/C=1-1273.
DR PDB; 7CWN; EM; 3.20 A; A/B/C=1-1273.
DR PDB; 7CWO; EM; 3.90 A; A=1-1273.
DR PDB; 7CWS; EM; 3.40 A; O/Q/R=14-1147.
DR PDB; 7CWT; EM; 3.70 A; A/B/C=14-1147.
DR PDB; 7CWU; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7CYH; EM; 3.90 A; A=334-527.
DR PDB; 7CYP; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7CYV; X-ray; 3.13 A; B=330-531.
DR PDB; 7CZP; EM; 3.00 A; A/B/C=1-1273.
DR PDB; 7CZQ; EM; 2.80 A; A/B/C=1-1273.
DR PDB; 7CZR; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7CZS; EM; 3.60 A; A/B/C=1-1273.
DR PDB; 7CZT; EM; 2.70 A; A/B/C=1-1273.
DR PDB; 7CZU; EM; 3.40 A; A/B/C=1-1273.
DR PDB; 7CZV; EM; 3.30 A; A/B/C=1-1273.
DR PDB; 7CZW; EM; 2.80 A; A/B/C=1-1273.
DR PDB; 7CZX; EM; 2.80 A; A/B/C=1-1273.
DR PDB; 7CZY; EM; 3.30 A; A/B/C=1-1273.
DR PDB; 7CZZ; EM; 3.20 A; A/B/C=1-1273.
DR PDB; 7D00; EM; 3.00 A; A/B/C=1-1273.
DR PDB; 7D03; EM; 3.20 A; A/B/C=1-1273.
DR PDB; 7D0B; EM; 3.90 A; A/B/C=1-1273.
DR PDB; 7D0C; EM; 3.40 A; A/B/C=1-1273.
DR PDB; 7D0D; EM; 3.80 A; A/B/C=1-1273.
DR PDB; 7D2Z; X-ray; 1.97 A; B=330-531.
DR PDB; 7D30; X-ray; 2.10 A; B=330-531.
DR PDB; 7D4G; EM; 3.90 A; B=13-290.
DR PDB; 7D6I; X-ray; 3.41 A; A=319-532.
DR PDB; 7DCC; EM; 4.30 A; E/I/K=1-1208.
DR PDB; 7DCX; EM; 5.90 A; C/D/K=1-1208.
DR PDB; 7DD2; EM; 5.60 A; C/D/K=1-1208.
DR PDB; 7DD8; EM; 7.50 A; C/D/E=1-1208.
DR PDB; 7DDD; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7DDN; EM; 6.30 A; A/B/C=1-1208.
DR PDB; 7DEO; X-ray; 2.50 A; B/D=334-530.
DR PDB; 7DET; X-ray; 2.20 A; A/C=334-530.
DR PDB; 7DEU; X-ray; 2.10 A; A=334-530.
DR PDB; 7DF3; EM; 2.70 A; A/B/C=1-1208.
DR PDB; 7DF4; EM; 3.80 A; B/C/D=1-1208.
DR PDB; 7DHX; X-ray; 2.30 A; B=319-527.
DR PDB; 7DJZ; X-ray; 2.40 A; C=319-541.
DR PDB; 7DK0; X-ray; 3.20 A; C=319-541.
DR PDB; 7DK2; X-ray; 3.00 A; C/F/I/L=319-541.
DR PDB; 7DK3; EM; 6.00 A; A/B/C=1-1208.
DR PDB; 7DK4; EM; 3.80 A; A/B/C=1-1208.
DR PDB; 7DK5; EM; 13.50 A; A/B/C=1-1208.
DR PDB; 7DK6; EM; 4.30 A; A/B/C=1-1208.
DR PDB; 7DK7; EM; 9.70 A; A/B/C=1-1208.
DR PDB; 7DMU; X-ray; 3.20 A; B/D=319-531.
DR PDB; 7DPM; X-ray; 3.30 A; C/F/I/L=319-541.
DR PDB; 7DQA; EM; 2.80 A; C=333-526.
DR PDB; 7DWX; EM; 8.30 A; E/F/G/H/I/J=1-1273.
DR PDB; 7DWY; EM; 2.70 A; A/B/C=1-1273.
DR PDB; 7DWZ; EM; 3.30 A; A/B/C=1-1273.
DR PDB; 7DX0; EM; 3.20 A; A/B/C=1-1273.
DR PDB; 7DX1; EM; 3.10 A; A/B/C=1-1273.
DR PDB; 7DX2; EM; 3.30 A; A/B/C=1-1273.
DR PDB; 7DX3; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7DX4; EM; 3.60 A; E=333-526.
DR PDB; 7DX5; EM; 3.30 A; A/B/C=1-1273.
DR PDB; 7DX6; EM; 3.00 A; A/B/C=1-1273.
DR PDB; 7DX7; EM; 3.40 A; A/B/C=1-1273.
DR PDB; 7DX8; EM; 2.90 A; A/B/C=1-1273.
DR PDB; 7DX9; EM; 3.60 A; A/B/C=1-1273.
DR PDB; 7DZW; EM; 3.45 A; A/B/C=14-1254.
DR PDB; 7DZX; EM; 3.53 A; A/B/C=27-1147.
DR PDB; 7DZY; EM; 3.60 A; A/B/C=27-1211.
DR PDB; 7E23; EM; 3.30 A; A=333-526.
DR PDB; 7E39; EM; 3.70 A; A=333-526.
DR PDB; 7E3B; EM; 4.20 A; A=333-526.
DR PDB; 7E3C; EM; 4.20 A; A=333-526.
DR PDB; 7E3J; X-ray; 2.99 A; B=333-527.
DR PDB; 7E3K; EM; 3.90 A; A/B/C=1-1208.
DR PDB; 7E3L; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7E3O; X-ray; 2.51 A; R=337-527.
DR PDB; 7E5O; X-ray; 2.80 A; A=322-536.
DR PDB; 7E5R; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7E5S; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7E5Y; X-ray; 3.59 A; A/R=319-541.
DR PDB; 7E7B; EM; 2.60 A; A/B/C=1-1211.
DR PDB; 7E7D; EM; 3.20 A; A/B/C=1-1211.
DR PDB; 7E7X; X-ray; 2.78 A; A/B=13-303.
DR PDB; 7E7Y; X-ray; 2.41 A; E/R=319-541.
DR PDB; 7E86; X-ray; 2.90 A; C=333-526.
DR PDB; 7E88; X-ray; 3.14 A; C/F/I/L=333-526.
DR PDB; 7E8C; EM; 3.16 A; A/B/C=1-1208.
DR PDB; 7E8F; EM; 3.18 A; A=13-303, R=319-541.
DR PDB; 7E8M; X-ray; 2.09 A; E=333-527.
DR PDB; 7E9N; EM; 3.69 A; A/B/C=27-1147.
DR PDB; 7E9O; EM; 3.41 A; A/B/C=1-1208.
DR PDB; 7E9P; EM; 3.69 A; B=1-1208.
DR PDB; 7E9Q; EM; 3.65 A; A/B/C=1-1208.
DR PDB; 7E9T; EM; 10.90 A; A/B/C=703-1234.
DR PDB; 7EAM; X-ray; 1.40 A; A/B=319-541.
DR PDB; 7EAN; X-ray; 1.91 A; A=319-541.
DR PDB; 7EAZ; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7EB0; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7EB3; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7EB4; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7EB5; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7EDF; EM; 3.20 A; A/B/C=16-1208.
DR PDB; 7EDG; EM; 3.20 A; A/B/C=16-1208.
DR PDB; 7EDH; EM; 3.60 A; A/B/C=16-1208.
DR PDB; 7EDI; EM; 3.30 A; A/B/C=16-1208.
DR PDB; 7EDJ; EM; 3.30 A; A/B/C=16-1208.
DR PDB; 7EFP; X-ray; 2.70 A; B=320-537.
DR PDB; 7EFR; X-ray; 2.49 A; B=321-537.
DR PDB; 7EH5; EM; 4.00 A; A/B/C=1-1208.
DR PDB; 7EJ4; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7EJ5; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7EJY; X-ray; 3.04 A; R=319-541.
DR PDB; 7EJZ; X-ray; 3.63 A; R=319-541.
DR PDB; 7EK0; X-ray; 2.70 A; R=319-541.
DR PDB; 7EK6; X-ray; 1.24 A; A=906-957, B=1175-1211.
DR PDB; 7EKC; X-ray; 2.80 A; B=319-541.
DR PDB; 7EKE; X-ray; 2.70 A; B=319-541.
DR PDB; 7EKF; X-ray; 2.85 A; B=319-541.
DR PDB; 7EKG; X-ray; 2.63 A; B=319-541.
DR PDB; 7EKH; X-ray; 2.40 A; B=319-541.
DR PDB; 7ENF; EM; 2.76 A; A/B/C=1-1208.
DR PDB; 7ENG; EM; 3.59 A; B=1-1208.
DR PDB; 7EU2; X-ray; 2.80 A; C/F=417-425.
DR PDB; 7EY0; EM; 3.20 A; N/R=1-1207.
DR PDB; 7EY4; EM; 3.69 A; N=1-290, R=1-1207.
DR PDB; 7EY5; EM; 3.40 A; A=1-1208.
DR PDB; 7EYA; EM; 3.77 A; N=1-290, R=1-1208.
DR PDB; 7EZV; EM; 3.30 A; A=1-1208.
DR PDB; 7F46; EM; 4.79 A; B/C=1-1208.
DR PDB; 7F4W; X-ray; 2.90 A; E/F=448-456.
DR PDB; 7F62; EM; 3.60 A; A=1-1208.
DR PDB; 7F63; EM; 3.90 A; A=1-1208.
DR PDB; 7F7E; X-ray; 2.49 A; E=333-527.
DR PDB; 7FAE; EM; 3.65 A; A/B/C=1-1208.
DR PDB; 7FAF; EM; 3.69 A; A/B/C=1-1208.
DR PDB; 7FCD; EM; 3.90 A; A/B/C=1-1208.
DR PDB; 7FCE; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7FDG; EM; 3.69 A; E=333-526.
DR PDB; 7FDH; EM; 3.72 A; E=333-526.
DR PDB; 7FDI; EM; 3.12 A; E=333-526.
DR PDB; 7FDK; EM; 3.69 A; E=333-526.
DR PDB; 7FEM; EM; 4.10 A; A/B/C=15-1208.
DR PDB; 7FET; EM; 3.70 A; A/B/C=15-1208.
DR PDB; 7FG2; EM; 4.40 A; A=1-1273.
DR PDB; 7FG3; EM; 3.90 A; A=1-1273.
DR PDB; 7FG7; EM; 6.90 A; A=1-1273.
DR PDB; 7FJO; EM; 3.34 A; A/B/C=16-1208.
DR PDB; 7JJC; X-ray; 2.36 A; E/F/G/H=679-685.
DR PDB; 7JJI; EM; 3.60 A; A/B/C=1-1273.
DR PDB; 7JJJ; EM; 4.50 A; A/B/C/D/E/F=1-1273.
DR PDB; 7JMO; X-ray; 2.36 A; A=319-541.
DR PDB; 7JMP; X-ray; 1.71 A; A=319-541.
DR PDB; 7JMW; X-ray; 2.89 A; A=319-541.
DR PDB; 7JV2; EM; 3.50 A; A=14-1211.
DR PDB; 7JV4; EM; 3.40 A; A/B/C=14-1211.
DR PDB; 7JV6; EM; 3.00 A; A/B/E=14-1211.
DR PDB; 7JVA; EM; 3.60 A; A=14-1211.
DR PDB; 7JVB; X-ray; 3.29 A; A/B=319-541.
DR PDB; 7JVC; EM; 3.30 A; A/B/E=14-1211.
DR PDB; 7JW0; EM; 4.30 A; A/B/E=14-1211.
DR PDB; 7JWB; EM; 6.00 A; A/B/C=1-1208.
DR PDB; 7JWY; EM; 2.50 A; A/B/C=14-1208.
DR PDB; 7JX3; X-ray; 2.65 A; R=328-531.
DR PDB; 7JZL; EM; 2.70 A; A/B/C=1-1208.
DR PDB; 7JZM; EM; 3.50 A; B=1-1208.
DR PDB; 7JZN; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7JZU; EM; 3.10 A; B=1-1208.
DR PDB; 7K43; EM; 2.60 A; A/B/E=14-1211.
DR PDB; 7K45; EM; 3.70 A; B=1-1208.
DR PDB; 7K4N; EM; 3.30 A; A/B/E=1-1208.
DR PDB; 7K8M; X-ray; 3.20 A; E=331-517.
DR PDB; 7K8S; EM; 3.40 A; A/B/C=1-1213.
DR PDB; 7K8T; EM; 3.40 A; A/B/C=1-1213.
DR PDB; 7K8U; EM; 3.80 A; A/B/C=1-1213.
DR PDB; 7K8V; EM; 3.80 A; A/B/C=1-1213.
DR PDB; 7K8W; EM; 3.60 A; A/B/G=1-1213.
DR PDB; 7K8X; EM; 3.90 A; A/B/C=1-1213.
DR PDB; 7K8Y; EM; 4.40 A; B/D/E=1-1213.
DR PDB; 7K8Z; EM; 3.50 A; A/B/C=1-1213.
DR PDB; 7K90; EM; 3.24 A; A/B/C=1-1208.
DR PDB; 7K9H; EM; 3.20 A; A/B/C=1-1213.
DR PDB; 7K9I; EM; 3.30 A; A=333-527.
DR PDB; 7K9J; EM; 3.00 A; A/B/C=1-1213.
DR PDB; 7K9K; EM; 3.14 A; A=333-527.
DR PDB; 7K9Z; X-ray; 2.95 A; E=319-541.
DR PDB; 7KDG; EM; 3.01 A; A/B/C=1-1208.
DR PDB; 7KDH; EM; 3.33 A; A/B/C=1-1208.
DR PDB; 7KDI; EM; 3.26 A; A/B/C=1-1208.
DR PDB; 7KDJ; EM; 3.49 A; A/B/C=1-1208.
DR PDB; 7KDK; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7KDL; EM; 2.96 A; A/B/C=1-1208.
DR PDB; 7KE4; EM; 3.21 A; A/B/C=1-1208.
DR PDB; 7KE6; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7KE7; EM; 3.32 A; A/B/C=1-1208.
DR PDB; 7KE8; EM; 3.26 A; A/B/C=1-1208.
DR PDB; 7KE9; EM; 3.08 A; A/B/C=1-1208.
DR PDB; 7KEA; EM; 3.33 A; A/B/C=1-1208.
DR PDB; 7KEB; EM; 3.48 A; A/B/C=1-1208.
DR PDB; 7KEC; EM; 3.84 A; A/B/C=1-1208.
DR PDB; 7KFV; X-ray; 2.10 A; A/B/E=319-541.
DR PDB; 7KFW; X-ray; 2.79 A; A/B/E=319-541.
DR PDB; 7KFX; X-ray; 2.23 A; A=319-541.
DR PDB; 7KFY; X-ray; 2.16 A; A=319-541.
