R1AB_SARS2
ID R1AB_SARS2 Reviewed; 7096 AA.
AC P0DTD1;
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=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Host translation inhibitor nsp1;
DE AltName: Full=Leader protein;
DE AltName: Full=Non-structural protein 1;
DE Short=nsp1;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p65 homolog;
DE Contains:
DE RecName: Full=Papain-like protease nsp3 {ECO:0000303|PubMed:32726803};
DE EC=3.4.19.12 {ECO:0000269|PubMed:32726803};
DE EC=3.4.22.-;
DE AltName: Full=Non-structural protein 3;
DE Short=nsp3;
DE AltName: Full=PL2-PRO;
DE AltName: Full=Papain-like proteinase;
DE Short=PL-PRO;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE Contains:
DE RecName: Full=3C-like proteinase nsp5;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.69 {ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481};
DE AltName: Full=Main protease;
DE Short=Mpro {ECO:0000303|PubMed:32272481};
DE AltName: Full=Non-structural protein 5;
DE Short=nsp5;
DE AltName: Full=SARS coronavirus main proteinase;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase nsp12;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=Non-structural protein 12;
DE Short=nsp12;
DE Contains:
DE RecName: Full=Helicase nsp13;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=Non-structural protein 13;
DE Short=nsp13;
DE Contains:
DE RecName: Full=Proofreading exoribonuclease nsp14;
DE Short=ExoN;
DE EC=3.1.13.-;
DE AltName: Full=Guanine-N7 methyltransferase;
DE AltName: Full=Non-structural protein 14;
DE Short=nsp14;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease nsp15;
DE EC=4.6.1.- {ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093};
DE AltName: Full=NendoU;
DE AltName: Full=Non-structural protein 15;
DE Short=nsp15;
DE Contains:
DE RecName: Full=2'-O-methyltransferase nsp16;
DE EC=2.1.1.57;
DE AltName: Full=Non-structural protein 16;
DE Short=nsp16;
GN Name=rep; ORFNames=1a-1b;
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 VARIANTS ILE-1001; ASP-1708; THR-2230 AND 3675-SER--PHE-3677.
RC STRAIN=20B/501Y.V1, 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 [3]
RP FUNCTION (HOST TRANSLATION INHIBITOR NSP1).
RX PubMed=33479166; DOI=10.1073/pnas.2017715118;
RA Lapointe C.P., Grosely R., Johnson A.G., Wang J., Fernandez I.S.,
RA Puglisi J.D.;
RT "Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome
RT inhibits translation initiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [4]
RP FUNCTION (2'-O-METHYLTRANSFERASE NSP16), SUBCELLULAR LOCATION
RP (2'-O-METHYLTRANSFERASE NSP16), FUNCTION (HOST TRANSLATION INHIBITOR NSP1),
RP FUNCTION(NON-STRUCTURAL PROTEIN 8), FUNCTION (NON-STRUCTURAL PROTEIN 9),
RP SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 8), AND SUBCELLULAR LOCATION
RP (NON-STRUCTURAL PROTEIN 9).
RX PubMed=33080218; DOI=10.1016/j.cell.2020.10.004;
RA Banerjee A.K., Blanco M.R., Bruce E.A., Honson D.D., Chen L.M., Chow A.,
RA Bhat P., Ollikainen N., Quinodoz S.A., Loney C., Thai J., Miller Z.D.,
RA Lin A.E., Schmidt M.M., Stewart D.G., Goldfarb D., De Lorenzo G.,
RA Rihn S.J., Voorhees R.M., Botten J.W., Majumdar D., Guttman M.;
RT "SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to
RT Suppress Host Defenses.";
RL Cell 183:1325-1339(2020).
RN [5]
RP FUNCTION (PAPAIN-LIKE PROTEASE NSP3), AND MUTAGENESIS OF CYS-1674.
RX PubMed=33727702; DOI=10.1038/s41564-021-00884-1;
RA Liu G., Lee J.H., Parker Z.M., Acharya D., Chiang J.J., van Gent M.,
RA Riedl W., Davis-Gardner M.E., Wies E., Chiang C., Gack M.U.;
RT "ISG15-dependent activation of the sensor MDA5 is antagonized by the SARS-
RT CoV-2 papain-like protease to evade host innate immunity.";
RL Nat. Microbiol. 6:467-478(2021).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 3C-LIKE PROTEINASE NSP5 AND IN
RP COMPLEX WITH MICHAEL ACCEPTOR INHIBITOR N3.
RA Liu X., Zhang B., Jin Z., Yang H., Rao Z.;
RT "The crystal structure of 2019-nCoV main protease in complex with an
RT inhibitor N3.";
RL Submitted (FEB-2020) to the PDB data bank.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3C-LIKE PROTEINASE NSP5 AND IN
RP COMPLEX WITH ALPHA-KETOAMIDE 13B INHIBITOR, SUBUNIT (3C-LIKE PROTEINASE
RP NSP5), FUNCTION (3C-LIKE PROTEINASE NSP5), CATALYTIC ACTIVITY (3C-LIKE
RP PROTEINASE NSP5), ACTIVE SITE (3C-LIKE PROTEINASE NSP5), AND ACTIVITY
RP REGULATION (3C-LIKE PROTEINASE NSP5).
RX PubMed=32198291; DOI=10.1126/science.abb3405;
RA Zhang L., Lin D., Sun X., Curth U., Drosten C., Sauerhering L., Becker S.,
RA Rox K., Hilgenfeld R.;
RT "Crystal structure of SARS-CoV-2 main protease provides a basis for design
RT of improved alpha-ketoamide inhibitors.";
RL Science 368:409-412(2020).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3C-LIKE PROTEINASE NSP5 AND IN
RP COMPLEX WITH MICHAEL ACCEPTOR INHIBITOR N3, FUNCTION (3C-LIKE PROTEINASE
RP NSP5) (3C-LIKE PROTEINASE NSP5), CATALYTIC ACTIVITY (3C-LIKE PROTEINASE
RP NSP5), AND ACTIVITY REGULATION (3C-LIKE PROTEINASE NSP5).
RX PubMed=32272481; DOI=10.1038/s41586-020-2223-y;
RA Jin Z., Du X., Xu Y., Deng Y., Liu M., Zhao Y., Zhang B., Li X., Zhang L.,
RA Peng C., Duan Y., Yu J., Wang L., Yang K., Liu F., Jiang R., Yang X.,
RA You T., Liu X., Yang X., Bai F., Liu H., Liu X., Guddat L.W., Xu W.,
RA Xiao G., Qin C., Shi Z., Jiang H., Rao Z., Yang H.;
RT "Structure of Mpro from COVID-19 virus and discovery of its inhibitors.";
RL Nature 582:289-293(2020).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 7; NON-STRUCTURAL PROTEIN 8 AND RNA-DIRECTED RNA POLYMERASE NSP12, SUBUNIT
RP (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL PROTEIN 8), SUBUNIT
RP (RNA-DIRECTED RNA POLYMERASE NSP12), FUNCTION (NON-STRUCTURAL PROTEIN 7),
RP FUNCTION (NON-STRUCTURAL PROTEIN 8), AND FUNCTION (RNA-DIRECTED RNA
RP POLYMERASE NSP12).
RX PubMed=32277040; DOI=10.1126/science.abb7498;
RA Gao Y., Yan L., Huang Y., Liu F., Zhao Y., Cao L., Wang T., Sun Q.,
RA Ming Z., Zhang L., Ge J., Zheng L., Zhang Y., Wang H., Zhu Y., Zhu C.,
RA Hu T., Hua T., Zhang B., Yang X., Li J., Yang H., Liu Z., Xu W.,
RA Guddat L.W., Wang Q., Lou Z., Rao Z.;
RT "Structure of the RNA-dependent RNA polymerase from COVID-19 virus.";
RL Science 368:779-782(2020).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.5 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 7; NON-STRUCTURAL PROTEIN 8 AND RNA-DIRECTED RNA POLYMERASE NSP12 IN
RP COMPLEX WITH REMDESIVIR ANTIVIRAL DRUG AND IN COMPLEX WITH ZINC ION,
RP SUBUNIT (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL PROTEIN 8),
RP SUBUNIT (RNA-DIRECTED RNA POLYMERASE), FUNCTION (NON-STRUCTURAL PROTEIN 7),
RP FUNCTION (NON-STRUCTURAL PROTEIN 8), FUNCTION (RNA-DIRECTED RNA POLYMERASE
RP NSP12), CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE NSP12), AND
RP ACTIVITY REGULATION (RNA-DIRECTED RNA POLYMERASE NSP12).
RX PubMed=32358203; DOI=10.1126/science.abc1560;
RA Yin W., Mao C., Luan X., Shen D.D., Shen Q., Su H., Wang X., Zhou F.,
RA Zhao W., Gao M., Chang S., Xie Y.C., Tian G., Jiang H.W., Tao S.C.,
RA Shen J., Jiang Y., Jiang H., Xu Y., Zhang S., Zhang Y., Xu H.E.;
RT "Structural basis for inhibition of the RNA-dependent RNA polymerase from
RT SARS-CoV-2 by remdesivir.";
RL Science 368:1499-1504(2020).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 3C-LIKE PROTEINASE NSP5 IN COMPLEX
RP WITH COMPOUND 11A AND COMPOUND 11B, FUNCTION (3C-LIKE PROTEINASE NSP5),
RP CATALYTIC ACTIVITY (3C-LIKE PROTEINASE NSP5), AND ACTIVITY REGULATION
RP (3C-LIKE PROTEINASE NSP5).
RX PubMed=32321856; DOI=10.1126/science.abb4489;
RA Dai W., Zhang B., Su H., Li J., Zhao Y., Xie X., Jin Z., Liu F., Li C.,
RA Li Y., Bai F., Wang H., Cheng X., Cen X., Hu S., Yang X., Wang J., Liu X.,
RA Xiao G., Jiang H., Rao Z., Zhang L.K., Xu Y., Yang H., Liu H.;
RT "Structure-based design of antiviral drug candidates targeting the SARS-
RT CoV-2 main protease.";
RL Science 368:1331-1335(2020).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 7; NON-STRUCTURAL PROTEIN 8 AND RNA-DIRECTED RNA POLYMERASE NSP12, SUBUNIT
RP (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL PROTEIN 8), SUBUNIT
RP (RNA-DIRECTED RNA POLYMERASE), FUNCTION (NON-STRUCTURAL PROTEIN 7),
RP FUNCTION (NON-STRUCTURAL PROTEIN 8), FUNCTION (RNA-DIRECTED RNA POLYMERASE
RP NSP12), AND CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE NSP12).
RX PubMed=32438371; DOI=10.1038/s41586-020-2368-8;
RA Hillen H.S., Kokic G., Farnung L., Dienemann C., Tegunov D., Cramer P.;
RT "Structure of replicating SARS-CoV-2 polymerase.";
RL Nature 584:154-156(2020).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) OF NON-STRUCTURAL PROTEIN 3 MACRO
RP DOMAIN, AND FUNCTION (PAPAIN-LIKE PROTEASE NSP3).
RX PubMed=32578982; DOI=10.1021/acs.biochem.0c00309;
RA Frick D.N., Virdi R.S., Vuksanovic N., Dahal N., Silvaggi N.R.;
RT "Molecular Basis for ADP-ribose Binding to the Mac1 Domain of SARS-CoV-2
RT Nsp3.";
RL Biochemistry 59:2608-2615(2020).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.93 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 7; NON-STRUCTURAL PROTEIN 8 AND RNA-DIRECTED RNA POLYMERASE IN COMPLEX WITH
RP ZINC ION, SUBUNIT (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL
RP PROTEIN 8), SUBUNIT (RNA-DIRECTED RNA POLYMERASE NSP12), FUNCTION
RP (NON-STRUCTURAL PROTEIN 7), FUNCTION (NON-STRUCTURAL PROTEIN 8), FUNCTION
RP (RNA-DIRECTED RNA POLYMERASE NSP12), CATALYTIC ACTIVITY (RNA-DIRECTED RNA
RP POLYMERASE NSP12), ACTIVITY REGULATION (RNA-DIRECTED RNA POLYMERASE NSP12),
RP AND MUTAGENESIS OF SER-5253.
RX PubMed=32526208; DOI=10.1016/j.cell.2020.05.034;
RA Wang Q., Wu J., Wang H., Gao Y., Liu Q., Mu A., Ji W., Yan L., Zhu Y.,
RA Zhu C., Fang X., Yang X., Huang Y., Gao H., Liu F., Ge J., Sun Q., Yang X.,
RA Xu W., Liu Z., Yang H., Lou Z., Jiang B., Guddat L.W., Gong P., Rao Z.;
RT "Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase.";
RL Cell 182:417-428(2020).
RN [15] {ECO:0007744|PDB:6YVA}
RP X-RAY CRYSTALLOGRAPHY (3.18 ANGSTROMS) OF NON-STRUCTURAL PROTEIN 3,
RP FUNCTION (PAPAIN-LIKE PROTEASE NSP3), CATALYTIC ACTIVITY (PAPAIN-LIKE
RP PROTEASE NSP3), ACTIVITY REGULATION (PAPAIN-LIKE PROTEASE NSP3), AND
RP MUTAGENESIS OF VAL-1629; PHE-1632; THR-1638; CYS-1674 AND TYR-1831.
RX PubMed=32726803; DOI=10.1038/s41586-020-2601-5;
RA Shin D., Mukherjee R., Grewe D., Bojkova D., Baek K., Bhattacharya A.,
RA Schulz L., Widera M., Mehdipour A.R., Tascher G., Geurink P.P., Wilhelm A.,
RA van der Heden van Noort G.J., Ovaa H., Mueller S., Knobeloch K.P.,
RA Rajalingam K., Schulman B.A., Cinatl J., Hummer G., Ciesek S., Dikic I.;
RT "Papain-like protease regulates SARS-CoV-2 viral spread and innate
RT immunity.";
RL Nature 587:657-662(2020).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.6 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 1, FUNCTION (NON-STRUCTURAL PROTEIN 1), AND MUTAGENESIS OF LYS-164 AND
RP HIS-165.
RX PubMed=32680882; DOI=10.1126/science.abc8665;
RA Thoms M., Buschauer R., Ameismeier M., Koepke L., Denk T.,
RA Hirschenberger M., Kratzat H., Hayn M., Mackens-Kiani T., Cheng J.,
RA Straub J.H., Stuerzel C.M., Froehlich T., Berninghausen O., Becker T.,
RA Kirchhoff F., Sparrer K.M.J., Beckmann R.;
RT "Structural basis for translational shutdown and immune evasion by the Nsp1
RT protein of SARS-CoV-2.";
RL Science 369:1249-1255(2020).
RN [17]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1).
RX PubMed=32733001; DOI=10.1038/s41467-020-17665-9;
RA Lei X., Dong X., Ma R., Wang W., Xiao X., Tian Z., Wang C., Wang Y., Li L.,
RA Ren L., Guo F., Zhao Z., Zhou Z., Xiang Z., Wang J.;
RT "Activation and evasion of type I interferon responses by SARS-CoV-2.";
RL Nat. Commun. 11:3810-3810(2020).
RN [18]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1), FUNCTION (NON-STRUCTURAL PROTEIN 6),
RP FUNCTION (HELICASE NSP13), INTERACTION WITH HOST TBK1 (NON-STRUCTURAL
RP PROTEIN 6), AND INTERACTION WITH HOST TBK1 (HELICASE NSP13).
RX PubMed=32979938; DOI=10.1016/j.celrep.2020.108234;
RA Xia H., Cao Z., Xie X., Zhang X., Chen J.Y., Wang H., Menachery V.D.,
RA Rajsbaum R., Shi P.Y.;
RT "Evasion of Type I Interferon by SARS-CoV-2.";
RL Cell Rep. 33:108234-108234(2020).
RN [19]
RP SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 1), SUBCELLULAR LOCATION
RP (NON-STRUCTURAL PROTEIN 2), SUBCELLULAR LOCATION (3C-LIKE PROTEINASE NSP5),
RP SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 7), SUBCELLULAR LOCATION
RP (NON-STRUCTURAL PROTEIN 8), SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN
RP 9), SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 10), AND SUBCELLULAR
RP LOCATION (PROOFREADING EXORIBONUCLEASE).
RX PubMed=33060197; DOI=10.1126/science.abe9403;
RG QCRG Structural Biology Consortium;
RG Zoonomia Consortium;
RA Gordon D.E., Hiatt J., Bouhaddou M., Rezelj V.V., Ulferts S., Braberg H.,
RA Jureka A.S., Obernier K., Guo J.Z., Batra J., Kaake R.M., Weckstein A.R.,
RA Owens T.W., Gupta M., Pourmal S., Titus E.W., Cakir M., Soucheray M.,
RA McGregor M., Cakir Z., Jang G., O'Meara M.J., Tummino T.A., Zhang Z.,
RA Foussard H., Rojc A., Zhou Y., Kuchenov D., Huettenhain R., Xu J.,
RA Eckhardt M., Swaney D.L., Fabius J.M., Ummadi M., Tutuncuoglu B.,
RA Rathore U., Modak M., Haas P., Haas K.M., Naing Z.Z.C., Pulido E.H.,
RA Shi Y., Barrio-Hernandez I., Memon D., Petsalaki E., Dunham A.,
RA Marrero M.C., Burke D., Koh C., Vallet T., Silvas J.A., Azumaya C.M.,
RA Billesboelle C., Brilot A.F., Campbell M.G., Diallo A., Dickinson M.S.,
RA Diwanji D., Herrera N., Hoppe N., Kratochvil H.T., Liu Y., Merz G.E.,
RA Moritz M., Nguyen H.C., Nowotny C., Puchades C., Rizo A.N.,
RA Schulze-Gahmen U., Smith A.M., Sun M., Young I.D., Zhao J., Asarnow D.,
RA Biel J., Bowen A., Braxton J.R., Chen J., Chio C.M., Chio U.S.,
RA Deshpande I., Doan L., Faust B., Flores S., Jin M., Kim K., Lam V.L.,
RA Li F., Li J., Li Y.L., Li Y., Liu X., Lo M., Lopez K.E., Melo A.A.,
RA Moss F.R. III, Nguyen P., Paulino J., Pawar K.I., Peters J.K.,
RA Pospiech T.H. Jr., Safari M., Sangwan S., Schaefer K., Thomas P.V.,
RA Thwin A.C., Trenker R., Tse E., Tsui T.K.M., Wang F., Whitis N., Yu Z.,
RA Zhang K., Zhang Y., Zhou F., Saltzberg D., Hodder A.J., Shun-Shion A.S.,
RA Williams D.M., White K.M., Rosales R., Kehrer T., Miorin L., Moreno E.,
RA Patel A.H., Rihn S., Khalid M.M., Vallejo-Gracia A., Fozouni P.,
RA Simoneau C.R., Roth T.L., Wu D., Karim M.A., Ghoussaini M., Dunham I.,
RA Berardi F., Weigang S., Chazal M., Park J., Logue J., McGrath M.,
RA Weston S., Haupt R., Hastie C.J., Elliott M., Brown F., Burness K.A.,
RA Reid E., Dorward M., Johnson C., Wilkinson S.G., Geyer A., Giesel D.M.,
RA Baillie C., Raggett S., Leech H., Toth R., Goodman N., Keough K.C.,
RA Lind A.L., Klesh R.J., Hemphill K.R., Carlson-Stevermer J., Oki J.,
RA Holden K., Maures T., Pollard K.S., Sali A., Agard D.A., Cheng Y.,
RA Fraser J.S., Frost A., Jura N., Kortemme T., Manglik A., Southworth D.R.,
RA Stroud R.M., Alessi D.R., Davies P., Frieman M.B., Ideker T., Abate C.,
RA Jouvenet N., Kochs G., Shoichet B., Ott M., Palmarini M., Shokat K.M.,
RA Garcia-Sastre A., Rassen J.A., Grosse R., Rosenberg O.S., Verba K.A.,
RA Basler C.F., Vignuzzi M., Peden A.A., Beltrao P., Krogan N.J.;
RT "Comparative host-coronavirus protein interaction networks reveal pan-viral
RT disease mechanisms.";
RL Science 0:0-0(2020).
RN [20]
RP FUNCTION (NON-STRUCTURAL PROTEIN 3), AND SUBCELLULAR LOCATION
RP (NON-STRUCTURAL PROTEIN 3).
RX PubMed=32763915; DOI=10.1126/science.abd3629;
RA Wolff G., Limpens R.W.A.L., Zevenhoven-Dobbe J.C., Laugks U., Zheng S.,
RA de Jong A.W.M., Koning R.I., Agard D.A., Gruenewald K., Koster A.J.,
RA Snijder E.J., Barcena M.;
RT "A molecular pore spans the double membrane of the coronavirus replication
RT organelle.";
RL Science 369:1395-1398(2020).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.8 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 1, FUNCTION (NON-STRUCTURAL PROTEIN 1), AND MUTAGENESIS OF
RP 154-TYR--PHE-157; 164-LYS-HIS-165 AND 171-ARG--ARG-175.
RX PubMed=32908316; DOI=10.1038/s41594-020-0511-8;
RA Schubert K., Karousis E.D., Jomaa A., Scaiola A., Echeverria B.,
RA Gurzeler L.A., Leibundgut M., Thiel V., Muehlemann O., Ban N.;
RT "SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation.";
RL Nat. Struct. Mol. Biol. 27:959-966(2020).
RN [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.3 ANGSTROMS) OF URIDYLATE-SPECIFIC
RP ENDORIBONUCLEASE NSP15 IN COMPLEX WITH UTP, CATALYTIC ACTIVITY
RP (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15), SUBUNIT (URIDYLATE-SPECIFIC
RP ENDORIBONUCLEASE NSP15), MUTAGENESIS OF HIS-6686 AND HIS-6701, AND ACTIVE
RP SITE (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15).
RX PubMed=33504779; DOI=10.1038/s41467-020-20608-z;
RA Pillon M.C., Frazier M.N., Dillard L.B., Williams J.G., Kocaman S.,
RA Krahn J.M., Perera L., Hayne C.K., Gordon J., Stewart Z.D., Sobhany M.,
RA Deterding L.J., Hsu A.L., Dandey V.P., Borgnia M.J., Stanley R.E.;
RT "Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight
RT into nuclease specificity and dynamics.";
RL Nat. Commun. 12:636-636(2021).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 6453-679 IN COMPLEX WITH
RP SUBSTRATE ANALOGS AND INHIBITOR, FUNCTION (URIDYLATE-SPECIFIC
RP ENDORIBONUCLEASE NSP15), CATALYTIC ACTIVITY (URIDYLATE-SPECIFIC
RP ENDORIBONUCLEASE NSP15), SUBUNIT (URIDYLATE-SPECIFIC ENDORIBONUCLEASE
RP NSP15), AND COFACTOR (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15).
RX PubMed=33564093; DOI=10.1038/s42003-021-01735-9;
RA Kim Y., Wower J., Maltseva N., Chang C., Jedrzejczak R., Wilamowski M.,
RA Kang S., Nicolaescu V., Randall G., Michalska K., Joachimiak A.;
RT "Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU
RT from SARS-CoV-2.";
RL Commun. Biol. 4:193-193(2021).
CC -!- FUNCTION: [Replicase polyprotein 1ab]: Multifunctional protein involved
CC in the transcription and replication of viral RNAs. Contains the
CC proteinases responsible for the cleavages of the polyprotein.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation
CC by associating with the open head conformation of the 40S subunit
CC (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316).
CC The C-terminus binds to and obstructs ribosomal mRNA entry tunnel
CC (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316).
CC Thereby inhibits antiviral response triggered by innate immunity or
CC interferons (PubMed:33080218, PubMed:32680882, PubMed:32979938). The
CC nsp1-40S ribosome complex further induces an endonucleolytic cleavage
CC near the 5'UTR of host mRNAs, targeting them for degradation (By
CC similarity). Viral mRNAs less susceptible to nsp1-mediated inhibition
CC of translation, because of their 5'-end leader sequence
CC (PubMed:32908316, PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32680882, ECO:0000269|PubMed:32908316,
CC ECO:0000269|PubMed:32979938, ECO:0000269|PubMed:33080218,
CC ECO:0000269|PubMed:33479166}.
CC -!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
CC of host cell survival signaling pathway by interacting with host PHB
CC and PHB2. Indeed, these two proteins play a role in maintaining the
CC functional integrity of the mitochondria and protecting cells from
CC various stresses. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Papain-like protease nsp3]: Responsible for the cleavages
CC located at the N-terminus of the replicase polyprotein. Participates
CC together with nsp4 in the assembly of virally-induced cytoplasmic
CC double-membrane vesicles necessary for viral replication (By
CC similarity). Forms a molecular pore spanning the double membrane of the
CC coronavirus replication organelle (PubMed:32763915). Antagonizes innate
CC immune induction of type I interferon by blocking the phosphorylation,
CC dimerization and subsequent nuclear translocation of host IRF3
CC (PubMed:32733001). Prevents also host NF-kappa-B signaling (By
CC similarity). In addition, PL-PRO possesses a
CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains from cellular substrates
CC (PubMed:32726803). Cleaves preferentially ISG15 from antiviral protein
CC IFIH1 (MDA5), but not DDX58 (RIG-I) (PubMed:33727702). Can play a role
CC in host ADP-ribosylation by binding ADP-ribose (PubMed:32578982).
CC {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32578982,
CC ECO:0000269|PubMed:32726803, ECO:0000269|PubMed:32733001,
CC ECO:0000269|PubMed:32763915, ECO:0000269|PubMed:33727702}.
CC -!- FUNCTION: [Non-structural protein 4]: Participates in the assembly of
CC virally-induced cytoplasmic double-membrane vesicles necessary for
CC viral replication. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [3C-like proteinase nsp5]: Cleaves the C-terminus of
CC replicase polyprotein at 11 sites (PubMed:32321856). Recognizes
CC substrates containing the core sequence [ILMVF]-Q-|-[SGACN]
CC (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose-
CC 1''-phosphate (ADRP) (By similarity) (PubMed:32198291,
CC PubMed:32272481). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481,
CC ECO:0000269|PubMed:32321856}.
CC -!- FUNCTION: [Non-structural protein 6]: Plays a role in the initial
CC induction of autophagosomes from host reticulum endoplasmic (By
CC similarity). Later, limits the expansion of these phagosomes that are
CC no longer able to deliver viral components to lysosomes (By
CC similarity). Binds to host TBK1 without affecting TBK1 phosphorylation;
CC the interaction with TBK1 decreases IRF3 phosphorylation, which leads
CC to reduced IFN-beta production (PubMed:32979938).
CC {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32979938}.
CC -!- FUNCTION: [Non-structural protein 7]: Plays a role in viral RNA
CC synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371,
CC PubMed:32526208). Forms a hexadecamer with nsp8 (8 subunits of each)
CC that may participate in viral replication by acting as a primase.
CC Alternatively, may synthesize substantially longer products than
CC oligonucleotide primers (By similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
CC -!- FUNCTION: [Non-structural protein 8]: Plays a role in viral RNA
CC synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371,
CC PubMed:32526208). Forms a hexadecamer with nsp7 (8 subunits of each)
CC that may participate in viral replication by acting as a primase.
CC Alternatively, may synthesize substantially longer products than
CC oligonucleotide primers (By similarity). Interacts with ribosome signal
CC recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9,
CC suppress protein integration into the cell membrane, thereby disrupting
CC host immune defenses (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208,
CC ECO:0000269|PubMed:33080218}.
