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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
 
 
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