DR PDB; 7KGJ; X-ray; 2.30 A; A=333-528.
DR PDB; 7KGK; X-ray; 2.60 A; A=333-527.
DR PDB; 7KJ2; EM; 3.60 A; A/B/C=14-1208.
DR PDB; 7KJ3; EM; 3.70 A; A/B/C=14-1208.
DR PDB; 7KJ4; EM; 3.40 A; A/B/C=14-1208.
DR PDB; 7KJ5; EM; 3.60 A; A/B/C=14-1208.
DR PDB; 7KKK; EM; 3.03 A; A/C/E=1-1208.
DR PDB; 7KKL; EM; 2.85 A; A/C/D=1-1208.
DR PDB; 7KL9; EM; 4.10 A; A/B/C=1-1208.
DR PDB; 7KLG; X-ray; 3.20 A; A/B=328-528.
DR PDB; 7KLH; X-ray; 3.00 A; A/B=328-528.
DR PDB; 7KLW; X-ray; 2.60 A; A=334-527.
DR PDB; 7KM5; X-ray; 3.19 A; A/B=319-535.
DR PDB; 7KMB; EM; 3.39 A; G=16-1208.
DR PDB; 7KMG; X-ray; 2.16 A; C/F=329-527.
DR PDB; 7KMH; X-ray; 1.72 A; C=329-527.
DR PDB; 7KMI; X-ray; 1.73 A; C=329-527.
DR PDB; 7KMK; EM; 4.20 A; A/B/C=1-1211.
DR PDB; 7KML; EM; 3.80 A; A/B/C=1-1211.
DR PDB; 7KMS; EM; 3.64 A; A/B/C=1-1208.
DR PDB; 7KMZ; EM; 3.62 A; A/B/C=1-1208.
DR PDB; 7KN3; X-ray; 2.25 A; A/B=319-541.
DR PDB; 7KN4; X-ray; 2.70 A; A/B=319-541.
DR PDB; 7KN5; X-ray; 1.87 A; A/B=319-541.
DR PDB; 7KN6; X-ray; 2.55 A; A=319-541.
DR PDB; 7KN7; X-ray; 2.73 A; A=319-541.
DR PDB; 7KNB; EM; 3.93 A; A/B/C=1-1208.
DR PDB; 7KNE; EM; 3.85 A; A/B/C=1-1208.
DR PDB; 7KNH; EM; 3.74 A; A/B/C=1-1208.
DR PDB; 7KNI; EM; 3.91 A; A/B/C=1-1208.
DR PDB; 7KQB; EM; 2.42 A; A/B/C=1-1208.
DR PDB; 7KQE; EM; 2.88 A; A/B/C=1-1208.
DR PDB; 7KRQ; EM; 3.44 A; A/B/C=1-1273.
DR PDB; 7KRR; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7KRS; EM; 3.20 A; A/B/C=1-1273.
DR PDB; 7KS9; EM; 4.75 A; A/B/C=1-1208.
DR PDB; 7KSG; EM; 3.33 A; A/B/C=1-1208.
DR PDB; 7KXJ; EM; 6.40 A; A/B/C=1-1211.
DR PDB; 7KXK; EM; 5.00 A; A/B/C=1-1211.
DR PDB; 7KZB; X-ray; 2.83 A; C=333-528.
DR PDB; 7L02; EM; 3.20 A; A/B/C=27-1147.
DR PDB; 7L06; EM; 3.30 A; A/B/C=27-1147.
DR PDB; 7L09; EM; 3.10 A; A/B/C=27-1147.
DR PDB; 7L0N; X-ray; 2.78 A; R/S=328-531.
DR PDB; 7L2C; X-ray; 3.65 A; A/B=1-334.
DR PDB; 7L2D; EM; 3.55 A; A/B/C=1-1208.
DR PDB; 7L2E; EM; 2.97 A; A/B/C=1-1208.
DR PDB; 7L2F; EM; 3.90 A; A/B/C=1-1208.
DR PDB; 7L3N; EM; 3.27 A; A/B/C=13-1208.
DR PDB; 7L4Z; X-ray; 3.96 A; A/B/C/D/E=319-541.
DR PDB; 7L56; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7L57; EM; 5.87 A; A/B/C=1-1208.
DR PDB; 7L58; EM; 5.07 A; A/B/C=1-1208.
DR PDB; 7L5B; X-ray; 3.18 A; A=319-537.
DR PDB; 7L7D; X-ray; 2.50 A; E=330-529.
DR PDB; 7L7E; X-ray; 3.00 A; G/K/S/b=330-529.
DR PDB; 7L7F; EM; 3.24 A; E/F=323-528.
DR PDB; 7L7K; EM; 3.29 A; A/B/C=1-1273.
DR PDB; 7LAA; EM; 3.42 A; A/B/C=27-1147.
DR PDB; 7LAB; EM; 2.97 A; A/B/C=27-1147.
DR PDB; 7LC8; NMR; -; A/B/C=1217-1237.
DR PDB; 7LCN; EM; 3.35 A; A/C/K=27-1147.
DR PDB; 7LD1; EM; 3.40 A; A/B/C=27-1147.
DR PDB; 7LDJ; X-ray; 2.36 A; A/B/C/D=331-527.
DR PDB; 7LJR; EM; 3.66 A; A/B/C=1-1208.
DR PDB; 7LM8; X-ray; 1.94 A; A=319-541.
DR PDB; 7LO4; X-ray; 2.46 A; B=333-530.
DR PDB; 7LOP; X-ray; 2.25 A; A/Z=319-541.
DR PDB; 7LQ7; X-ray; 3.40 A; A/B/E=333-530.
DR PDB; 7LQV; EM; 3.25 A; A/B/C=14-1208.
DR PDB; 7LQW; EM; 4.47 A; A/B/C=14-1208.
DR PDB; 7LRS; EM; 3.89 A; C=332-527.
DR PDB; 7LRT; EM; 3.54 A; A/B/C=14-1208.
DR PDB; 7LS9; EM; 3.42 A; A/B/C=1-1208.
DR PDB; 7LSS; EM; 3.72 A; A/B/C=1-1208.
DR PDB; 7LWI; EM; 3.07 A; A/B/C=1-1208.
DR PDB; 7LWJ; EM; 3.24 A; A/B/C=1-1208.
DR PDB; 7LWK; EM; 2.92 A; A/B/C=1-1208.
DR PDB; 7LWL; EM; 2.84 A; A/B/C=1-1208.
DR PDB; 7LWM; EM; 2.83 A; A/B/C=1-1208.
DR PDB; 7LWN; EM; 2.94 A; A/B/C=1-1208.
DR PDB; 7LWO; EM; 2.85 A; A/B/C=1-1208.
DR PDB; 7LWP; EM; 3.01 A; A/B/C=1-1208.
DR PDB; 7LWQ; EM; 3.44 A; A/B/C=1-1208.
DR PDB; 7LWS; EM; 3.22 A; A/B/C=1-1208.
DR PDB; 7LWT; EM; 3.19 A; A/B/C=1-1208.
DR PDB; 7LWU; EM; 3.22 A; A/B/C=1-1208.
DR PDB; 7LWV; EM; 3.12 A; A/B/C=1-1208.
DR PDB; 7LWW; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7LX5; EM; 3.44 A; B=1-1208.
DR PDB; 7LXW; EM; 2.80 A; A=1-1208.
DR PDB; 7LXX; EM; 3.00 A; A=1-1208.
DR PDB; 7LXY; EM; 2.20 A; A/B/J=1-1208.
DR PDB; 7LXZ; EM; 2.60 A; A/B/K=1-1208.
DR PDB; 7LY0; EM; 2.60 A; A=1-1208.
DR PDB; 7LY2; EM; 2.50 A; A/B/J=1-1208.
DR PDB; 7LY3; X-ray; 3.00 A; A/B=14-307.
DR PDB; 7LYK; EM; 3.65 A; A/B/C=1-1208.
DR PDB; 7LYL; EM; 3.72 A; A/B/C=1-1208.
DR PDB; 7LYM; EM; 3.57 A; A/B/C=1-1208.
DR PDB; 7LYN; EM; 3.32 A; A/B/C=1-1208.
DR PDB; 7LYO; EM; 3.32 A; A/B/C=1-1208.
DR PDB; 7LYP; EM; 4.05 A; A/B/C=1-1208.
DR PDB; 7LYQ; EM; 3.34 A; A/B/C=1-1208.
DR PDB; 7M0J; EM; 3.52 A; A/B/C=16-1208.
DR PDB; 7M3I; X-ray; 2.80 A; C/R=319-591.
DR PDB; 7M42; EM; 3.30 A; E=319-541.
DR PDB; 7M53; X-ray; 1.40 A; A=1146-1161.
DR PDB; 7M6D; X-ray; 3.10 A; C=328-533.
DR PDB; 7M6E; EM; 3.30 A; A/B/E=1-1208.
DR PDB; 7M6F; EM; 3.90 A; A/B/E=1-1208.
DR PDB; 7M6G; EM; 3.70 A; A/B/C=1-1208.
DR PDB; 7M6H; EM; 4.00 A; A/B/C=1-1213.
DR PDB; 7M6I; EM; 4.00 A; A/B/C=1-1213.
DR PDB; 7M71; EM; 2.66 A; A/B=1-1208.
DR PDB; 7M7B; EM; 2.95 A; A=1-1208.
DR PDB; 7M7W; X-ray; 2.65 A; R/S=328-531.
DR PDB; 7M8J; EM; 3.48 A; A=14-270.
DR PDB; 7M8K; EM; -; A/B/C=1-1208.
DR PDB; 7M8S; X-ray; 2.35 A; C/F=386-395.
DR PDB; 7M8T; X-ray; 1.50 A; C=370-378.
DR PDB; 7M8U; X-ray; 1.45 A; C=896-904.
DR PDB; 7MDW; EM; 3.58 A; R=333-526.
DR PDB; 7ME7; EM; 3.73 A; R=333-526.
DR PDB; 7MEJ; EM; 3.55 A; R=333-526.
DR PDB; 7MF1; X-ray; 2.09 A; A=333-530.
DR PDB; 7MFU; X-ray; 1.70 A; A/D=332-528.
DR PDB; 7MJG; EM; 2.81 A; A/B/C=1-1208.
DR PDB; 7MJH; EM; 2.66 A; A/B/C=1-1208.
DR PDB; 7MJI; EM; 2.81 A; B=1-1208.
DR PDB; 7MJJ; EM; 3.32 A; A/B/C=1-1208.
DR PDB; 7MJK; EM; 2.73 A; A/B/C=1-1208.
DR PDB; 7MJL; EM; 2.95 A; A=1-1208.
DR PDB; 7MJM; EM; 2.83 A; A/B/C=1-1208.
DR PDB; 7MJN; EM; 3.29 A; B=1-1208.
DR PDB; 7MKB; X-ray; 1.90 A; C=269-277.
DR PDB; 7MKL; EM; 3.20 A; A/B/C=27-1147.
DR PDB; 7MKM; EM; 3.16 A; A=333-520.
DR PDB; 7MLZ; EM; 3.71 A; A=331-527.
DR PDB; 7MM0; EM; 3.15 A; A/B/C=14-1208.
DR PDB; 7MMO; X-ray; 2.43 A; C/F=329-527.
DR PDB; 7MSQ; X-ray; 2.29 A; A/B=333-528.
DR PDB; 7MTC; EM; 2.60 A; A/B/C=14-1211.
DR PDB; 7MTD; EM; 3.50 A; A/B/C=14-1211.
DR PDB; 7MTE; EM; 3.20 A; A/B/C=14-1211.
DR PDB; 7MW2; EM; 2.97 A; A/B/C=1-1208.
DR PDB; 7MW3; EM; 3.15 A; A/B/C=1-1208.
DR PDB; 7MW4; EM; 3.42 A; A/B/C=1-1208.
DR PDB; 7MW5; EM; 3.42 A; A/B/C=1-1208.
DR PDB; 7MW6; EM; 3.22 A; A/B/C=1-1208.
DR PDB; 7MY2; EM; 2.65 A; B/C/E=1-1208.
DR PDB; 7MY3; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 7MY8; NMR; -; A=816-857.
DR PDB; 7MZF; X-ray; 2.49 A; A=331-527.
DR PDB; 7MZG; X-ray; 2.00 A; A=331-527.
DR PDB; 7MZH; X-ray; 2.10 A; A/E=331-527.
DR PDB; 7MZI; X-ray; 1.85 A; A=331-527.
DR PDB; 7MZJ; X-ray; 2.40 A; A/B=331-527.
DR PDB; 7MZK; X-ray; 2.25 A; A/B=331-527.
DR PDB; 7MZL; X-ray; 3.70 A; A=331-527.
DR PDB; 7MZM; X-ray; 2.30 A; A=331-527.
DR PDB; 7MZN; X-ray; 3.10 A; A=331-527.
DR PDB; 7N0G; EM; 3.02 A; A/B/C=1-1208.
DR PDB; 7N0H; EM; 3.34 A; A/B/C=1-1208.
DR PDB; 7N1A; X-ray; 2.06 A; C/F=269-277.
DR PDB; 7N1B; X-ray; 2.81 A; C/F=1000-1008.
DR PDB; 7N1E; X-ray; 2.30 A; C=1000-1008.
DR PDB; 7N1F; X-ray; 2.39 A; C=269-277.
DR PDB; 7N1Q; EM; 3.44 A; A/B/C=1-1273.
DR PDB; 7N1T; EM; 3.44 A; A/B/C=1-1273.
DR PDB; 7N1U; EM; 3.14 A; A/B/C=1-1273.
DR PDB; 7N1V; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7N1W; EM; 3.33 A; A/B/C=1-1273.
DR PDB; 7N1X; EM; 4.00 A; A/B/C=1-1273.
DR PDB; 7N1Y; EM; 4.30 A; A/B/C=1-1273.
DR PDB; 7N3I; X-ray; 2.03 A; C=328-533.
DR PDB; 7N4I; X-ray; 2.28 A; C=331-527.
DR PDB; 7N4J; X-ray; 2.21 A; A=331-527.
DR PDB; 7N4L; X-ray; 3.60 A; A=331-527.
DR PDB; 7N4M; X-ray; 3.79 A; A=331-527.
DR PDB; 7N5H; EM; 3.24 A; A/B/C=1-1208.
DR PDB; 7N62; EM; 4.00 A; A=1-1273.
DR PDB; 7N64; EM; 4.20 A; A/B=1-1273.
DR PDB; 7N6D; X-ray; 2.30 A; C/G/K/O=269-277.
DR PDB; 7N6E; X-ray; 3.20 A; C/F=269-277.
DR PDB; 7N8H; EM; 2.30 A; A/F/K=1-1208.
DR PDB; 7N8I; EM; 3.00 A; A=1-1208.
DR PDB; 7N9A; EM; 3.50 A; E=334-528.
DR PDB; 7N9B; EM; 3.80 A; A/B/C=1-1208.
DR PDB; 7N9C; EM; 3.71 A; A/B/C=1-1208.
DR PDB; 7N9E; EM; 3.52 A; A/B/C=1-1208.