CC -!- FUNCTION: [Non-structural protein 9]: May participate in viral
CC replication by acting as a ssRNA-binding protein (By similarity).
CC Interacts with ribosome signal recognition particle RNA (SRP)
CC (PubMed:33080218). Together with NSP9, suppress protein integration
CC into the cell membrane, thereby disrupting host immune defenses
CC (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:33080218}.
CC -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
CC 2'-O-methyltransferase activities. Therefore plays an essential role in
CC viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [RNA-directed RNA polymerase nsp12]: Responsible for
CC replication and transcription of the viral RNA genome.
CC {ECO:0000305|PubMed:32277040, ECO:0000305|PubMed:32358203,
CC ECO:0000305|PubMed:32438371, ECO:0000305|PubMed:32526208}.
CC -!- FUNCTION: [Helicase nsp13]: Multi-functional protein with a zinc-
CC binding domain in N-terminus displaying RNA and DNA duplex-unwinding
CC activities with 5' to 3' polarity. Activity of helicase is dependent on
CC magnesium (By similarity). Binds to host TBK1 and inhibits TBK1
CC phosphorylation; the interaction with TBK1 decreases IRF3
CC phosphorylation, which leads to reduced IFN-beta production
CC (PubMed:32979938). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32979938}.
CC -!- FUNCTION: [Proofreading exoribonuclease nsp14]: Enzyme possessing two
CC different activities: an exoribonuclease activity acting on both ssRNA
CC and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase
CC activity. Acts as a proofreading exoribonuclease for RNA replication,
CC thereby lowering The sensitivity of the virus to RNA mutagens.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Uridylate-specific endoribonuclease nsp15]: Plays a role in
CC viral transcription/replication and prevents the simultaneous
CC activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR
CC (By similarity). Acts by degrading the 5'-polyuridines generated during
CC replication of the poly(A) region of viral genomic and subgenomic RNAs
CC (PubMed:33504779, PubMed:33564093). Catalyzes a two-step reaction in
CC which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O
CC transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P)
CC (PubMed:33504779, PubMed:33564093). If not degraded, poly(U) RNA would
CC hybridize with poly(A) RNA tails and activate host dsRNA sensors (By
CC similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:33504779}.
CC -!- FUNCTION: [2'-O-methyltransferase nsp16]: Methyltransferase that
CC mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of
CC viral mRNAs (By similarity). N7-methyl guanosine cap is a prerequisite
CC for binding of nsp16. Therefore plays an essential role in viral mRNAs
CC cap methylation which is essential to evade immune system (By
CC similarity). May disrupt host mRNA splicing in nucleus by interacting
CC with pre-mRNA Recognition Domains ofthe U1 and U2 snRNAs
CC (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:33080218}.
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208};
CC -!- CATALYTIC ACTIVITY: [Helicase nsp13]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY: [Helicase nsp13]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides
CC corresponding to the two self-cleavage sites of the SARS 3C-like
CC proteinase are the two most reactive peptide substrates. The enzyme
CC exhibits a strong preference for substrates containing Gln at P1
CC position and Leu at P2 position.; EC=3.4.22.69;
CC Evidence={ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481,
CC ECO:0000269|PubMed:32321856};
CC -!- CATALYTIC ACTIVITY: [Papain-like protease nsp3]:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:32726803};
CC -!- CATALYTIC ACTIVITY: [2'-O-methyltransferase nsp16]:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease nsp15]:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093};
CC -!- COFACTOR: [Uridylate-specific endoribonuclease nsp15]:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:33564093};
CC Note=Likely affects Nsp15 binding to RNA.
CC {ECO:0000250|UniProtKB:P0C6X7};
CC -!- ACTIVITY REGULATION: [Papain-like protease nsp3]: Inhibited in vitro by
CC GRL-0617. {ECO:0000269|PubMed:32726803}.
CC -!- ACTIVITY REGULATION: [Proofreading exoribonuclease nsp14]: Inhibited by
CC Remdesivir antiviral drug (GS-5734). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- ACTIVITY REGULATION: [RNA-directed RNA polymerase nsp12]: Inhibited by
CC Remdesivir antiviral drug (GS-5734) through non-obligate RNA chain
CC termination. {ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32526208}.
CC -!- ACTIVITY REGULATION: [3C-like proteinase nsp5]: Inhibited by pyridone-
CC containing alpha-ketoamides compounds 13a and 13b. In turn, alpha-
CC ketoamide 13b (tert-butyl (1-((S)-1-(((S)-4-(benzylamino)-3,4-dioxo-1-
CC ((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-3-cyclopropyl-1-oxopropan-
CC 2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate) inhibits SARS-CoV-2
CC replication in human lung cells (PubMed:32198291). Inhibited ex vivo by
CC michael acceptor inhibitor N3 (PubMed:32272481). Inhibited ex vivo by
CC compound 11a and 11b (PubMed:32321856). {ECO:0000269|PubMed:32198291,
CC ECO:0000269|PubMed:32272481, ECO:0000269|PubMed:32321856}.
CC -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Papain-like protease nsp3]: May for homohexamers.
CC {ECO:0000269|PubMed:32763915}.
CC -!- SUBUNIT: [3C-like proteinase nsp5]: 3CL-PRO exists as monomer and
CC homodimer. Only the homodimer shows catalytic activity.
CC {ECO:0000269|PubMed:32198291}.
CC -!- SUBUNIT: [Non-structural protein 4]: Interacts with PL-PRO and nsp6.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 6]: Interacts with host TBK1; this
CC interaction decreases by 57% IRF3 phosphorylation, which leads to
CC reduced IFN-beta production. {ECO:0000269|PubMed:32979938}.
CC -!- SUBUNIT: [Non-structural protein 7]: Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure (By similarity). Interacts with RNA-directed RNA
CC polymerase (PubMed:32277040, PubMed:32358203, PubMed:32438371,
CC PubMed:32526208). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
CC -!- SUBUNIT: [Non-structural protein 8]: Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure (By similarity). Interacts with RNA-directed RNA
CC polymerase (PubMed:32277040, PubMed:32358203, PubMed:32438371,
CC PubMed:32526208). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
CC -!- SUBUNIT: [Non-structural protein 9]: Is a dimer.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 10]: Forms a dodecamer and interacts
CC with nsp14 and nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase nsp12]: Interacts with nsp7 and
CC nsp8. {ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
CC -!- SUBUNIT: [Helicase nsp13]: Interacts with host TBK1; this interaction
CC inhibits TBK1 phosphorylation and decreases by 75% IRF3
CC phosphorylation, which leads to reduced IFN-beta production.
CC {ECO:0000269|PubMed:32979938}.
CC -!- SUBUNIT: [Proofreading exoribonuclease nsp14]: Interacts (via N-
CC terminus) with DDX1. Interacts with nsp10.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Uridylate-specific endoribonuclease nsp15]: Homohexamer.
CC {ECO:0000269|PubMed:33504779}.
CC -!- SUBUNIT: [2'-O-methyltransferase nsp16]: Interacts with nsp10.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- INTERACTION:
CC P0DTD1; PRO_0000449621 [P0DTD1]: rep; NbExp=2; IntAct=EBI-25492095, EBI-25492388;
CC P0DTD1; PRO_0000449623 [P0DTD1]: rep; NbExp=2; IntAct=EBI-25492095, EBI-25475864;
CC PRO_0000449620; P21281: ATP6V1B2; Xeno; NbExp=2; IntAct=EBI-25475859, EBI-4290814;
CC PRO_0000449620; Q8WVV9: HNRNPLL; Xeno; NbExp=2; IntAct=EBI-25475859, EBI-535849;
CC PRO_0000449620; P52306: RAP1GDS1; Xeno; NbExp=5; IntAct=EBI-25475859, EBI-746389;
CC PRO_0000449620; Q9NUL3: STAU2; Xeno; NbExp=2; IntAct=EBI-25475859, EBI-722938;
CC PRO_0000449621; P0DTC9: N; NbExp=13; IntAct=EBI-25492388, EBI-25475856;
CC PRO_0000449621; PRO_0000449619 [P0DTD1]: rep; NbExp=4; IntAct=EBI-25492388, EBI-25475847;
CC PRO_0000449621; Q8IYX8: CEP57L1; Xeno; NbExp=3; IntAct=EBI-25492388, EBI-1104570;
CC PRO_0000449621; Q9BZS1: FOXP3; Xeno; NbExp=4; IntAct=EBI-25492388, EBI-983719;
CC PRO_0000449621; P51114: FXR1; Xeno; NbExp=5; IntAct=EBI-25492388, EBI-713291;
CC PRO_0000449621; P51116: FXR2; Xeno; NbExp=4; IntAct=EBI-25492388, EBI-740459;
CC PRO_0000449621; Q9BYX4: IFIH1; Xeno; NbExp=2; IntAct=EBI-25492388, EBI-6115771;
CC PRO_0000449621; P05161: ISG15; Xeno; NbExp=13; IntAct=EBI-25492388, EBI-746466;
CC PRO_0000449621; Q64339: Isg15; Xeno; NbExp=5; IntAct=EBI-25492388, EBI-8345781;
CC PRO_0000449621; Q9H000: MKRN2; Xeno; NbExp=4; IntAct=EBI-25492388, EBI-2341005;
CC PRO_0000449621; Q13064: MKRN3; Xeno; NbExp=3; IntAct=EBI-25492388, EBI-2340269;
CC PRO_0000449621; O75360: PROP1; Xeno; NbExp=3; IntAct=EBI-25492388, EBI-9027467;
CC PRO_0000449621; Q9H5L6: THAP9; Xeno; NbExp=3; IntAct=EBI-25492388, EBI-10982953;
CC PRO_0000449621; J3QS39: UBB; Xeno; NbExp=6; IntAct=EBI-25492388, EBI-25691162;
CC PRO_0000449621; P0CG48: UBC; Xeno; NbExp=2; IntAct=EBI-25492388, EBI-3390054;
CC PRO_0000449622; O95429: BAG4; Xeno; NbExp=3; IntAct=EBI-25475862, EBI-2949658;
CC PRO_0000449622; P60880: SNAP25; Xeno; NbExp=3; IntAct=EBI-25475862, EBI-524785;
CC PRO_0000449623; PRO_0000449623 [P0DTD1]: rep; NbExp=17; IntAct=EBI-25475864, EBI-25475864;
CC PRO_0000449623; O95786: DDX58; Xeno; NbExp=2; IntAct=EBI-25475864, EBI-995350;
CC PRO_0000449623; Q92769: HDAC2; Xeno; NbExp=2; IntAct=EBI-25475864, EBI-301821;
CC PRO_0000449623; Q9Y6K9-1: IKBKG; Xeno; NbExp=2; IntAct=EBI-25475864, EBI-27121550;
CC PRO_0000449623; Q7Z434: MAVS; Xeno; NbExp=2; IntAct=EBI-25475864, EBI-995373;
CC PRO_0000449623; E9Q5R7: Nlrp12; Xeno; NbExp=2; IntAct=EBI-25475864, EBI-26583426;
CC PRO_0000449623; P59046: NLRP12; Xeno; NbExp=3; IntAct=EBI-25475864, EBI-6374637;
CC PRO_0000449623; P22061: PCMT1; Xeno; NbExp=2; IntAct=EBI-25475864, EBI-353343;
CC PRO_0000449623; Q15750: TAB1; Xeno; NbExp=2; IntAct=EBI-25475864, EBI-358643;
CC PRO_0000449624; P26842: CD27; Xeno; NbExp=3; IntAct=EBI-25475868, EBI-520729;
CC PRO_0000449624; Q16553: LY6E; Xeno; NbExp=3; IntAct=EBI-25475868, EBI-18234679;
CC PRO_0000449625; P0DTC7: 7a; NbExp=3; IntAct=EBI-25475871, EBI-25475903;
CC PRO_0000449625; PRO_0000449619 [P0DTD1]: rep; NbExp=3; IntAct=EBI-25475871, EBI-25475847;
CC PRO_0000449625; PRO_0000449625 [P0DTD1]: rep; NbExp=6; IntAct=EBI-25475871, EBI-25475871;
CC PRO_0000449625; PRO_0000449626 [P0DTD1]: rep; NbExp=44; IntAct=EBI-25475871, EBI-25475874;
CC PRO_0000449625; PRO_0000449629 [P0DTD1]: rep; NbExp=24; IntAct=EBI-25475871, EBI-25475885;
CC PRO_0000449626; PRO_0000449626 [P0DTD1]: rep; NbExp=8; IntAct=EBI-25475874, EBI-25475874;
CC PRO_0000449626; Q86Y26: NUTM1; Xeno; NbExp=3; IntAct=EBI-25475874, EBI-10178410;
CC PRO_0000449627; PRO_0000449625 [P0DTD1]: rep; NbExp=3; IntAct=EBI-25475877, EBI-25475871;
CC PRO_0000449627; PRO_0000449627 [P0DTD1]: rep; NbExp=3; IntAct=EBI-25475877, EBI-25475877;
CC PRO_0000449627; P51114: FXR1; Xeno; NbExp=3; IntAct=EBI-25475877, EBI-713291;
CC PRO_0000449627; P51116: FXR2; Xeno; NbExp=3; IntAct=EBI-25475877, EBI-740459;
CC PRO_0000449627; Q86YT6: MIB1; Xeno; NbExp=3; IntAct=EBI-25475877, EBI-2129148;
CC PRO_0000449627; A8MTQ0: NOTO; Xeno; NbExp=3; IntAct=EBI-25475877, EBI-17490746;
CC PRO_0000449627; Q04864: REL; Xeno; NbExp=3; IntAct=EBI-25475877, EBI-307352;
CC PRO_0000449627; P23497: SP100; Xeno; NbExp=3; IntAct=EBI-25475877, EBI-751145;
CC PRO_0000449627; P15884: TCF4; Xeno; NbExp=3; IntAct=EBI-25475877, EBI-533224;
CC PRO_0000449628; PRO_0000449621 [P0DTD1]: rep; NbExp=4; IntAct=EBI-25475880, EBI-25492388;
CC PRO_0000449628; PRO_0000449628 [P0DTD1]: rep; NbExp=5; IntAct=EBI-25475880, EBI-25475880;
CC PRO_0000449628; PRO_0000449631 [P0DTD1]: rep; NbExp=17; IntAct=EBI-25475880, EBI-25475920;
CC PRO_0000449628; PRO_0000449633 [P0DTD1]: rep; NbExp=24; IntAct=EBI-25475880, EBI-25492395;
CC PRO_0000449628; O15226: NKRF; Xeno; NbExp=3; IntAct=EBI-25475880, EBI-766011;
CC PRO_0000449629; PRO_0000449626 [P0DTD1]: rep; NbExp=10; IntAct=EBI-25475885, EBI-25475874;
CC PRO_0000449629; PRO_0000449627 [P0DTD1]: rep; NbExp=2; IntAct=EBI-25475885, EBI-25475877;
CC PRO_0000449629; Q13546: RIPK1; Xeno; NbExp=5; IntAct=EBI-25475885, EBI-358507;
CC PRO_0000449630; O75360: PROP1; Xeno; NbExp=3; IntAct=EBI-25475888, EBI-9027467;
CC PRO_0000449630; Q9UHD2: TBK1; Xeno; NbExp=6; IntAct=EBI-25475888, EBI-356402;
CC PRO_0000449630; Q92995: USP13; Xeno; NbExp=4; IntAct=EBI-25475888, EBI-714351;
CC PRO_0000449631; PRO_0000449631 [P0DTD1]: rep; NbExp=2; IntAct=EBI-25475920, EBI-25475920;
CC PRO_0000449631; Q9BXI9: C1QTNF6; Xeno; NbExp=4; IntAct=EBI-25475920, EBI-10301084;
CC PRO_0000449631; Q2TAC2: CCDC57; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-2808286;
CC PRO_0000449631; Q9BV73: CEP250; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-1053100;
CC PRO_0000449631; P53675: CLTCL1; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-358826;
CC PRO_0000449631; Q9Y2V7: COG6; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-3866319;
CC PRO_0000449631; Q08379: GOLGA2; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-618309;
CC PRO_0000449631; A6NEM1: GOLGA6L9; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-5916454;
CC PRO_0000449631; Q9Y6K9: IKBKG; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-81279;
CC PRO_0000449631; O60229: KALRN; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-949233;
CC PRO_0000449631; P52954: LBX1; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-20141748;
CC PRO_0000449631; Q9Y6D9: MAD1L1; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-742610;
CC PRO_0000449631; Q5JR59: MTUS2; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-742948;
CC PRO_0000449631; A8MTQ0: NOTO; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-17490746;
CC PRO_0000449631; O75360: PROP1; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-9027467;
CC PRO_0000449631; Q04864: REL; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-307352;
CC PRO_0000449631; Q15427: SF3B4; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-348469;
CC PRO_0000449631; Q96R06: SPAG5; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-413317;
CC PRO_0000449631; Q13077: TRAF1; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-359224;
CC PRO_0000449631; Q12933: TRAF2; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-355744;
CC PRO_0000449631; P14373: TRIM27; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-719493;
CC PRO_0000449631; Q86XT4: TRIM50; Xeno; NbExp=3; IntAct=EBI-25475920, EBI-9867283;
CC PRO_0000449632; PRO_0000449632 [P0DTD1]: rep; NbExp=3; IntAct=EBI-25475891, EBI-25475891;
CC PRO_0000449632; O75360: PROP1; Xeno; NbExp=3; IntAct=EBI-25475891, EBI-9027467;
CC PRO_0000449633; Q4VCS5: AMOT; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-2511319;
CC PRO_0000449633; Q8WWH4: ASZ1; Xeno; NbExp=4; IntAct=EBI-25492395, EBI-12239061;
CC PRO_0000449633; Q9H257: CARD9; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-751319;
CC PRO_0000449633; O60826: CCDC22; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-3943153;
CC PRO_0000449633; O95273: CCNDBP1; Xeno; NbExp=5; IntAct=EBI-25492395, EBI-748961;
CC PRO_0000449633; Q9Y2V7: COG6; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-3866319;
CC PRO_0000449633; Q04446: GBE1; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-726347;
CC PRO_0000449633; Q08379: GOLGA2; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-618309;
CC PRO_0000449633; A6NEM1: GOLGA6L9; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-5916454;
CC PRO_0000449633; Q8IX15: HOMEZ; Xeno; NbExp=4; IntAct=EBI-25492395, EBI-10742083;
CC PRO_0000449633; Q9UKT9: IKZF3; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-747204;
CC PRO_0000449633; O60229: KALRN; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-949233;
CC PRO_0000449633; P13646: KRT13; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-1223876;
CC PRO_0000449633; Q7Z3Y8: KRT27; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-3044087;
CC PRO_0000449633; Q15323: KRT31; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-948001;
CC PRO_0000449633; Q14532: KRT32; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-1044146;
CC PRO_0000449633; Q6A163: KRT39; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-11958242;
CC PRO_0000449633; P28838: LAP3; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-2339312;
CC PRO_0000449633; P52954: LBX1; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-20141748;
CC PRO_0000449633; Q6UWW0: LCN15; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-12176085;
CC PRO_0000449633; Q5JR59: MTUS2; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-742948;
CC PRO_0000449633; A8MTQ0: NOTO; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-17490746;
CC PRO_0000449633; Q9HBI0: PARVG; Xeno; NbExp=5; IntAct=EBI-25492395, EBI-3921217;
CC PRO_0000449633; Q8ND90: PNMA1; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-302345;
CC PRO_0000449633; Q86W92: PPFIBP1; Xeno; NbExp=4; IntAct=EBI-25492395, EBI-1045582;
CC PRO_0000449633; O75360: PROP1; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-9027467;
CC PRO_0000449633; P41219: PRPH; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-752074;
CC PRO_0000449633; P11217: PYGM; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-357469;
CC PRO_0000449633; Q8TBN0: RAB3IL1; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-743796;
CC PRO_0000449633; Q96QF0: RAB3IP; Xeno; NbExp=4; IntAct=EBI-25492395, EBI-747844;
CC PRO_0000449633; Q04864: REL; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-307352;
CC PRO_0000449633; Q9UHV2: SERTAD1; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-748601;
CC PRO_0000449633; Q96R06: SPAG5; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-413317;
CC PRO_0000449633; Q9Y2D8: SSX2IP; Xeno; NbExp=4; IntAct=EBI-25492395, EBI-2212028;
CC PRO_0000449633; Q8N0S2: SYCE1; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-6872807;
CC PRO_0000449633; Q8WW24: TEKT4; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-750487;
CC PRO_0000449633; Q9H5L6: THAP9; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-10982953;
CC PRO_0000449633; Q9C040: TRIM2; Xeno; NbExp=4; IntAct=EBI-25492395, EBI-749840;
CC PRO_0000449633; P14373: TRIM27; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-719493;
CC PRO_0000449633; O75382: TRIM3; Xeno; NbExp=4; IntAct=EBI-25492395, EBI-2129889;
CC PRO_0000449633; Q13049: TRIM32; Xeno; NbExp=4; IntAct=EBI-25492395, EBI-742790;
CC PRO_0000449633; Q9BYV2: TRIM54; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-2130429;
CC PRO_0000449633; Q9UHP3: USP25; Xeno; NbExp=6; IntAct=EBI-25492395, EBI-2513462;
CC PRO_0000449633; P08670: VIM; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-353844;
CC PRO_0000449633; Q8N1B4: VPS52; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-2799833;
CC PRO_0000449633; Q9UGI0: ZRANB1; Xeno; NbExp=3; IntAct=EBI-25492395, EBI-527853;
CC -!- SUBCELLULAR LOCATION: [Host translation inhibitor nsp1]: Host cytoplasm
CC {ECO:0000269|PubMed:33060197}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 2]: Host cytoplasm
CC {ECO:0000269|PubMed:33060197}. Host endosome
CC {ECO:0000269|PubMed:33060197}.
CC -!- SUBCELLULAR LOCATION: [Papain-like protease nsp3]: Host membrane
CC {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32763915}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32763915}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0C6X7}. Note=Localizes in virally-induced
CC cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [3C-like proteinase nsp5]: Host cytoplasm
CC {ECO:0000269|PubMed:33060197}. Host Golgi apparatus
CC {ECO:0000269|PubMed:33060197}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm
CC {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum
CC {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm
CC {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}. Host
CC endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8,
CC nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear.
CC Late in infection, they merge into confluent complexes.
CC {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm
CC {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}. Host
CC endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8,
CC nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear.
CC Late in infection, they merge into confluent complexes.
CC {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm
CC {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum
CC {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Proofreading exoribonuclease nsp14]: Host
CC cytoplasm {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum
CC {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Helicase nsp13]: Host endoplasmic reticulum-
CC Golgi intermediate compartment {ECO:0000250|UniProtKB:P0C6X7}. Note=The
CC helicase interacts with the N protein in membranous complexes and
CC colocalizes with sites of synthesis of new viral RNA.
CC {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease nsp15]: Host
CC cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [2'-O-methyltransferase nsp16]: Host nucleus.
CC Host cytoplasm {ECO:0000269|PubMed:33080218}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Normal translation results in Replicase polyprotein 1a.
CC Ribosomal frameshifting at the end of this protein occurs at low
CC frequency and produces Replicase polyprotein 1ab.;
CC Name=Replicase polyprotein 1ab;
CC IsoId=P0DTD1-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a;
CC IsoId=P0DTC1-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- POLYMORPHISM: Variant B.1.1.7 is also called Variant Of Concern (VOC)
CC 202012/01, Variant Under Investigation (VUI) 202012/01, or 20B/501Y.V1.
CC {ECO:0000305|PubMed:33413740}.
CC -!- POLYMORPHISM: Variant Omicron/BA.1 and BA.2 belong to a lineage first
CC isolated in South Africa (November 2021). {ECO:0000305}.
CC -!- MISCELLANEOUS: [Replicase polyprotein 1ab]: Produced by -1 ribosomal
CC frameshifting at the 1a-1b genes boundary.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
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DR EMBL; MN908947; QHD43415.1; -; Genomic_RNA.
DR RefSeq; YP_009724389.1; NC_045512.2.
DR PDB; 5R7Y; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5R7Z; X-ray; 1.59 A; A=3264-3569.
DR PDB; 5R80; X-ray; 1.93 A; A=3264-3569.
DR PDB; 5R81; X-ray; 1.95 A; A=3264-3569.
DR PDB; 5R82; X-ray; 1.31 A; A=3264-3569.
DR PDB; 5R83; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5R84; X-ray; 1.83 A; A=3264-3569.
DR PDB; 5R8T; X-ray; 1.27 A; A=3264-3569.
DR PDB; 5RE4; X-ray; 1.88 A; A=3264-3569.
DR PDB; 5RE5; X-ray; 2.07 A; A=3264-3569.
DR PDB; 5RE6; X-ray; 1.87 A; A=3264-3569.
DR PDB; 5RE7; X-ray; 1.79 A; A=3264-3569.
DR PDB; 5RE8; X-ray; 1.81 A; A=3264-3569.
DR PDB; 5RE9; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5REA; X-ray; 1.63 A; A=3264-3569.
DR PDB; 5REB; X-ray; 1.68 A; A=3264-3569.
DR PDB; 5REC; X-ray; 1.73 A; A=3264-3569.
DR PDB; 5RED; X-ray; 1.47 A; A=3264-3569.
DR PDB; 5REE; X-ray; 1.77 A; A=3264-3569.
DR PDB; 5REF; X-ray; 1.61 A; A=3264-3569.
DR PDB; 5REG; X-ray; 1.67 A; A=3264-3569.
DR PDB; 5REH; X-ray; 1.80 A; A=3264-3569.
DR PDB; 5REI; X-ray; 1.82 A; A=3264-3569.
DR PDB; 5REJ; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5REK; X-ray; 1.74 A; A=3264-3569.
DR PDB; 5REL; X-ray; 1.62 A; A=3264-3569.
DR PDB; 5REM; X-ray; 1.96 A; A=3264-3569.
DR PDB; 5REN; X-ray; 2.15 A; A=3264-3569.
DR PDB; 5REO; X-ray; 1.88 A; A=3264-3569.
DR PDB; 5REP; X-ray; 1.81 A; A=3264-3569.
DR PDB; 5RER; X-ray; 1.88 A; A=3264-3569.
DR PDB; 5RES; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5RET; X-ray; 1.68 A; A=3264-3569.
DR PDB; 5REU; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5REV; X-ray; 1.60 A; A=3264-3569.
DR PDB; 5REW; X-ray; 1.55 A; A=3264-3569.
DR PDB; 5REX; X-ray; 2.07 A; A=3264-3569.
DR PDB; 5REY; X-ray; 1.96 A; A=3264-3569.
DR PDB; 5REZ; X-ray; 1.79 A; A=3264-3569.
DR PDB; 5RF0; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5RF1; X-ray; 1.73 A; A=3264-3569.
DR PDB; 5RF2; X-ray; 1.53 A; A=3264-3569.
DR PDB; 5RF3; X-ray; 1.50 A; A=3264-3569.
DR PDB; 5RF4; X-ray; 1.61 A; A=3264-3569.
DR PDB; 5RF5; X-ray; 1.74 A; A=3264-3569.
DR PDB; 5RF6; X-ray; 1.45 A; A=3264-3569.
DR PDB; 5RF7; X-ray; 1.54 A; A=3264-3569.
DR PDB; 5RF8; X-ray; 1.44 A; A=3264-3569.
DR PDB; 5RF9; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RFA; X-ray; 1.52 A; A=3264-3569.
DR PDB; 5RFB; X-ray; 1.48 A; A=3264-3569.
DR PDB; 5RFC; X-ray; 1.40 A; A=3264-3569.
DR PDB; 5RFD; X-ray; 1.41 A; A=3264-3569.
DR PDB; 5RFE; X-ray; 1.46 A; A=3264-3569.
DR PDB; 5RFF; X-ray; 1.78 A; A=3264-3569.
DR PDB; 5RFG; X-ray; 2.32 A; A=3264-3569.
DR PDB; 5RFH; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RFI; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5RFJ; X-ray; 1.80 A; A=3264-3569.
DR PDB; 5RFK; X-ray; 1.75 A; A=3264-3569.
DR PDB; 5RFL; X-ray; 1.64 A; A=3264-3569.
DR PDB; 5RFM; X-ray; 2.06 A; A=3264-3569.
DR PDB; 5RFN; X-ray; 1.80 A; A=3264-3569.
DR PDB; 5RFO; X-ray; 1.83 A; A=3264-3569.
DR PDB; 5RFP; X-ray; 2.03 A; A=3264-3569.
DR PDB; 5RFQ; X-ray; 1.76 A; A=3264-3569.
DR PDB; 5RFR; X-ray; 1.71 A; A=3264-3569.
DR PDB; 5RFS; X-ray; 1.70 A; A=3264-3569.
DR PDB; 5RFT; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RFU; X-ray; 1.53 A; A=3264-3569.
DR PDB; 5RFV; X-ray; 1.48 A; A=3264-3569.
DR PDB; 5RFW; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RFX; X-ray; 1.55 A; A=3264-3569.
DR PDB; 5RFY; X-ray; 1.90 A; A=3264-3569.
DR PDB; 5RFZ; X-ray; 1.68 A; A=3264-3569.
DR PDB; 5RG0; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5RG1; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5RG2; X-ray; 1.63 A; A=3264-3569.
DR PDB; 5RG3; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RGG; X-ray; 2.26 A; A=3264-3569.
DR PDB; 5RGH; X-ray; 1.70 A; A=3264-3569.
DR PDB; 5RGI; X-ray; 1.57 A; A=3264-3569.
DR PDB; 5RGJ; X-ray; 1.34 A; A=3264-3569.
DR PDB; 5RGK; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RGL; X-ray; 1.76 A; A=3264-3569.
DR PDB; 5RGM; X-ray; 2.04 A; A=3264-3569.
DR PDB; 5RGN; X-ray; 1.86 A; A=3264-3569.
DR PDB; 5RGO; X-ray; 1.74 A; A=3264-3569.
DR PDB; 5RGP; X-ray; 2.07 A; A=3264-3569.
DR PDB; 5RGQ; X-ray; 2.15 A; A=3264-3569.
DR PDB; 5RGR; X-ray; 1.41 A; A=3264-3569.
DR PDB; 5RGS; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5RGT; X-ray; 2.22 A; A=3264-3569.
DR PDB; 5RGU; X-ray; 2.11 A; A=3264-3569.
DR PDB; 5RGV; X-ray; 1.82 A; A=3264-3569.
DR PDB; 5RGW; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RGX; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5RGY; X-ray; 1.98 A; A=3264-3569.
DR PDB; 5RGZ; X-ray; 1.52 A; A=3264-3569.
DR PDB; 5RH0; X-ray; 1.92 A; A=3264-3569.
DR PDB; 5RH1; X-ray; 1.96 A; A=3264-3569.
DR PDB; 5RH2; X-ray; 1.83 A; A=3264-3569.
DR PDB; 5RH3; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5RH4; X-ray; 1.34 A; A=3264-3569.
DR PDB; 5RH5; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5RH6; X-ray; 1.60 A; A=3264-3569.
DR PDB; 5RH7; X-ray; 1.71 A; A=3264-3569.
DR PDB; 5RH8; X-ray; 1.81 A; A=3264-3569.
DR PDB; 5RH9; X-ray; 1.91 A; A=3264-3569.
DR PDB; 5RHA; X-ray; 1.51 A; A=3264-3569.
DR PDB; 5RHB; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RHC; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RHD; X-ray; 1.57 A; A=3264-3569.
DR PDB; 5RHE; X-ray; 1.56 A; A=3264-3569.
DR PDB; 5RHF; X-ray; 1.76 A; A=3264-3569.
DR PDB; 5RL0; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5RL1; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5RL2; X-ray; 1.48 A; A=3264-3569.
DR PDB; 5RL3; X-ray; 1.51 A; A=3264-3569.
DR PDB; 5RL4; X-ray; 1.53 A; A=3264-3569.
DR PDB; 5RL5; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RL6; X-ray; 1.92 A; A/B=5325-5925.
DR PDB; 5RL7; X-ray; 1.89 A; A/B=5325-5925.
DR PDB; 5RL8; X-ray; 2.21 A; A/B=5325-5925.
DR PDB; 5RL9; X-ray; 1.79 A; A/B=5325-5925.
DR PDB; 5RLB; X-ray; 1.98 A; A/B=5325-5925.
DR PDB; 5RLC; X-ray; 1.92 A; A/B=5325-5925.
DR PDB; 5RLD; X-ray; 2.23 A; A/B=5325-5925.
DR PDB; 5RLE; X-ray; 2.27 A; A/B=5325-5925.
DR PDB; 5RLF; X-ray; 2.23 A; A/B=5325-5925.
DR PDB; 5RLG; X-ray; 1.96 A; A/B=5325-5925.
DR PDB; 5RLH; X-ray; 2.38 A; A/B=5325-5925.
DR PDB; 5RLI; X-ray; 2.26 A; A/B=5325-5925.
DR PDB; 5RLJ; X-ray; 1.88 A; A/B=5325-5925.
DR PDB; 5RLK; X-ray; 1.96 A; A/B=5325-5925.
DR PDB; 5RLL; X-ray; 2.08 A; A/B=5325-5925.
DR PDB; 5RLM; X-ray; 1.86 A; A/B=5325-5925.
DR PDB; 5RLN; X-ray; 2.15 A; A/B=5325-5925.
DR PDB; 5RLO; X-ray; 2.10 A; A/B=5325-5925.
DR PDB; 5RLP; X-ray; 2.56 A; A/B=5325-5925.
DR PDB; 5RLQ; X-ray; 2.23 A; A/B=5325-5925.
DR PDB; 5RLR; X-ray; 2.32 A; A/B=5325-5925.
DR PDB; 5RLS; X-ray; 2.28 A; A/B=5325-5925.
DR PDB; 5RLT; X-ray; 2.43 A; A/B=5325-5925.
DR PDB; 5RLU; X-ray; 2.35 A; A/B=5325-5925.
DR PDB; 5RLV; X-ray; 2.21 A; A/B=5325-5925.
DR PDB; 5RLW; X-ray; 1.97 A; A/B=5325-5925.
DR PDB; 5RLY; X-ray; 2.43 A; A/B=5325-5925.
DR PDB; 5RLZ; X-ray; 1.97 A; A/B=5325-5925.
DR PDB; 5RM0; X-ray; 1.91 A; A/B=5325-5925.
DR PDB; 5RM1; X-ray; 1.90 A; A/B=5325-5925.
DR PDB; 5RM2; X-ray; 1.82 A; A/B=5325-5925.
DR PDB; 5RM3; X-ray; 2.09 A; A/B=5325-5925.
DR PDB; 5RM4; X-ray; 2.96 A; A/B=5325-5925.
DR PDB; 5RM5; X-ray; 2.06 A; A/B=5325-5925.
DR PDB; 5RM6; X-ray; 2.13 A; A/B=5325-5925.
DR PDB; 5RM7; X-ray; 1.84 A; A/B=5325-5925.
DR PDB; 5RM8; X-ray; 2.14 A; A/B=5325-5925.
DR PDB; 5RM9; X-ray; 2.08 A; A/B=5325-5925.
DR PDB; 5RMA; X-ray; 1.89 A; A/B=5325-5925.
DR PDB; 5RMB; X-ray; 2.21 A; A/B=5325-5925.
DR PDB; 5RMC; X-ray; 2.15 A; A/B=5325-5925.
DR PDB; 5RMD; X-ray; 1.92 A; A/B=5325-5925.
DR PDB; 5RME; X-ray; 2.23 A; A/B=5325-5925.
DR PDB; 5RMF; X-ray; 2.23 A; A/B=5325-5925.
DR PDB; 5RMG; X-ray; 2.12 A; A/B=5325-5925.
DR PDB; 5RMH; X-ray; 2.02 A; A/B=5325-5925.
DR PDB; 5RMI; X-ray; 2.12 A; A/B=5325-5925.
DR PDB; 5RMJ; X-ray; 2.10 A; A/B=5325-5925.
DR PDB; 5RMK; X-ray; 2.08 A; A/B=5325-5925.
DR PDB; 5RML; X-ray; 2.43 A; A/B=5325-5925.
DR PDB; 5RMM; X-ray; 2.20 A; A/B=5325-5925.
DR PDB; 5ROB; X-ray; 1.87 A; A/B=5325-5925.
DR PDB; 5RS7; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RS8; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RS9; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSB; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSC; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RSD; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSE; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSF; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSG; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSH; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSI; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RSJ; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSK; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSL; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSM; X-ray; 1.02 A; A/B=1025-1191.
DR PDB; 5RSN; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSO; X-ray; 1.03 A; A/B=1025-1191.
DR PDB; 5RSP; X-ray; 1.02 A; A/B=1025-1191.
DR PDB; 5RSQ; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSR; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSS; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RST; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSU; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSV; X-ray; 1.03 A; A/B=1025-1191.
DR PDB; 5RSW; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSX; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RSY; X-ray; 1.04 A; A/B=1025-1191.
DR PDB; 5RSZ; X-ray; 1.02 A; A/B=1025-1191.
DR PDB; 5RT0; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RT1; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RT2; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RT3; X-ray; 1.05 A; A/B=1025-1191.
DR PDB; 5RT4; X-ray; 1.02 A; A/B=1025-1191.
DR PDB; 5RT5; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RT6; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RT7; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RT8; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RT9; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RTA; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTB; X-ray; 1.04 A; A/B=1025-1191.
DR PDB; 5RTC; X-ray; 1.06 A; A/B=1025-1191.
DR PDB; 5RTD; X-ray; 1.04 A; A/B=1025-1191.
DR PDB; 5RTE; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTF; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTG; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RTH; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTI; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RTJ; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTK; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTL; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTM; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTN; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTO; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTP; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTQ; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTR; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTS; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTT; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTU; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTV; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTW; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTX; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTY; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RTZ; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU0; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU1; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU2; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU3; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU4; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU5; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU6; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU7; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU8; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RU9; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUA; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUC; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUD; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUE; X-ray; 1.02 A; A/B=1025-1191.
DR PDB; 5RUF; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUG; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUH; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUI; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUJ; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RUK; X-ray; 1.05 A; A/B=1025-1191.
DR PDB; 5RUL; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUM; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUN; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUO; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUP; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUQ; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUR; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUS; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUT; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUU; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RUV; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUW; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUX; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUY; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RUZ; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RV0; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RV1; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RV2; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5RV3; X-ray; 1.02 A; A/B=1025-1191.
DR PDB; 5RV4; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RV5; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RV6; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RV7; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RV8; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RV9; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RVA; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RVB; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RVC; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RVD; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RVE; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RVF; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RVG; X-ray; 1.00 A; A/B=1025-1191.
DR PDB; 5RVH; X-ray; 0.98 A; A/B=1025-1191.
DR PDB; 5RVI; X-ray; 0.94 A; A/B=1025-1191.
DR PDB; 5RVJ; X-ray; 1.20 A; A=1024-1192.
DR PDB; 5RVK; X-ray; 1.46 A; A=1024-1192.
DR PDB; 5RVL; X-ray; 1.36 A; A=1024-1192.
DR PDB; 5RVM; X-ray; 1.03 A; A=1024-1192.
DR PDB; 5RVN; X-ray; 1.26 A; A=1024-1192.
DR PDB; 5RVO; X-ray; 1.52 A; A=1024-1192.
DR PDB; 5RVP; X-ray; 1.04 A; A=1024-1192.
DR PDB; 5RVQ; X-ray; 1.08 A; A=1024-1192.
DR PDB; 5RVR; X-ray; 1.04 A; A=1024-1192.
DR PDB; 5RVS; X-ray; 1.52 A; A=1024-1192.
DR PDB; 5RVT; X-ray; 1.26 A; A=1024-1192.
DR PDB; 5RVU; X-ray; 1.20 A; A=1024-1192.
DR PDB; 5RVV; X-ray; 1.42 A; A=1024-1192.
DR PDB; 5S18; X-ray; 1.13 A; A/B=1025-1191.
DR PDB; 5S1A; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S1C; X-ray; 1.17 A; A/B=1025-1191.
DR PDB; 5S1E; X-ray; 1.17 A; A/B=1025-1191.
DR PDB; 5S1G; X-ray; 1.11 A; A/B=1025-1191.
DR PDB; 5S1I; X-ray; 1.07 A; A/B=1025-1191.
DR PDB; 5S1K; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S1M; X-ray; 1.18 A; A/B=1025-1191.
DR PDB; 5S1O; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S1Q; X-ray; 1.13 A; A/B=1025-1191.
DR PDB; 5S1S; X-ray; 1.16 A; A/B=1025-1191.
DR PDB; 5S1U; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S1W; X-ray; 1.14 A; A/B=1025-1191.
DR PDB; 5S1Y; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S20; X-ray; 1.04 A; A/B=1025-1191.
DR PDB; 5S22; X-ray; 1.18 A; A/B=1025-1191.
DR PDB; 5S24; X-ray; 1.14 A; A/B=1025-1191.
DR PDB; 5S26; X-ray; 1.12 A; A/B=1025-1191.
DR PDB; 5S27; X-ray; 1.13 A; A/B=1025-1191.
DR PDB; 5S28; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S29; X-ray; 1.30 A; A/B=1025-1191.
DR PDB; 5S2A; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S2B; X-ray; 1.11 A; A/B=1025-1191.
DR PDB; 5S2C; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S2D; X-ray; 1.06 A; A/B=1025-1191.
DR PDB; 5S2E; X-ray; 1.12 A; A/B=1025-1191.
DR PDB; 5S2F; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S2G; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S2H; X-ray; 1.07 A; A/B=1025-1191.
DR PDB; 5S2I; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S2J; X-ray; 1.11 A; A/B=1025-1191.
DR PDB; 5S2K; X-ray; 1.10 A; A/B=1025-1191.
DR PDB; 5S2L; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S2M; X-ray; 1.14 A; A/B=1025-1191.
DR PDB; 5S2N; X-ray; 1.13 A; A/B=1025-1191.
DR PDB; 5S2O; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S2P; X-ray; 1.03 A; A/B=1025-1191.
DR PDB; 5S2Q; X-ray; 1.28 A; A/B=1025-1191.
DR PDB; 5S2R; X-ray; 1.13 A; A/B=1025-1191.
DR PDB; 5S2S; X-ray; 1.10 A; A/B=1025-1191.
DR PDB; 5S2T; X-ray; 1.11 A; A/B=1025-1191.
DR PDB; 5S2U; X-ray; 1.03 A; A/B=1025-1191.
DR PDB; 5S2V; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S2W; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S2X; X-ray; 1.06 A; A/B=1025-1191.
DR PDB; 5S2Y; X-ray; 1.05 A; A/B=1025-1191.
DR PDB; 5S2Z; X-ray; 1.07 A; A/B=1025-1191.
DR PDB; 5S30; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S31; X-ray; 1.15 A; A/B=1025-1191.
DR PDB; 5S32; X-ray; 1.17 A; A/B=1025-1191.
DR PDB; 5S33; X-ray; 1.06 A; A/B=1025-1191.
DR PDB; 5S34; X-ray; 1.06 A; A/B=1025-1191.
DR PDB; 5S35; X-ray; 1.10 A; A/B=1025-1191.
DR PDB; 5S36; X-ray; 1.06 A; A/B=1025-1191.
DR PDB; 5S37; X-ray; 1.22 A; A/B=1025-1191.
DR PDB; 5S38; X-ray; 1.07 A; A/B=1025-1191.
DR PDB; 5S39; X-ray; 1.16 A; A/B=1025-1191.
DR PDB; 5S3A; X-ray; 1.18 A; A/B=1025-1191.
DR PDB; 5S3B; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S3C; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S3D; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S3E; X-ray; 1.05 A; A/B=1025-1191.
DR PDB; 5S3F; X-ray; 1.16 A; A/B=1025-1191.
DR PDB; 5S3G; X-ray; 1.14 A; A/B=1025-1191.
DR PDB; 5S3H; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S3I; X-ray; 1.17 A; A/B=1025-1191.
DR PDB; 5S3J; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S3K; X-ray; 1.17 A; A/B=1025-1191.
DR PDB; 5S3L; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S3M; X-ray; 1.26 A; A/B=1025-1191.
DR PDB; 5S3N; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S3O; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S3P; X-ray; 1.10 A; A/B=1025-1191.
DR PDB; 5S3Q; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S3R; X-ray; 1.04 A; A/B=1025-1191.
DR PDB; 5S3S; X-ray; 1.04 A; A/B=1025-1191.
DR PDB; 5S3T; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S3U; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S3V; X-ray; 1.12 A; A/B=1025-1191.
DR PDB; 5S3W; X-ray; 0.99 A; A/B=1025-1191.
DR PDB; 5S3X; X-ray; 1.13 A; A/B=1025-1191.
DR PDB; 5S3Y; X-ray; 1.11 A; A/B=1025-1191.
DR PDB; 5S3Z; X-ray; 1.31 A; A/B=1025-1191.
DR PDB; 5S40; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S41; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S42; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S43; X-ray; 1.11 A; A/B=1025-1191.
DR PDB; 5S44; X-ray; 1.06 A; A/B=1025-1191.
DR PDB; 5S45; X-ray; 1.16 A; A/B=1025-1191.
DR PDB; 5S46; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S47; X-ray; 1.09 A; A/B=1025-1191.
DR PDB; 5S48; X-ray; 1.07 A; A/B=1025-1191.
DR PDB; 5S49; X-ray; 1.03 A; A/B=1025-1191.
DR PDB; 5S4A; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S4B; X-ray; 1.19 A; A/B=1025-1191.
DR PDB; 5S4C; X-ray; 1.01 A; A/B=1025-1191.
DR PDB; 5S4D; X-ray; 1.22 A; A/B=1025-1191.
DR PDB; 5S4E; X-ray; 1.07 A; A/B=1025-1191.
DR PDB; 5S4F; X-ray; 1.13 A; A/B=1025-1191.
DR PDB; 5S4G; X-ray; 1.17 A; A/B=1025-1191.
DR PDB; 5S4H; X-ray; 1.18 A; A/B=1025-1191.
DR PDB; 5S4I; X-ray; 1.13 A; A/B=1025-1191.
DR PDB; 5S4J; X-ray; 1.12 A; A/B=1025-1191.
DR PDB; 5S4K; X-ray; 1.08 A; A/B=1025-1191.
DR PDB; 5S6X; X-ray; 2.32 A; A/B=6453-6798.
DR PDB; 5S6Y; X-ray; 2.32 A; A/B=6453-6798.
DR PDB; 5S6Z; X-ray; 2.28 A; A/B=6453-6798.
DR PDB; 5S70; X-ray; 2.33 A; A/B=6453-6798.
DR PDB; 5S71; X-ray; 1.94 A; A/B=6453-6798.
DR PDB; 5S72; X-ray; 2.51 A; A/B=6453-6798.
DR PDB; 5S73; X-ray; 1.06 A; A/B=1025-1191.
DR PDB; 5S74; X-ray; 0.96 A; A/B=1025-1191.
DR PDB; 5SA4; X-ray; 2.05 A; A/B=6453-6798.
DR PDB; 5SA5; X-ray; 2.09 A; A/B=6453-6798.
DR PDB; 5SA6; X-ray; 2.52 A; A/B=6453-6798.
DR PDB; 5SA7; X-ray; 2.22 A; A/B=6453-6798.
DR PDB; 5SA8; X-ray; 2.30 A; A/B=6453-6798.
DR PDB; 5SA9; X-ray; 1.92 A; A/B=6453-6798.
DR PDB; 5SAA; X-ray; 2.24 A; A/B=6453-6798.
DR PDB; 5SAB; X-ray; 2.49 A; A/B=6453-6798.
DR PDB; 5SAC; X-ray; 2.03 A; A/B=6453-6798.
DR PDB; 5SAD; X-ray; 1.96 A; A/B=6453-6798.
DR PDB; 5SAE; X-ray; 2.12 A; A/B=6453-6798.
DR PDB; 5SAF; X-ray; 2.11 A; A/B=6453-6798.
DR PDB; 5SAG; X-ray; 1.88 A; A/B=6453-6798.
DR PDB; 5SAH; X-ray; 2.16 A; A/B=6453-6798.
DR PDB; 5SAI; X-ray; 2.02 A; A/B=6453-6798.
DR PDB; 5SBF; X-ray; 1.64 A; A/B=6453-6798.
DR PDB; 5SKW; X-ray; 2.09 A; D=5932-6452.
DR PDB; 5SKX; X-ray; 2.34 A; D=5932-6452.
DR PDB; 5SKY; X-ray; 2.25 A; D=5932-6452.
DR PDB; 5SKZ; X-ray; 1.96 A; D=5932-6452.
DR PDB; 5SL0; X-ray; 2.00 A; D=5932-6452.
DR PDB; 5SL1; X-ray; 2.38 A; D=5932-6452.
DR PDB; 5SL2; X-ray; 1.74 A; D=5932-6452.
DR PDB; 5SL3; X-ray; 1.99 A; D=5932-6452.
DR PDB; 5SL4; X-ray; 1.94 A; D=5932-6452.
DR PDB; 5SL5; X-ray; 2.36 A; D=5932-6452.
DR PDB; 5SL6; X-ray; 2.29 A; D=5932-6452.
DR PDB; 5SL7; X-ray; 1.84 A; D=5932-6452.
DR PDB; 5SL8; X-ray; 2.07 A; D=5932-6452.
DR PDB; 5SL9; X-ray; 1.75 A; D=5932-6452.
DR PDB; 5SLA; X-ray; 1.70 A; D=5932-6452.
DR PDB; 5SLB; X-ray; 1.80 A; D=5932-6452.
DR PDB; 5SLC; X-ray; 1.67 A; D=5932-6452.
DR PDB; 5SLD; X-ray; 1.58 A; D=5932-6452.
DR PDB; 5SLE; X-ray; 2.01 A; D=5932-6452.
DR PDB; 5SLF; X-ray; 2.01 A; D=5932-6452.
DR PDB; 5SLG; X-ray; 1.97 A; D=5932-6452.
DR PDB; 5SLH; X-ray; 1.82 A; D=5932-6452.
DR PDB; 5SLI; X-ray; 2.30 A; D=5932-6452.
DR PDB; 5SLJ; X-ray; 2.31 A; D=5932-6452.
DR PDB; 5SLK; X-ray; 2.21 A; D=5932-6452.
DR PDB; 5SLL; X-ray; 1.81 A; D=5932-6452.
DR PDB; 5SLM; X-ray; 2.05 A; D=5932-6452.
DR PDB; 5SLN; X-ray; 2.21 A; D=5932-6452.
DR PDB; 5SLO; X-ray; 1.83 A; D=5932-6452.
DR PDB; 5SLP; X-ray; 1.82 A; D=5932-6452.
DR PDB; 5SLQ; X-ray; 2.11 A; D=5932-6452.
DR PDB; 5SLR; X-ray; 1.86 A; D=5932-6452.
DR PDB; 5SLS; X-ray; 2.29 A; D=5932-6452.
DR PDB; 5SLT; X-ray; 1.90 A; D=5932-6452.
DR PDB; 5SLU; X-ray; 2.09 A; D=5932-6452.
DR PDB; 5SLV; X-ray; 2.05 A; D=5932-6452.
DR PDB; 5SLW; X-ray; 2.05 A; D=5932-6452.
DR PDB; 5SLX; X-ray; 1.76 A; D=5932-6452.
DR PDB; 5SLY; X-ray; 2.02 A; D=5932-6452.
DR PDB; 5SLZ; X-ray; 2.54 A; D=5932-6452.
DR PDB; 5SM0; X-ray; 2.09 A; D=5932-6452.
DR PDB; 5SM1; X-ray; 1.94 A; D=5932-6452.
DR PDB; 5SM2; X-ray; 1.78 A; D=5932-6452.
DR PDB; 5SM3; X-ray; 2.20 A; D=5932-6452.
DR PDB; 5SM4; X-ray; 2.16 A; D=5932-6452.
DR PDB; 5SM5; X-ray; 1.95 A; D=5932-6452.
DR PDB; 5SM6; X-ray; 2.29 A; D=5932-6452.
DR PDB; 5SM7; X-ray; 1.95 A; D=5932-6452.
DR PDB; 5SM8; X-ray; 1.95 A; D=5932-6452.
DR PDB; 5SM9; X-ray; 2.01 A; D=5932-6452.
DR PDB; 5SMA; X-ray; 2.01 A; D=5932-6452.
DR PDB; 5SMB; X-ray; 2.18 A; D=5932-6452.
DR PDB; 5SMC; X-ray; 2.19 A; D=5932-6452.
DR PDB; 5SMD; X-ray; 1.83 A; D=5932-6452.
DR PDB; 5SME; X-ray; 1.91 A; D=5932-6452.
DR PDB; 5SMF; X-ray; 2.01 A; D=5932-6452.
DR PDB; 5SMG; X-ray; 1.87 A; D=5932-6452.
DR PDB; 5SMH; X-ray; 2.64 A; D=5932-6452.
DR PDB; 5SMI; X-ray; 2.08 A; D=5932-6452.
DR PDB; 5SMK; X-ray; 1.65 A; D=5932-6452.
DR PDB; 6LU7; X-ray; 2.16 A; A=3264-3569.
DR PDB; 6LZE; X-ray; 1.50 A; A=3264-3566.
DR PDB; 6M03; X-ray; 2.00 A; A=3264-3569.
DR PDB; 6M0K; X-ray; 1.50 A; A=3264-3567.
DR PDB; 6M2N; X-ray; 2.20 A; A/B/C/D=3264-3569.
DR PDB; 6M2Q; X-ray; 1.70 A; A=3264-3569.
DR PDB; 6M71; EM; 2.90 A; C=3860-3942, D=3943-4090, A=4393-5324.
DR PDB; 6VWW; X-ray; 2.20 A; A/B=6453-6798.
DR PDB; 6VXS; X-ray; 2.03 A; A/B=1024-1192.
DR PDB; 6W01; X-ray; 1.90 A; A/B=6453-6798.
DR PDB; 6W02; X-ray; 1.50 A; A/B=1024-1192.
DR PDB; 6W4B; X-ray; 2.95 A; A/B=4141-4253.
DR PDB; 6W4H; X-ray; 1.80 A; A=6799-7096, B=4254-4392.
DR PDB; 6W61; X-ray; 2.00 A; B=4254-4392, A=6799-7096.
DR PDB; 6W63; X-ray; 2.10 A; A=3264-3569.