DR PDB; 7N9T; EM; 3.18 A; A/B/C=25-1147.
DR PDB; 7NAB; X-ray; 2.15 A; C/D=1140-1165.
DR PDB; 7ND3; EM; 3.70 A; A/B/C=1-1208.
DR PDB; 7ND4; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7ND5; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7ND6; EM; 7.30 A; A/B/C=1-1208.
DR PDB; 7ND7; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7ND8; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7ND9; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7NDA; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 7NDB; EM; 4.60 A; A/B/C=1-1208.
DR PDB; 7NDC; EM; 4.10 A; A/B/C=1-1208.
DR PDB; 7NDD; EM; 4.20 A; A/B/C=1-1208.
DR PDB; 7NEG; X-ray; 2.19 A; E=333-528.
DR PDB; 7NEH; X-ray; 1.77 A; E=333-528.
DR PDB; 7NKT; X-ray; 2.30 A; AAA=319-541.
DR PDB; 7NP1; X-ray; 2.80 A; A/B/C/D=319-541.
DR PDB; 7NS6; EM; 3.18 A; I/J/K/L/M/N=1-1208.
DR PDB; 7NT9; EM; 3.36 A; A/B/C=1-1208.
DR PDB; 7NTA; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7NTC; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7NX6; X-ray; 2.25 A; E=333-528.
DR PDB; 7NX7; X-ray; 2.30 A; E=333-528.
DR PDB; 7NX8; X-ray; 1.95 A; E=333-528.
DR PDB; 7NX9; X-ray; 2.40 A; E=333-528.
DR PDB; 7NXA; X-ray; 2.50 A; E=333-528.
DR PDB; 7NXB; X-ray; 2.67 A; E=333-528.
DR PDB; 7NXC; X-ray; 3.14 A; B=333-528.
DR PDB; 7NY5; EM; 3.70 A; A/E/G=1-1208.
DR PDB; 7OAN; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7OAO; X-ray; 1.50 A; EEE=330-532.
DR PDB; 7OAP; X-ray; 1.90 A; EEE=331-532.
DR PDB; 7OAQ; X-ray; 1.55 A; EEE=330-532.
DR PDB; 7OAU; X-ray; 1.65 A; AAA/EEE=330-532.
DR PDB; 7OAY; X-ray; 2.34 A; AAA/CCC/EEE/GGG/III/KKK=330-532.
DR PDB; 7OD3; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7ODL; EM; 3.03 A; A/B/C=1-1208.
DR PDB; 7OLZ; X-ray; 1.75 A; A=333-527.
DR PDB; 7OR9; X-ray; 2.34 A; E=333-528.
DR PDB; 7ORA; X-ray; 2.60 A; C/R=333-528.
DR PDB; 7ORB; X-ray; 2.50 A; R/X=333-528.
DR PDB; 7OWX; X-ray; 1.93 A; A/B/C/D=1177-1203.
DR PDB; 7P3D; X-ray; 1.67 A; C=269-277.
DR PDB; 7P3E; X-ray; 2.00 A; C/F=269-277.
DR PDB; 7P77; EM; 2.98 A; B/C/E=1-1208.
DR PDB; 7P78; EM; 3.32 A; A/C/E=1-1208.
DR PDB; 7P79; EM; 4.00 A; A/C/E=1-1208.
DR PDB; 7P7A; EM; 4.76 A; B/C/E=1-1208.
DR PDB; 7P7B; EM; 3.13 A; A/B/C=1-1208.
DR PDB; 7PQY; X-ray; 3.00 A; A/E=333-526.
DR PDB; 7PQZ; X-ray; 3.20 A; E=333-526.
DR PDB; 7PR0; X-ray; 2.92 A; A/D/E=333-526.
DR PDB; 7PRY; X-ray; 3.10 A; E/I=333-526.
DR PDB; 7PRZ; X-ray; 3.20 A; E=333-526.
DR PDB; 7PS0; X-ray; 2.92 A; A/E=333-526.
DR PDB; 7PS1; X-ray; 2.40 A; E=333-526.
DR PDB; 7PS2; X-ray; 2.99 A; G=333-526.
DR PDB; 7PS4; X-ray; 1.94 A; A/E=333-526.
DR PDB; 7PS5; X-ray; 3.14 A; E=333-526.
DR PDB; 7PS6; X-ray; 2.26 A; E=333-526.
DR PDB; 7PS7; X-ray; 3.90 A; E/R=333-526.
DR PDB; 7Q0A; EM; 4.80 A; A/B/C=1-1208.
DR PDB; 7Q0G; X-ray; 1.82 A; E=333-526.
DR PDB; 7Q0H; X-ray; 3.65 A; E=333-526.
DR PDB; 7Q0I; X-ray; 2.39 A; C/D=13-305.
DR PDB; 7Q1Z; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7Q6E; EM; 2.70 A; A/B/C=1-1205.
DR PDB; 7Q9F; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7Q9G; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 7Q9I; EM; 4.90 A; A/B/C=1-1208.
DR PDB; 7Q9J; EM; 4.00 A; A/B/C=1-1205.
DR PDB; 7Q9K; EM; 4.50 A; A/B/C=1-1208.
DR PDB; 7Q9M; EM; 3.70 A; A/B/C=1-1208.
DR PDB; 7Q9P; EM; 4.50 A; A/B/C=1-1205.
DR PDB; 7QO9; EM; 3.88 A; A/B=1-1208.
DR PDB; 7R0Z; EM; 3.50 A; A=1-1208.
DR PDB; 7R10; EM; 4.00 A; A=1-1208.
DR PDB; 7R11; EM; 3.50 A; A=1-1208.
DR PDB; 7R12; EM; 3.30 A; A=1-1208.
DR PDB; 7R13; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7R14; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7R16; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7R17; EM; 3.70 A; A/B/C=1-1208.
DR PDB; 7R18; EM; 3.00 A; A/B/C=1-1146.
DR PDB; 7R19; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 7R1A; EM; 3.90 A; A/B/C=1-1208.
DR PDB; 7R1B; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7R6W; X-ray; 1.83 A; R=328-531.
DR PDB; 7R6X; X-ray; 2.95 A; R=328-531.
DR PDB; 7R7N; EM; 3.95 A; E=1-1208.
DR PDB; 7R8L; X-ray; 2.60 A; E=334-528.
DR PDB; 7R8M; EM; 3.40 A; A/B/C=1-1213.
DR PDB; 7R8N; EM; 3.55 A; A/B/E=1-1213.
DR PDB; 7R8O; EM; 3.50 A; A/B/E=1-1213.
DR PDB; 7R95; NMR; -; A=919-965.
DR PDB; 7RA8; EM; 3.10 A; A/B/E=1-1208.
DR PDB; 7RAL; EM; -; B=1-1208.
DR PDB; 7RAQ; X-ray; 1.74 A; P=1149-1167.
DR PDB; 7RBY; X-ray; 2.82 A; A/C=329-538.
DR PDB; 7RKU; X-ray; 3.20 A; A/B/C/D=328-533.
DR PDB; 7RKV; EM; 3.45 A; A/B/C=1-1213.
DR PDB; 7RNJ; X-ray; 2.67 A; B=1146-1159.
DR PDB; 7RPV; X-ray; 3.54 A; E/F/G/H=320-537.
DR PDB; 7RR0; EM; 3.12 A; A=334-527.
DR PDB; 7RTD; X-ray; 2.05 A; C=269-277.
DR PDB; 7RTR; X-ray; 2.60 A; C=269-277.
DR PDB; 7RW2; EM; 3.50 A; A/B/C=1-1208.
DR PDB; 7RXD; EM; 3.60 A; R=334-526.
DR PDB; 7RZQ; EM; 2.09 A; A/B/C=917-988, D/E/F=1162-1201.
DR PDB; 7RZR; EM; 2.27 A; A/B/C=917-988, D/E/F=1162-1201.
DR PDB; 7RZS; EM; 2.52 A; A/B/C=917-988, D/E/F=1162-1201.
DR PDB; 7RZT; EM; 2.35 A; A/B/C=917-988, D/E/F=1162-1201.
DR PDB; 7RZU; EM; 2.30 A; A/B/C=917-988, D/E/F=1162-1201.
DR PDB; 7RZV; EM; 2.11 A; A/B/C=917-988, D/E/F=1157-1201.
DR PDB; 7S0B; X-ray; 2.90 A; E/F=319-533.
DR PDB; 7S0C; EM; 3.25 A; A/B/C=1-1213.
DR PDB; 7S0D; EM; 3.50 A; A/B/C=1-1213.
DR PDB; 7S0E; EM; 4.90 A; A=1-1213.
DR PDB; 7S4S; X-ray; 2.05 A; A=319-541.
DR PDB; 7S5P; X-ray; 2.86 A; A=319-541.
DR PDB; 7S5Q; X-ray; 2.88 A; A=319-541.
DR PDB; 7S5R; X-ray; 2.45 A; A=319-541.
DR PDB; 7SBK; EM; 3.44 A; A/B/C=1-1273.
DR PDB; 7SBL; EM; 3.44 A; A/B/C=1-1273.
DR PDB; 7SBO; EM; 3.44 A; A/B/C=1-1273.
DR PDB; 7SBP; EM; 3.44 A; A/B/C=1-1273.
DR PDB; 7SBQ; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7SBR; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7SBS; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7SBT; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 7SC1; EM; 3.20 A; A/B/C=1-1213.
DR PDB; 7SJS; X-ray; 1.61 A; C=1140-1164.
DR PDB; 7SN2; EM; 4.30 A; A=1-1208.
DR PDB; 7SN3; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7SO9; EM; 2.40 A; A/F/K=1-1208.
DR PDB; 7SOA; EM; 3.10 A; A=1-1208.
DR PDB; 7SOB; EM; 2.40 A; A/D/K=1-1208.
DR PDB; 7SOC; EM; 3.30 A; A=1-1208.
DR PDB; 7SOD; EM; 3.20 A; A=1-1208.
DR PDB; 7SOE; EM; 2.80 A; A/C/F=1-1208.
DR PDB; 7SOF; EM; 3.60 A; A=1-1208.
DR PDB; 7SPO; X-ray; 1.92 A; A/B=330-532.
DR PDB; 7SPP; X-ray; 1.96 A; A=319-535.
DR PDB; 7SXR; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7SXS; EM; 2.64 A; A/B/C=1-1208.
DR PDB; 7SXT; EM; 2.31 A; A/B/C=1-1208.
DR PDB; 7SXU; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7SXV; EM; 2.79 A; A/B/C=1-1208.
DR PDB; 7SXW; EM; 2.85 A; A/B/C=1-1208.
DR PDB; 7SXX; EM; 2.66 A; A/B/C=1-1208.
DR PDB; 7SXY; EM; 2.79 A; B=1-1208.
DR PDB; 7SXZ; EM; 2.61 A; A/B/C=1-1208.
DR PDB; 7SY0; EM; 3.00 A; B=1-1208.
DR PDB; 7SY1; EM; 2.83 A; A/B/C=1-1208.
DR PDB; 7SY2; EM; 3.11 A; B=1-1208.
DR PDB; 7SY3; EM; 2.95 A; A/B/C=1-1208.
DR PDB; 7SY4; EM; 3.35 A; B=1-1208.
DR PDB; 7SY5; EM; 2.59 A; A/B/C=1-1208.
DR PDB; 7SY6; EM; 2.81 A; B=1-1208.
DR PDB; 7SY7; EM; 2.81 A; A/B/C=1-1208.
DR PDB; 7SY8; EM; 3.14 A; B=1-1208.
DR PDB; 7T01; EM; 2.69 A; A=329-529.
DR PDB; 7T9J; EM; 2.79 A; A/B/C=1-1208.
DR PDB; 7T9K; EM; 2.45 A; A/B/C=1-1208.
DR PDB; 7T9L; EM; 2.66 A; A=1-1208.
DR PDB; 7TAS; EM; 3.20 A; E=1-1208.
DR PDB; 7TAT; EM; 3.20 A; A/B/C=1-1208.
DR PDB; 7TB8; EM; 2.83 A; A/B/C=14-1208.
DR PDB; 7TBF; EM; 3.10 A; A=332-527.
DR PDB; 7TC9; EM; 5.08 A; B=332-526.
DR PDB; 7TCA; EM; 3.85 A; A/B/C=14-1205.
DR PDB; 7TCC; EM; 3.86 A; A/B/C=14-1205.
DR PDB; 7TE1; X-ray; 3.50 A; D/E=319-529.
DR PDB; 7TEW; EM; 3.52 A; B=1-1206.
DR PDB; 7TEX; EM; 3.27 A; A/B/C=1-1206.
DR PDB; 7TEY; EM; 2.25 A; A/B/C=1-1206.
DR PDB; 7TEZ; EM; 3.27 A; B=1-1208.
DR PDB; 7TF0; EM; 3.02 A; A/B/C=1-1208.
DR PDB; 7TF1; EM; 3.57 A; A/B/C/D/E/F=1-1208.
DR PDB; 7TF2; EM; 3.62 A; A/B/C/D/E/F=1-1208.
DR PDB; 7TF3; EM; 2.25 A; A/B/C=1-1208.
DR PDB; 7TF4; EM; 3.01 A; A/B/C/D/E/F=1-1208.
DR PDB; 7TF5; EM; 3.16 A; A/B/C/D/E/F=1-1208.
DR PDB; 7TGW; EM; 3.00 A; A/B/C=14-1211.
DR PDB; 7TGX; EM; 3.20 A; A/B/C=14-1211.
DR PDB; 7TGY; EM; 3.00 A; A/B/C=14-1211.
DR PDB; 7THE; EM; 3.79 A; A=333-527.
DR PDB; 7THK; EM; 3.11 A; A/B/C=1-1205.
DR PDB; 7THT; EM; 3.42 A; C/S/V=27-1147.
DR PDB; 7TIK; EM; 2.40 A; A/B/C=917-988, D/E/F=1157-1201.
DR PDB; 7TLA; EM; 3.13 A; A/B/C=1-1208.
DR PDB; 7TLB; EM; 3.06 A; A/B/C=1-1208.
DR PDB; 7TLC; EM; 2.83 A; A/B/C=1-1208.
DR PDB; 7TLD; EM; 2.89 A; A/B/C=1-1208.
DR PDB; 7TN0; X-ray; 2.85 A; I/S=324-531.
DR PDB; 7TOU; EM; 3.24 A; A/B/C=1-1208.
DR PDB; 7TOV; EM; 3.16 A; A/B/C=1-1208.
DR PDB; 7TOW; X-ray; 2.15 A; D/E=808-833.
DR PDB; 7TOX; EM; 3.62 A; A/B/C=1-1208.
DR PDB; 7TOY; EM; 3.53 A; A/B/C=1-1208.
DR PDB; 7TOZ; EM; 4.07 A; A/B/C=1-1208.
DR PDB; 7TP0; EM; 3.57 A; A/B/C=1-1208.
DR PDB; 7TP1; EM; 3.81 A; A/B/C=1-1208.
DR PDB; 7TP2; EM; 3.72 A; A/B/C=1-1208.
DR PDB; 7TP3; X-ray; 2.33 A; Z=319-541.