DR PDB; 6W6Y; X-ray; 1.45 A; A/B=1024-1192.
DR PDB; 6W75; X-ray; 1.95 A; B/D=4254-4392, A/C=6799-7096.
DR PDB; 6W9C; X-ray; 2.70 A; A/B/C=1564-1878.
DR PDB; 6W9Q; X-ray; 2.05 A; A=4141-4253.
DR PDB; 6WC1; X-ray; 2.40 A; A/B=4141-4253.
DR PDB; 6WCF; X-ray; 1.06 A; A=1024-1192.
DR PDB; 6WEN; X-ray; 1.35 A; A=1024-1192.
DR PDB; 6WEY; X-ray; 0.95 A; A=1025-1195.
DR PDB; 6WIQ; X-ray; 2.85 A; A=3860-3942, B=4019-4140.
DR PDB; 6WJT; X-ray; 2.00 A; A/C=6799-7096, B/D=4254-4392.
DR PDB; 6WKQ; X-ray; 1.98 A; A/C=6799-7096, B/D=4254-4392.
DR PDB; 6WKS; X-ray; 1.80 A; AAA=6799-7096, BBB=4254-4392.
DR PDB; 6WLC; X-ray; 1.82 A; A/B=6453-6798.
DR PDB; 6WNP; X-ray; 1.44 A; A=3264-3569.
DR PDB; 6WOJ; X-ray; 2.20 A; A/B/C/D=1023-1197.
DR PDB; 6WQ3; X-ray; 2.10 A; A=6799-7096, B=4254-4392.
DR PDB; 6WQD; X-ray; 1.95 A; A/C=3860-3942, B/D=4019-4140.
DR PDB; 6WQF; X-ray; 2.30 A; A=3264-3569.
DR PDB; 6WRH; X-ray; 1.60 A; A=1564-1878.
DR PDB; 6WRZ; X-ray; 2.25 A; A=6799-7096, B=4254-4392.
DR PDB; 6WTC; X-ray; 1.85 A; A/C=3860-3942, B/D=4019-4140.
DR PDB; 6WTJ; X-ray; 1.90 A; A=3264-3569.
DR PDB; 6WTK; X-ray; 2.00 A; A=3264-3569.
DR PDB; 6WTM; X-ray; 1.85 A; A/B=3264-3569.
DR PDB; 6WTT; X-ray; 2.15 A; A/B/C=3264-3567.
DR PDB; 6WUU; X-ray; 2.79 A; A/B/C/D=1562-1879.
DR PDB; 6WVN; X-ray; 2.00 A; A=6799-7096, B=4254-4392.
DR PDB; 6WX4; X-ray; 1.66 A; D=1562-1879.
DR PDB; 6WXC; X-ray; 1.85 A; A/B=6453-6798.
DR PDB; 6WXD; X-ray; 2.00 A; A/B=4141-4253.
DR PDB; 6WZU; X-ray; 1.79 A; A=1564-1878.
DR PDB; 6X1B; X-ray; 1.97 A; A/B=6453-6798.
DR PDB; 6X4I; X-ray; 1.85 A; A/B=6453-6798.
DR PDB; 6XA4; X-ray; 1.65 A; A=3264-3569.
DR PDB; 6XA9; X-ray; 2.90 A; A/C/E=1563-1878.
DR PDB; 6XAA; X-ray; 2.70 A; A=1563-1878.
DR PDB; 6XB0; X-ray; 1.80 A; A=3264-3569.
DR PDB; 6XB1; X-ray; 1.80 A; A=3264-3569.
DR PDB; 6XB2; X-ray; 2.10 A; A=3264-3569.
DR PDB; 6XBG; X-ray; 1.45 A; A/B=3264-3569.
DR PDB; 6XBH; X-ray; 1.60 A; A=3264-3569.
DR PDB; 6XBI; X-ray; 1.70 A; A/B=3264-3569.
DR PDB; 6XCH; X-ray; 2.20 A; A=3264-3569.
DR PDB; 6XDH; X-ray; 2.35 A; A/B=6453-6798.
DR PDB; 6XFN; X-ray; 1.70 A; A=3264-3569.
DR PDB; 6XG3; X-ray; 2.48 A; A=1564-1878.
DR PDB; 6XHM; X-ray; 1.41 A; A/B=3264-3569.
DR PDB; 6XHU; X-ray; 1.80 A; A/C=3264-3569.
DR PDB; 6XIP; X-ray; 1.50 A; A/C=3860-3942, B/D=4019-4140.
DR PDB; 6XKF; X-ray; 1.80 A; A/B=3264-3569.
DR PDB; 6XKH; X-ray; 1.28 A; A=3264-3569.
DR PDB; 6XKM; X-ray; 2.25 A; A=6799-7096, B=4254-4392.
DR PDB; 6XMK; X-ray; 1.70 A; A/B=3264-3568.
DR PDB; 6XOA; X-ray; 2.10 A; A/B/C/D=3264-3569.
DR PDB; 6XQS; X-ray; 1.90 A; A=3264-3569.
DR PDB; 6XQT; X-ray; 2.30 A; A/B=3264-3569.
DR PDB; 6XQU; X-ray; 2.20 A; A=3264-3569.
DR PDB; 6XR3; X-ray; 1.45 A; A=3264-3569.
DR PDB; 6Y2E; X-ray; 1.75 A; A=3264-3569.
DR PDB; 6Y2F; X-ray; 2.16 A; A=3264-3569.
DR PDB; 6Y2G; X-ray; 2.16 A; A=3264-3569.
DR PDB; 6Y84; X-ray; 1.39 A; A=3264-3569.
DR PDB; 6YB7; X-ray; 1.25 A; A=3264-3569.
DR PDB; 6YNQ; X-ray; 1.80 A; A=3264-3569.
DR PDB; 6YVA; X-ray; 3.18 A; A=1564-1878.
DR PDB; 6YVF; X-ray; 1.60 A; A=3264-3569.
DR PDB; 6YWK; X-ray; 2.20 A; A/B/C/D/E=1025-1194.
DR PDB; 6YWL; X-ray; 2.50 A; A/B/C/D/E=1025-1194.
DR PDB; 6YWM; X-ray; 2.16 A; A/B/C=1025-1194.
DR PDB; 6YYT; EM; 2.90 A; A=4424-5321, B=3948-4133, C=3860-3932.
DR PDB; 6YZ1; X-ray; 2.40 A; A=6798-7096, B=4263-4384.
DR PDB; 6Z2E; X-ray; 1.70 A; AAA=3264-3569.
DR PDB; 6Z5T; X-ray; 1.57 A; A/B=1024-1197.
DR PDB; 6Z6I; X-ray; 2.00 A; A/B/C/D=1024-1197.
DR PDB; 6Z72; X-ray; 2.30 A; A/B/C/D=1024-1197.
DR PDB; 6ZCT; X-ray; 2.55 A; A=4263-4384.
DR PDB; 6ZLW; EM; 2.60 A; i=1-180.
DR PDB; 6ZM7; EM; 2.70 A; CF=1-180.
DR PDB; 6ZME; EM; 3.00 A; CF=1-180.
DR PDB; 6ZMI; EM; 2.60 A; i=1-180.
DR PDB; 6ZMO; EM; 3.10 A; i=1-180.
DR PDB; 6ZMT; EM; 3.00 A; i=1-180.
DR PDB; 6ZN5; EM; 3.20 A; i=1-180.
DR PDB; 6ZOJ; EM; 2.80 A; j=1-180.
DR PDB; 6ZOK; EM; 2.80 A; j=1-180.
DR PDB; 6ZON; EM; 3.00 A; J=1-180.
DR PDB; 6ZP4; EM; 2.90 A; J=1-180.
DR PDB; 6ZPE; X-ray; 1.58 A; A=4263-4384.
DR PDB; 6ZRT; X-ray; 2.10 A; A=3264-3569.
DR PDB; 6ZRU; X-ray; 2.10 A; A=3264-3569.
DR PDB; 6ZSL; X-ray; 1.94 A; A/B=5325-5925.
DR PDB; 7A1U; X-ray; 1.67 A; A=3264-3569.
DR PDB; 7ABU; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7ADW; X-ray; 1.63 A; A=3264-3569.
DR PDB; 7AEG; X-ray; 1.70 A; A=3264-3568.
DR PDB; 7AEH; X-ray; 1.30 A; A=3264-3568.
DR PDB; 7AF0; X-ray; 1.70 A; A=3264-3569.
DR PDB; 7AGA; X-ray; 1.68 A; A=3264-3569.
DR PDB; 7AHA; X-ray; 1.68 A; A=3264-3569.
DR PDB; 7AK4; X-ray; 1.63 A; AA=3264-3569.
DR PDB; 7AKU; X-ray; 2.50 A; A=3264-3568.
DR PDB; 7ALH; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7ALI; X-ray; 1.65 A; A/B=3264-3569.
DR PDB; 7AMJ; X-ray; 1.59 A; A=3264-3569.
DR PDB; 7ANS; X-ray; 1.70 A; A=3264-3569.
DR PDB; 7AOL; X-ray; 1.47 A; A=3264-3569.
DR PDB; 7AP6; X-ray; 1.78 A; A=3264-3569.
DR PDB; 7APH; X-ray; 1.65 A; AA=3264-3569.
DR PDB; 7AQE; X-ray; 1.39 A; A=3264-3569.
DR PDB; 7AQI; X-ray; 1.70 A; A=3264-3569.
DR PDB; 7AQJ; X-ray; 2.59 A; A=3264-3569.
DR PDB; 7AR5; X-ray; 1.40 A; A=3264-3569.
DR PDB; 7AR6; X-ray; 1.40 A; A=3264-3569.
DR PDB; 7ARF; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7AU4; X-ray; 1.82 A; A=3264-3569.
DR PDB; 7AVD; X-ray; 1.80 A; A/B=3264-3569.
DR PDB; 7AWR; X-ray; 1.34 A; A=3264-3569.
DR PDB; 7AWS; X-ray; 1.81 A; A=3264-3569.
DR PDB; 7AWU; X-ray; 2.07 A; A=3264-3569.
DR PDB; 7AWW; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7AX6; X-ray; 1.95 A; A=3264-3569.
DR PDB; 7AXM; X-ray; 1.40 A; A=3264-3569.
DR PDB; 7AXO; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7AY7; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7B2J; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7B2U; X-ray; 1.55 A; A/B=3264-3569.
DR PDB; 7B3E; X-ray; 1.77 A; A/B=3264-3569.
DR PDB; 7B5Z; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7B77; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7B83; X-ray; 1.80 A; A=3264-3569.
DR PDB; 7BAJ; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7BAK; X-ray; 2.05 A; A=3264-3569.
DR PDB; 7BAL; X-ray; 1.85 A; A=3264-3569.
DR PDB; 7BB2; X-ray; 1.60 A; A/B=3264-3569.
DR PDB; 7BE7; X-ray; 1.68 A; A/B=3264-3569.
DR PDB; 7BF3; X-ray; 2.00 A; A/B/C/D/E=1025-1194.
DR PDB; 7BF4; X-ray; 1.55 A; A=1025-1194.
DR PDB; 7BF5; X-ray; 2.05 A; A/B/C/D/E=1025-1194.
DR PDB; 7BF6; X-ray; 2.15 A; A/B/C=1025-1194.
DR PDB; 7BFB; X-ray; 2.05 A; A/B=3264-3569.
DR PDB; 7BGP; X-ray; 1.68 A; A/B=3264-3569.
DR PDB; 7BIJ; X-ray; 1.47 A; AAA=3264-3569.
DR PDB; 7BQ7; X-ray; 2.37 A; A=6799-7096, B=4254-4392.
DR PDB; 7BQY; X-ray; 1.70 A; A=3264-3569.
DR PDB; 7BRO; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7BRP; X-ray; 1.80 A; A/B=3264-3569.
DR PDB; 7BTF; EM; 2.95 A; A=4393-5324, B=3943-4090, C=3860-3942.
DR PDB; 7BUY; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7BV1; EM; 2.80 A; C=3860-3942, B=3943-4140, A=4393-5324.
DR PDB; 7BV2; EM; 2.50 A; C=3860-3942, B=3943-4140, A=4393-5324.
DR PDB; 7BWQ; X-ray; 2.95 A; A/B/C/D/E/F=4141-4253.
DR PDB; 7BZF; EM; 3.26 A; A=4393-5324, B=3943-4140, D=3943-4140, E=3860-3942.
DR PDB; 7C2I; X-ray; 2.50 A; A=6799-7096, B=4254-4392.
DR PDB; 7C2J; X-ray; 2.80 A; A=6799-7096, B=4254-4392.
DR PDB; 7C2K; EM; 2.93 A; A=4393-5324, B=3943-4140, D=3943-4140, E=3860-3942.
DR PDB; 7C2Q; X-ray; 1.93 A; A/B=3266-3561.
DR PDB; 7C2Y; X-ray; 1.91 A; A/B=3264-3561.
DR PDB; 7C6S; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7C6U; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7C7P; X-ray; 1.74 A; A/B=3264-3569.
DR PDB; 7C8B; X-ray; 2.20 A; A=3264-3569.
DR PDB; 7C8R; X-ray; 2.30 A; A=3264-3569.
DR PDB; 7C8T; X-ray; 2.05 A; A=3264-3569.
DR PDB; 7C8U; X-ray; 2.35 A; A=3264-3569.
DR PDB; 7CA8; X-ray; 2.45 A; A/B=3264-3561.
DR PDB; 7CAM; X-ray; 2.85 A; A/B=3264-3569.
DR PDB; 7CB7; X-ray; 1.69 A; A/B=3264-3569.
DR PDB; 7CBT; X-ray; 2.35 A; A/B=3264-3569.
DR PDB; 7CJD; X-ray; 2.50 A; A/B/C/D=1564-1881.
DR PDB; 7CJM; X-ray; 3.20 A; B=1564-1878.
DR PDB; 7CMD; X-ray; 2.59 A; A/B/C/D=1564-1881.
DR PDB; 7COM; X-ray; 2.25 A; A/B=3264-3569.
DR PDB; 7CUT; X-ray; 1.82 A; A=3264-3569.
DR PDB; 7CUU; X-ray; 1.68 A; A/B=3264-3569.
DR PDB; 7CWB; X-ray; 1.90 A; A=3264-3569.
DR PDB; 7CWC; X-ray; 2.10 A; A/B=3264-3569.
DR PDB; 7CX9; X-ray; 1.73 A; A=3264-3569.
DR PDB; 7D1M; X-ray; 1.35 A; A/B=3264-3569.
DR PDB; 7D1O; X-ray; 1.78 A; A=3264-3569.
DR PDB; 7D7K; X-ray; 1.90 A; A/B=1567-1878.
DR PDB; 7D7L; X-ray; 2.11 A; A/B=1567-1878.
DR PDB; 7DDC; X-ray; 2.17 A; A=3264-3569.
DR PDB; 7DG6; X-ray; 2.40 A; A=3264-3565.
DR PDB; 7DIY; X-ray; 2.69 A; A=4254-4392, B=5926-6214.
DR PDB; 7DVX; X-ray; 1.80 A; A=3264-3569, C=3850-3869.
DR PDB; 7DVY; X-ray; 1.80 A; A=3264-3569, C=4244-4263.
DR PDB; 7DW0; X-ray; 1.81 A; A=3264-3569, C=6443-6462.
DR PDB; 7DW6; X-ray; 1.70 A; A=3264-3569, C=6789-6808.
DR PDB; 7E18; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7E19; X-ray; 2.15 A; A=3264-3569.
DR PDB; 7E5X; X-ray; 2.19 A; A/B/C/D=3264-3569.
DR PDB; 7E6K; X-ray; 1.60 A; A=3264-3568.
DR PDB; 7EQ4; X-ray; 1.25 A; A=11-125.
DR PDB; 7JFQ; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7JHE; X-ray; 2.25 A; A=6799-7096, B=4254-4392.
DR PDB; 7JIB; X-ray; 2.65 A; A=6799-7096, B=4254-4392.
DR PDB; 7JKV; X-ray; 1.25 A; A/B=3264-3569.
DR PDB; 7JME; X-ray; 1.55 A; A=1025-1195.
DR PDB; 7JOY; X-ray; 2.00 A; A/B=3264-3569.
DR PDB; 7JP0; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7JP1; X-ray; 1.80 A; A=3264-3569.
DR PDB; 7JPE; X-ray; 2.18 A; A=6799-7096, B=4254-4392.
DR PDB; 7JPY; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7JPZ; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7JQ0; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7JQ1; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7JQ2; X-ray; 1.40 A; A=3264-3569.
DR PDB; 7JQ3; X-ray; 2.10 A; A=3264-3569.
DR PDB; 7JQ4; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7JQ5; X-ray; 1.90 A; A=3264-3569.
DR PDB; 7JQB; EM; 2.70 A; F=145-180.
DR PDB; 7JQC; EM; 3.30 A; F=145-180.
DR PDB; 7JR3; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7JR4; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7JST; X-ray; 1.85 A; A=3264-3569.
DR PDB; 7JSU; X-ray; 1.83 A; A=3264-3569.
DR PDB; 7JT0; X-ray; 1.73 A; A=3264-3569.
DR PDB; 7JT7; X-ray; 1.94 A; A=3264-3569.
DR PDB; 7JU7; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7JUN; Other; 2.30 A; A=3264-3569.
DR PDB; 7JVZ; X-ray; 2.50 A; A=3264-3569.
DR PDB; 7JW8; X-ray; 1.84 A; A/B/C/D=3264-3569.
DR PDB; 7JYC; X-ray; 1.79 A; A=3264-3569.
DR PDB; 7JYY; X-ray; 2.05 A; A/C=6799-7096, B/D=4254-4392.
DR PDB; 7JZ0; X-ray; 2.15 A; A/C=6799-7096, B/D=4254-4392.
DR PDB; 7K0E; X-ray; 1.90 A; A/B=3264-3568.
DR PDB; 7K0F; X-ray; 1.65 A; A/B=3264-3568.
DR PDB; 7K0R; EM; 3.30 A; A/B/C/D/E/F=6453-6798.
DR PDB; 7K1L; X-ray; 2.25 A; A/B=6453-6798.
DR PDB; 7K1O; X-ray; 2.40 A; A/B/C=6453-6798.
DR PDB; 7K3N; X-ray; 1.65 A; A=1-180.
DR PDB; 7K3T; X-ray; 1.20 A; A=3264-3569.
DR PDB; 7K40; X-ray; 1.35 A; A=3264-3569.
DR PDB; 7K5I; EM; 2.90 A; 1=1-180.
DR PDB; 7K6D; X-ray; 1.48 A; A=3264-3569.
DR PDB; 7K6E; X-ray; 1.63 A; A=3264-3569.
DR PDB; 7K7P; X-ray; 1.77 A; B=10-127.
DR PDB; 7K9P; X-ray; 2.60 A; A/B=6453-6798.
DR PDB; 7KAG; X-ray; 3.21 A; A/B=819-929.
DR PDB; 7KEG; X-ray; 2.90 A; A/B=6453-6798.
DR PDB; 7KEH; X-ray; 2.59 A; A/B=6453-6798.
DR PDB; 7KF4; X-ray; 2.61 A; A/B/C/D/E/F=6453-6798.
DR PDB; 7KFI; X-ray; 1.60 A; A/B=3264-3569.
DR PDB; 7KG3; X-ray; 1.45 A; A=1025-1191.
DR PDB; 7KHP; X-ray; 1.95 A; A/B=3264-3569.
DR PDB; 7KOA; X-ray; 2.40 A; A=6799-7096, B=4254-4392.
DR PDB; 7KPH; X-ray; 1.46 A; A=3264-3569.
DR PDB; 7KQO; X-ray; 0.85 A; A/B=1025-1191.
DR PDB; 7KQP; X-ray; 0.88 A; A/B=1025-1191.
DR PDB; 7KQW; X-ray; 0.93 A; A=1024-1192.
DR PDB; 7KR0; X-ray; 0.77 A; A=1024-1192.
DR PDB; 7KR1; X-ray; 1.55 A; A=1024-1192.
DR PDB; 7KRI; X-ray; 1.58 A; A/B/C=4141-4253.
DR PDB; 7KVL; X-ray; 2.09 A; A/B=3264-3569.
DR PDB; 7KVR; X-ray; 2.12 A; A/B=3264-3569.
DR PDB; 7KX5; X-ray; 2.60 A; A=3264-3569.
DR PDB; 7KXB; X-ray; 1.55 A; A=1025-1191.
DR PDB; 7KYU; X-ray; 1.48 A; A=3264-3569.
DR PDB; 7L0D; X-ray; 2.39 A; A=3264-3569.
DR PDB; 7L10; X-ray; 1.63 A; A=3264-3569.
DR PDB; 7L11; X-ray; 1.80 A; A/B=3264-3569.
DR PDB; 7L12; X-ray; 1.80 A; A=3264-3569.
DR PDB; 7L13; X-ray; 2.17 A; A/B=3264-3569.
DR PDB; 7L14; X-ray; 1.80 A; A/B=3264-3569.
DR PDB; 7L1F; EM; 3.89 A; A=4424-5321, C=4020-4133, D=3861-3923.
DR PDB; 7L5D; X-ray; 1.58 A; A=3264-3569.
DR PDB; 7L6R; X-ray; 1.98 A; A=6799-7096, B=4254-4392.
DR PDB; 7L6T; X-ray; 1.78 A; A=6799-7096, B=4254-4392.
DR PDB; 7L8I; X-ray; 2.10 A; A/B=3264-3569.
DR PDB; 7L8J; X-ray; 2.45 A; A=3264-3569.
DR PDB; 7LB7; Other; 2.00 A; A=3264-3569.
DR PDB; 7LBN; X-ray; 1.76 A; A=3264-3569.
DR PDB; 7LBR; X-ray; 2.20 A; A/B=1564-1878.
DR PDB; 7LBS; X-ray; 2.80 A; A/B=1564-1878.
DR PDB; 7LCO; X-ray; 1.90 A; A=3264-3569.
DR PDB; 7LCS; X-ray; 1.85 A; A=3264-3569.
DR PDB; 7LCT; X-ray; 1.93 A; A=3264-3569.
DR PDB; 7LDL; X-ray; 2.00 A; A/B=3264-3569.
DR PDB; 7LDX; X-ray; 2.23 A; A/B=3264-3569.
DR PDB; 7LFE; X-ray; 2.79 A; A/B=3264-3569.
DR PDB; 7LFP; X-ray; 2.20 A; A/B=3264-3569.
DR PDB; 7LFZ; X-ray; 1.90 A; C=5916-5924.
DR PDB; 7LG2; X-ray; 2.40 A; C=4094-4102.
DR PDB; 7LG3; X-ray; 2.30 A; C=3886-3894.
DR PDB; 7LG7; X-ray; 2.30 A; A=1025-1191.
DR PDB; 7LGO; X-ray; 2.45 A; A/B=1907-2021.
DR PDB; 7LHQ; NMR; -; A=3860-3942.
DR PDB; 7LKD; X-ray; 2.01 A; A/B=3264-3569.
DR PDB; 7LKE; X-ray; 2.69 A; A=3264-3569.
DR PDB; 7LKR; X-ray; 1.65 A; A/B=3264-3568.
DR PDB; 7LKS; X-ray; 1.70 A; A/B=3264-3568.
DR PDB; 7LKT; X-ray; 1.50 A; A/B=3264-3568.
DR PDB; 7LKU; X-ray; 1.65 A; A/B=3264-3568.
DR PDB; 7LKV; X-ray; 1.55 A; A/B=3264-3568.
DR PDB; 7LKW; X-ray; 1.70 A; A/B=3264-3568.
DR PDB; 7LKX; X-ray; 1.60 A; A/B=3264-3568.
DR PDB; 7LLF; X-ray; 2.30 A; A/B=1564-1878.
DR PDB; 7LLZ; X-ray; 2.90 A; A/B=1564-1878.
DR PDB; 7LMD; X-ray; 1.96 A; A=3264-3569.
DR PDB; 7LME; X-ray; 2.10 A; A/B=3264-3569.
DR PDB; 7LMF; X-ray; 2.20 A; A/B=3264-3569.
DR PDB; 7LOS; X-ray; 2.90 A; A/B=1564-1878.
DR PDB; 7LTJ; X-ray; 1.80 A; A=3264-3569.
DR PDB; 7LTN; X-ray; 1.79 A; A=3264-3569.
DR PDB; 7LW3; X-ray; 2.30 A; A=6799-7096, B=4254-4392.
DR PDB; 7LW4; X-ray; 2.50 A; A=6799-7096, B=4254-4392.
DR PDB; 7LYH; X-ray; 1.90 A; A=3264-3569.
DR PDB; 7LYI; X-ray; 1.90 A; A=3264-3569.
DR PDB; 7LZT; X-ray; 1.55 A; A=3264-3568.
DR PDB; 7LZU; X-ray; 1.60 A; A/B=3264-3568.
DR PDB; 7LZV; X-ray; 1.60 A; A/B=3264-3568.
DR PDB; 7LZW; X-ray; 2.20 A; A/B=3264-3568.
DR PDB; 7LZX; X-ray; 1.65 A; A/B=3264-3568.
DR PDB; 7LZY; X-ray; 1.85 A; A=3264-3568.
DR PDB; 7LZZ; X-ray; 2.00 A; A=3264-3568.
DR PDB; 7M00; X-ray; 2.00 A; A/B=3264-3568.
DR PDB; 7M01; X-ray; 1.65 A; A/B=3264-3568.
DR PDB; 7M02; X-ray; 1.80 A; A/B=3264-3568.
DR PDB; 7M03; X-ray; 2.00 A; A/B=3264-3568.
DR PDB; 7M04; X-ray; 1.75 A; A/B=3264-3568.
DR PDB; 7M2P; X-ray; 1.70 A; A=3264-3569.
DR PDB; 7M8M; X-ray; 1.78 A; A/B=3264-3569.
DR PDB; 7M8N; X-ray; 1.96 A; A/B=3264-3569.
DR PDB; 7M8O; X-ray; 2.44 A; A/B=3264-3569.
DR PDB; 7M8P; X-ray; 2.23 A; A/B=3264-3569.
DR PDB; 7M8X; X-ray; 1.74 A; A=3264-3569.
DR PDB; 7M8Y; X-ray; 1.75 A; A=3264-3569.
DR PDB; 7M8Z; X-ray; 1.79 A; A=3264-3569.
DR PDB; 7M90; X-ray; 2.19 A; A=3264-3569.
DR PDB; 7M91; X-ray; 1.95 A; A=3264-3569.
DR PDB; 7MBG; X-ray; 1.86 A; A/B=3264-3569.
DR PDB; 7MBI; X-ray; 2.15 A; A/B/C/D=3264-3569.
DR PDB; 7MC5; X-ray; 1.64 A; A=5928-6214, M=4253-4392.
DR PDB; 7MC6; X-ray; 2.10 A; A=5926-6214, M=4253-4392.
DR PDB; 7ME0; EM; 2.48 A; A/B/C/D/E/F=6453-6798.
DR PDB; 7MGR; X-ray; 1.94 A; A=3264-3569.
DR PDB; 7MGS; X-ray; 1.84 A; A=3264-3569.
DR PDB; 7MHF; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7MHG; X-ray; 1.53 A; A=3264-3569.
DR PDB; 7MHH; X-ray; 2.19 A; A=3264-3569.
DR PDB; 7MHI; X-ray; 1.88 A; A=3264-3569.
DR PDB; 7MHJ; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7MHK; X-ray; 1.96 A; A=3264-3569.
DR PDB; 7MHL; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7MHM; X-ray; 1.53 A; A=3264-3569.
DR PDB; 7MHN; X-ray; 2.19 A; A=3264-3569.
DR PDB; 7MHO; X-ray; 1.88 A; A=3264-3569.
DR PDB; 7MHP; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7MHQ; X-ray; 1.96 A; A=3264-3569.
DR PDB; 7MLF; X-ray; 2.60 A; A=3264-3567.
DR PDB; 7MLG; X-ray; 2.50 A; A=3264-3569.
DR PDB; 7MNG; X-ray; 1.70 A; A=3264-3569.
DR PDB; 7MPB; X-ray; 2.30 A; A/B=3264-3569.
DR PDB; 7MRR; X-ray; 2.32 A; A=3264-3569.
DR PDB; 7MSW; EM; 3.76 A; A=181-818.
DR PDB; 7MSX; EM; 3.15 A; A=181-818.
DR PDB; 7N06; EM; 2.20 A; A/B/C/D/E/F=6453-6797.
DR PDB; 7N0B; EM; 3.90 A; A=4254-4392, B=5926-6452.
DR PDB; 7N0C; EM; 3.40 A; A=4254-4392, B=5926-6452.
DR PDB; 7N0D; EM; 2.50 A; A/C/E/G=4254-4392, B/D/F/H=5926-6452.
DR PDB; 7N33; EM; 2.50 A; A/B/C/D/E/F=6453-6796.
DR PDB; 7N3K; X-ray; 3.00 A; A/B/C/D/E/F/G/H=4141-4253.
DR PDB; 7N44; X-ray; 1.94 A; A=3264-3569.
DR PDB; 7N5Z; X-ray; 1.76 A; A=3264-3569.
DR PDB; 7N6N; X-ray; 2.80 A; A/B=3259-3569, C=3259-3263.
DR PDB; 7N7R; X-ray; 2.01 A; A/B=6453-6798.
DR PDB; 7N7U; X-ray; 2.06 A; A/B=6453-6798.
DR PDB; 7N7W; X-ray; 2.42 A; A/B=6453-6798.
DR PDB; 7N7Y; X-ray; 2.09 A; A/B=6453-6798.
DR PDB; 7N83; X-ray; 1.91 A; A/B=6453-6798.
DR PDB; 7N89; X-ray; 2.00 A; A/B=3264-3569.
DR PDB; 7N8C; Other; 2.20 A; A=3264-3569.
DR PDB; 7NBR; X-ray; 2.40 A; AAA=3264-3569.
DR PDB; 7NBS; X-ray; 1.70 A; AAA=3264-3569.
DR PDB; 7NBT; X-ray; 1.63 A; AAA=3264-3569.
DR PDB; 7NBY; X-ray; 1.93 A; A/B=3264-3569.
DR PDB; 7NEO; X-ray; 1.64 A; AAA/BBB=3264-3569.
DR PDB; 7NEV; X-ray; 1.70 A; A=3264-3569.
DR PDB; 7NF5; X-ray; 1.94 A; A=3264-3569.
DR PDB; 7NFV; X-ray; 1.42 A; AAA=1564-1878.
DR PDB; 7NG3; X-ray; 1.80 A; A/B=3264-3569.
DR PDB; 7NG6; X-ray; 1.87 A; A/B=3264-3569.
DR PDB; 7NIO; X-ray; 2.20 A; A/E=5325-5925.
DR PDB; 7NN0; X-ray; 3.04 A; A/B/C/D=5325-5925.
DR PDB; 7NNG; X-ray; 2.38 A; A/B=5325-5925.
DR PDB; 7NT4; X-ray; 2.68 A; A/B=1564-1878.
DR PDB; 7NTS; X-ray; 1.48 A; A=3264-3569.
DR PDB; 7O46; X-ray; 2.23 A; A=3264-3569.
DR PDB; 7O7Y; EM; 2.20 A; BK=4365-4399.
DR PDB; 7O7Z; EM; 2.40 A; BK=1-7096.
DR PDB; 7O80; EM; 2.90 A; BK=1-7096.
DR PDB; 7O81; EM; 3.10 A; BK=1-7096.
DR PDB; 7ORR; X-ray; 1.79 A; A=4263-4384.
DR PDB; 7ORU; X-ray; 1.67 A; A=4263-4384.
DR PDB; 7ORV; X-ray; 1.95 A; A=4263-4384.
DR PDB; 7ORW; X-ray; 1.95 A; A=4263-4384.
DR PDB; 7QBB; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7QGI; X-ray; 1.65 A; D=5932-6449.
DR PDB; 7QIF; X-ray; 2.53 A; D=5932-6452.
DR PDB; 7R2V; X-ray; 2.53 A; A/B=5950-6449.
DR PDB; 7R7H; X-ray; 2.15 A; A/B=3264-3569.
DR PDB; 7RB0; EM; 2.98 A; A/B/C/D/E/F=6453-6798.
DR PDB; 7RB2; EM; 3.27 A; A/B/C/D/E/F=6453-6798.
DR PDB; 7RBZ; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7RC0; X-ray; 1.65 A; A=3264-3569.
DR PDB; 7RFR; X-ray; 1.63 A; A/B=3264-3569.
DR PDB; 7RFS; X-ray; 1.91 A; A=3264-3569.
DR PDB; 7RFU; X-ray; 2.50 A; A=3264-3569.
DR PDB; 7RFW; X-ray; 1.73 A; A=3264-3569.
DR PDB; 7RLS; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7RM2; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7RMB; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7RME; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7RMT; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7RMZ; X-ray; 2.10 A; A=3264-3569.
DR PDB; 7RN0; X-ray; 2.25 A; A=3264-3569.
DR PDB; 7RN1; X-ray; 2.30 A; A=3264-3569.
DR PDB; 7RN4; X-ray; 1.85 A; A=3264-3569.
DR PDB; 7RNH; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7RNK; X-ray; 2.10 A; A=3264-3569.
DR PDB; 7RNW; X-ray; 2.35 A; A/B/C/D=3264-3569.
DR PDB; 7RQG; X-ray; 2.17 A; A/B/C/D=2662-2763.
DR PDB; 7S3K; X-ray; 1.90 A; A=3264-3569.
DR PDB; 7S3S; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7S4B; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7S82; EM; 3.50 A; A/B/C/D=3259-3569.
DR PDB; 7SI9; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7T42; X-ray; 1.60 A; A/B=3264-3568.
DR PDB; 7T43; X-ray; 1.70 A; A/B=3264-3568.
DR PDB; 7T44; X-ray; 1.45 A; A/B=3264-3568.
DR PDB; 7T45; X-ray; 1.65 A; A/B=3264-3568.
DR PDB; 7T46; X-ray; 1.45 A; A/B=3264-3568.
DR PDB; 7T48; X-ray; 1.90 A; A=3264-3568.
DR PDB; 7T49; X-ray; 1.75 A; A/B=3264-3568.
DR PDB; 7T4A; X-ray; 1.80 A; A/B=3264-3568.
DR PDB; 7T4B; X-ray; 1.60 A; A/B=3264-3568.
DR PDB; 7T9W; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2048-2152.
DR PDB; 7TDU; Other; 1.85 A; A=3264-3569.
DR PDB; 7TE0; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7TEH; X-ray; 1.80 A; A=3264-3569.
DR PDB; 7TFR; X-ray; 1.80 A; A=3264-3569.
DR PDB; 7THH; X-ray; 1.32 A; A/B/C/D/E/F=1496-1623.
DR PDB; 7TI9; X-ray; 2.73 A; A=818-929.
DR PDB; 7TJ2; EM; 3.20 A; A/B/C/D/E/F=6453-6798.
DR PDB; 7TQ5; X-ray; 1.65 A; A/B=3264-3568.
DR PDB; 7TQ6; X-ray; 1.55 A; A/B=3264-3568.
DR PDB; 7TQV; EM; 3.43 A; A/B/C/D/E/F=6453-6798.
DR PDB; 7TWF; X-ray; 1.10 A; A/B=1025-1191.
DR PDB; 7TWG; X-ray; 1.10 A; A/B=1025-1191.
DR PDB; 7TWH; X-ray; 1.10 A; A/B=1025-1191.
DR PDB; 7TWI; X-ray; 1.10 A; A/B=1025-1191.
DR PDB; 7TWJ; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWN; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWO; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWP; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWQ; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWR; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWS; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWT; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWV; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWW; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWX; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TWY; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TX0; X-ray; 0.84 A; A/B=1025-1191.
DR PDB; 7TX1; X-ray; 0.90 A; A/B=1025-1191.
DR PDB; 7TX3; Other; 1.60 A; A/B=1025-1191.
DR PDB; 7TX4; Other; 1.90 A; A=1024-1192.
DR PDB; 7TX5; Other; 1.95 A; A=1024-1192.
DR PDB; 7ULT; X-ray; 1.90 A; A/C=6799-7096, B/D=4254-4392.
DR PDB; 7VAH; X-ray; 1.49 A; A=3264-3569.
DR PDB; 7WOH; X-ray; 1.72 A; A/B=3264-3566.
DR PDBsum; 5R7Y; -.
DR PDBsum; 5R7Z; -.
DR PDBsum; 5R80; -.
DR PDBsum; 5R81; -.
DR PDBsum; 5R82; -.
DR PDBsum; 5R83; -.
DR PDBsum; 5R84; -.
DR PDBsum; 5R8T; -.
DR PDBsum; 5RE4; -.
DR PDBsum; 5RE5; -.
DR PDBsum; 5RE6; -.
DR PDBsum; 5RE7; -.
DR PDBsum; 5RE8; -.
DR PDBsum; 5RE9; -.
DR PDBsum; 5REA; -.
DR PDBsum; 5REB; -.
DR PDBsum; 5REC; -.
DR PDBsum; 5RED; -.
DR PDBsum; 5REE; -.
DR PDBsum; 5REF; -.
DR PDBsum; 5REG; -.
DR PDBsum; 5REH; -.
DR PDBsum; 5REI; -.
DR PDBsum; 5REJ; -.
DR PDBsum; 5REK; -.
DR PDBsum; 5REL; -.
DR PDBsum; 5REM; -.
DR PDBsum; 5REN; -.
DR PDBsum; 5REO; -.
DR PDBsum; 5REP; -.
DR PDBsum; 5RER; -.
DR PDBsum; 5RES; -.
DR PDBsum; 5RET; -.
DR PDBsum; 5REU; -.
DR PDBsum; 5REV; -.
DR PDBsum; 5REW; -.
DR PDBsum; 5REX; -.
DR PDBsum; 5REY; -.
DR PDBsum; 5REZ; -.
DR PDBsum; 5RF0; -.
DR PDBsum; 5RF1; -.
DR PDBsum; 5RF2; -.
DR PDBsum; 5RF3; -.
DR PDBsum; 5RF4; -.
DR PDBsum; 5RF5; -.
DR PDBsum; 5RF6; -.
DR PDBsum; 5RF7; -.
DR PDBsum; 5RF8; -.
DR PDBsum; 5RF9; -.
DR PDBsum; 5RFA; -.
DR PDBsum; 5RFB; -.
DR PDBsum; 5RFC; -.
DR PDBsum; 5RFD; -.
DR PDBsum; 5RFE; -.
DR PDBsum; 5RFF; -.
DR PDBsum; 5RFG; -.
DR PDBsum; 5RFH; -.
DR PDBsum; 5RFI; -.
DR PDBsum; 5RFJ; -.
DR PDBsum; 5RFK; -.
DR PDBsum; 5RFL; -.
DR PDBsum; 5RFM; -.
DR PDBsum; 5RFN; -.
DR PDBsum; 5RFO; -.
DR PDBsum; 5RFP; -.
DR PDBsum; 5RFQ; -.
DR PDBsum; 5RFR; -.
DR PDBsum; 5RFS; -.
DR PDBsum; 5RFT; -.
DR PDBsum; 5RFU; -.
DR PDBsum; 5RFV; -.
DR PDBsum; 5RFW; -.
DR PDBsum; 5RFX; -.
DR PDBsum; 5RFY; -.
DR PDBsum; 5RFZ; -.
DR PDBsum; 5RG0; -.
DR PDBsum; 5RG1; -.
DR PDBsum; 5RG2; -.
DR PDBsum; 5RG3; -.
DR PDBsum; 5RGG; -.
DR PDBsum; 5RGH; -.
DR PDBsum; 5RGI; -.
DR PDBsum; 5RGJ; -.
DR PDBsum; 5RGK; -.
DR PDBsum; 5RGL; -.
DR PDBsum; 5RGM; -.
DR PDBsum; 5RGN; -.
DR PDBsum; 5RGO; -.
DR PDBsum; 5RGP; -.
DR PDBsum; 5RGQ; -.
DR PDBsum; 5RGR; -.
DR PDBsum; 5RGS; -.
DR PDBsum; 5RGT; -.
DR PDBsum; 5RGU; -.
DR PDBsum; 5RGV; -.
DR PDBsum; 5RGW; -.
DR PDBsum; 5RGX; -.
DR PDBsum; 5RGY; -.
DR PDBsum; 5RGZ; -.
DR PDBsum; 5RH0; -.
DR PDBsum; 5RH1; -.
DR PDBsum; 5RH2; -.
DR PDBsum; 5RH3; -.
DR PDBsum; 5RH4; -.
DR PDBsum; 5RH5; -.
DR PDBsum; 5RH6; -.
DR PDBsum; 5RH7; -.
DR PDBsum; 5RH8; -.
DR PDBsum; 5RH9; -.
DR PDBsum; 5RHA; -.
DR PDBsum; 5RHB; -.
DR PDBsum; 5RHC; -.
DR PDBsum; 5RHD; -.
DR PDBsum; 5RHE; -.
DR PDBsum; 5RHF; -.
DR PDBsum; 5RL0; -.
DR PDBsum; 5RL1; -.
DR PDBsum; 5RL2; -.
DR PDBsum; 5RL3; -.
DR PDBsum; 5RL4; -.
DR PDBsum; 5RL5; -.
DR PDBsum; 5RL6; -.
DR PDBsum; 5RL7; -.
DR PDBsum; 5RL8; -.
DR PDBsum; 5RL9; -.
DR PDBsum; 5RLB; -.
DR PDBsum; 5RLC; -.
DR PDBsum; 5RLD; -.
DR PDBsum; 5RLE; -.
DR PDBsum; 5RLF; -.
DR PDBsum; 5RLG; -.
DR PDBsum; 5RLH; -.
DR PDBsum; 5RLI; -.
DR PDBsum; 5RLJ; -.
DR PDBsum; 5RLK; -.
DR PDBsum; 5RLL; -.
DR PDBsum; 5RLM; -.
DR PDBsum; 5RLN; -.
DR PDBsum; 5RLO; -.
DR PDBsum; 5RLP; -.
DR PDBsum; 5RLQ; -.
DR PDBsum; 5RLR; -.
DR PDBsum; 5RLS; -.
DR PDBsum; 5RLT; -.
DR PDBsum; 5RLU; -.
DR PDBsum; 5RLV; -.
DR PDBsum; 5RLW; -.
DR PDBsum; 5RLY; -.
DR PDBsum; 5RLZ; -.
DR PDBsum; 5RM0; -.
DR PDBsum; 5RM1; -.
DR PDBsum; 5RM2; -.
DR PDBsum; 5RM3; -.
DR PDBsum; 5RM4; -.
DR PDBsum; 5RM5; -.
DR PDBsum; 5RM6; -.
DR PDBsum; 5RM7; -.
DR PDBsum; 5RM8; -.
DR PDBsum; 5RM9; -.
DR PDBsum; 5RMA; -.
DR PDBsum; 5RMB; -.
DR PDBsum; 5RMC; -.
DR PDBsum; 5RMD; -.
DR PDBsum; 5RME; -.
DR PDBsum; 5RMF; -.
DR PDBsum; 5RMG; -.
DR PDBsum; 5RMH; -.
DR PDBsum; 5RMI; -.
DR PDBsum; 5RMJ; -.
DR PDBsum; 5RMK; -.
DR PDBsum; 5RML; -.
DR PDBsum; 5RMM; -.
DR PDBsum; 5ROB; -.
DR PDBsum; 5RS7; -.
DR PDBsum; 5RS8; -.
DR PDBsum; 5RS9; -.
DR PDBsum; 5RSB; -.
DR PDBsum; 5RSC; -.
DR PDBsum; 5RSD; -.
DR PDBsum; 5RSE; -.
DR PDBsum; 5RSF; -.
DR PDBsum; 5RSG; -.
DR PDBsum; 5RSH; -.
DR PDBsum; 5RSI; -.
DR PDBsum; 5RSJ; -.
DR PDBsum; 5RSK; -.
DR PDBsum; 5RSL; -.
DR PDBsum; 5RSM; -.
DR PDBsum; 5RSN; -.
DR PDBsum; 5RSO; -.
DR PDBsum; 5RSP; -.
DR PDBsum; 5RSQ; -.
DR PDBsum; 5RSR; -.
DR PDBsum; 5RSS; -.
DR PDBsum; 5RST; -.
DR PDBsum; 5RSU; -.
DR PDBsum; 5RSV; -.
DR PDBsum; 5RSW; -.
DR PDBsum; 5RSX; -.
DR PDBsum; 5RSY; -.
DR PDBsum; 5RSZ; -.
DR PDBsum; 5RT0; -.
DR PDBsum; 5RT1; -.
DR PDBsum; 5RT2; -.
DR PDBsum; 5RT3; -.
DR PDBsum; 5RT4; -.
DR PDBsum; 5RT5; -.
DR PDBsum; 5RT6; -.
DR PDBsum; 5RT7; -.
DR PDBsum; 5RT8; -.
DR PDBsum; 5RT9; -.
DR PDBsum; 5RTA; -.
DR PDBsum; 5RTB; -.
DR PDBsum; 5RTC; -.
DR PDBsum; 5RTD; -.
DR PDBsum; 5RTE; -.
DR PDBsum; 5RTF; -.
DR PDBsum; 5RTG; -.
DR PDBsum; 5RTH; -.
DR PDBsum; 5RTI; -.
DR PDBsum; 5RTJ; -.
DR PDBsum; 5RTK; -.
DR PDBsum; 5RTL; -.
DR PDBsum; 5RTM; -.
DR PDBsum; 5RTN; -.
DR PDBsum; 5RTO; -.
DR PDBsum; 5RTP; -.
DR PDBsum; 5RTQ; -.
DR PDBsum; 5RTR; -.
DR PDBsum; 5RTS; -.
DR PDBsum; 5RTT; -.
DR PDBsum; 5RTU; -.
DR PDBsum; 5RTV; -.
DR PDBsum; 5RTW; -.
DR PDBsum; 5RTX; -.
DR PDBsum; 5RTY; -.
DR PDBsum; 5RTZ; -.
DR PDBsum; 5RU0; -.
DR PDBsum; 5RU1; -.
DR PDBsum; 5RU2; -.
DR PDBsum; 5RU3; -.
DR PDBsum; 5RU4; -.
DR PDBsum; 5RU5; -.
DR PDBsum; 5RU6; -.
DR PDBsum; 5RU7; -.
DR PDBsum; 5RU8; -.
DR PDBsum; 5RU9; -.
DR PDBsum; 5RUA; -.
DR PDBsum; 5RUC; -.
DR PDBsum; 5RUD; -.
DR PDBsum; 5RUE; -.
DR PDBsum; 5RUF; -.
DR PDBsum; 5RUG; -.
DR PDBsum; 5RUH; -.
DR PDBsum; 5RUI; -.
DR PDBsum; 5RUJ; -.
DR PDBsum; 5RUK; -.
DR PDBsum; 5RUL; -.
DR PDBsum; 5RUM; -.
DR PDBsum; 5RUN; -.
DR PDBsum; 5RUO; -.
DR PDBsum; 5RUP; -.
DR PDBsum; 5RUQ; -.
DR PDBsum; 5RUR; -.
DR PDBsum; 5RUS; -.
DR PDBsum; 5RUT; -.
DR PDBsum; 5RUU; -.
DR PDBsum; 5RUV; -.
DR PDBsum; 5RUW; -.
DR PDBsum; 5RUX; -.
DR PDBsum; 5RUY; -.
DR PDBsum; 5RUZ; -.
DR PDBsum; 5RV0; -.
DR PDBsum; 5RV1; -.
DR PDBsum; 5RV2; -.
DR PDBsum; 5RV3; -.
DR PDBsum; 5RV4; -.
DR PDBsum; 5RV5; -.
DR PDBsum; 5RV6; -.
DR PDBsum; 5RV7; -.
DR PDBsum; 5RV8; -.
DR PDBsum; 5RV9; -.
DR PDBsum; 5RVA; -.
DR PDBsum; 5RVB; -.
DR PDBsum; 5RVC; -.
DR PDBsum; 5RVD; -.
DR PDBsum; 5RVE; -.
DR PDBsum; 5RVF; -.
DR PDBsum; 5RVG; -.
DR PDBsum; 5RVH; -.
DR PDBsum; 5RVI; -.
DR PDBsum; 5RVJ; -.
DR PDBsum; 5RVK; -.
DR PDBsum; 5RVL; -.
DR PDBsum; 5RVM; -.
DR PDBsum; 5RVN; -.
DR PDBsum; 5RVO; -.
DR PDBsum; 5RVP; -.
DR PDBsum; 5RVQ; -.
DR PDBsum; 5RVR; -.
DR PDBsum; 5RVS; -.
DR PDBsum; 5RVT; -.
DR PDBsum; 5RVU; -.
DR PDBsum; 5RVV; -.
DR PDBsum; 5S18; -.
DR PDBsum; 5S1A; -.
DR PDBsum; 5S1C; -.
DR PDBsum; 5S1E; -.
DR PDBsum; 5S1G; -.
DR PDBsum; 5S1I; -.
DR PDBsum; 5S1K; -.
DR PDBsum; 5S1M; -.
DR PDBsum; 5S1O; -.
DR PDBsum; 5S1Q; -.
DR PDBsum; 5S1S; -.
DR PDBsum; 5S1U; -.
DR PDBsum; 5S1W; -.
DR PDBsum; 5S1Y; -.
DR PDBsum; 5S20; -.
DR PDBsum; 5S22; -.
DR PDBsum; 5S24; -.
DR PDBsum; 5S26; -.
DR PDBsum; 5S27; -.
DR PDBsum; 5S28; -.
DR PDBsum; 5S29; -.
DR PDBsum; 5S2A; -.
DR PDBsum; 5S2B; -.
DR PDBsum; 5S2C; -.
DR PDBsum; 5S2D; -.
DR PDBsum; 5S2E; -.
DR PDBsum; 5S2F; -.
DR PDBsum; 5S2G; -.
DR PDBsum; 5S2H; -.
DR PDBsum; 5S2I; -.
DR PDBsum; 5S2J; -.
DR PDBsum; 5S2K; -.
DR PDBsum; 5S2L; -.
DR PDBsum; 5S2M; -.
DR PDBsum; 5S2N; -.
DR PDBsum; 5S2O; -.
DR PDBsum; 5S2P; -.
DR PDBsum; 5S2Q; -.
DR PDBsum; 5S2R; -.
DR PDBsum; 5S2S; -.
DR PDBsum; 5S2T; -.
DR PDBsum; 5S2U; -.
DR PDBsum; 5S2V; -.
DR PDBsum; 5S2W; -.
DR PDBsum; 5S2X; -.
DR PDBsum; 5S2Y; -.
DR PDBsum; 5S2Z; -.
DR PDBsum; 5S30; -.
DR PDBsum; 5S31; -.
DR PDBsum; 5S32; -.
DR PDBsum; 5S33; -.
DR PDBsum; 5S34; -.
DR PDBsum; 5S35; -.
DR PDBsum; 5S36; -.
DR PDBsum; 5S37; -.
DR PDBsum; 5S38; -.
DR PDBsum; 5S39; -.
DR PDBsum; 5S3A; -.
DR PDBsum; 5S3B; -.
DR PDBsum; 5S3C; -.
DR PDBsum; 5S3D; -.
DR PDBsum; 5S3E; -.
DR PDBsum; 5S3F; -.
DR PDBsum; 5S3G; -.
DR PDBsum; 5S3H; -.
DR PDBsum; 5S3I; -.
DR PDBsum; 5S3J; -.
DR PDBsum; 5S3K; -.
DR PDBsum; 5S3L; -.
DR PDBsum; 5S3M; -.
DR PDBsum; 5S3N; -.
DR PDBsum; 5S3O; -.
DR PDBsum; 5S3P; -.
DR PDBsum; 5S3Q; -.
DR PDBsum; 5S3R; -.
DR PDBsum; 5S3S; -.
DR PDBsum; 5S3T; -.
DR PDBsum; 5S3U; -.
DR PDBsum; 5S3V; -.
DR PDBsum; 5S3W; -.
DR PDBsum; 5S3X; -.
DR PDBsum; 5S3Y; -.
DR PDBsum; 5S3Z; -.
DR PDBsum; 5S40; -.
DR PDBsum; 5S41; -.
DR PDBsum; 5S42; -.
DR PDBsum; 5S43; -.
DR PDBsum; 5S44; -.
DR PDBsum; 5S45; -.
DR PDBsum; 5S46; -.
DR PDBsum; 5S47; -.
DR PDBsum; 5S48; -.
DR PDBsum; 5S49; -.
DR PDBsum; 5S4A; -.
DR PDBsum; 5S4B; -.
DR PDBsum; 5S4C; -.
DR PDBsum; 5S4D; -.
DR PDBsum; 5S4E; -.
DR PDBsum; 5S4F; -.
DR PDBsum; 5S4G; -.
DR PDBsum; 5S4H; -.
DR PDBsum; 5S4I; -.
DR PDBsum; 5S4J; -.
DR PDBsum; 5S4K; -.
DR PDBsum; 5S6X; -.
DR PDBsum; 5S6Y; -.
DR PDBsum; 5S6Z; -.
DR PDBsum; 5S70; -.
DR PDBsum; 5S71; -.
DR PDBsum; 5S72; -.
DR PDBsum; 5S73; -.
DR PDBsum; 5S74; -.
DR PDBsum; 5SA4; -.
DR PDBsum; 5SA5; -.
DR PDBsum; 5SA6; -.
DR PDBsum; 5SA7; -.
DR PDBsum; 5SA8; -.
DR PDBsum; 5SA9; -.
DR PDBsum; 5SAA; -.
DR PDBsum; 5SAB; -.
DR PDBsum; 5SAC; -.
DR PDBsum; 5SAD; -.
DR PDBsum; 5SAE; -.
DR PDBsum; 5SAF; -.
DR PDBsum; 5SAG; -.
DR PDBsum; 5SAH; -.
DR PDBsum; 5SAI; -.
DR PDBsum; 5SBF; -.
DR PDBsum; 5SKW; -.
DR PDBsum; 5SKX; -.
DR PDBsum; 5SKY; -.
DR PDBsum; 5SKZ; -.
DR PDBsum; 5SL0; -.
DR PDBsum; 5SL1; -.
DR PDBsum; 5SL2; -.
DR PDBsum; 5SL3; -.
DR PDBsum; 5SL4; -.
DR PDBsum; 5SL5; -.
DR PDBsum; 5SL6; -.
DR PDBsum; 5SL7; -.
DR PDBsum; 5SL8; -.