DR PDB; 7TP4; X-ray; 1.95 A; Z=333-530.
DR PDB; 7TP7; EM; 3.48 A; A/B/C=1-1208.
DR PDB; 7TP8; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7TP9; EM; 3.48 A; A/B/C=1-1208.
DR PDB; 7TPA; EM; 3.60 A; A/B/C=1-1208.
DR PDB; 7TPC; EM; 3.91 A; A/B/C=1-1208.
DR PDB; 7TPE; EM; 4.00 A; A/B/C=1-1208.
DR PDB; 7TPF; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7TPH; EM; 3.58 A; A/B/C=1-1208.
DR PDB; 7TPL; EM; 3.87 A; A/B/C=1-1208.
DR PDB; 7V26; EM; 3.85 A; A/C/E=1-1208.
DR PDB; 7V2A; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7V76; EM; 3.20 A; A/B/C=1-1208.
DR PDB; 7V77; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 7V78; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7V79; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 7V7A; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7V7D; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7V7E; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 7V7F; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 7V7G; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7V7H; EM; 3.20 A; A/B/C/D/E/F=1-1208.
DR PDB; 7V7I; EM; 3.30 A; A/B/C/D/E/F=1-1208.
DR PDB; 7V7J; EM; 3.40 A; A/B/C/D/E/F=1-1208.
DR PDB; 7V7N; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 7V7O; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 7V7P; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 7V7Q; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7V7R; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 7V7S; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7V7T; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7V7U; EM; 3.00 A; A/B/C=1-1208.
DR PDB; 7V7V; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7V7Z; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7V80; EM; 3.90 A; A=1-1208.
DR PDB; 7V81; EM; 3.20 A; A/B/C=1-1208.
DR PDB; 7V82; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7V83; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7V84; EM; 3.00 A; A=1-1208.
DR PDB; 7V85; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 7V86; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7V87; EM; 3.30 A; A=1-1208.
DR PDB; 7V88; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 7V89; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7V8A; EM; 2.70 A; A/B/C=1-1208.
DR PDB; 7V8B; EM; 3.20 A; A=1-1208.
DR PDB; 7V8C; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7VMU; X-ray; 2.89 A; B=335-515.
DR PDB; 7VNB; X-ray; 2.27 A; B=319-531.
DR PDB; 7VNC; EM; 3.70 A; A/B/C=14-1208.
DR PDB; 7VND; EM; 3.60 A; A/B/C=14-1208.
DR PDB; 7VNE; EM; 3.50 A; A/B/C=14-1208.
DR PDB; 7VX1; EM; 3.50 A; A/B/C=1-1206.
DR PDB; 7VX4; EM; 3.90 A; E=1-1206.
DR PDB; 7VX5; EM; 3.80 A; E=1-1208.
DR PDB; 7VX9; EM; 4.00 A; A/B/D=14-1146.
DR PDB; 7VXA; EM; 3.90 A; A/B/D=1-1208.
DR PDB; 7VXB; EM; 3.90 A; A/B/D=1-1208.
DR PDB; 7VXC; EM; 3.90 A; A/B/D=1-1208.
DR PDB; 7VXD; EM; 4.00 A; A/B/D=1-1206.
DR PDB; 7VXE; EM; 3.20 A; A/B/C=1-1208.
DR PDB; 7VXF; EM; 3.60 A; A/B/D=1-1206.
DR PDB; 7VXI; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7VXK; EM; 3.70 A; A/B/D=1-1206.
DR PDB; 7VXM; EM; 3.60 A; A/B/D=1-1206.
DR PDB; 7VYR; X-ray; 2.20 A; C/R=319-541.
DR PDB; 7W92; EM; 3.10 A; A/B/C=1-1206.
DR PDB; 7W94; EM; 3.40 A; A/B/C=1-1206.
DR PDB; 7W98; EM; 3.60 A; A/B/C=1-1206.
DR PDB; 7W99; EM; 3.40 A; A/C/D=1-1206.
DR PDB; 7W9B; EM; 3.40 A; B/C/D=1-1206.
DR PDB; 7W9C; EM; 3.20 A; B/C/D=1-1206.
DR PDB; 7W9E; EM; 3.10 A; A/B/C=1-1206.
DR PDB; 7W9F; EM; 3.60 A; E=333-526.
DR PDB; 7W9I; EM; 3.40 A; E=333-526.
DR PDB; 7WBL; EM; 3.40 A; B=333-527.
DR PDB; 7WBP; X-ray; 3.00 A; B=319-541.
DR PDB; 7WBQ; X-ray; 3.34 A; B/D=319-541.
DR PDB; 7WCR; EM; 3.50 A; A=1-1206.
DR PDB; 7WCZ; EM; 3.50 A; A/B/C=1-1206.
DR PDB; 7WD0; EM; 3.30 A; A/B/C=1-1206.
DR PDB; 7WD7; EM; 3.50 A; A/B/C=1-1206.
DR PDB; 7WD8; EM; 4.30 A; A/B=1-1206.
DR PDB; 7WD9; EM; 3.70 A; A/B/C=1-1206.
DR PDB; 7WDF; EM; 3.90 A; A/B/C=1-1206.
DR PDB; 7WED; EM; 3.50 A; E=330-530.
DR PDB; 7WEV; EM; 3.60 A; A/B/C=1-1206.
DR PDB; 7WK2; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7WK3; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 7WK8; EM; 3.61 A; A/B=1-1208.
DR PDB; 7WK9; EM; 3.48 A; A/B/C=1-1208.
DR PDB; 7WKA; EM; 3.64 A; A/B/C=1-1208.
DR PDB; 7WLC; EM; 4.00 A; E=330-530.
DR PDB; 7WPH; X-ray; 2.89 A; A/B=319-591.
DR PDB; 7WUE; X-ray; 3.20 A; A/B=333-527.
DR PDB; 7WUH; EM; 4.70 A; A/C/E=14-1208.
DR PDB; 7WVN; EM; 3.40 A; A/B/C=1-1205.
DR PDB; 7WVO; EM; 3.41 A; A/B/C=1-1205.
DR PDB; 7WVP; EM; 3.70 A; B/C/D=1-1208.
DR PDB; 7WVQ; EM; 4.04 A; B/C/D=1-1208.
DR PDB; 7X08; EM; 2.70 A; A/B/C=1-1273.
DR PDB; 7X7D; X-ray; 2.92 A; A/D/E=334-527.
DR PDB; 7Z0Y; X-ray; 2.95 A; R=331-527.
DR PDB; 7Z1A; X-ray; 2.59 A; A/C=330-532.
DR PDB; 7Z1B; X-ray; 2.30 A; A/C=330-532.
DR PDB; 7Z1C; X-ray; 1.90 A; A/C=330-532.
DR PDB; 7Z1D; X-ray; 1.55 A; EEE=330-532.
DR PDB; 7Z1E; X-ray; 1.59 A; EEE=330-532.
DR PDBsum; 6LVN; -.
DR PDBsum; 6LXT; -.
DR PDBsum; 6LZG; -.
DR PDBsum; 6M0J; -.
DR PDBsum; 6M17; -.
DR PDBsum; 6M1V; -.
DR PDBsum; 6VSB; -.
DR PDBsum; 6VW1; -.
DR PDBsum; 6VXX; -.
DR PDBsum; 6VYB; -.
DR PDBsum; 6W41; -.
DR PDBsum; 6WPS; -.
DR PDBsum; 6WPT; -.
DR PDBsum; 6X29; -.
DR PDBsum; 6X2A; -.
DR PDBsum; 6X2B; -.
DR PDBsum; 6X2C; -.
DR PDBsum; 6X45; -.
DR PDBsum; 6X6P; -.
DR PDBsum; 6X79; -.
DR PDBsum; 6XC2; -.
DR PDBsum; 6XC3; -.
DR PDBsum; 6XC4; -.
DR PDBsum; 6XC7; -.
DR PDBsum; 6XCM; -.
DR PDBsum; 6XCN; -.
DR PDBsum; 6XDG; -.
DR PDBsum; 6XE1; -.
DR PDBsum; 6XEY; -.
DR PDBsum; 6XF5; -.
DR PDBsum; 6XF6; -.
DR PDBsum; 6XKL; -.
DR PDBsum; 6XKP; -.
DR PDBsum; 6XKQ; -.
DR PDBsum; 6XLU; -.
DR PDBsum; 6XM0; -.
DR PDBsum; 6XM3; -.
DR PDBsum; 6XM4; -.
DR PDBsum; 6XM5; -.
DR PDBsum; 6XR8; -.
DR PDBsum; 6XRA; -.
DR PDBsum; 6XS6; -.
DR PDBsum; 6YLA; -.
DR PDBsum; 6YM0; -.
DR PDBsum; 6YOR; -.
DR PDBsum; 6YZ5; -.
DR PDBsum; 6YZ7; -.
DR PDBsum; 6Z2M; -.
DR PDBsum; 6Z43; -.
DR PDBsum; 6Z97; -.
DR PDBsum; 6ZB4; -.
DR PDBsum; 6ZB5; -.
DR PDBsum; 6ZBP; -.
DR PDBsum; 6ZCZ; -.
DR PDBsum; 6ZDG; -.
DR PDBsum; 6ZDH; -.
DR PDBsum; 6ZER; -.
DR PDBsum; 6ZFO; -.
DR PDBsum; 6ZGE; -.
DR PDBsum; 6ZGG; -.
DR PDBsum; 6ZGI; -.
DR PDBsum; 6ZH9; -.
DR PDBsum; 6ZHD; -.
DR PDBsum; 6ZLR; -.
DR PDBsum; 6ZOW; -.
DR PDBsum; 6ZOX; -.
DR PDBsum; 6ZOY; -.
DR PDBsum; 6ZOZ; -.
DR PDBsum; 6ZP0; -.
DR PDBsum; 6ZP1; -.
DR PDBsum; 6ZP2; -.
DR PDBsum; 6ZP5; -.
DR PDBsum; 6ZP7; -.
DR PDBsum; 6ZWV; -.
DR PDBsum; 6ZXN; -.
DR PDBsum; 7A25; -.
DR PDBsum; 7A29; -.
DR PDBsum; 7A4N; -.
DR PDBsum; 7A5R; -.
DR PDBsum; 7A5S; -.
DR PDBsum; 7A91; -.
DR PDBsum; 7A92; -.
DR PDBsum; 7A93; -.
DR PDBsum; 7A94; -.
DR PDBsum; 7A95; -.
DR PDBsum; 7A96; -.
DR PDBsum; 7A97; -.
DR PDBsum; 7A98; -.
DR PDBsum; 7AD1; -.
DR PDBsum; 7AKD; -.
DR PDBsum; 7B14; -.
DR PDBsum; 7B17; -.
DR PDBsum; 7B18; -.
DR PDBsum; 7B3O; -.
DR PDBsum; 7B62; -.
DR PDBsum; 7BEH; -.
DR PDBsum; 7BEI; -.
DR PDBsum; 7BEJ; -.
DR PDBsum; 7BEK; -.
DR PDBsum; 7BEL; -.
DR PDBsum; 7BEM; -.
DR PDBsum; 7BEN; -.
DR PDBsum; 7BEO; -.
DR PDBsum; 7BEP; -.
DR PDBsum; 7BH9; -.
DR PDBsum; 7BNM; -.
DR PDBsum; 7BNN; -.
DR PDBsum; 7BNO; -.
DR PDBsum; 7BWJ; -.
DR PDBsum; 7BYR; -.
DR PDBsum; 7BZ5; -.
DR PDBsum; 7C01; -.
DR PDBsum; 7C2L; -.
DR PDBsum; 7C53; -.
DR PDBsum; 7C8D; -.
DR PDBsum; 7C8J; -.
DR PDBsum; 7C8V; -.
DR PDBsum; 7C8W; -.
DR PDBsum; 7CAB; -.
DR PDBsum; 7CAC; -.
DR PDBsum; 7CAH; -.
DR PDBsum; 7CAI; -.
DR PDBsum; 7CAK; -.
DR PDBsum; 7CAN; -.
DR PDBsum; 7CDI; -.
DR PDBsum; 7CDJ; -.
DR PDBsum; 7CH4; -.
DR PDBsum; 7CH5; -.
DR PDBsum; 7CHB; -.
DR PDBsum; 7CHC; -.
DR PDBsum; 7CHE; -.
DR PDBsum; 7CHF; -.
DR PDBsum; 7CHH; -.
DR PDBsum; 7CHO; -.
DR PDBsum; 7CHP; -.
DR PDBsum; 7CHS; -.
DR PDBsum; 7CJF; -.
DR PDBsum; 7CM4; -.
DR PDBsum; 7CN4; -.
DR PDBsum; 7CN9; -.
DR PDBsum; 7CT5; -.
DR PDBsum; 7CWL; -.
DR PDBsum; 7CWM; -.
DR PDBsum; 7CWN; -.
DR PDBsum; 7CWO; -.
DR PDBsum; 7CWS; -.
DR PDBsum; 7CWT; -.
DR PDBsum; 7CWU; -.
DR PDBsum; 7CYH; -.
DR PDBsum; 7CYP; -.
DR PDBsum; 7CYV; -.
DR PDBsum; 7CZP; -.
DR PDBsum; 7CZQ; -.
DR PDBsum; 7CZR; -.
DR PDBsum; 7CZS; -.
DR PDBsum; 7CZT; -.
DR PDBsum; 7CZU; -.
DR PDBsum; 7CZV; -.
DR PDBsum; 7CZW; -.
DR PDBsum; 7CZX; -.
DR PDBsum; 7CZY; -.
DR PDBsum; 7CZZ; -.
DR PDBsum; 7D00; -.
DR PDBsum; 7D03; -.
DR PDBsum; 7D0B; -.
DR PDBsum; 7D0C; -.
DR PDBsum; 7D0D; -.
DR PDBsum; 7D2Z; -.
DR PDBsum; 7D30; -.
DR PDBsum; 7D4G; -.
DR PDBsum; 7D6I; -.
DR PDBsum; 7DCC; -.
DR PDBsum; 7DCX; -.
DR PDBsum; 7DD2; -.
DR PDBsum; 7DD8; -.
DR PDBsum; 7DDD; -.
DR PDBsum; 7DDN; -.
DR PDBsum; 7DEO; -.
DR PDBsum; 7DET; -.
DR PDBsum; 7DEU; -.
DR PDBsum; 7DF3; -.
DR PDBsum; 7DF4; -.
DR PDBsum; 7DHX; -.
DR PDBsum; 7DJZ; -.
DR PDBsum; 7DK0; -.
DR PDBsum; 7DK2; -.
DR PDBsum; 7DK3; -.
DR PDBsum; 7DK4; -.
DR PDBsum; 7DK5; -.
DR PDBsum; 7DK6; -.
DR PDBsum; 7DK7; -.
DR PDBsum; 7DMU; -.
DR PDBsum; 7DPM; -.
DR PDBsum; 7DQA; -.
DR PDBsum; 7DWX; -.
DR PDBsum; 7DWY; -.
DR PDBsum; 7DWZ; -.