DR PDBsum; 5SL9; -.
DR PDBsum; 5SLA; -.
DR PDBsum; 5SLB; -.
DR PDBsum; 5SLC; -.
DR PDBsum; 5SLD; -.
DR PDBsum; 5SLE; -.
DR PDBsum; 5SLF; -.
DR PDBsum; 5SLG; -.
DR PDBsum; 5SLH; -.
DR PDBsum; 5SLI; -.
DR PDBsum; 5SLJ; -.
DR PDBsum; 5SLK; -.
DR PDBsum; 5SLL; -.
DR PDBsum; 5SLM; -.
DR PDBsum; 5SLN; -.
DR PDBsum; 5SLO; -.
DR PDBsum; 5SLP; -.
DR PDBsum; 5SLQ; -.
DR PDBsum; 5SLR; -.
DR PDBsum; 5SLS; -.
DR PDBsum; 5SLT; -.
DR PDBsum; 5SLU; -.
DR PDBsum; 5SLV; -.
DR PDBsum; 5SLW; -.
DR PDBsum; 5SLX; -.
DR PDBsum; 5SLY; -.
DR PDBsum; 5SLZ; -.
DR PDBsum; 5SM0; -.
DR PDBsum; 5SM1; -.
DR PDBsum; 5SM2; -.
DR PDBsum; 5SM3; -.
DR PDBsum; 5SM4; -.
DR PDBsum; 5SM5; -.
DR PDBsum; 5SM6; -.
DR PDBsum; 5SM7; -.
DR PDBsum; 5SM8; -.
DR PDBsum; 5SM9; -.
DR PDBsum; 5SMA; -.
DR PDBsum; 5SMB; -.
DR PDBsum; 5SMC; -.
DR PDBsum; 5SMD; -.
DR PDBsum; 5SME; -.
DR PDBsum; 5SMF; -.
DR PDBsum; 5SMG; -.
DR PDBsum; 5SMH; -.
DR PDBsum; 5SMI; -.
DR PDBsum; 5SMK; -.
DR PDBsum; 6LU7; -.
DR PDBsum; 6LZE; -.
DR PDBsum; 6M03; -.
DR PDBsum; 6M0K; -.
DR PDBsum; 6M2N; -.
DR PDBsum; 6M2Q; -.
DR PDBsum; 6M71; -.
DR PDBsum; 6VWW; -.
DR PDBsum; 6VXS; -.
DR PDBsum; 6W01; -.
DR PDBsum; 6W02; -.
DR PDBsum; 6W4B; -.
DR PDBsum; 6W4H; -.
DR PDBsum; 6W61; -.
DR PDBsum; 6W63; -.
DR PDBsum; 6W6Y; -.
DR PDBsum; 6W75; -.
DR PDBsum; 6W9C; -.
DR PDBsum; 6W9Q; -.
DR PDBsum; 6WC1; -.
DR PDBsum; 6WCF; -.
DR PDBsum; 6WEN; -.
DR PDBsum; 6WEY; -.
DR PDBsum; 6WIQ; -.
DR PDBsum; 6WJT; -.
DR PDBsum; 6WKQ; -.
DR PDBsum; 6WKS; -.
DR PDBsum; 6WLC; -.
DR PDBsum; 6WNP; -.
DR PDBsum; 6WOJ; -.
DR PDBsum; 6WQ3; -.
DR PDBsum; 6WQD; -.
DR PDBsum; 6WQF; -.
DR PDBsum; 6WRH; -.
DR PDBsum; 6WRZ; -.
DR PDBsum; 6WTC; -.
DR PDBsum; 6WTJ; -.
DR PDBsum; 6WTK; -.
DR PDBsum; 6WTM; -.
DR PDBsum; 6WTT; -.
DR PDBsum; 6WUU; -.
DR PDBsum; 6WVN; -.
DR PDBsum; 6WX4; -.
DR PDBsum; 6WXC; -.
DR PDBsum; 6WXD; -.
DR PDBsum; 6WZU; -.
DR PDBsum; 6X1B; -.
DR PDBsum; 6X4I; -.
DR PDBsum; 6XA4; -.
DR PDBsum; 6XA9; -.
DR PDBsum; 6XAA; -.
DR PDBsum; 6XB0; -.
DR PDBsum; 6XB1; -.
DR PDBsum; 6XB2; -.
DR PDBsum; 6XBG; -.
DR PDBsum; 6XBH; -.
DR PDBsum; 6XBI; -.
DR PDBsum; 6XCH; -.
DR PDBsum; 6XDH; -.
DR PDBsum; 6XFN; -.
DR PDBsum; 6XG3; -.
DR PDBsum; 6XHM; -.
DR PDBsum; 6XHU; -.
DR PDBsum; 6XIP; -.
DR PDBsum; 6XKF; -.
DR PDBsum; 6XKH; -.
DR PDBsum; 6XKM; -.
DR PDBsum; 6XMK; -.
DR PDBsum; 6XOA; -.
DR PDBsum; 6XQS; -.
DR PDBsum; 6XQT; -.
DR PDBsum; 6XQU; -.
DR PDBsum; 6XR3; -.
DR PDBsum; 6Y2E; -.
DR PDBsum; 6Y2F; -.
DR PDBsum; 6Y2G; -.
DR PDBsum; 6Y84; -.
DR PDBsum; 6YB7; -.
DR PDBsum; 6YNQ; -.
DR PDBsum; 6YVA; -.
DR PDBsum; 6YVF; -.
DR PDBsum; 6YWK; -.
DR PDBsum; 6YWL; -.
DR PDBsum; 6YWM; -.
DR PDBsum; 6YYT; -.
DR PDBsum; 6YZ1; -.
DR PDBsum; 6Z2E; -.
DR PDBsum; 6Z5T; -.
DR PDBsum; 6Z6I; -.
DR PDBsum; 6Z72; -.
DR PDBsum; 6ZCT; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZPE; -.
DR PDBsum; 6ZRT; -.
DR PDBsum; 6ZRU; -.
DR PDBsum; 6ZSL; -.
DR PDBsum; 7A1U; -.
DR PDBsum; 7ABU; -.
DR PDBsum; 7ADW; -.
DR PDBsum; 7AEG; -.
DR PDBsum; 7AEH; -.
DR PDBsum; 7AF0; -.
DR PDBsum; 7AGA; -.
DR PDBsum; 7AHA; -.
DR PDBsum; 7AK4; -.
DR PDBsum; 7AKU; -.
DR PDBsum; 7ALH; -.
DR PDBsum; 7ALI; -.
DR PDBsum; 7AMJ; -.
DR PDBsum; 7ANS; -.
DR PDBsum; 7AOL; -.
DR PDBsum; 7AP6; -.
DR PDBsum; 7APH; -.
DR PDBsum; 7AQE; -.
DR PDBsum; 7AQI; -.
DR PDBsum; 7AQJ; -.
DR PDBsum; 7AR5; -.
DR PDBsum; 7AR6; -.
DR PDBsum; 7ARF; -.
DR PDBsum; 7AU4; -.
DR PDBsum; 7AVD; -.
DR PDBsum; 7AWR; -.
DR PDBsum; 7AWS; -.
DR PDBsum; 7AWU; -.
DR PDBsum; 7AWW; -.
DR PDBsum; 7AX6; -.
DR PDBsum; 7AXM; -.
DR PDBsum; 7AXO; -.
DR PDBsum; 7AY7; -.
DR PDBsum; 7B2J; -.
DR PDBsum; 7B2U; -.
DR PDBsum; 7B3E; -.
DR PDBsum; 7B5Z; -.
DR PDBsum; 7B77; -.
DR PDBsum; 7B83; -.
DR PDBsum; 7BAJ; -.
DR PDBsum; 7BAK; -.
DR PDBsum; 7BAL; -.
DR PDBsum; 7BB2; -.
DR PDBsum; 7BE7; -.
DR PDBsum; 7BF3; -.
DR PDBsum; 7BF4; -.
DR PDBsum; 7BF5; -.
DR PDBsum; 7BF6; -.
DR PDBsum; 7BFB; -.
DR PDBsum; 7BGP; -.
DR PDBsum; 7BIJ; -.
DR PDBsum; 7BQ7; -.
DR PDBsum; 7BQY; -.
DR PDBsum; 7BRO; -.
DR PDBsum; 7BRP; -.
DR PDBsum; 7BTF; -.
DR PDBsum; 7BUY; -.
DR PDBsum; 7BV1; -.
DR PDBsum; 7BV2; -.
DR PDBsum; 7BWQ; -.
DR PDBsum; 7BZF; -.
DR PDBsum; 7C2I; -.
DR PDBsum; 7C2J; -.
DR PDBsum; 7C2K; -.
DR PDBsum; 7C2Q; -.
DR PDBsum; 7C2Y; -.
DR PDBsum; 7C6S; -.
DR PDBsum; 7C6U; -.
DR PDBsum; 7C7P; -.
DR PDBsum; 7C8B; -.
DR PDBsum; 7C8R; -.
DR PDBsum; 7C8T; -.
DR PDBsum; 7C8U; -.
DR PDBsum; 7CA8; -.
DR PDBsum; 7CAM; -.
DR PDBsum; 7CB7; -.
DR PDBsum; 7CBT; -.
DR PDBsum; 7CJD; -.
DR PDBsum; 7CJM; -.
DR PDBsum; 7CMD; -.
DR PDBsum; 7COM; -.
DR PDBsum; 7CUT; -.
DR PDBsum; 7CUU; -.
DR PDBsum; 7CWB; -.
DR PDBsum; 7CWC; -.
DR PDBsum; 7CX9; -.
DR PDBsum; 7D1M; -.
DR PDBsum; 7D1O; -.
DR PDBsum; 7D7K; -.
DR PDBsum; 7D7L; -.
DR PDBsum; 7DDC; -.
DR PDBsum; 7DG6; -.
DR PDBsum; 7DIY; -.
DR PDBsum; 7DVX; -.
DR PDBsum; 7DVY; -.
DR PDBsum; 7DW0; -.
DR PDBsum; 7DW6; -.
DR PDBsum; 7E18; -.
DR PDBsum; 7E19; -.
DR PDBsum; 7E5X; -.
DR PDBsum; 7E6K; -.
DR PDBsum; 7EQ4; -.
DR PDBsum; 7JFQ; -.
DR PDBsum; 7JHE; -.
DR PDBsum; 7JIB; -.
DR PDBsum; 7JKV; -.
DR PDBsum; 7JME; -.
DR PDBsum; 7JOY; -.
DR PDBsum; 7JP0; -.
DR PDBsum; 7JP1; -.
DR PDBsum; 7JPE; -.
DR PDBsum; 7JPY; -.
DR PDBsum; 7JPZ; -.
DR PDBsum; 7JQ0; -.
DR PDBsum; 7JQ1; -.
DR PDBsum; 7JQ2; -.
DR PDBsum; 7JQ3; -.
DR PDBsum; 7JQ4; -.
DR PDBsum; 7JQ5; -.
DR PDBsum; 7JQB; -.
DR PDBsum; 7JQC; -.
DR PDBsum; 7JR3; -.
DR PDBsum; 7JR4; -.
DR PDBsum; 7JST; -.
DR PDBsum; 7JSU; -.
DR PDBsum; 7JT0; -.
DR PDBsum; 7JT7; -.
DR PDBsum; 7JU7; -.
DR PDBsum; 7JUN; -.
DR PDBsum; 7JVZ; -.
DR PDBsum; 7JW8; -.
DR PDBsum; 7JYC; -.
DR PDBsum; 7JYY; -.
DR PDBsum; 7JZ0; -.
DR PDBsum; 7K0E; -.
DR PDBsum; 7K0F; -.
DR PDBsum; 7K0R; -.
DR PDBsum; 7K1L; -.
DR PDBsum; 7K1O; -.
DR PDBsum; 7K3N; -.
DR PDBsum; 7K3T; -.
DR PDBsum; 7K40; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7K6D; -.
DR PDBsum; 7K6E; -.
DR PDBsum; 7K7P; -.
DR PDBsum; 7K9P; -.
DR PDBsum; 7KAG; -.
DR PDBsum; 7KEG; -.
DR PDBsum; 7KEH; -.
DR PDBsum; 7KF4; -.
DR PDBsum; 7KFI; -.
DR PDBsum; 7KG3; -.
DR PDBsum; 7KHP; -.
DR PDBsum; 7KOA; -.
DR PDBsum; 7KPH; -.
DR PDBsum; 7KQO; -.
DR PDBsum; 7KQP; -.
DR PDBsum; 7KQW; -.
DR PDBsum; 7KR0; -.
DR PDBsum; 7KR1; -.
DR PDBsum; 7KRI; -.
DR PDBsum; 7KVL; -.
DR PDBsum; 7KVR; -.
DR PDBsum; 7KX5; -.
DR PDBsum; 7KXB; -.
DR PDBsum; 7KYU; -.
DR PDBsum; 7L0D; -.
DR PDBsum; 7L10; -.
DR PDBsum; 7L11; -.
DR PDBsum; 7L12; -.
DR PDBsum; 7L13; -.
DR PDBsum; 7L14; -.
DR PDBsum; 7L1F; -.
DR PDBsum; 7L5D; -.
DR PDBsum; 7L6R; -.
DR PDBsum; 7L6T; -.
DR PDBsum; 7L8I; -.
DR PDBsum; 7L8J; -.
DR PDBsum; 7LB7; -.
DR PDBsum; 7LBN; -.
DR PDBsum; 7LBR; -.
DR PDBsum; 7LBS; -.
DR PDBsum; 7LCO; -.
DR PDBsum; 7LCS; -.
DR PDBsum; 7LCT; -.
DR PDBsum; 7LDL; -.
DR PDBsum; 7LDX; -.
DR PDBsum; 7LFE; -.
DR PDBsum; 7LFP; -.
DR PDBsum; 7LFZ; -.
DR PDBsum; 7LG2; -.
DR PDBsum; 7LG3; -.
DR PDBsum; 7LG7; -.
DR PDBsum; 7LGO; -.
DR PDBsum; 7LHQ; -.
DR PDBsum; 7LKD; -.
DR PDBsum; 7LKE; -.
DR PDBsum; 7LKR; -.
DR PDBsum; 7LKS; -.
DR PDBsum; 7LKT; -.
DR PDBsum; 7LKU; -.
DR PDBsum; 7LKV; -.
DR PDBsum; 7LKW; -.
DR PDBsum; 7LKX; -.
DR PDBsum; 7LLF; -.
DR PDBsum; 7LLZ; -.
DR PDBsum; 7LMD; -.
DR PDBsum; 7LME; -.
DR PDBsum; 7LMF; -.
DR PDBsum; 7LOS; -.
DR PDBsum; 7LTJ; -.
DR PDBsum; 7LTN; -.
DR PDBsum; 7LW3; -.
DR PDBsum; 7LW4; -.
DR PDBsum; 7LYH; -.
DR PDBsum; 7LYI; -.
DR PDBsum; 7LZT; -.
DR PDBsum; 7LZU; -.
DR PDBsum; 7LZV; -.
DR PDBsum; 7LZW; -.
DR PDBsum; 7LZX; -.
DR PDBsum; 7LZY; -.
DR PDBsum; 7LZZ; -.
DR PDBsum; 7M00; -.
DR PDBsum; 7M01; -.
DR PDBsum; 7M02; -.
DR PDBsum; 7M03; -.
DR PDBsum; 7M04; -.
DR PDBsum; 7M2P; -.
DR PDBsum; 7M8M; -.
DR PDBsum; 7M8N; -.
DR PDBsum; 7M8O; -.
DR PDBsum; 7M8P; -.
DR PDBsum; 7M8X; -.
DR PDBsum; 7M8Y; -.
DR PDBsum; 7M8Z; -.
DR PDBsum; 7M90; -.
DR PDBsum; 7M91; -.
DR PDBsum; 7MBG; -.
DR PDBsum; 7MBI; -.
DR PDBsum; 7MC5; -.
DR PDBsum; 7MC6; -.
DR PDBsum; 7ME0; -.
DR PDBsum; 7MGR; -.
DR PDBsum; 7MGS; -.
DR PDBsum; 7MHF; -.
DR PDBsum; 7MHG; -.
DR PDBsum; 7MHH; -.
DR PDBsum; 7MHI; -.
DR PDBsum; 7MHJ; -.
DR PDBsum; 7MHK; -.
DR PDBsum; 7MHL; -.
DR PDBsum; 7MHM; -.
DR PDBsum; 7MHN; -.
DR PDBsum; 7MHO; -.
DR PDBsum; 7MHP; -.
DR PDBsum; 7MHQ; -.
DR PDBsum; 7MLF; -.
DR PDBsum; 7MLG; -.
DR PDBsum; 7MNG; -.
DR PDBsum; 7MPB; -.
DR PDBsum; 7MRR; -.
DR PDBsum; 7MSW; -.
DR PDBsum; 7MSX; -.
DR PDBsum; 7N06; -.
DR PDBsum; 7N0B; -.
DR PDBsum; 7N0C; -.
DR PDBsum; 7N0D; -.
DR PDBsum; 7N33; -.
DR PDBsum; 7N3K; -.
DR PDBsum; 7N44; -.
DR PDBsum; 7N5Z; -.
DR PDBsum; 7N6N; -.
DR PDBsum; 7N7R; -.
DR PDBsum; 7N7U; -.
DR PDBsum; 7N7W; -.
DR PDBsum; 7N7Y; -.
DR PDBsum; 7N83; -.
DR PDBsum; 7N89; -.
DR PDBsum; 7N8C; -.
DR PDBsum; 7NBR; -.
DR PDBsum; 7NBS; -.
DR PDBsum; 7NBT; -.
DR PDBsum; 7NBY; -.
DR PDBsum; 7NEO; -.
DR PDBsum; 7NEV; -.
DR PDBsum; 7NF5; -.
DR PDBsum; 7NFV; -.
DR PDBsum; 7NG3; -.
DR PDBsum; 7NG6; -.
DR PDBsum; 7NIO; -.
DR PDBsum; 7NN0; -.
DR PDBsum; 7NNG; -.
DR PDBsum; 7NT4; -.
DR PDBsum; 7NTS; -.
DR PDBsum; 7O46; -.
DR PDBsum; 7O7Y; -.
DR PDBsum; 7O7Z; -.
DR PDBsum; 7O80; -.
DR PDBsum; 7O81; -.
DR PDBsum; 7ORR; -.
DR PDBsum; 7ORU; -.
DR PDBsum; 7ORV; -.
DR PDBsum; 7ORW; -.
DR PDBsum; 7QBB; -.
DR PDBsum; 7QGI; -.
DR PDBsum; 7QIF; -.
DR PDBsum; 7R2V; -.
DR PDBsum; 7R7H; -.
DR PDBsum; 7RB0; -.
DR PDBsum; 7RB2; -.
DR PDBsum; 7RBZ; -.
DR PDBsum; 7RC0; -.
DR PDBsum; 7RFR; -.
DR PDBsum; 7RFS; -.
DR PDBsum; 7RFU; -.
DR PDBsum; 7RFW; -.
DR PDBsum; 7RLS; -.
DR PDBsum; 7RM2; -.
DR PDBsum; 7RMB; -.
DR PDBsum; 7RME; -.
DR PDBsum; 7RMT; -.
DR PDBsum; 7RMZ; -.
DR PDBsum; 7RN0; -.
DR PDBsum; 7RN1; -.
DR PDBsum; 7RN4; -.
DR PDBsum; 7RNH; -.
DR PDBsum; 7RNK; -.
DR PDBsum; 7RNW; -.
DR PDBsum; 7RQG; -.
DR PDBsum; 7S3K; -.
DR PDBsum; 7S3S; -.
DR PDBsum; 7S4B; -.
DR PDBsum; 7S82; -.
DR PDBsum; 7SI9; -.
DR PDBsum; 7T42; -.
DR PDBsum; 7T43; -.
DR PDBsum; 7T44; -.
DR PDBsum; 7T45; -.
DR PDBsum; 7T46; -.
DR PDBsum; 7T48; -.
DR PDBsum; 7T49; -.
DR PDBsum; 7T4A; -.
DR PDBsum; 7T4B; -.
DR PDBsum; 7T9W; -.
DR PDBsum; 7TDU; -.
DR PDBsum; 7TE0; -.
DR PDBsum; 7TEH; -.
DR PDBsum; 7TFR; -.
DR PDBsum; 7THH; -.
DR PDBsum; 7TI9; -.
DR PDBsum; 7TJ2; -.
DR PDBsum; 7TQ5; -.
DR PDBsum; 7TQ6; -.
DR PDBsum; 7TQV; -.
DR PDBsum; 7TWF; -.
DR PDBsum; 7TWG; -.
DR PDBsum; 7TWH; -.
DR PDBsum; 7TWI; -.
DR PDBsum; 7TWJ; -.
DR PDBsum; 7TWN; -.
DR PDBsum; 7TWO; -.
DR PDBsum; 7TWP; -.
DR PDBsum; 7TWQ; -.
DR PDBsum; 7TWR; -.
DR PDBsum; 7TWS; -.
DR PDBsum; 7TWT; -.
DR PDBsum; 7TWV; -.
DR PDBsum; 7TWW; -.
DR PDBsum; 7TWX; -.
DR PDBsum; 7TWY; -.
DR PDBsum; 7TX0; -.
DR PDBsum; 7TX1; -.
DR PDBsum; 7TX3; -.
DR PDBsum; 7TX4; -.
DR PDBsum; 7TX5; -.
DR PDBsum; 7ULT; -.
DR PDBsum; 7VAH; -.
DR PDBsum; 7WOH; -.
DR SMR; P0DTD1; -.
DR BioGRID; 4383850; 243.
DR BioGRID; 4383851; 389.
DR BioGRID; 4383852; 359.
DR BioGRID; 4383853; 1431.
DR BioGRID; 4383854; 316.
DR BioGRID; 4383855; 1268.
DR BioGRID; 4383856; 524.
DR BioGRID; 4383857; 294.
DR BioGRID; 4383858; 273.
DR BioGRID; 4383859; 198.
DR BioGRID; 4383860; 359.
DR BioGRID; 4383861; 419.
DR BioGRID; 4383862; 369.
DR BioGRID; 4383863; 278.
DR BioGRID; 4383864; 525.
DR ComplexPortal; CPX-5685; SARS-CoV-2 main protease complex.
DR ComplexPortal; CPX-5687; SARS-CoV-2 NSP9 complex.
DR ComplexPortal; CPX-5688; SARS-CoV-2 NSP10-NSP16 2'-O-methyltransferase complex.
DR ComplexPortal; CPX-5689; SARS-CoV-2 NSP15 complex.
DR ComplexPortal; CPX-5690; SARS-CoV-2 primase complex.
DR ComplexPortal; CPX-5691; SARS-CoV-2 NSP3-NSP4-NSP6 complex.
DR ComplexPortal; CPX-5692; SARS-CoV-2 3'-5' exoribonuclease proof-reading complex.
DR ComplexPortal; CPX-5742; SARS-CoV-2 polymerase complex.
DR ComplexPortal; CPX-6442; SARS-CoV-2 replication and transcription complex.
DR ComplexPortal; CPX-7041; SARS-CoV-2 Cap(0)-replication and transcription complex.
DR IntAct; P0DTD1; 981.
DR BindingDB; P0DTD1; -.
DR ChEMBL; CHEMBL4523582; -.
DR DrugBank; DB15797; GC-373.
DR DrugBank; DB15796; GC-376 free acid.
DR DrugBank; DB16691; Nirmatrelvir.
DR DrugBank; DB16514; PF-07304814.
DR DrugBank; DB14761; Remdesivir.
DR DrugCentral; P0DTD1; -.
DR DNASU; 43740578; -.
DR GeneID; 43740578; -.
DR KEGG; vg:43740578; -.
DR BRENDA; 2.7.7.48; 16869.
DR Reactome; R-HSA-191859; snRNP Assembly. [P0DTD1-1]
DR Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway. [P0DTD1-1]
DR Reactome; R-HSA-9694271; Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC).
DR Reactome; R-HSA-9694301; Maturation of replicase proteins.
DR Reactome; R-HSA-9694676; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR Reactome; R-HSA-9694686; Replication of the SARS-CoV-2 genome.
DR Reactome; R-HSA-9694786; Transcription of SARS-CoV-2 sgRNAs.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SABIO-RK; P0DTD1; -.
DR Proteomes; UP000464024; Genome.
DR GO; GO:0039714; C:cytoplasmic viral factory; ISS:UniProtKB.
DR GO; GO:0062243; C:double membrane vesicle viral factory outer membrane; TAS:Reactome.
DR GO; GO:1905369; C:endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:1902555; C:endoribonuclease complex; IPI:ComplexPortal.
DR GO; GO:1905354; C:exoribonuclease complex; IPI:ComplexPortal.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0044174; C:host cell endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; IC:ComplexPortal.
DR GO; GO:0005845; C:mRNA cap binding complex; IPI:ComplexPortal.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0031381; C:viral RNA-directed RNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019785; F:ISG15-specific peptidase activity; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:ComplexPortal.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039519; P:modulation by virus of host autophagy; ISS:UniProtKB.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:1902680; P:positive regulation of RNA biosynthetic process; IMP:ComplexPortal.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:ComplexPortal.
DR GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; ISS:UniProtKB.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; ISS:UniProtKB.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; ISS:UniProtKB.
DR GO; GO:0039604; P:suppression by virus of host translation; ISS:UniProtKB.
DR GO; GO:0039501; P:suppression by virus of host type I interferon production; ISS:UniProtKB.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; ISS:UniProtKB.
DR GO; GO:0039723; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001172; P:transcription, RNA-templated; ISS:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0046786; P:viral replication complex formation and maintenance; IC:ComplexPortal.
DR GO; GO:0039694; P:viral RNA genome replication; IDA:ComplexPortal.
DR GO; GO:0019083; P:viral transcription; ISS:UniProtKB.
DR CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21516; cv_beta_Nsp2_SARS-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21591; SARS-CoV-like_RdRp; 1.
DR CDD; cd21525; SUD_C_SARS-CoV_Nsp3; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR DisProt; DP02925; -.
DR Gene3D; 1.10.150.420; -; 1.
DR Gene3D; 1.10.1840.10; -; 1.
DR Gene3D; 1.10.8.1190; -; 1.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.30.160.820; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.220.20; -; 1.
DR Gene3D; 3.40.220.30; -; 1.
DR Gene3D; 3.40.30.150; -; 1.
DR Gene3D; 3.40.50.11020; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044315; NSP14_betaCoV.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR044330; NSP15_alpha_betaCoV_N.
DR InterPro; IPR044322; NSP15_M_alpha_beta_CoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR021590; NSP1_bCoV.
DR InterPro; IPR038030; NSP1_sf_bCoV.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044389; NSP2_SARS-CoV-like.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR024358; NSP3_N_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR038166; NSP3_PL2pro_sf_bCoV.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044864; NSP3_SUD-N_bCoV.
DR InterPro; IPR043478; NSP3_SUD-N_sf_bCoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044367; NSP6_betaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013016; Peptidase_C16_CoV.
DR InterPro; IPR008740; Peptidase_C30_CoV.
DR InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043177; PLpro_N_sf_CoV.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR044351; RdRp_SARS-CoV-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR009469; RNA_pol_N_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF16251; bCoV_NAR; 1.
DR Pfam; PF11501; bCoV_NSP1; 1.