DR PDBsum; 7DX0; -.
DR PDBsum; 7DX1; -.
DR PDBsum; 7DX2; -.
DR PDBsum; 7DX3; -.
DR PDBsum; 7DX4; -.
DR PDBsum; 7DX5; -.
DR PDBsum; 7DX6; -.
DR PDBsum; 7DX7; -.
DR PDBsum; 7DX8; -.
DR PDBsum; 7DX9; -.
DR PDBsum; 7DZW; -.
DR PDBsum; 7DZX; -.
DR PDBsum; 7DZY; -.
DR PDBsum; 7E23; -.
DR PDBsum; 7E39; -.
DR PDBsum; 7E3B; -.
DR PDBsum; 7E3C; -.
DR PDBsum; 7E3J; -.
DR PDBsum; 7E3K; -.
DR PDBsum; 7E3L; -.
DR PDBsum; 7E3O; -.
DR PDBsum; 7E5O; -.
DR PDBsum; 7E5R; -.
DR PDBsum; 7E5S; -.
DR PDBsum; 7E5Y; -.
DR PDBsum; 7E7B; -.
DR PDBsum; 7E7D; -.
DR PDBsum; 7E7X; -.
DR PDBsum; 7E7Y; -.
DR PDBsum; 7E86; -.
DR PDBsum; 7E88; -.
DR PDBsum; 7E8C; -.
DR PDBsum; 7E8F; -.
DR PDBsum; 7E8M; -.
DR PDBsum; 7E9N; -.
DR PDBsum; 7E9O; -.
DR PDBsum; 7E9P; -.
DR PDBsum; 7E9Q; -.
DR PDBsum; 7E9T; -.
DR PDBsum; 7EAM; -.
DR PDBsum; 7EAN; -.
DR PDBsum; 7EAZ; -.
DR PDBsum; 7EB0; -.
DR PDBsum; 7EB3; -.
DR PDBsum; 7EB4; -.
DR PDBsum; 7EB5; -.
DR PDBsum; 7EDF; -.
DR PDBsum; 7EDG; -.
DR PDBsum; 7EDH; -.
DR PDBsum; 7EDI; -.
DR PDBsum; 7EDJ; -.
DR PDBsum; 7EFP; -.
DR PDBsum; 7EFR; -.
DR PDBsum; 7EH5; -.
DR PDBsum; 7EJ4; -.
DR PDBsum; 7EJ5; -.
DR PDBsum; 7EJY; -.
DR PDBsum; 7EJZ; -.
DR PDBsum; 7EK0; -.
DR PDBsum; 7EK6; -.
DR PDBsum; 7EKC; -.
DR PDBsum; 7EKE; -.
DR PDBsum; 7EKF; -.
DR PDBsum; 7EKG; -.
DR PDBsum; 7EKH; -.
DR PDBsum; 7ENF; -.
DR PDBsum; 7ENG; -.
DR PDBsum; 7EU2; -.
DR PDBsum; 7EY0; -.
DR PDBsum; 7EY4; -.
DR PDBsum; 7EY5; -.
DR PDBsum; 7EYA; -.
DR PDBsum; 7EZV; -.
DR PDBsum; 7F46; -.
DR PDBsum; 7F4W; -.
DR PDBsum; 7F62; -.
DR PDBsum; 7F63; -.
DR PDBsum; 7F7E; -.
DR PDBsum; 7FAE; -.
DR PDBsum; 7FAF; -.
DR PDBsum; 7FCD; -.
DR PDBsum; 7FCE; -.
DR PDBsum; 7FDG; -.
DR PDBsum; 7FDH; -.
DR PDBsum; 7FDI; -.
DR PDBsum; 7FDK; -.
DR PDBsum; 7FEM; -.
DR PDBsum; 7FET; -.
DR PDBsum; 7FG2; -.
DR PDBsum; 7FG3; -.
DR PDBsum; 7FG7; -.
DR PDBsum; 7FJO; -.
DR PDBsum; 7JJC; -.
DR PDBsum; 7JJI; -.
DR PDBsum; 7JJJ; -.
DR PDBsum; 7JMO; -.
DR PDBsum; 7JMP; -.
DR PDBsum; 7JMW; -.
DR PDBsum; 7JV2; -.
DR PDBsum; 7JV4; -.
DR PDBsum; 7JV6; -.
DR PDBsum; 7JVA; -.
DR PDBsum; 7JVB; -.
DR PDBsum; 7JVC; -.
DR PDBsum; 7JW0; -.
DR PDBsum; 7JWB; -.
DR PDBsum; 7JWY; -.
DR PDBsum; 7JX3; -.
DR PDBsum; 7JZL; -.
DR PDBsum; 7JZM; -.
DR PDBsum; 7JZN; -.
DR PDBsum; 7JZU; -.
DR PDBsum; 7K43; -.
DR PDBsum; 7K45; -.
DR PDBsum; 7K4N; -.
DR PDBsum; 7K8M; -.
DR PDBsum; 7K8S; -.
DR PDBsum; 7K8T; -.
DR PDBsum; 7K8U; -.
DR PDBsum; 7K8V; -.
DR PDBsum; 7K8W; -.
DR PDBsum; 7K8X; -.
DR PDBsum; 7K8Y; -.
DR PDBsum; 7K8Z; -.
DR PDBsum; 7K90; -.
DR PDBsum; 7K9H; -.
DR PDBsum; 7K9I; -.
DR PDBsum; 7K9J; -.
DR PDBsum; 7K9K; -.
DR PDBsum; 7K9Z; -.
DR PDBsum; 7KDG; -.
DR PDBsum; 7KDH; -.
DR PDBsum; 7KDI; -.
DR PDBsum; 7KDJ; -.
DR PDBsum; 7KDK; -.
DR PDBsum; 7KDL; -.
DR PDBsum; 7KE4; -.
DR PDBsum; 7KE6; -.
DR PDBsum; 7KE7; -.
DR PDBsum; 7KE8; -.
DR PDBsum; 7KE9; -.
DR PDBsum; 7KEA; -.
DR PDBsum; 7KEB; -.
DR PDBsum; 7KEC; -.
DR PDBsum; 7KFV; -.
DR PDBsum; 7KFW; -.
DR PDBsum; 7KFX; -.
DR PDBsum; 7KFY; -.
DR PDBsum; 7KGJ; -.
DR PDBsum; 7KGK; -.
DR PDBsum; 7KJ2; -.
DR PDBsum; 7KJ3; -.
DR PDBsum; 7KJ4; -.
DR PDBsum; 7KJ5; -.
DR PDBsum; 7KKK; -.
DR PDBsum; 7KKL; -.
DR PDBsum; 7KL9; -.
DR PDBsum; 7KLG; -.
DR PDBsum; 7KLH; -.
DR PDBsum; 7KLW; -.
DR PDBsum; 7KM5; -.
DR PDBsum; 7KMB; -.
DR PDBsum; 7KMG; -.
DR PDBsum; 7KMH; -.
DR PDBsum; 7KMI; -.
DR PDBsum; 7KMK; -.
DR PDBsum; 7KML; -.
DR PDBsum; 7KMS; -.
DR PDBsum; 7KMZ; -.
DR PDBsum; 7KN3; -.
DR PDBsum; 7KN4; -.
DR PDBsum; 7KN5; -.
DR PDBsum; 7KN6; -.
DR PDBsum; 7KN7; -.
DR PDBsum; 7KNB; -.
DR PDBsum; 7KNE; -.
DR PDBsum; 7KNH; -.
DR PDBsum; 7KNI; -.
DR PDBsum; 7KQB; -.
DR PDBsum; 7KQE; -.
DR PDBsum; 7KRQ; -.
DR PDBsum; 7KRR; -.
DR PDBsum; 7KRS; -.
DR PDBsum; 7KS9; -.
DR PDBsum; 7KSG; -.
DR PDBsum; 7KXJ; -.
DR PDBsum; 7KXK; -.
DR PDBsum; 7KZB; -.
DR PDBsum; 7L02; -.
DR PDBsum; 7L06; -.
DR PDBsum; 7L09; -.
DR PDBsum; 7L0N; -.
DR PDBsum; 7L2C; -.
DR PDBsum; 7L2D; -.
DR PDBsum; 7L2E; -.
DR PDBsum; 7L2F; -.
DR PDBsum; 7L3N; -.
DR PDBsum; 7L4Z; -.
DR PDBsum; 7L56; -.
DR PDBsum; 7L57; -.
DR PDBsum; 7L58; -.
DR PDBsum; 7L5B; -.
DR PDBsum; 7L7D; -.
DR PDBsum; 7L7E; -.
DR PDBsum; 7L7F; -.
DR PDBsum; 7L7K; -.
DR PDBsum; 7LAA; -.
DR PDBsum; 7LAB; -.
DR PDBsum; 7LC8; -.
DR PDBsum; 7LCN; -.
DR PDBsum; 7LD1; -.
DR PDBsum; 7LDJ; -.
DR PDBsum; 7LJR; -.
DR PDBsum; 7LM8; -.
DR PDBsum; 7LO4; -.
DR PDBsum; 7LOP; -.
DR PDBsum; 7LQ7; -.
DR PDBsum; 7LQV; -.
DR PDBsum; 7LQW; -.
DR PDBsum; 7LRS; -.
DR PDBsum; 7LRT; -.
DR PDBsum; 7LS9; -.
DR PDBsum; 7LSS; -.
DR PDBsum; 7LWI; -.
DR PDBsum; 7LWJ; -.
DR PDBsum; 7LWK; -.
DR PDBsum; 7LWL; -.
DR PDBsum; 7LWM; -.
DR PDBsum; 7LWN; -.
DR PDBsum; 7LWO; -.
DR PDBsum; 7LWP; -.
DR PDBsum; 7LWQ; -.
DR PDBsum; 7LWS; -.
DR PDBsum; 7LWT; -.
DR PDBsum; 7LWU; -.
DR PDBsum; 7LWV; -.
DR PDBsum; 7LWW; -.
DR PDBsum; 7LX5; -.
DR PDBsum; 7LXW; -.
DR PDBsum; 7LXX; -.
DR PDBsum; 7LXY; -.
DR PDBsum; 7LXZ; -.
DR PDBsum; 7LY0; -.
DR PDBsum; 7LY2; -.
DR PDBsum; 7LY3; -.
DR PDBsum; 7LYK; -.
DR PDBsum; 7LYL; -.
DR PDBsum; 7LYM; -.
DR PDBsum; 7LYN; -.
DR PDBsum; 7LYO; -.
DR PDBsum; 7LYP; -.
DR PDBsum; 7LYQ; -.
DR PDBsum; 7M0J; -.
DR PDBsum; 7M3I; -.
DR PDBsum; 7M42; -.
DR PDBsum; 7M53; -.
DR PDBsum; 7M6D; -.
DR PDBsum; 7M6E; -.
DR PDBsum; 7M6F; -.
DR PDBsum; 7M6G; -.
DR PDBsum; 7M6H; -.
DR PDBsum; 7M6I; -.
DR PDBsum; 7M71; -.
DR PDBsum; 7M7B; -.
DR PDBsum; 7M7W; -.
DR PDBsum; 7M8J; -.
DR PDBsum; 7M8K; -.
DR PDBsum; 7M8S; -.
DR PDBsum; 7M8T; -.
DR PDBsum; 7M8U; -.
DR PDBsum; 7MDW; -.
DR PDBsum; 7ME7; -.
DR PDBsum; 7MEJ; -.
DR PDBsum; 7MF1; -.
DR PDBsum; 7MFU; -.
DR PDBsum; 7MJG; -.
DR PDBsum; 7MJH; -.
DR PDBsum; 7MJI; -.
DR PDBsum; 7MJJ; -.
DR PDBsum; 7MJK; -.
DR PDBsum; 7MJL; -.
DR PDBsum; 7MJM; -.
DR PDBsum; 7MJN; -.
DR PDBsum; 7MKB; -.
DR PDBsum; 7MKL; -.
DR PDBsum; 7MKM; -.
DR PDBsum; 7MLZ; -.
DR PDBsum; 7MM0; -.
DR PDBsum; 7MMO; -.
DR PDBsum; 7MSQ; -.
DR PDBsum; 7MTC; -.
DR PDBsum; 7MTD; -.
DR PDBsum; 7MTE; -.
DR PDBsum; 7MW2; -.
DR PDBsum; 7MW3; -.
DR PDBsum; 7MW4; -.
DR PDBsum; 7MW5; -.
DR PDBsum; 7MW6; -.
DR PDBsum; 7MY2; -.
DR PDBsum; 7MY3; -.
DR PDBsum; 7MY8; -.
DR PDBsum; 7MZF; -.
DR PDBsum; 7MZG; -.
DR PDBsum; 7MZH; -.
DR PDBsum; 7MZI; -.
DR PDBsum; 7MZJ; -.
DR PDBsum; 7MZK; -.
DR PDBsum; 7MZL; -.
DR PDBsum; 7MZM; -.
DR PDBsum; 7MZN; -.
DR PDBsum; 7N0G; -.
DR PDBsum; 7N0H; -.
DR PDBsum; 7N1A; -.
DR PDBsum; 7N1B; -.
DR PDBsum; 7N1E; -.
DR PDBsum; 7N1F; -.
DR PDBsum; 7N1Q; -.
DR PDBsum; 7N1T; -.
DR PDBsum; 7N1U; -.
DR PDBsum; 7N1V; -.
DR PDBsum; 7N1W; -.
DR PDBsum; 7N1X; -.
DR PDBsum; 7N1Y; -.
DR PDBsum; 7N3I; -.
DR PDBsum; 7N4I; -.
DR PDBsum; 7N4J; -.
DR PDBsum; 7N4L; -.
DR PDBsum; 7N4M; -.
DR PDBsum; 7N5H; -.
DR PDBsum; 7N62; -.
DR PDBsum; 7N64; -.
DR PDBsum; 7N6D; -.
DR PDBsum; 7N6E; -.
DR PDBsum; 7N8H; -.
DR PDBsum; 7N8I; -.
DR PDBsum; 7N9A; -.
DR PDBsum; 7N9B; -.
DR PDBsum; 7N9C; -.
DR PDBsum; 7N9E; -.
DR PDBsum; 7N9T; -.
DR PDBsum; 7NAB; -.
DR PDBsum; 7ND3; -.
DR PDBsum; 7ND4; -.
DR PDBsum; 7ND5; -.
DR PDBsum; 7ND6; -.
DR PDBsum; 7ND7; -.
DR PDBsum; 7ND8; -.
DR PDBsum; 7ND9; -.
DR PDBsum; 7NDA; -.
DR PDBsum; 7NDB; -.
DR PDBsum; 7NDC; -.
DR PDBsum; 7NDD; -.
DR PDBsum; 7NEG; -.
DR PDBsum; 7NEH; -.
DR PDBsum; 7NKT; -.
DR PDBsum; 7NP1; -.
DR PDBsum; 7NS6; -.
DR PDBsum; 7NT9; -.
DR PDBsum; 7NTA; -.
DR PDBsum; 7NTC; -.
DR PDBsum; 7NX6; -.
DR PDBsum; 7NX7; -.