DR Pfam; PF12379; bCoV_NSP3_N; 1.
DR Pfam; PF12124; bCoV_SUD_C; 1.
DR Pfam; PF11633; bCoV_SUD_M; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF19216; CoV_NSP15_M; 1.
DR Pfam; PF19219; CoV_NSP15_N; 1.
DR Pfam; PF19212; CoV_NSP2_C; 1.
DR Pfam; PF19211; CoV_NSP2_N; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; SSF159936; SSF159936; 1.
DR SUPFAM; SSF160099; SSF160099; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51963; BCOV_NSP1_C; 1.
DR PROSITE; PS51942; BCOV_NSP3C_C; 1.
DR PROSITE; PS51941; BCOV_NSP3C_M; 1.
DR PROSITE; PS51994; BCOV_NSP3E_G2M; 1.
DR PROSITE; PS51945; BCOV_NSP3E_NAB; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51962; COV_NSP1; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51991; COV_NSP2_C; 1.
DR PROSITE; PS51990; COV_NSP2_M; 1.
DR PROSITE; PS51989; COV_NSP2_N; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51940; SARS_NSP3C_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Decay of host mRNAs by virus; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
KW Host cytoplasm; Host endoplasmic reticulum; Host endosome;
KW Host gene expression shutoff by virus; Host Golgi apparatus; Host membrane;
KW Host mRNA suppression by virus; Host nucleus; Host-virus interaction;
KW Hydrolase; Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host ISG15 by virus;
KW Inhibition of host NF-kappa-B by virus;
KW Inhibition of host RLR pathway by virus; Inhibition of host TBK1 by virus;
KW Inhibition of host TLR pathway by virus; Leucine-rich repeat; Lyase;
KW Membrane; Metal-binding; Methyltransferase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..7096
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000449618"
FT CHAIN 1..180
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449619"
FT CHAIN 181..818
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449620"
FT CHAIN 819..2763
FT /note="Papain-like protease nsp3"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449621"
FT CHAIN 2764..3263
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449622"
FT CHAIN 3264..3569
FT /note="3C-like proteinase nsp5"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449623"
FT CHAIN 3570..3859
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449624"
FT CHAIN 3860..3942
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449625"
FT CHAIN 3943..4140
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449626"
FT CHAIN 4141..4253
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449627"
FT CHAIN 4254..4392
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449628"
FT CHAIN 4393..5324
FT /note="RNA-directed RNA polymerase nsp12"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449629"
FT CHAIN 5325..5925
FT /note="Helicase nsp13"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449630"
FT CHAIN 5926..6452
FT /note="Proofreading exoribonuclease nsp14"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449631"
FT CHAIN 6453..6798
FT /note="Uridylate-specific endoribonuclease nsp15"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449632"
FT CHAIN 6799..7096
FT /note="2'-O-methyltransferase nsp16"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449633"
FT TOPO_DOM 1..2225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2226..2246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2247..2317
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 2318..2338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2339..2775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2776..2796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2797..3044
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3045..3065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3066..3099
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3100..3120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3121..3127
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3128..3148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3149..3586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3587..3607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3608
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3609..3629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3630..3634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3635..3655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3656..3673
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3674..3694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3695..3729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3730..3750
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3751..3778
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3779..3799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3800..7096
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 12..127
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 148..179
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 183..456
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 458..688
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT REPEAT 545..569
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT DOMAIN 690..818
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT REPEAT 697..719
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT DOMAIN 821..929
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1025..1194
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1231..1359
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1367..1494
FT /note="Macro 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1496..1561
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1565..1620
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1634..1898
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT REPEAT 1680..1702
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT DOMAIN 1911..2021
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2046..2155
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2660..2763
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3165..3263
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT REPEAT 3185..3206
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 3264..3569
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3860..3942
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT REPEAT 3935..3959
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 3943..4140
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT REPEAT 3977..4004
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT DOMAIN 4141..4253
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4254..4392
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4399..4653
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT REPEAT 4591..4616
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT DOMAIN 4757..5324
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 5004..5166
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5325..5408
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT REPEAT 5552..5572
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT DOMAIN 5581..5762
FT /note="(+)RNA virus helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 5763..5932
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 5997..6212
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6221..6452
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6453..6513
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6514..6639
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6656..6795
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6800..7094
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT REPEAT 6817..6841
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT ZN_FING 1752..1789
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT REGION 154..180
FT /note="Binding to 40s ribosome mRNA entry channel"
FT /evidence="ECO:0000269|PubMed:32680882,
FT ECO:0000269|PubMed:32908316"
FT REGION 200..236
FT /note="C2H2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 323..344
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 370..416
FT /note="C2HC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 926..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4937..4947
FT /note="Interaction with RMP Remdesivir"
FT /evidence="ECO:0000269|PubMed:32358203"
FT REGION 6339..6353
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT COMPBIAS 927..947
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1674
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444,
FT ECO:0000269|PubMed:32726803"
FT ACT_SITE 1835
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3304
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772,
FT ECO:0000305|PubMed:32198291"
FT ACT_SITE 3408
FT /note="Nucleophile; for 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772,
FT ECO:0000269|PubMed:32198291"
FT ACT_SITE 5151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 6015
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6017
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6686
FT /note="Proton donor; for uridylate-specific
FT endoribonuclease nsp15 activity"
FT /evidence="ECO:0000269|PubMed:33504779,
FT ECO:0000269|PubMed:33564093"
FT ACT_SITE 6701
FT /note="Proton acceptor; for uridylate-specific
FT endoribonuclease nsp15 activity"
FT /evidence="ECO:0000269|PubMed:33504779,
FT ECO:0000269|PubMed:33564093"
FT ACT_SITE 6741
FT /note="For uridylate-specific endoribonuclease nsp15
FT activity"
FT /evidence="ECO:0000269|PubMed:33504779"
FT ACT_SITE 6844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6928
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6968
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 7001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT BINDING 4693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT BINDING 4698
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT BINDING 4702
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT BINDING 4879
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT BINDING 5034
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT BINDING 5037
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT BINDING 5038
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT BINDING 5329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5606..5613
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT BINDING 6132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6256..6262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6741..6745
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000269|PubMed:33504779,
FT ECO:0000269|PubMed:33564093"
FT BINDING 6792..6796
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000269|PubMed:33564093"
FT SITE 180..181
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 818..819
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 2763..2764
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 3263..3264
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 3569..3570
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 3859..3860
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 3942..3943
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 4140..4141
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 4253..4254
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 4392..4393
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 5324..5325
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 5925..5926
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 6452..6453
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 6741
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:33504779,
FT ECO:0000269|PubMed:33564093"
FT SITE 6745
FT /note="Uracil recognition site"
FT /evidence="ECO:0000269|PubMed:33504779,
FT ECO:0000269|PubMed:33564093"
FT SITE 6798..6799
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT VARIANT 135
FT /note="S -> R (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 141..143
FT /note="Missing (in strain: Omicron/BA.4)"
FT /evidence="ECO:0000305"
FT VARIANT 265
FT /note="T -> I (in strain: Iota/B.1.526, Beta/B.1.351 and
FT Epsilon/B.1.427/B.1.429)"
FT /evidence="ECO:0000305"
FT VARIANT 842
FT /note="T -> I (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 856
FT /note="K -> R (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 1001
FT /note="T -> I (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 1055
FT /note="T -> A (in strain: Mu/B.1.621)"
FT /evidence="ECO:0000305"
FT VARIANT 1188
FT /note="S -> L (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 1246
FT /note="T -> I (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 1307
FT /note="G -> S (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT VARIANT 1538
FT /note="T -> I (in strain: Mu/B.1.621)"
FT /evidence="ECO:0000305"
FT VARIANT 1554
FT /note="D -> G (in strain: Theta/P.3)"
FT /evidence="ECO:0000305"
FT VARIANT 1567
FT /note="T -> I (in strain: Kappa/B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 1655
FT /note="K -> N (in strain: Beta/B.1.351)"
FT /evidence="ECO:0000305"
FT VARIANT 1708
FT /note="A -> D (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 1795
FT /note="K -> Q (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 2007
FT /note="T -> I (in strain: Eta/B.1.525)"
FT /evidence="ECO:0000305"
FT VARIANT 2083..2084
FT /note="SL -> I (in strain:Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 2230
FT /note="I -> T (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 2287
FT /note="P -> S (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 2387
FT /note="F -> V (in strain: Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 2625
FT /note="S -> F (in strain: Theta/P.3)"
FT /evidence="ECO:0000305"
FT VARIANT 2710
FT /note="A -> T (in strain:Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 2980
FT /note="D -> N (in strain: Theta/P.3)"
FT /evidence="ECO:0000305"
FT VARIANT 3027
FT /note="L -> F (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 3090
FT /note="T -> I (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 3201
FT /note="L -> F (in strain: Omicron/BA.2, Omicron/BA.2.12.1)"
FT /evidence="ECO:0000305"
FT VARIANT 3201
FT /note="L -> P (in strain: Iota/B.1.526, Lambda/C.37 and
FT Theta/P.3)"
FT /evidence="ECO:0000305"
FT VARIANT 3255
FT /note="T -> I (in strain: Lambda/C.37, Mu/B.1.621, 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 3353
FT /note="K -> R (in strain: Beta/B.1.351)"
FT /evidence="ECO:0000305"
FT VARIANT 3395
FT /note="P -> 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 3468
FT /note="L -> V (in strain: Zeta/P.2)"
FT /evidence="ECO:0000305"
FT VARIANT 3646
FT /note="T -> A (in strain: Kappa/B.1.617.1)"
FT VARIANT 3674..3676
FT /note="Missing (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 3675..3677
FT /note="Missing (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 3675
FT /note="S -> K (in strain: Alpha/B.1.1.7, Beta/B.1.351,
FT Gamma/P.1, Eta/B.1.525, Iota/B.1.526 and Lambda/C.37)"
FT /evidence="ECO:0000305"
FT VARIANT 3676..3678
FT /note="Missing (in strain: Alpha/B.1.1.7, Beta/B.1.351,
FT Gamma/P.1, Eta/B.1.525, Iota/B.1.526 and Lambda/C.37)"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:33413740"
FT VARIANT 3681
FT /note="D -> E (in strain: Theta/P.3)"
FT /evidence="ECO:0000305"
FT VARIANT 3729
FT /note="Q -> R (in strain: Mu/B.1.621)"
FT /evidence="ECO:0000305"
FT VARIANT 3758
FT /note="I -> V (in strain: Omicron/BA.1)"
FT /evidence="ECO:0000305"
FT VARIANT 3930
FT /note="L -> F (in strain: Theta/P.3 and Zeta/P.2)"
FT /evidence="ECO:0000305"
FT VARIANT 4715
FT /note="P -> F (in strain: Eta/B.1.525)"
FT /evidence="ECO:0000305"
FT VARIANT 4715
FT /note="P -> L (in strain: Alpha/B.1.1.7, Beta/B.1.351,
FT Gamma/P.1, Delta/B.1.617.2 Iota/B.1.526, Kappa/B.1.617.1,
FT Lambda/C.7, Epsilon/B.1.427/B.1.429, Theta/P.3, Zeta/P.2,
FT Mu/B.1.621, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 5063
FT /note="G -> S (in strain: Delta/B.1.617.2)"
FT /evidence="ECO:0000305"
FT VARIANT 5401
FT /note="P -> L (in strain: Delta/B.1.617.2)"
FT /evidence="ECO:0000305"
FT VARIANT 5412
FT /note="Q -> H (in strain: Iota/B.1.526)"
FT /evidence="ECO:0000305"
FT VARIANT 5584
FT /note="D -> Y (in strain: Epsilon/B.1.427/B.1.429)"
FT /evidence="ECO:0000305"
FT VARIANT 5665
FT /note="E -> D (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 5692
FT /note="A -> V (in strain: Theta/P.3)"
FT /evidence="ECO:0000305"
FT VARIANT 5716
FT /note="R -> C (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 5743
FT /note="P -> S (in strain: Mu/B.1.621)"
FT /evidence="ECO:0000305"
FT VARIANT 5753
FT /note="M -> I (in strain: Kappa/B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 5967
FT /note="I -> V (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 6564
FT /note="T -> I (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 6711
FT /note="K -> R (in strain: Kappa/B.1.617.1)"
FT /evidence="ECO:0000305"
FT MUTAGEN 154..157
FT /note="YEDF->AEDA: Complete loss of ribosome binding and
FT cellular translation inhibition."
FT /evidence="ECO:0000269|PubMed:32908316"
FT MUTAGEN 164..165
FT /note="KH->AA: Complete loss of ribosome binding and
FT cellular translation inhibition."
FT /evidence="ECO:0000269|PubMed:32908316"
FT MUTAGEN 164
FT /note="K->A: Complete loss of ribosome binding and cellular
FT translation inhibition."
FT /evidence="ECO:0000269|PubMed:32680882"
FT MUTAGEN 165
FT /note="H->A: Complete loss of ribosome binding and cellular
FT translation inhibition."
FT /evidence="ECO:0000269|PubMed:32680882"
FT MUTAGEN 171..175
FT /note="RELMR->EELME: Complete loss of ribosome binding and
FT cellular translation inhibition."
FT /evidence="ECO:0000269|PubMed:32908316"
FT MUTAGEN 1629
FT /note="V->A: Partial loss of ISG15 cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1632
FT /note="F->A: Partial loss of ISG15 cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1638
FT /note="T->A: Partial loss of ubiquitin cleavage in vitro;
FT no effect on ISG15 cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1638
FT /note="T->L: Increased cleavage of ubiquitin in vitro; no
FT effect on ISG15 cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1674
FT /note="C->A: Unable to remove host IFIH1 (MDA5)
FT ISGylation."
FT /evidence="ECO:0000269|PubMed:33727702"
FT MUTAGEN 1674
FT /note="C->S: Complete loss of PL-pro activity."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1831
FT /note="Y->G,T: Reduced inhibition by GRL-0617."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 5253
FT /note="S->A: Reduces RdRp inhibition by remdesivir."
FT /evidence="ECO:0000269|PubMed:32526208"
FT MUTAGEN 6686
FT /note="H->A: Complete loss of NSP15 endonuclease activity."
FT /evidence="ECO:0000269|PubMed:33504779"
FT MUTAGEN 6701
FT /note="H->A: Complete loss of NSP15 endonuclease activity."
FT /evidence="ECO:0000269|PubMed:33504779"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:7EQ4"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:7EQ4"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:7EQ4"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:7EQ4"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:7EQ4"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:7EQ4"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:7EQ4"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7K7P"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:7EQ4"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:7EQ4"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:7EQ4"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:7EQ4"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:7MSX"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:7MSX"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:7MSX"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 384..391
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 409..417
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 420..432
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 443..454
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 455..466
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 471..478
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 484..491
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 496..504
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 507..515
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 539..547
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 559..573
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 605..617
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 625..635
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 636..641
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 642..653
FT /evidence="ECO:0007829|PDB:7MSX"
FT HELIX 673..682
FT /evidence="ECO:0007829|PDB:7MSX"
FT STRAND 821..824
FT /evidence="ECO:0007829|PDB:7TI9"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:7TI9"
FT STRAND 830..833
FT /evidence="ECO:0007829|PDB:7TI9"
FT STRAND 836..843
FT /evidence="ECO:0007829|PDB:7TI9"
FT TURN 847..849
FT /evidence="ECO:0007829|PDB:7TI9"
FT HELIX 850..856
FT /evidence="ECO:0007829|PDB:7TI9"
FT STRAND 859..863
FT /evidence="ECO:0007829|PDB:7TI9"
FT HELIX 868..883
FT /evidence="ECO:0007829|PDB:7TI9"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:7TI9"
FT HELIX 887..890
FT /evidence="ECO:0007829|PDB:7TI9"
FT TURN 891..894
FT /evidence="ECO:0007829|PDB:7TI9"
FT HELIX 897..901
FT /evidence="ECO:0007829|PDB:7TI9"
FT STRAND 906..909
FT /evidence="ECO:0007829|PDB:7TI9"
FT STRAND 918..925
FT /evidence="ECO:0007829|PDB:7TI9"
FT STRAND 1030..1033
FT /evidence="ECO:0007829|PDB:7BF3"
FT STRAND 1035..1043
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1045..1052
FT /evidence="ECO:0007829|PDB:7KR0"
FT STRAND 1055..1060
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1070..1078
FT /evidence="ECO:0007829|PDB:7KR0"
FT TURN 1079..1081
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1082..1094
FT /evidence="ECO:0007829|PDB:7KR0"
FT STRAND 1102..1106
FT /evidence="ECO:0007829|PDB:7KR0"
FT TURN 1108..1110
FT /evidence="ECO:0007829|PDB:7KR0"
FT STRAND 1112..1117
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1122..1124
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1130..1136
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1137..1140
FT /evidence="ECO:0007829|PDB:7KR0"
FT STRAND 1141..1146
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1152..1154
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1158..1168
FT /evidence="ECO:0007829|PDB:7KR0"
FT STRAND 1171..1176
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1180..1191
FT /evidence="ECO:0007829|PDB:7KR0"
FT HELIX 1497..1508
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1509..1511
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1514..1516
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1524..1530
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1533..1538
FT /evidence="ECO:0007829|PDB:7THH"
FT TURN 1539..1542
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1543..1546
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1549..1551
FT /evidence="ECO:0007829|PDB:7THH"
FT HELIX 1553..1561
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1567..1578
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1580..1585
FT /evidence="ECO:0007829|PDB:7THH"
FT HELIX 1590..1594
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1595..1599
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1605..1607
FT /evidence="ECO:0007829|PDB:6W9C"
FT HELIX 1611..1613
FT /evidence="ECO:0007829|PDB:7THH"
FT STRAND 1617..1620
FT /evidence="ECO:0007829|PDB:7THH"
FT HELIX 1625..1635
FT /evidence="ECO:0007829|PDB:6WRH"
FT HELIX 1642..1653
FT /evidence="ECO:0007829|PDB:6WRH"
FT TURN 1671..1673
FT /evidence="ECO:0007829|PDB:6WX4"
FT HELIX 1674..1683
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1690..1692
FT /evidence="ECO:0007829|PDB:6WRH"
FT HELIX 1693..1703
FT /evidence="ECO:0007829|PDB:6WRH"
FT HELIX 1708..1718
FT /evidence="ECO:0007829|PDB:6WRH"
FT HELIX 1728..1737
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1745..1752
FT /evidence="ECO:0007829|PDB:6WRH"
FT TURN 1753..1755
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1756..1763
FT /evidence="ECO:0007829|PDB:6WRH"
FT HELIX 1765..1768
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1769..1772
FT /evidence="ECO:0007829|PDB:6WRH"
FT HELIX 1776..1781
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1783..1786
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1790..1816
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1822..1830
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1833..1849
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1852..1869
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1871..1874
FT /evidence="ECO:0007829|PDB:6WRH"
FT STRAND 1914..1916
FT /evidence="ECO:0007829|PDB:7LGO"
FT STRAND 1929..1931
FT /evidence="ECO:0007829|PDB:7LGO"
FT HELIX 1935..1942
FT /evidence="ECO:0007829|PDB:7LGO"
FT TURN 1943..1946
FT /evidence="ECO:0007829|PDB:7LGO"
FT STRAND 1954..1959
FT /evidence="ECO:0007829|PDB:7LGO"
FT STRAND 1965..1971
FT /evidence="ECO:0007829|PDB:7LGO"
FT HELIX 1972..1974
FT /evidence="ECO:0007829|PDB:7LGO"
FT HELIX 1977..1979
FT /evidence="ECO:0007829|PDB:7LGO"
FT STRAND 1983..1985
FT /evidence="ECO:0007829|PDB:7LGO"
FT STRAND 1988..1997
FT /evidence="ECO:0007829|PDB:7LGO"
FT TURN 2000..2002
FT /evidence="ECO:0007829|PDB:7LGO"
FT HELIX 2003..2012
FT /evidence="ECO:0007829|PDB:7LGO"
FT STRAND 2060..2065
FT /evidence="ECO:0007829|PDB:7T9W"
FT STRAND 2070..2072
FT /evidence="ECO:0007829|PDB:7T9W"
FT STRAND 2075..2079
FT /evidence="ECO:0007829|PDB:7T9W"
FT STRAND 2087..2089
FT /evidence="ECO:0007829|PDB:7T9W"
FT HELIX 2092..2100
FT /evidence="ECO:0007829|PDB:7T9W"
FT HELIX 2112..2116
FT /evidence="ECO:0007829|PDB:7T9W"
FT HELIX 2122..2125
FT /evidence="ECO:0007829|PDB:7T9W"
FT HELIX 2126..2129
FT /evidence="ECO:0007829|PDB:7T9W"
FT HELIX 2135..2141
FT /evidence="ECO:0007829|PDB:7T9W"
FT STRAND 2673..2675
FT /evidence="ECO:0007829|PDB:7RQG"
FT HELIX 2685..2693
FT /evidence="ECO:0007829|PDB:7RQG"
FT STRAND 2697..2699
FT /evidence="ECO:0007829|PDB:7RQG"
FT HELIX 2701..2706
FT /evidence="ECO:0007829|PDB:7RQG"
FT STRAND 2711..2714
FT /evidence="ECO:0007829|PDB:7RQG"
FT HELIX 2715..2720
FT /evidence="ECO:0007829|PDB:7RQG"
FT HELIX 2723..2735
FT /evidence="ECO:0007829|PDB:7RQG"
FT STRAND 2740..2743
FT /evidence="ECO:0007829|PDB:7RQG"
FT HELIX 3274..3277
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3280..3285
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3288..3295
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3298..3302
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3303..3306
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3311..3313
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3317..3321
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3326..3328
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3329..3333
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3336..3338
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3340..3346
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3349..3356
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3363..3366
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3374..3381
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3384..3392
FT /evidence="ECO:0007829|PDB:7K3T"
FT TURN 3406..3409
FT /evidence="ECO:0007829|PDB:7LDX"
FT STRAND 3411..3416
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3419..3429
FT /evidence="ECO:0007829|PDB:7K3T"
FT TURN 3431..3433
FT /evidence="ECO:0007829|PDB:7K40"
FT STRAND 3435..3438
FT /evidence="ECO:0007829|PDB:7K3T"
FT STRAND 3444..3447
FT /evidence="ECO:0007829|PDB:7JKV"
FT STRAND 3450..3453
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3464..3476
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3480..3482
FT /evidence="ECO:0007829|PDB:7MHL"
FT HELIX 3490..3499
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3507..3512
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3514..3520
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3524..3537
FT /evidence="ECO:0007829|PDB:7K3T"
FT TURN 3538..3541
FT /evidence="ECO:0007829|PDB:7M00"
FT STRAND 3544..3546
FT /evidence="ECO:0007829|PDB:7CA8"
FT STRAND 3547..3549
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3556..3564
FT /evidence="ECO:0007829|PDB:7K3T"
FT HELIX 3565..3568
FT /evidence="ECO:0007829|PDB:7C8T"