DR PDBsum; 7NX8; -.
DR PDBsum; 7NX9; -.
DR PDBsum; 7NXA; -.
DR PDBsum; 7NXB; -.
DR PDBsum; 7NXC; -.
DR PDBsum; 7NY5; -.
DR PDBsum; 7OAN; -.
DR PDBsum; 7OAO; -.
DR PDBsum; 7OAP; -.
DR PDBsum; 7OAQ; -.
DR PDBsum; 7OAU; -.
DR PDBsum; 7OAY; -.
DR PDBsum; 7OD3; -.
DR PDBsum; 7ODL; -.
DR PDBsum; 7OLZ; -.
DR PDBsum; 7OR9; -.
DR PDBsum; 7ORA; -.
DR PDBsum; 7ORB; -.
DR PDBsum; 7OWX; -.
DR PDBsum; 7P3D; -.
DR PDBsum; 7P3E; -.
DR PDBsum; 7P77; -.
DR PDBsum; 7P78; -.
DR PDBsum; 7P79; -.
DR PDBsum; 7P7A; -.
DR PDBsum; 7P7B; -.
DR PDBsum; 7PQY; -.
DR PDBsum; 7PQZ; -.
DR PDBsum; 7PR0; -.
DR PDBsum; 7PRY; -.
DR PDBsum; 7PRZ; -.
DR PDBsum; 7PS0; -.
DR PDBsum; 7PS1; -.
DR PDBsum; 7PS2; -.
DR PDBsum; 7PS4; -.
DR PDBsum; 7PS5; -.
DR PDBsum; 7PS6; -.
DR PDBsum; 7PS7; -.
DR PDBsum; 7Q0A; -.
DR PDBsum; 7Q0G; -.
DR PDBsum; 7Q0H; -.
DR PDBsum; 7Q0I; -.
DR PDBsum; 7Q1Z; -.
DR PDBsum; 7Q6E; -.
DR PDBsum; 7Q9F; -.
DR PDBsum; 7Q9G; -.
DR PDBsum; 7Q9I; -.
DR PDBsum; 7Q9J; -.
DR PDBsum; 7Q9K; -.
DR PDBsum; 7Q9M; -.
DR PDBsum; 7Q9P; -.
DR PDBsum; 7QO9; -.
DR PDBsum; 7R0Z; -.
DR PDBsum; 7R10; -.
DR PDBsum; 7R11; -.
DR PDBsum; 7R12; -.
DR PDBsum; 7R13; -.
DR PDBsum; 7R14; -.
DR PDBsum; 7R16; -.
DR PDBsum; 7R17; -.
DR PDBsum; 7R18; -.
DR PDBsum; 7R19; -.
DR PDBsum; 7R1A; -.
DR PDBsum; 7R1B; -.
DR PDBsum; 7R6W; -.
DR PDBsum; 7R6X; -.
DR PDBsum; 7R7N; -.
DR PDBsum; 7R8L; -.
DR PDBsum; 7R8M; -.
DR PDBsum; 7R8N; -.
DR PDBsum; 7R8O; -.
DR PDBsum; 7R95; -.
DR PDBsum; 7RA8; -.
DR PDBsum; 7RAL; -.
DR PDBsum; 7RAQ; -.
DR PDBsum; 7RBY; -.
DR PDBsum; 7RKU; -.
DR PDBsum; 7RKV; -.
DR PDBsum; 7RNJ; -.
DR PDBsum; 7RPV; -.
DR PDBsum; 7RR0; -.
DR PDBsum; 7RTD; -.
DR PDBsum; 7RTR; -.
DR PDBsum; 7RW2; -.
DR PDBsum; 7RXD; -.
DR PDBsum; 7RZQ; -.
DR PDBsum; 7RZR; -.
DR PDBsum; 7RZS; -.
DR PDBsum; 7RZT; -.
DR PDBsum; 7RZU; -.
DR PDBsum; 7RZV; -.
DR PDBsum; 7S0B; -.
DR PDBsum; 7S0C; -.
DR PDBsum; 7S0D; -.
DR PDBsum; 7S0E; -.
DR PDBsum; 7S4S; -.
DR PDBsum; 7S5P; -.
DR PDBsum; 7S5Q; -.
DR PDBsum; 7S5R; -.
DR PDBsum; 7SBK; -.
DR PDBsum; 7SBL; -.
DR PDBsum; 7SBO; -.
DR PDBsum; 7SBP; -.
DR PDBsum; 7SBQ; -.
DR PDBsum; 7SBR; -.
DR PDBsum; 7SBS; -.
DR PDBsum; 7SBT; -.
DR PDBsum; 7SC1; -.
DR PDBsum; 7SJS; -.
DR PDBsum; 7SN2; -.
DR PDBsum; 7SN3; -.
DR PDBsum; 7SO9; -.
DR PDBsum; 7SOA; -.
DR PDBsum; 7SOB; -.
DR PDBsum; 7SOC; -.
DR PDBsum; 7SOD; -.
DR PDBsum; 7SOE; -.
DR PDBsum; 7SOF; -.
DR PDBsum; 7SPO; -.
DR PDBsum; 7SPP; -.
DR PDBsum; 7SXR; -.
DR PDBsum; 7SXS; -.
DR PDBsum; 7SXT; -.
DR PDBsum; 7SXU; -.
DR PDBsum; 7SXV; -.
DR PDBsum; 7SXW; -.
DR PDBsum; 7SXX; -.
DR PDBsum; 7SXY; -.
DR PDBsum; 7SXZ; -.
DR PDBsum; 7SY0; -.
DR PDBsum; 7SY1; -.
DR PDBsum; 7SY2; -.
DR PDBsum; 7SY3; -.
DR PDBsum; 7SY4; -.
DR PDBsum; 7SY5; -.
DR PDBsum; 7SY6; -.
DR PDBsum; 7SY7; -.
DR PDBsum; 7SY8; -.
DR PDBsum; 7T01; -.
DR PDBsum; 7T9J; -.
DR PDBsum; 7T9K; -.
DR PDBsum; 7T9L; -.
DR PDBsum; 7TAS; -.
DR PDBsum; 7TAT; -.
DR PDBsum; 7TB8; -.
DR PDBsum; 7TBF; -.
DR PDBsum; 7TC9; -.
DR PDBsum; 7TCA; -.
DR PDBsum; 7TCC; -.
DR PDBsum; 7TE1; -.
DR PDBsum; 7TEW; -.
DR PDBsum; 7TEX; -.
DR PDBsum; 7TEY; -.
DR PDBsum; 7TEZ; -.
DR PDBsum; 7TF0; -.
DR PDBsum; 7TF1; -.
DR PDBsum; 7TF2; -.
DR PDBsum; 7TF3; -.
DR PDBsum; 7TF4; -.
DR PDBsum; 7TF5; -.
DR PDBsum; 7TGW; -.
DR PDBsum; 7TGX; -.
DR PDBsum; 7TGY; -.
DR PDBsum; 7THE; -.
DR PDBsum; 7THK; -.
DR PDBsum; 7THT; -.
DR PDBsum; 7TIK; -.
DR PDBsum; 7TLA; -.
DR PDBsum; 7TLB; -.
DR PDBsum; 7TLC; -.
DR PDBsum; 7TLD; -.
DR PDBsum; 7TN0; -.
DR PDBsum; 7TOU; -.
DR PDBsum; 7TOV; -.
DR PDBsum; 7TOW; -.
DR PDBsum; 7TOX; -.
DR PDBsum; 7TOY; -.
DR PDBsum; 7TOZ; -.
DR PDBsum; 7TP0; -.
DR PDBsum; 7TP1; -.
DR PDBsum; 7TP2; -.
DR PDBsum; 7TP3; -.
DR PDBsum; 7TP4; -.
DR PDBsum; 7TP7; -.
DR PDBsum; 7TP8; -.
DR PDBsum; 7TP9; -.
DR PDBsum; 7TPA; -.
DR PDBsum; 7TPC; -.
DR PDBsum; 7TPE; -.
DR PDBsum; 7TPF; -.
DR PDBsum; 7TPH; -.
DR PDBsum; 7TPL; -.
DR PDBsum; 7V26; -.
DR PDBsum; 7V2A; -.
DR PDBsum; 7V76; -.
DR PDBsum; 7V77; -.
DR PDBsum; 7V78; -.
DR PDBsum; 7V79; -.
DR PDBsum; 7V7A; -.
DR PDBsum; 7V7D; -.
DR PDBsum; 7V7E; -.
DR PDBsum; 7V7F; -.
DR PDBsum; 7V7G; -.
DR PDBsum; 7V7H; -.
DR PDBsum; 7V7I; -.
DR PDBsum; 7V7J; -.
DR PDBsum; 7V7N; -.
DR PDBsum; 7V7O; -.
DR PDBsum; 7V7P; -.
DR PDBsum; 7V7Q; -.
DR PDBsum; 7V7R; -.
DR PDBsum; 7V7S; -.
DR PDBsum; 7V7T; -.
DR PDBsum; 7V7U; -.
DR PDBsum; 7V7V; -.
DR PDBsum; 7V7Z; -.
DR PDBsum; 7V80; -.
DR PDBsum; 7V81; -.
DR PDBsum; 7V82; -.
DR PDBsum; 7V83; -.
DR PDBsum; 7V84; -.
DR PDBsum; 7V85; -.
DR PDBsum; 7V86; -.
DR PDBsum; 7V87; -.
DR PDBsum; 7V88; -.
DR PDBsum; 7V89; -.
DR PDBsum; 7V8A; -.
DR PDBsum; 7V8B; -.
DR PDBsum; 7V8C; -.
DR PDBsum; 7VMU; -.
DR PDBsum; 7VNB; -.
DR PDBsum; 7VNC; -.
DR PDBsum; 7VND; -.
DR PDBsum; 7VNE; -.
DR PDBsum; 7VX1; -.
DR PDBsum; 7VX4; -.
DR PDBsum; 7VX5; -.
DR PDBsum; 7VX9; -.
DR PDBsum; 7VXA; -.
DR PDBsum; 7VXB; -.
DR PDBsum; 7VXC; -.
DR PDBsum; 7VXD; -.
DR PDBsum; 7VXE; -.
DR PDBsum; 7VXF; -.
DR PDBsum; 7VXI; -.
DR PDBsum; 7VXK; -.
DR PDBsum; 7VXM; -.
DR PDBsum; 7VYR; -.
DR PDBsum; 7W92; -.
DR PDBsum; 7W94; -.
DR PDBsum; 7W98; -.
DR PDBsum; 7W99; -.
DR PDBsum; 7W9B; -.
DR PDBsum; 7W9C; -.
DR PDBsum; 7W9E; -.
DR PDBsum; 7W9F; -.
DR PDBsum; 7W9I; -.
DR PDBsum; 7WBL; -.
DR PDBsum; 7WBP; -.
DR PDBsum; 7WBQ; -.
DR PDBsum; 7WCR; -.
DR PDBsum; 7WCZ; -.
DR PDBsum; 7WD0; -.
DR PDBsum; 7WD7; -.
DR PDBsum; 7WD8; -.
DR PDBsum; 7WD9; -.
DR PDBsum; 7WDF; -.
DR PDBsum; 7WED; -.
DR PDBsum; 7WEV; -.
DR PDBsum; 7WK2; -.
DR PDBsum; 7WK3; -.
DR PDBsum; 7WK8; -.
DR PDBsum; 7WK9; -.
DR PDBsum; 7WKA; -.
DR PDBsum; 7WLC; -.
DR PDBsum; 7WPH; -.
DR PDBsum; 7WUE; -.
DR PDBsum; 7WUH; -.
DR PDBsum; 7WVN; -.
DR PDBsum; 7WVO; -.
DR PDBsum; 7WVP; -.
DR PDBsum; 7WVQ; -.
DR PDBsum; 7X08; -.
DR PDBsum; 7X7D; -.
DR PDBsum; 7Z0Y; -.
DR PDBsum; 7Z1A; -.
DR PDBsum; 7Z1B; -.
DR PDBsum; 7Z1C; -.
DR PDBsum; 7Z1D; -.
DR PDBsum; 7Z1E; -.
DR SASBDB; P0DTC2; -.
DR SMR; P0DTC2; -.
DR BioGRID; 4383848; 803.
DR ComplexPortal; CPX-5682; SARS-CoV-2 cleaved Spike protein complex.
DR ComplexPortal; CPX-7042; SARS-CoV-2 uncleaved Spike protein complex.
DR ComplexPortal; CPX-7043; SARS-CoV-2 post-fusion S2 Spike complex.
DR IntAct; P0DTC2; 186.
DR ChEMBL; CHEMBL4662936; -.
DR DrugBank; DB15691; Anti-SARS-CoV-2 REGN-COV2.
DR DrugBank; DB15718; Bamlanivimab.
DR DrugBank; DB15941; Casirivimab.
DR DrugBank; DB16393; Cilgavimab.
DR DrugBank; DB15897; Etesevimab.
DR DrugBank; DB15940; Imdevimab.
DR DrugBank; DB16405; Regdanvimab.
DR DrugBank; DB16355; Sotrovimab.
DR DrugBank; DB16394; Tixagevimab.
DR GlyConnect; 2838; 126 N-Linked glycans (16 sites), 4 O-Linked glycans (2 sites).
DR GlyConnect; 2839; 81 N-Linked glycans (21 sites).
DR GlyConnect; 2840; 109 N-Linked glycans (22 sites).
DR GlyConnect; 2951; 2 O-Linked glycans (6 sites).
DR GlyConnect; 2952; 2 O-Linked glycans (18 sites).
DR GlyConnect; 2953; 2 O-Linked glycans (13 sites).
DR GlyConnect; 2956; 66 N-Linked glycans (2 sites), 20 O-Linked glycans (1 site).
DR GlyConnect; 2957; 35 N-Linked glycans (2 sites), 17 O-Linked glycans (1 site).
DR GlyGen; P0DTC2; 51 sites, 293 N-linked glycans (23 sites), 18 O-linked glycans (28 sites).
DR ABCD; P0DTC2; 887 sequenced antibodies.
DR DNASU; 43740568; -.
DR GeneID; 43740568; -.
DR KEGG; vg:43740568; -.
DR Reactome; R-HSA-9694322; Virion Assembly and Release.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-9694635; Translation of Structural Proteins.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SABIO-RK; P0DTC2; -.
DR SIGNOR; P0DTC2; -.
DR PRO; PR:P0DTC2; -.
DR Proteomes; UP000464024; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IPI:ComplexPortal.
DR GO; GO:0019031; C:viral envelope; IDA:UniProtKB.
DR GO; GO:0055036; C:virion membrane; TAS:Reactome.
DR GO; GO:0046789; F:host cell surface receptor binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0061025; P:membrane fusion; IDA:ComplexPortal.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IC:ComplexPortal.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IC:ComplexPortal.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:UniProtKB.
DR GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0019058; P:viral life cycle; IC:ComplexPortal.
DR CDD; cd21480; SARS-CoV-2_Spike_S1_RBD; 1.
DR CDD; cd21624; SARS-CoV-like_Spike_S1_NTD; 1.
DR DisProt; DP02772; -.
DR Gene3D; 2.60.120.960; -; 1.
DR HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR InterPro; IPR032500; bCoV_S1_N.
DR InterPro; IPR042578; BETA_CORONA_SPIKE.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR043002; Spike_N_sf.
DR InterPro; IPR044341; Spike_S1_N_SARS-CoV-like.
DR InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR InterPro; IPR044366; Spike_S1_RBD_SARS-CoV-2.
DR InterPro; IPR036326; Spike_S1_RBD_sf_bCoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF16451; bCoV_S1_N; 1.
DR Pfam; PF09408; bCoV_S1_RBD; 1.
DR Pfam; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR SUPFAM; SSF143587; SSF143587; 1.
DR PROSITE; PS51921; BCOV_S1_CTD; 1.
DR PROSITE; PS51922; BCOV_S1_NTD; 1.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host tetherin by virus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Superantigen; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
KW Virulence; Virus entry into host cell.
FT SIGNAL 1..13
FT /evidence="ECO:0000269|PubMed:34210893"
FT CHAIN 14..1273
FT /note="Spike glycoprotein"
FT /id="PRO_0000449646"
FT CHAIN 14..685
FT /note="Spike protein S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000449647"
FT CHAIN 686..1273
FT /note="Spike protein S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000449648"
FT CHAIN 816..1273
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000449649"
FT TOPO_DOM 14..1213
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1214..1234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1235..1273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 14..303
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 334..527
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT ECO:0000269|PubMed:32132184"
FT REGION 280..301
FT /note="Putative superantigen; may bind T-cell receptor
FT alpha/TRAC"
FT /evidence="ECO:0000303|PubMed:32989130"
FT REGION 319..541
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000269|PubMed:32132184"
FT REGION 403..405
FT /note="Integrin-binding motif;"
FT /evidence="ECO:0000269|PubMed:33102950"
FT REGION 437..508
FT /note="Receptor-binding motif; binding to human ACE2"
FT /evidence="ECO:0000250|UniProtKB:P59594"
FT REGION 448..456
FT /note="Immunodominant HLA epitope recognized by the CD8+;
FT called NF9 peptide"
FT /evidence="ECO:0000269|PubMed:34171266"
FT REGION 681..684
FT /note="Putative superantigen; may bind T-cell receptor
FT beta/TRBC1"
FT /evidence="ECO:0000303|PubMed:32989130"
FT REGION 816..837
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 835..855
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 920..970
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1163..1202
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 949..993
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1176..1203
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1237..1241
FT /note="Binding to host endocytosis trafficking protein
FT SNX27"
FT /evidence="ECO:0000269|PubMed:34504087"
FT MOTIF 1257..1262
FT /note="Diacidic ER export motif (host COPII)"
FT /evidence="ECO:0000269|PubMed:34504087"
FT MOTIF 1261..1267
FT /note="Binding to host plasma membrane localising/FERM
FT domain proteins"
FT /evidence="ECO:0000269|PubMed:34504087"
FT MOTIF 1269..1273
FT /note="KxHxx, ER retrieval signal (COPI)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:34504087"
FT SITE 685..686
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32362314,
FT ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616"
FT SITE 815..816
FT /note="Cleavage; by host TMPRSS2 or CTSL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616"
FT LIPID 1235
FT /note="S-palmitoyl cysteine; by host ZDHHC20"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1236
FT /note="S-palmitoyl cysteine; by host ZDHHC20"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1240
FT /note="S-palmitoyl cysteine; by host ZDHHC20"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1241
FT /note="S-palmitoyl cysteine; by host ZDHHC20"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1243
FT /note="S-palmitoyl cysteine; by host ZDHHC20"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1247
FT /note="S-palmitoyl cysteine; by host ZDHHC20; partial"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1248
FT /note="S-palmitoyl cysteine; by host ZDHHC20; partial"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1250
FT /note="S-palmitoyl cysteine; by host ZDHHC20; partial"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1253
FT /note="S-palmitoyl cysteine; by host ZDHHC20; partial"
FT /evidence="ECO:0000269|PubMed:34599882"
FT LIPID 1254
FT /note="S-palmitoyl cysteine; by host ZDHHC20; partial"
FT /evidence="ECO:0000269|PubMed:34599882"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 323
FT /note="O-linked (GalNAc) threonine; by host"
FT /evidence="ECO:0000269|PubMed:32363391"
FT CARBOHYD 325
FT /note="O-linked (HexNAc...) serine; by host"
FT /evidence="ECO:0000269|PubMed:32363391"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 676
FT /note="O-linked (GlcNAc...) threonine; by host GALNT1"
FT /evidence="ECO:0000269|PubMed:34732583"
FT CARBOHYD 678
FT /note="O-linked (GlcNAc...) threonine; by host GALNT1"
FT /evidence="ECO:0000269|PubMed:34732583"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1074
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1098
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1134
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT CARBOHYD 1158
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1173
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1194
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT DISULFID 15..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 131..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270,
FT ECO:0000269|PubMed:32155444, ECO:0007744|PDB:6VXX"
FT DISULFID 291..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270,
FT ECO:0000269|PubMed:32155444, ECO:0007744|PDB:6VXX"
FT DISULFID 336..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32245784"
FT DISULFID 379..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32245784"
FT DISULFID 391..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32225175,
FT ECO:0000269|PubMed:32225176, ECO:0000269|PubMed:32245784,
FT ECO:0007744|PDB:6VXX"
FT DISULFID 480..488
FT /evidence="ECO:0000269|PubMed:32245784"
FT DISULFID 538..590
FT /evidence="ECO:0000269|PubMed:32155444,
FT ECO:0007744|PDB:6VXX"
FT DISULFID 617..649
FT /evidence="ECO:0000269|PubMed:32155444,
FT ECO:0007744|PDB:6VXX"
FT DISULFID 662..671
FT /evidence="ECO:0000269|PubMed:32155444,
FT ECO:0007744|PDB:6VXX"
FT DISULFID 738..760
FT /evidence="ECO:0000269|PubMed:32155444,
FT ECO:0007744|PDB:6VXX"
FT DISULFID 743..749
FT /evidence="ECO:0000269|PubMed:32155444,
FT ECO:0007744|PDB:6VXX"
FT DISULFID 840..851
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 1032..1043
FT /evidence="ECO:0000269|PubMed:32155444,
FT ECO:0007744|PDB:6VXX"
FT DISULFID 1082..1126
FT /evidence="ECO:0000269|PubMed:32155444,
FT ECO:0007744|PDB:6VXX"
FT VARIANT 5
FT /note="L -> F (in strain: Iota/B.1.526)"
FT /evidence="ECO:0000305"
FT VARIANT 13
FT /note="S -> I (in strain: Epsilon/B.1.427/B.1.429; may
FT change signal peptide cleavage to position 16-17)"
FT /evidence="ECO:0000269|PubMed:34210893, ECO:0000305"
FT VARIANT 18
FT /note="L -> F (in strain: Beta/B.1.351, Gamma/P.1, 19B/
FT 501Y)"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:33690265"
FT VARIANT 19
FT /note="T -> R (in strain: Delta/B.1.617.2, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 20
FT /note="T -> N (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 24..27
FT /note="LPPA -> S (in strain: Omicron/BA.2, Omicron/
FT BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 26
FT /note="P -> S (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 67
FT /note="A -> V (in strain: Eta/B.1.525, Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 69..70
FT /note="Missing (in strain: Alpha/B.1.1.7, Eta/B.1.525, 19B/
FT 501T, Omicron/BA.1, Omicron/BA.4, Omicron/BA.5; May
FT compensate for reduced infectivity of RBD escape mutants)"
FT /evidence="ECO:0000269|PubMed:34166617,
FT ECO:0000305|PubMed:33413740"
FT VARIANT 75
FT /note="G -> V (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 76
FT /note="T -> I (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 80
FT /note="D -> A (in strain: Beta/B.1.351)"
FT /evidence="ECO:0000305|PubMed:33690265"
FT VARIANT 95
FT /note="T -> I (in strain: Iota/B.1.526, Mu/B.1.621,
FT B.1.1.318, Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 102
FT /note="R -> I (in strain: A23.1)"
FT /evidence="ECO:0000305"
FT VARIANT 138
FT /note="D -> Y (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 142..145
FT /note="GVYY -> D (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 142
FT /note="G -> D (in strain: Kappa/B.1.617.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 144
FT /note="Missing (in strain: Alpha/B.1.1.7, Eta/B.1.525,
FT B.1.1.318)"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:33413740"
FT VARIANT 152
FT /note="W -> C (in strain: Epsilon/B.1.427/B.1.429; when
FT coupled with S13I induces resistance to NTD antibodies by
FT changing disulfid bond in positions 15-136 to 136-152)"
FT /evidence="ECO:0000269|PubMed:34210893, ECO:0000305"
FT VARIANT 154
FT /note="E -> K (in strain: Kappa/B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 156..158
FT /note="EFR -> G (in strain: Delta/B.1.617.2)"
FT VARIANT 157
FT /note="F -> L (in strain: A23.1)"
FT /evidence="ECO:0000305"
FT VARIANT 190
FT /note="R -> S (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 211..212
FT /note="NL -> I (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 213
FT /note="V -> G (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 214
FT /note="R -> REPE (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 215
FT /note="D -> G (in strain: Beta/B.1.351)"
FT /evidence="ECO:0000305|PubMed:33690265"
FT VARIANT 222
FT /note="A -> V (in strain: 20A.EU1)"
FT /evidence="ECO:0000305"
FT VARIANT 246..252
FT /note="Missing (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 253
FT /note="D -> G (in strain: Iota/B.1.526)"
FT /evidence="ECO:0000305"
FT VARIANT 253
FT /note="D -> N (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 339
FT /note="G -> D (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 346
FT /note="R -> K (in strain: Mu/B.1.621)"
FT /evidence="ECO:0000305"
FT VARIANT 371
FT /note="S -> L (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 373
FT /note="S -> P (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 375
FT /note="S -> F (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 376
FT /note="T -> A (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 405
FT /note="D -> N (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 408
FT /note="R -> S (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 417
FT /note="K -> N (in strain: Beta/B.1.351, Gamma/P.1, Omicron/
FT BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.4,
FT Omicron/BA.5; May enhance affinity to human ACE2 receptor)"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:33690265"
FT VARIANT 417
FT /note="K -> T (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 440
FT /note="N -> K (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 446
FT /note="G -> S (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 452
FT /note="L -> Q (in strain: Omicron/BA.2.12.1)"
FT /evidence="ECO:0000305"
FT VARIANT 452
FT /note="L -> R (in strain: Delta/B.1.617.2, Epsilon/B.1.427/
FT B.1.429, Kappa/B.1.617.1, Lambda/C.37, 19B/501Y, Omicron/
FT BA.4, Omicron/BA.5; Contributes to cellular immunity
FT evasion and increases infectivity)"
FT /evidence="ECO:0000269|PubMed:34171266, ECO:0000305"
FT VARIANT 453
FT /note="Y -> F (in strain: B.1.1.298)"
FT /evidence="ECO:0000269|PubMed:34171266"
FT VARIANT 477
FT /note="S -> N (in strain: 20A.EU2, Iota/B.1.526, Omicron/
FT BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.4,
FT Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 478
FT /note="T -> K (in strain: Delta/B.1.617.2, Omicron/BA.1,
FT Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.4, Omicron/
FT BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 484
FT /note="E -> A (in strain: Omicron/BA.1, Omicron/BA.2
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 484
FT /note="E -> K (in strain: Beta/B.1.351, Eta/B.1.525, Theta/
FT P.3, Iota/B.1.526, B.1.1.318, Gamma/P.1, Zeta/P.2 and Mu/
FT B.1.621; May enhance affinity to human ACE2 receptor)"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:33690265"
FT VARIANT 484
FT /note="E -> Q (in strain: Kappa/B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 486
FT /note="F -> V (in strain: Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 490
FT /note="F -> S (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 493
FT /note="Q -> R (in strain: Omicron/BA.1, Omicron/BA.2
FT Omicron/BA.2.12.1)"
FT /evidence="ECO:0000305"
FT VARIANT 496
FT /note="G -> S (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 498
FT /note="Q -> R (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 501
FT /note="N -> T (in strain: 19B/501T)"
FT /evidence="ECO:0000305"
FT VARIANT 501
FT /note="N -> Y (in strain: Alpha/B.1.1.7, Beta/B.1.351,
FT Gamma/P.1, Theta/P.3, Mu/B.1.621, 19B/501Y, Omicron/BA.1,
FT Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.4, Omicron/
FT BA.5; May enhance affinity to human ACE2 receptor)"
FT /evidence="ECO:0000269|PubMed:32732280, ECO:0000305,
FT ECO:0000305|PubMed:33413740, ECO:0000305|PubMed:33690265"
FT VARIANT 505
FT /note="Y -> H (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 547
FT /note="T -> K (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 570
FT /note="A -> D (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 613
FT /note="Q -> H (in strain: A23.1)"
FT /evidence="ECO:0000305"
FT VARIANT 614
FT /note="D -> G (in strain: Alpha/B.1.1.7, Beta/B.1.351,
FT Gamma/P.1, Delta/B.1.617.2, Epsilon/B.1.427/B.1.429, Eta/
FT B.1.525, Theta/P.3, Iota/B.1.526, Kappa/B.1.617.1, Lambda/
FT C.37, B.1.1.318, Zeta/P.2, Mu/B.1.621, 20A.EU1, 20A.EU2,
FT Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/
FT BA.4, Omicron/BA.5; common variant; binds to hACE2 more
FT efficiently; produces more infectious particles when
FT cultured in primary human epithelial cells; does not
FT significantly shift SARS-CoV-2 neutralization properties)"
FT /evidence="ECO:0000269|PubMed:33417835, ECO:0000305,
FT ECO:0000305|PubMed:32132184, ECO:0000305|PubMed:32697968,
FT ECO:0000305|PubMed:32820179, ECO:0000305|PubMed:33106671,
FT ECO:0000305|PubMed:33184236, ECO:0000305|PubMed:33413740,
FT ECO:0000305|PubMed:33636719"
FT VARIANT 653
FT /note="A -> V (in strain: 19B/501Y)"
FT /evidence="ECO:0000305"
FT VARIANT 655
FT /note="H -> Y (in strain: Gamma/P.1, 19B/501T, 19B/501Y,
FT Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/
FT BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 677
FT /note="Q -> H (in strain: Eta/B.1.525)"
FT /evidence="ECO:0000305"
FT VARIANT 679
FT /note="N -> K (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 681
FT /note="P -> H (in strain: Alpha/B.1.1.7, Theta/P.3, Mu/
FT B.1.621, B.1.1.318, A23.1, Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:33413740"
FT VARIANT 681
FT /note="P -> R (in strain: Delta/B.1.617.2, Kappa/
FT B.1.617.1)"
FT VARIANT 701
FT /note="A -> V (in strain: Beta/B.1.351, Iota/B.1.526)"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:33690265"
FT VARIANT 704
FT /note="S -> L (in strain: Omicron/BA.2.12.1)"
FT /evidence="ECO:0000305"
FT VARIANT 716
FT /note="T -> I (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 764
FT /note="N -> K (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 796
FT /note="D -> H (in strain: B.1.1.318)"
FT /evidence="ECO:0000305"
FT VARIANT 796
FT /note="D -> Y (in strain: 19B/501Y, Omicron/BA.1, Omicron/
FT BA.2, Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 856
FT /note="N -> K (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 859
FT /note="T -> N (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 888
FT /note="F -> L (in strain: Eta/B.1.525)"
FT /evidence="ECO:0000305"
FT VARIANT 950
FT /note="D -> N (in strain: Delta/B.1.617.2, Mu/B.1.621)"
FT /evidence="ECO:0000305"
FT VARIANT 954
FT /note="Q -> H (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 969
FT /note="N -> K (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 981
FT /note="L -> F (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 982
FT /note="S -> A (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 1027
FT /note="T -> I (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 1071
FT /note="Q -> H (in strain: Kappa/B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 1092
FT /note="E -> K (in strain: Theta/P.3)"
FT /evidence="ECO:0000305"
FT VARIANT 1101
FT /note="H -> Y (in strain: Theta/P.3)"
FT /evidence="ECO:0000305"
FT VARIANT 1118
FT /note="D -> H (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 1176
FT /note="V -> F (in strain: Gamma/P.1, Theta/P.3, Zeta/P.2)"
FT /evidence="ECO:0000305"
FT VARIANT 1219
FT /note="G -> V (in strain: 19B/501Y)"
FT /evidence="ECO:0000305"
FT MUTAGEN 69..70
FT /note="Missing: Increased incorporation of cleaved spike
FT into virions."