FT HELIX 3860..3878
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 3881..3883
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 3885..3899
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 3904..3920
FT /evidence="ECO:0007829|PDB:6XIP"
FT TURN 3922..3924
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 3927..3930
FT /evidence="ECO:0007829|PDB:6WTC"
FT HELIX 3952..3970
FT /evidence="ECO:0007829|PDB:6YYT"
FT HELIX 3996..4017
FT /evidence="ECO:0007829|PDB:7C2K"
FT HELIX 4021..4040
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 4043..4053
FT /evidence="ECO:0007829|PDB:6XIP"
FT STRAND 4058..4060
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 4061..4066
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4069..4074
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 4077..4083
FT /evidence="ECO:0007829|PDB:6XIP"
FT STRAND 4088..4091
FT /evidence="ECO:0007829|PDB:6XIP"
FT STRAND 4094..4102
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 4111..4113
FT /evidence="ECO:0007829|PDB:6XIP"
FT TURN 4116..4118
FT /evidence="ECO:0007829|PDB:6XIP"
FT HELIX 4119..4121
FT /evidence="ECO:0007829|PDB:6XIP"
FT STRAND 4124..4132
FT /evidence="ECO:0007829|PDB:6XIP"
FT STRAND 4144..4160
FT /evidence="ECO:0007829|PDB:7KRI"
FT STRAND 4168..4175
FT /evidence="ECO:0007829|PDB:7KRI"
FT STRAND 4178..4187
FT /evidence="ECO:0007829|PDB:7KRI"
FT STRAND 4193..4195
FT /evidence="ECO:0007829|PDB:7KRI"
FT HELIX 4198..4200
FT /evidence="ECO:0007829|PDB:7KRI"
FT STRAND 4203..4209
FT /evidence="ECO:0007829|PDB:7KRI"
FT STRAND 4213..4219
FT /evidence="ECO:0007829|PDB:7KRI"
FT STRAND 4222..4231
FT /evidence="ECO:0007829|PDB:7KRI"
FT HELIX 4236..4249
FT /evidence="ECO:0007829|PDB:7KRI"
FT HELIX 4263..4271
FT /evidence="ECO:0007829|PDB:6ZPE"
FT STRAND 4273..4275
FT /evidence="ECO:0007829|PDB:6ZPE"
FT HELIX 4276..4285
FT /evidence="ECO:0007829|PDB:6ZPE"
FT STRAND 4307..4311
FT /evidence="ECO:0007829|PDB:6ZPE"
FT STRAND 4318..4322
FT /evidence="ECO:0007829|PDB:6ZPE"
FT HELIX 4324..4326
FT /evidence="ECO:0007829|PDB:6ZPE"
FT HELIX 4328..4332
FT /evidence="ECO:0007829|PDB:6ZPE"
FT HELIX 4339..4341
FT /evidence="ECO:0007829|PDB:6W4H"
FT STRAND 4348..4353
FT /evidence="ECO:0007829|PDB:6ZPE"
FT HELIX 4354..4356
FT /evidence="ECO:0007829|PDB:6ZPE"
FT HELIX 4360..4366
FT /evidence="ECO:0007829|PDB:6ZPE"
FT TURN 4371..4373
FT /evidence="ECO:0007829|PDB:6ZPE"
FT STRAND 4374..4376
FT /evidence="ECO:0007829|PDB:6ZPE"
FT TURN 4377..4380
FT /evidence="ECO:0007829|PDB:6ZPE"
FT HELIX 4383..4385
FT /evidence="ECO:0007829|PDB:7KOA"
FT HELIX 4394..4404
FT /evidence="ECO:0007829|PDB:7C2K"
FT STRAND 4410..4412
FT /evidence="ECO:0007829|PDB:7C2K"
FT STRAND 4416..4418
FT /evidence="ECO:0007829|PDB:7BTF"
FT STRAND 4424..4430
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4435..4441
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4449..4451
FT /evidence="ECO:0007829|PDB:7C2K"
FT HELIX 4453..4455
FT /evidence="ECO:0007829|PDB:7C2K"
FT STRAND 4457..4461
FT /evidence="ECO:0007829|PDB:7C2K"
FT STRAND 4463..4465
FT /evidence="ECO:0007829|PDB:7C2K"
FT HELIX 4477..4481
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4482..4484
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4486..4488
FT /evidence="ECO:0007829|PDB:7C2K"
FT STRAND 4493..4496
FT /evidence="ECO:0007829|PDB:7C2K"
FT STRAND 4498..4501
FT /evidence="ECO:0007829|PDB:7C2K"
FT STRAND 4503..4508
FT /evidence="ECO:0007829|PDB:7C2K"
FT STRAND 4513..4515
FT /evidence="ECO:0007829|PDB:6M71"
FT HELIX 4516..4524
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4528..4530
FT /evidence="ECO:0007829|PDB:7BV1"
FT HELIX 4532..4540
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4546..4550
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4552..4555
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4557..4559
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4563..4567
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4568..4570
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4571..4591
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4593..4596
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4599..4601
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4602..4606
FT /evidence="ECO:0007829|PDB:6YYT"
FT STRAND 4623..4625
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4627..4639
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4642..4647
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4649..4651
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4653..4655
FT /evidence="ECO:0007829|PDB:6YYT"
FT HELIX 4668..4678
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4690..4692
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4696..4709
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4710..4712
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4715..4717
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4718..4727
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4730..4740
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4741..4743
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4744..4747
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4753..4756
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4760..4768
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4770..4776
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4777..4784
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4789..4796
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4809..4817
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4818..4821
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4840..4845
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4846..4850
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4858..4868
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4869..4872
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4873..4875
FT /evidence="ECO:0007829|PDB:6YYT"
FT HELIX 4882..4884
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4890..4893
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4898..4900
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4904..4910
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4913..4922
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4923..4925
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4931..4936
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4941..4943
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4948..4951
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4954..4973
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 4976..4979
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4986..4988
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 4989..4997
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 4998..5000
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5002..5008
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5014..5017
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5020..5030
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5031..5033
FT /evidence="ECO:0007829|PDB:7BV2"
FT TURN 5035..5037
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5040..5054
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5058..5060
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5062..5067
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5074..5076
FT /evidence="ECO:0007829|PDB:6YYT"
FT HELIX 5079..5100
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5104..5106
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5110..5124
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5131..5144
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5145..5150
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5153..5159
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5160..5164
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5166..5168
FT /evidence="ECO:0007829|PDB:6M71"
FT HELIX 5171..5181
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5188..5190
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5192..5194
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5197..5199
FT /evidence="ECO:0007829|PDB:6M71"
FT STRAND 5204..5206
FT /evidence="ECO:0007829|PDB:6M71"
FT STRAND 5207..5214
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5217..5223
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5226..5234
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5235..5237
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5239..5242
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5244..5258
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5259..5263
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5264..5266
FT /evidence="ECO:0007829|PDB:6YYT"
FT HELIX 5267..5286
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5302..5308
FT /evidence="ECO:0007829|PDB:6YYT"
FT HELIX 5310..5314
FT /evidence="ECO:0007829|PDB:7BV2"
FT HELIX 5315..5317
FT /evidence="ECO:0007829|PDB:7BV2"
FT STRAND 5327..5329
FT /evidence="ECO:0007829|PDB:5RLL"
FT TURN 5330..5332
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5335..5337
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5339..5343
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5351..5358
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5359..5362
FT /evidence="ECO:0007829|PDB:5RLG"
FT STRAND 5366..5373
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5384..5386
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5387..5390
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5393..5396
FT /evidence="ECO:0007829|PDB:5RL9"
FT TURN 5397..5399
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5405..5409
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5410..5413
FT /evidence="ECO:0007829|PDB:5ROB"
FT TURN 5416..5419
FT /evidence="ECO:0007829|PDB:7NIO"
FT HELIX 5428..5435
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5441..5449
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5452..5470
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5476..5481
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5483..5485
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5487..5491
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5493..5495
FT /evidence="ECO:0007829|PDB:5RM2"
FT STRAND 5501..5503
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5506..5511
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5513..5517
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5521..5525
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5533..5539
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5548..5551
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5584..5589
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5590..5597
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5599..5605
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5608..5610
FT /evidence="ECO:0007829|PDB:7NIO"
FT HELIX 5612..5622
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5623..5626
FT /evidence="ECO:0007829|PDB:5RLL"
FT STRAND 5628..5634
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5635..5648
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5651..5653
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5654..5656
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5660..5662
FT /evidence="ECO:0007829|PDB:7NIO"
FT STRAND 5669..5673
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5677..5683
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5684..5686
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5689..5697
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5700..5702
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5705..5714
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5715..5724
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5743..5745
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5748..5755
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5759..5761
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5764..5768
FT /evidence="ECO:0007829|PDB:5RM2"
FT HELIX 5770..5780
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5786..5789
FT /evidence="ECO:0007829|PDB:5RM2"
FT STRAND 5795..5799
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5805..5807
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5810..5812
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5814..5826
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5828..5832
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5834..5838
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5840..5850
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5854..5856
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5857..5860
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5865..5871
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5877..5880
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5882..5889
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5892..5901
FT /evidence="ECO:0007829|PDB:5RL9"
FT HELIX 5903..5908
FT /evidence="ECO:0007829|PDB:5RL9"
FT STRAND 5911..5913
FT /evidence="ECO:0007829|PDB:5RL9"
FT TURN 5945..5947
FT /evidence="ECO:0007829|PDB:7MC5"
FT TURN 5951..5953
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 5956..5958
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 5961..5963
FT /evidence="ECO:0007829|PDB:7QGI"
FT TURN 5964..5966
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 5968..5970
FT /evidence="ECO:0007829|PDB:7N0C"
FT STRAND 5978..5980
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 5992..5994
FT /evidence="ECO:0007829|PDB:7N0C"
FT HELIX 6001..6006
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 6008..6010
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6011..6021
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6023..6025
FT /evidence="ECO:0007829|PDB:7N0D"
FT STRAND 6029..6036
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6041..6044
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6047..6051
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6053..6055
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6057..6060
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 6069..6079
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 6084..6099
FT /evidence="ECO:0007829|PDB:7MC5"
FT TURN 6100..6102
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6107..6112
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 6114..6120
FT /evidence="ECO:0007829|PDB:7MC5"
FT TURN 6121..6123
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6124..6126
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6133..6138
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6141..6143
FT /evidence="ECO:0007829|PDB:7MC5"
FT TURN 6144..6147
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6148..6150
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6152..6154
FT /evidence="ECO:0007829|PDB:7MC6"
FT STRAND 6160..6163
FT /evidence="ECO:0007829|PDB:7MC5"
FT STRAND 6165..6168
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 6169..6171
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 6178..6185
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 6195..6211
FT /evidence="ECO:0007829|PDB:7MC5"
FT HELIX 6227..6249
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6252..6258
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6265..6267
FT /evidence="ECO:0007829|PDB:7N0D"
FT STRAND 6271..6277
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6282..6284
FT /evidence="ECO:0007829|PDB:7QGI"
FT HELIX 6288..6292
FT /evidence="ECO:0007829|PDB:7QGI"
FT TURN 6295..6297
FT /evidence="ECO:0007829|PDB:7N0D"
FT STRAND 6298..6302
FT /evidence="ECO:0007829|PDB:7N0D"
FT STRAND 6304..6311
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6314..6316
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6319..6326
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6333..6337
FT /evidence="ECO:0007829|PDB:7QGI"
FT HELIX 6339..6341
FT /evidence="ECO:0007829|PDB:7N0C"
FT STRAND 6343..6353
FT /evidence="ECO:0007829|PDB:7QGI"
FT HELIX 6358..6361
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6364..6366
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6398..6400
FT /evidence="ECO:0007829|PDB:7QGI"
FT HELIX 6401..6404
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6405..6407
FT /evidence="ECO:0007829|PDB:7N0D"
FT HELIX 6410..6428
FT /evidence="ECO:0007829|PDB:7QGI"
FT STRAND 6431..6436
FT /evidence="ECO:0007829|PDB:7QGI"
FT HELIX 6441..6447
FT /evidence="ECO:0007829|PDB:7QGI"
FT HELIX 6454..6464
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6476..6479
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6482..6487
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6490..6496
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6499..6501
FT /evidence="ECO:0007829|PDB:6WLC"
FT HELIX 6503..6511
FT /evidence="ECO:0007829|PDB:6WLC"
FT HELIX 6521..6526
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6531..6536
FT /evidence="ECO:0007829|PDB:6WLC"
FT TURN 6540..6543
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6544..6548
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6550..6553
FT /evidence="ECO:0007829|PDB:6WLC"
FT TURN 6555..6557
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6558..6562
FT /evidence="ECO:0007829|PDB:6WLC"
FT HELIX 6566..6568
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6569..6571
FT /evidence="ECO:0007829|PDB:6X1B"
FT STRAND 6573..6576
FT /evidence="ECO:0007829|PDB:6WLC"
FT HELIX 6582..6588
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6590..6598
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6612..6614
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6617..6619
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6622..6624
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6629..6634
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6637..6639
FT /evidence="ECO:0007829|PDB:5SAG"
FT STRAND 6652..6654
FT /evidence="ECO:0007829|PDB:7KEG"
FT HELIX 6660..6667
FT /evidence="ECO:0007829|PDB:6WLC"
FT HELIX 6670..6676
FT /evidence="ECO:0007829|PDB:6WLC"
FT TURN 6680..6683
FT /evidence="ECO:0007829|PDB:6X4I"
FT HELIX 6684..6687
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6689..6691
FT /evidence="ECO:0007829|PDB:7KEG"
FT STRAND 6693..6696
FT /evidence="ECO:0007829|PDB:6WLC"
FT HELIX 6703..6712
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6715..6718
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6726..6734
FT /evidence="ECO:0007829|PDB:6WLC"
FT TURN 6735..6737
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6740..6747
FT /evidence="ECO:0007829|PDB:6WLC"
FT HELIX 6751..6758
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6765..6774
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6777..6786
FT /evidence="ECO:0007829|PDB:6WLC"
FT STRAND 6789..6795
FT /evidence="ECO:0007829|PDB:6WLC"
FT HELIX 6800..6803
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6804..6808
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 6811..6814
FT /evidence="ECO:0007829|PDB:7L6T"
FT TURN 6826..6829
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 6840..6852
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6860..6862
FT /evidence="ECO:0007829|PDB:7LW3"
FT STRAND 6864..6869
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 6878..6886
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6892..6899
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6905..6911
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 6913..6915
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6916..6920
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6922..6927
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 6932..6935
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 6947..6958
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6959..6969
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6971..6973
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 6976..6982
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 6985..6993
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 6994..6996
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 7002..7009
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 7019..7032
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 7040..7043
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 7056..7058
FT /evidence="ECO:0007829|PDB:7L6T"
FT HELIX 7062..7064
FT /evidence="ECO:0007829|PDB:6W4H"
FT HELIX 7067..7074
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 7078..7081
FT /evidence="ECO:0007829|PDB:7L6T"
FT STRAND 7088..7090
FT /evidence="ECO:0007829|PDB:7L6T"
SQ SEQUENCE 7096 AA; 794058 MW; A4E62D97150BB8CC CRC64;
MESLVPGFNE KTHVQLSLPV LQVRDVLVRG FGDSVEEVLS EARQHLKDGT CGLVEVEKGV
LPQLEQPYVF IKRSDARTAP HGHVMVELVA ELEGIQYGRS GETLGVLVPH VGEIPVAYRK
VLLRKNGNKG AGGHSYGADL KSFDLGDELG TDPYEDFQEN WNTKHSSGVT RELMRELNGG
AYTRYVDNNF CGPDGYPLEC IKDLLARAGK ASCTLSEQLD FIDTKRGVYC CREHEHEIAW
YTERSEKSYE LQTPFEIKLA KKFDTFNGEC PNFVFPLNSI IKTIQPRVEK KKLDGFMGRI
RSVYPVASPN ECNQMCLSTL MKCDHCGETS WQTGDFVKAT CEFCGTENLT KEGATTCGYL
PQNAVVKIYC PACHNSEVGP EHSLAEYHNE SGLKTILRKG GRTIAFGGCV FSYVGCHNKC
AYWVPRASAN IGCNHTGVVG EGSEGLNDNL LEILQKEKVN INIVGDFKLN EEIAIILASF
SASTSAFVET VKGLDYKAFK QIVESCGNFK VTKGKAKKGA WNIGEQKSIL SPLYAFASEA
ARVVRSIFSR TLETAQNSVR VLQKAAITIL DGISQYSLRL IDAMMFTSDL ATNNLVVMAY
ITGGVVQLTS QWLTNIFGTV YEKLKPVLDW LEEKFKEGVE FLRDGWEIVK FISTCACEIV
GGQIVTCAKE IKESVQTFFK LVNKFLALCA DSIIIGGAKL KALNLGETFV THSKGLYRKC
VKSREETGLL MPLKAPKEII FLEGETLPTE VLTEEVVLKT GDLQPLEQPT SEAVEAPLVG
TPVCINGLML LEIKDTEKYC ALAPNMMVTN NTFTLKGGAP TKVTFGDDTV IEVQGYKSVN
ITFELDERID KVLNEKCSAY TVELGTEVNE FACVVADAVI KTLQPVSELL TPLGIDLDEW
SMATYYLFDE SGEFKLASHM YCSFYPPDED EEEGDCEEEE FEPSTQYEYG TEDDYQGKPL
EFGATSAALQ PEEEQEEDWL DDDSQQTVGQ QDGSEDNQTT TIQTIVEVQP QLEMELTPVV
QTIEVNSFSG YLKLTDNVYI KNADIVEEAK KVKPTVVVNA ANVYLKHGGG VAGALNKATN
NAMQVESDDY IATNGPLKVG GSCVLSGHNL AKHCLHVVGP NVNKGEDIQL LKSAYENFNQ
HEVLLAPLLS AGIFGADPIH SLRVCVDTVR TNVYLAVFDK NLYDKLVSSF LEMKSEKQVE
QKIAEIPKEE VKPFITESKP SVEQRKQDDK KIKACVEEVT TTLEETKFLT ENLLLYIDIN
GNLHPDSATL VSDIDITFLK KDAPYIVGDV VQEGVLTAVV IPTKKAGGTT EMLAKALRKV
PTDNYITTYP GQGLNGYTVE EAKTVLKKCK SAFYILPSII SNEKQEILGT VSWNLREMLA
HAEETRKLMP VCVETKAIVS TIQRKYKGIK IQEGVVDYGA RFYFYTSKTT VASLINTLND
LNETLVTMPL GYVTHGLNLE EAARYMRSLK VPATVSVSSP DAVTAYNGYL TSSSKTPEEH
FIETISLAGS YKDWSYSGQS TQLGIEFLKR GDKSVYYTSN PTTFHLDGEV ITFDNLKTLL
SLREVRTIKV FTTVDNINLH TQVVDMSMTY GQQFGPTYLD GADVTKIKPH NSHEGKTFYV
LPNDDTLRVE AFEYYHTTDP SFLGRYMSAL NHTKKWKYPQ VNGLTSIKWA DNNCYLATAL
LTLQQIELKF NPPALQDAYY RARAGEAANF CALILAYCNK TVGELGDVRE TMSYLFQHAN
LDSCKRVLNV VCKTCGQQQT TLKGVEAVMY MGTLSYEQFK KGVQIPCTCG KQATKYLVQQ
ESPFVMMSAP PAQYELKHGT FTCASEYTGN YQCGHYKHIT SKETLYCIDG ALLTKSSEYK
GPITDVFYKE NSYTTTIKPV TYKLDGVVCT EIDPKLDNYY KKDNSYFTEQ PIDLVPNQPY
PNASFDNFKF VCDNIKFADD LNQLTGYKKP ASRELKVTFF PDLNGDVVAI DYKHYTPSFK
KGAKLLHKPI VWHVNNATNK ATYKPNTWCI RCLWSTKPVE TSNSFDVLKS EDAQGMDNLA
CEDLKPVSEE VVENPTIQKD VLECNVKTTE VVGDIILKPA NNSLKITEEV GHTDLMAAYV
DNSSLTIKKP NELSRVLGLK TLATHGLAAV NSVPWDTIAN YAKPFLNKVV STTTNIVTRC
LNRVCTNYMP YFFTLLLQLC TFTRSTNSRI KASMPTTIAK NTVKSVGKFC LEASFNYLKS
PNFSKLINII IWFLLLSVCL GSLIYSTAAL GVLMSNLGMP SYCTGYREGY LNSTNVTIAT
YCTGSIPCSV CLSGLDSLDT YPSLETIQIT ISSFKWDLTA FGLVAEWFLA YILFTRFFYV
LGLAAIMQLF FSYFAVHFIS NSWLMWLIIN LVQMAPISAM VRMYIFFASF YYVWKSYVHV
VDGCNSSTCM MCYKRNRATR VECTTIVNGV RRSFYVYANG GKGFCKLHNW NCVNCDTFCA
GSTFISDEVA RDLSLQFKRP INPTDQSSYI VDSVTVKNGS IHLYFDKAGQ KTYERHSLSH
FVNLDNLRAN NTKGSLPINV IVFDGKSKCE ESSAKSASVY YSQLMCQPIL LLDQALVSDV
GDSAEVAVKM FDAYVNTFSS TFNVPMEKLK TLVATAEAEL AKNVSLDNVL STFISAARQG
FVDSDVETKD VVECLKLSHQ SDIEVTGDSC NNYMLTYNKV ENMTPRDLGA CIDCSARHIN
AQVAKSHNIA LIWNVKDFMS LSEQLRKQIR SAAKKNNLPF KLTCATTRQV VNVVTTKIAL
KGGKIVNNWL KQLIKVTLVF LFVAAIFYLI TPVHVMSKHT DFSSEIIGYK AIDGGVTRDI
ASTDTCFANK HADFDTWFSQ RGGSYTNDKA CPLIAAVITR EVGFVVPGLP GTILRTTNGD
FLHFLPRVFS AVGNICYTPS KLIEYTDFAT SACVLAAECT IFKDASGKPV PYCYDTNVLE
GSVAYESLRP DTRYVLMDGS IIQFPNTYLE GSVRVVTTFD SEYCRHGTCE RSEAGVCVST
SGRWVLNNDY YRSLPGVFCG VDAVNLLTNM FTPLIQPIGA LDISASIVAG GIVAIVVTCL
AYYFMRFRRA FGEYSHVVAF NTLLFLMSFT VLCLTPVYSF LPGVYSVIYL YLTFYLTNDV
SFLAHIQWMV MFTPLVPFWI TIAYIICIST KHFYWFFSNY LKRRVVFNGV SFSTFEEAAL
CTFLLNKEMY LKLRSDVLLP LTQYNRYLAL YNKYKYFSGA MDTTSYREAA CCHLAKALND
FSNSGSDVLY QPPQTSITSA VLQSGFRKMA FPSGKVEGCM VQVTCGTTTL NGLWLDDVVY
CPRHVICTSE DMLNPNYEDL LIRKSNHNFL VQAGNVQLRV IGHSMQNCVL KLKVDTANPK
TPKYKFVRIQ PGQTFSVLAC YNGSPSGVYQ CAMRPNFTIK GSFLNGSCGS VGFNIDYDCV
SFCYMHHMEL PTGVHAGTDL EGNFYGPFVD RQTAQAAGTD TTITVNVLAW LYAAVINGDR
WFLNRFTTTL NDFNLVAMKY NYEPLTQDHV DILGPLSAQT GIAVLDMCAS LKELLQNGMN
GRTILGSALL EDEFTPFDVV RQCSGVTFQS AVKRTIKGTH HWLLLTILTS LLVLVQSTQW
SLFFFLYENA FLPFAMGIIA MSAFAMMFVK HKHAFLCLFL LPSLATVAYF NMVYMPASWV
MRIMTWLDMV DTSLSGFKLK DCVMYASAVV LLILMTARTV YDDGARRVWT LMNVLTLVYK
VYYGNALDQA ISMWALIISV TSNYSGVVTT VMFLARGIVF MCVEYCPIFF ITGNTLQCIM
LVYCFLGYFC TCYFGLFCLL NRYFRLTLGV YDYLVSTQEF RYMNSQGLLP PKNSIDAFKL
NIKLLGVGGK PCIKVATVQS KMSDVKCTSV VLLSVLQQLR VESSSKLWAQ CVQLHNDILL
AKDTTEAFEK MVSLLSVLLS MQGAVDINKL CEEMLDNRAT LQAIASEFSS LPSYAAFATA
QEAYEQAVAN GDSEVVLKKL KKSLNVAKSE FDRDAAMQRK LEKMADQAMT QMYKQARSED
KRAKVTSAMQ TMLFTMLRKL DNDALNNIIN NARDGCVPLN IIPLTTAAKL MVVIPDYNTY
KNTCDGTTFT YASALWEIQQ VVDADSKIVQ LSEISMDNSP NLAWPLIVTA LRANSAVKLQ
NNELSPVALR QMSCAAGTTQ TACTDDNALA YYNTTKGGRF VLALLSDLQD LKWARFPKSD
GTGTIYTELE PPCRFVTDTP KGPKVKYLYF IKGLNNLNRG MVLGSLAATV RLQAGNATEV
PANSTVLSFC AFAVDAAKAY KDYLASGGQP ITNCVKMLCT HTGTGQAITV TPEANMDQES
FGGASCCLYC RCHIDHPNPK GFCDLKGKYV QIPTTCANDP VGFTLKNTVC TVCGMWKGYG
CSCDQLREPM LQSADAQSFL NRVCGVSAAR LTPCGTGTST DVVYRAFDIY NDKVAGFAKF
LKTNCCRFQE KDEDDNLIDS YFVVKRHTFS NYQHEETIYN LLKDCPAVAK HDFFKFRIDG
DMVPHISRQR LTKYTMADLV YALRHFDEGN CDTLKEILVT YNCCDDDYFN KKDWYDFVEN
PDILRVYANL GERVRQALLK TVQFCDAMRN AGIVGVLTLD NQDLNGNWYD FGDFIQTTPG
SGVPVVDSYY SLLMPILTLT RALTAESHVD TDLTKPYIKW DLLKYDFTEE RLKLFDRYFK
YWDQTYHPNC VNCLDDRCIL HCANFNVLFS TVFPPTSFGP LVRKIFVDGV PFVVSTGYHF
RELGVVHNQD VNLHSSRLSF KELLVYAADP AMHAASGNLL LDKRTTCFSV AALTNNVAFQ
TVKPGNFNKD FYDFAVSKGF FKEGSSVELK HFFFAQDGNA AISDYDYYRY NLPTMCDIRQ
LLFVVEVVDK YFDCYDGGCI NANQVIVNNL DKSAGFPFNK WGKARLYYDS MSYEDQDALF
AYTKRNVIPT ITQMNLKYAI SAKNRARTVA GVSICSTMTN RQFHQKLLKS IAATRGATVV
IGTSKFYGGW HNMLKTVYSD VENPHLMGWD YPKCDRAMPN MLRIMASLVL ARKHTTCCSL
SHRFYRLANE CAQVLSEMVM CGGSLYVKPG GTSSGDATTA YANSVFNICQ AVTANVNALL
STDGNKIADK YVRNLQHRLY ECLYRNRDVD TDFVNEFYAY LRKHFSMMIL SDDAVVCFNS
TYASQGLVAS IKNFKSVLYY QNNVFMSEAK CWTETDLTKG PHEFCSQHTM LVKQGDDYVY
LPYPDPSRIL GAGCFVDDIV KTDGTLMIER FVSLAIDAYP LTKHPNQEYA DVFHLYLQYI
RKLHDELTGH MLDMYSVMLT NDNTSRYWEP EFYEAMYTPH TVLQAVGACV LCNSQTSLRC
GACIRRPFLC CKCCYDHVIS TSHKLVLSVN PYVCNAPGCD VTDVTQLYLG GMSYYCKSHK
PPISFPLCAN GQVFGLYKNT CVGSDNVTDF NAIATCDWTN AGDYILANTC TERLKLFAAE
TLKATEETFK LSYGIATVRE VLSDRELHLS WEVGKPRPPL NRNYVFTGYR VTKNSKVQIG
EYTFEKGDYG DAVVYRGTTT YKLNVGDYFV LTSHTVMPLS APTLVPQEHY VRITGLYPTL
NISDEFSSNV ANYQKVGMQK YSTLQGPPGT GKSHFAIGLA LYYPSARIVY TACSHAAVDA
LCEKALKYLP IDKCSRIIPA RARVECFDKF KVNSTLEQYV FCTVNALPET TADIVVFDEI
SMATNYDLSV VNARLRAKHY VYIGDPAQLP APRTLLTKGT LEPEYFNSVC RLMKTIGPDM
FLGTCRRCPA EIVDTVSALV YDNKLKAHKD KSAQCFKMFY KGVITHDVSS AINRPQIGVV
REFLTRNPAW RKAVFISPYN SQNAVASKIL GLPTQTVDSS QGSEYDYVIF TQTTETAHSC
NVNRFNVAIT RAKVGILCIM SDRDLYDKLQ FTSLEIPRRN VATLQAENVT GLFKDCSKVI
TGLHPTQAPT HLSVDTKFKT EGLCVDIPGI PKDMTYRRLI SMMGFKMNYQ VNGYPNMFIT
REEAIRHVRA WIGFDVEGCH ATREAVGTNL PLQLGFSTGV NLVAVPTGYV DTPNNTDFSR
VSAKPPPGDQ FKHLIPLMYK GLPWNVVRIK IVQMLSDTLK NLSDRVVFVL WAHGFELTSM
KYFVKIGPER TCCLCDRRAT CFSTASDTYA CWHHSIGFDY VYNPFMIDVQ QWGFTGNLQS
NHDLYCQVHG NAHVASCDAI MTRCLAVHEC FVKRVDWTIE YPIIGDELKI NAACRKVQHM
VVKAALLADK FPVLHDIGNP KAIKCVPQAD VEWKFYDAQP CSDKAYKIEE LFYSYATHSD
KFTDGVCLFW NCNVDRYPAN SIVCRFDTRV LSNLNLPGCD GGSLYVNKHA FHTPAFDKSA
FVNLKQLPFF YYSDSPCESH GKQVVSDIDY VPLKSATCIT RCNLGGAVCR HHANEYRLYL
DAYNMMISAG FSLWVYKQFD TYNLWNTFTR LQSLENVAFN VVNKGHFDGQ QGEVPVSIIN
NTVYTKVDGV DVELFENKTT LPVNVAFELW AKRNIKPVPE VKILNNLGVD IAANTVIWDY
KRDAPAHIST IGVCSMTDIA KKPTETICAP LTVFFDGRVD GQVDLFRNAR NGVLITEGSV
KGLQPSVGPK QASLNGVTLI GEAVKTQFNY YKKVDGVVQQ LPETYFTQSR NLQEFKPRSQ
MEIDFLELAM DEFIERYKLE GYAFEHIVYG DFSHSQLGGL HLLIGLAKRF KESPFELEDF
IPMDSTVKNY FITDAQTGSS KCVCSVIDLL LDDFVEIIKS QDLSVVSKVV KVTIDYTEIS
FMLWCKDGHV ETFYPKLQSS QAWQPGVAMP NLYKMQRMLL EKCDLQNYGD SATLPKGIMM
NVAKYTQLCQ YLNTLTLAVP YNMRVIHFGA GSDKGVAPGT AVLRQWLPTG TLLVDSDLND
FVSDADSTLI GDCATVHTAN KWDLIISDMY DPKTKNVTKE NDSKEGFFTY ICGFIQQKLA
LGGSVAIKIT EHSWNADLYK LMGHFAWWTA FVTNVNASSS EAFLIGCNYL GKPREQIDGY
VMHANYIFWR NTNPIQLSSY SLFDMSKFPL KLRGTAVMSL KEGQINDMIL SLLSKGRLII
RENNRVVISS DVLVNN