FT /evidence="ECO:0000269|PubMed:34166617"
FT MUTAGEN 121
FT /note="N->Q: Partial loss of biliverdin affinity."
FT /evidence="ECO:0000269|PubMed:33888467"
FT MUTAGEN 190
FT /note="R->K: Partial loss of biliverdin affinity."
FT /evidence="ECO:0000269|PubMed:33888467"
FT MUTAGEN 234
FT /note="N->Q: Increased resistance to neutralizing
FT antibodies."
FT /evidence="ECO:0000269|PubMed:32730807"
FT MUTAGEN 331
FT /note="N->Q: Reduced viral infectivity."
FT /evidence="ECO:0000269|PubMed:32730807"
FT MUTAGEN 343
FT /note="N->Q: Reduced viral infectivity."
FT /evidence="ECO:0000269|PubMed:32730807"
FT MUTAGEN 452
FT /note="L->R: Increased resistance to neutralizing
FT antibodies. Decreases HLA binding to NF9 epitope. Increased
FT binding affinity to human ACE2."
FT /evidence="ECO:0000269|PubMed:32730807,
FT ECO:0000269|PubMed:34171266"
FT MUTAGEN 453
FT /note="Y->F: Decreased HLA binding to NF9 epitope.
FT Increased binding affinity to human ACE2."
FT /evidence="ECO:0000269|PubMed:34171266"
FT MUTAGEN 475
FT /note="A->V: Increased resistance to neutralizing
FT antibodies."
FT /evidence="ECO:0000269|PubMed:32730807"
FT MUTAGEN 483
FT /note="V->A: Increased resistance to neutralizing
FT antibodies."
FT /evidence="ECO:0000269|PubMed:32730807"
FT MUTAGEN 490
FT /note="F->L: Increased resistance to neutralizing
FT antibodies and human covalescent sera neutralization."
FT /evidence="ECO:0000269|PubMed:32730807"
FT MUTAGEN 493
FT /note="Q->N: Reduced host ACE2-binding affinity in vitro."
FT /evidence="ECO:0000269|PubMed:32225175"
FT MUTAGEN 493
FT /note="Q->Y: Reduced host ACE2-binding affinity in vitro."
FT /evidence="ECO:0000269|PubMed:32225175"
FT MUTAGEN 501
FT /note="N->T: Reduced host ACE2-binding affinity in vitro."
FT /evidence="ECO:0000269|PubMed:32225175"
FT MUTAGEN 501
FT /note="N->Y: Increased binding affinity to human ACE2."
FT /evidence="ECO:0000269|PubMed:34171266"
FT MUTAGEN 519
FT /note="H->P: Increased resistance to human covalescent sera
FT neutralization."
FT /evidence="ECO:0000269|PubMed:32730807"
FT MUTAGEN 614
FT /note="D->G: Increase of pseudotyped VSV particle
FT production ex vivo. Increase of viral load in hamster upper
FT respiratory tract. Produces more infectious particles when
FT cultured in primary human epithelial cells; increases
FT replication and transmissibility in hamsters and ferrets."
FT /evidence="ECO:0000269|PubMed:32697968,
FT ECO:0000269|PubMed:33106671, ECO:0000269|PubMed:33636719"
FT MUTAGEN 673
FT /note="S->A: No effect on O-glycosylation by host GALNT1."
FT /evidence="ECO:0000269|PubMed:34732583"
FT MUTAGEN 676
FT /note="T->A: Partial loss of O-glycoslyation by host
FT GALNT1."
FT /evidence="ECO:0000269|PubMed:34732583"
FT MUTAGEN 678
FT /note="T->A: Complete loss of O-glycosylation by host
FT GALNT1."
FT /evidence="ECO:0000269|PubMed:34732583"
FT MUTAGEN 679..684
FT /note="NSPRRA->IL: About 50% stronger entry efficiency in
FT Vero E6 cells while 30% weaker entry efficiency in hACE2-
FT expressing BHK cells."
FT /evidence="ECO:0000269|PubMed:32155444"
FT MUTAGEN 680
FT /note="S->A: No effect on O-glycosylation by host GALNT1."
FT /evidence="ECO:0000269|PubMed:34732583"
FT MUTAGEN 681..684
FT /note="PRRA->RRRK: Optimized cleavage by host furin."
FT /evidence="ECO:0000269|PubMed:32362314"
FT MUTAGEN 681
FT /note="P->A,H,R: Complete loss of O-glycosylation by host
FT GALNT1."
FT /evidence="ECO:0000269|PubMed:34732583"
FT MUTAGEN 682..685
FT /note="RRAR->SRAG: Stabilization in prefusion state (in
FT vaccine Ad26.COV2.S/Janssen Pharmaceutical)."
FT /evidence="ECO:0000305|PubMed:34322129"
FT MUTAGEN 682..684
FT /note="Missing: Complete loss of cleavage by host furin."
FT /evidence="ECO:0000269|PubMed:32362314"
FT MUTAGEN 684
FT /note="A->K,R: Partial improvement of cleavage by host
FT furin."
FT /evidence="ECO:0000269|PubMed:32703818"
FT MUTAGEN 986..987
FT /note="KV->PP: Stabilization in prefusion state (in vaccine
FT BNT162b2/Pfizer-Biontech, vaccine mRNA-1273/Moderna,
FT vaccine Ad26.COV2.S/Janssen Pharmaceutical)."
FT /evidence="ECO:0000269|PubMed:34322129"
FT MUTAGEN 1269
FT /note="K->A: Complete loss of COPI binding and increase in
FT cell fusion."
FT /evidence="ECO:0000269|PubMed:34504087"
FT MUTAGEN 1271
FT /note="H->K: Improved COPI binding, reduced cell fusion and
FT reduced levels of S1/S2 cleavage."
FT /evidence="ECO:0000269|PubMed:34504087"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:7Q0I"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:7B62"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:7KEA"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:7B62"
FT TURN 70..74
FT /evidence="ECO:0007829|PDB:7CN4"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7B62"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:7WK2"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:7SXT"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:7WK2"
FT STRAND 126..146
FT /evidence="ECO:0007829|PDB:7B62"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 151..171
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:7KQE"
FT STRAND 184..197
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 200..215
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:7CN4"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:7LY2"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:7SY3"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:7E7B"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:7B62"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:7V83"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:7B62"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:7SXT"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:7D2Z"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:7R6W"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:7EAM"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:7EAM"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:7OLZ"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:7EAM"
FT TURN 384..388
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 389..403
FT /evidence="ECO:0007829|PDB:7EAM"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:6XLU"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:7K9H"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:7EAM"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:7EAM"
FT TURN 444..447
FT /evidence="ECO:0007829|PDB:7K90"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:7MZK"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:7C2L"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:7RKU"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:7LD1"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:7MSQ"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:7LDJ"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:6ZGE"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 506..516
FT /evidence="ECO:0007829|PDB:7EAM"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:7SXT"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:7NEH"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:7L0N"
FT STRAND 536..543
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 546..554
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:7LXY"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:7LXY"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 609..613
FT /evidence="ECO:0007829|PDB:7LXY"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 620..623
FT /evidence="ECO:0007829|PDB:6XLU"
FT TURN 624..628
FT /evidence="ECO:0007829|PDB:6XLU"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:6XLU"
FT STRAND 637..640
FT /evidence="ECO:0007829|PDB:6XLU"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 654..660
FT /evidence="ECO:0007829|PDB:6XLU"
FT STRAND 663..667
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:7LXY"
FT TURN 678..680
FT /evidence="ECO:0007829|PDB:7CN4"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:7DZW"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:7N0G"
FT STRAND 692..696
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 711..728
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 733..736
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 738..743
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 747..753
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 754..756
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 759..782
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 786..790
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:7LXY"
FT TURN 803..805
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:7DF3"
FT STRAND 809..813
FT /evidence="ECO:0007829|PDB:6XLU"
FT HELIX 817..825
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 828..830
FT /evidence="ECO:0007829|PDB:7DZW"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:7E7B"
FT HELIX 835..838
FT /evidence="ECO:0007829|PDB:6XLU"
FT STRAND 842..845
FT /evidence="ECO:0007829|PDB:6XLU"
FT STRAND 848..850
FT /evidence="ECO:0007829|PDB:7EDF"
FT HELIX 851..854
FT /evidence="ECO:0007829|PDB:7LXY"
FT TURN 855..857
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 858..861
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 867..884
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 887..889
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:7SO9"
FT HELIX 898..907
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 909..956
FT /evidence="ECO:0007829|PDB:7EK6"
FT HELIX 965..967
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 970..973
FT /evidence="ECO:0007829|PDB:7CZT"
FT HELIX 977..983
FT /evidence="ECO:0007829|PDB:7LXY"
FT TURN 986..989
FT /evidence="ECO:0007829|PDB:6ZB4"
FT TURN 994..996
FT /evidence="ECO:0007829|PDB:7EDF"
FT HELIX 1009..1021
FT /evidence="ECO:0007829|PDB:6M1V"
FT HELIX 1022..1025
FT /evidence="ECO:0007829|PDB:6M1V"
FT HELIX 1029..1031
FT /evidence="ECO:0007829|PDB:6M1V"
FT TURN 1032..1034
FT /evidence="ECO:0007829|PDB:7A29"
FT TURN 1040..1042
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 1043..1056
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 1059..1079
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 1081..1083
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 1086..1100
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 1102..1105
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 1107..1109
FT /evidence="ECO:0007829|PDB:7N8H"
FT STRAND 1112..1114
FT /evidence="ECO:0007829|PDB:7LWW"
FT STRAND 1119..1125
FT /evidence="ECO:0007829|PDB:7LXY"
FT STRAND 1126..1129
FT /evidence="ECO:0007829|PDB:7T9K"
FT STRAND 1130..1134
FT /evidence="ECO:0007829|PDB:7P77"
FT TURN 1140..1144
FT /evidence="ECO:0007829|PDB:7LXY"
FT HELIX 1148..1155
FT /evidence="ECO:0007829|PDB:7M53"
FT HELIX 1169..1171
FT /evidence="ECO:0007829|PDB:6XRA"
FT HELIX 1180..1192
FT /evidence="ECO:0007829|PDB:7EK6"
FT HELIX 1193..1196
FT /evidence="ECO:0007829|PDB:7EK6"
FT HELIX 1218..1236
FT /evidence="ECO:0007829|PDB:7LC8"
SQ SEQUENCE 1273 AA; 141178 MW; B17BE6D9F1C4EA34 CRC64;
MFVFLVLLPL VSSQCVNLTT RTQLPPAYTN SFTRGVYYPD KVFRSSVLHS TQDLFLPFFS
NVTWFHAIHV SGTNGTKRFD NPVLPFNDGV YFASTEKSNI IRGWIFGTTL DSKTQSLLIV
NNATNVVIKV CEFQFCNDPF LGVYYHKNNK SWMESEFRVY SSANNCTFEY VSQPFLMDLE
GKQGNFKNLR EFVFKNIDGY FKIYSKHTPI NLVRDLPQGF SALEPLVDLP IGINITRFQT
LLALHRSYLT PGDSSSGWTA GAAAYYVGYL QPRTFLLKYN ENGTITDAVD CALDPLSETK
CTLKSFTVEK GIYQTSNFRV QPTESIVRFP NITNLCPFGE VFNATRFASV YAWNRKRISN
CVADYSVLYN SASFSTFKCY GVSPTKLNDL CFTNVYADSF VIRGDEVRQI APGQTGKIAD
YNYKLPDDFT GCVIAWNSNN LDSKVGGNYN YLYRLFRKSN LKPFERDIST EIYQAGSTPC
NGVEGFNCYF PLQSYGFQPT NGVGYQPYRV VVLSFELLHA PATVCGPKKS TNLVKNKCVN
FNFNGLTGTG VLTESNKKFL PFQQFGRDIA DTTDAVRDPQ TLEILDITPC SFGGVSVITP
GTNTSNQVAV LYQDVNCTEV PVAIHADQLT PTWRVYSTGS NVFQTRAGCL IGAEHVNNSY
ECDIPIGAGI CASYQTQTNS PRRARSVASQ SIIAYTMSLG AENSVAYSNN SIAIPTNFTI
SVTTEILPVS MTKTSVDCTM YICGDSTECS NLLLQYGSFC TQLNRALTGI AVEQDKNTQE
VFAQVKQIYK TPPIKDFGGF NFSQILPDPS KPSKRSFIED LLFNKVTLAD AGFIKQYGDC
LGDIAARDLI CAQKFNGLTV LPPLLTDEMI AQYTSALLAG TITSGWTFGA GAALQIPFAM
QMAYRFNGIG VTQNVLYENQ KLIANQFNSA IGKIQDSLSS TASALGKLQD VVNQNAQALN
TLVKQLSSNF GAISSVLNDI LSRLDKVEAE VQIDRLITGR LQSLQTYVTQ QLIRAAEIRA
SANLAATKMS ECVLGQSKRV DFCGKGYHLM SFPQSAPHGV VFLHVTYVPA QEKNFTTAPA
ICHDGKAHFP REGVFVSNGT HWFVTQRNFY EPQIITTDNT FVSGNCDVVI GIVNNTVYDP
LQPELDSFKE ELDKYFKNHT SPDVDLGDIS GINASVVNIQ KEIDRLNEVA KNLNESLIDL
QELGKYEQYI KWPWYIWLGF IAGLIAIVMV TIMLCCMTSC CSCLKGCCSC GSCCKFDEDD
SEPVLKGVKL HYT
