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   28-JUN-2023, entry version 17.
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=RNA-capping enzyme subunit nsp9;
DE     AltName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE              EC=2.7.7.50 {ECO:0000269|PubMed:35944563};
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=Guanine-N7 methyltransferase nsp14;
DE              EC=2.1.1.56 {ECO:0000269|PubMed:35944563};
DE              EC=3.1.13.-;
DE     AltName: Full=Non-structural protein 14;
DE              Short=nsp14;
DE     AltName: Full=Proofreading exoribonuclease nsp14;
DE              Short=ExoN;
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   DISORDERED REGIONS.
RX   PubMed=35108439; DOI=10.1111/febs.16379;
RA   Quaglia F., Salladini E., Carraro M., Minervini G., Tosatto S.C.E.,
RA   Le Mercier P.;
RT   "SARS-CoV-2 variants preferentially emerge at intrinsically disordered
RT   protein sites helping immune evasion.";
RL   FEBS J. 289:4240-4250(2022).
RN   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16] {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   [17]
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   [18]
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   [19]
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   [20]
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   [21]
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   [22]
RP   FUNCTION (RNA-CAPPING ENZYME NSP9), FUNCTION (RNA-DIRECTED RNA POLYMERASE
RP   NSP12), FUNCTION (GUANINE-N7 METHYLTRANSFERASE NSP14), FUNCTION
RP   (NON-STRUCTURAL PROTEIN 10), FUNCTION (2'-O-METHYLTRANSFERASE NSP16),
RP   MUTAGENESIS OF ASN-4141; ASN-4142 AND ARG-5125, INTERACTION WITH NSP9
RP   (RNA-DIRECTED RNA POLYMERASE NSP12), AND INTERACTION WITH NSP12
RP   (RNA-CAPPING ENZYME NSP9).
RX   PubMed=35944563; DOI=10.1038/s41586-022-05185-z;
RA   Park G.J., Osinski A., Hernandez G., Eitson J.L., Majumdar A., Tonelli M.,
RA   Henzler-Wildman K., Pawlowski K., Chen Z., Li Y., Schoggins J.W.,
RA   Tagliabracci V.S.;
RT   "The mechanism of RNA capping by SARS-CoV-2.";
RL   Nature 0:0-0(2022).
RN   [23]
RP   REVIEW, FUNCTION (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP15), SUBUNIT
RP   (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL PROTEIN 8), SUBUNIT
RP   (RNA-DIRECTED RNA POLYMERASE NSP12), AND SUBUNIT (NON-STRUCTURAL PROTEIN
RP   13).
RX   PubMed=34562452; DOI=10.1016/j.jbc.2021.101218;
RA   Perry J.K., Appleby T.C., Bilello J.P., Feng J.Y., Schmitz U.,
RA   Campbell E.A.;
RT   "An atomistic model of the coronavirus replication-transcription complex as
RT   a hexamer assembled around nsp15.";
RL   J. Biol. Chem. 297:101218-101218(2021).
RN   [24]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NSP12).
RX   PubMed=33713597; DOI=10.1016/j.molcel.2021.02.036;
RA   Wang D., Jiang A., Feng J., Li G., Guo D., Sajid M., Wu K., Zhang Q.,
RA   Ponty Y., Will S., Liu F., Yu X., Li S., Liu Q., Yang X.L., Guo M., Li X.,
RA   Chen M., Shi Z.L., Lan K., Chen Y., Zhou Y.;
RT   "The SARS-CoV-2 subgenome landscape and its novel regulatory features.";
RL   Mol. Cell 81:2135-2147(2021).
RN   [25]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 15).
RX   PubMed=35706445; DOI=10.3389/fgene.2022.904513;
RA   Liang J., Shi J., Chen S., Duan G., Yang F., Cheng Z., Li X., Ruan J.,
RA   Mi D., Gao S.;
RT   "How the Replication and Transcription Complex Functions in Jumping
RT   Transcription of SARS-CoV-2.";
RL   Front. Genet. 13:904513-904513(2022).
RN   [26]
RP   FUNCTION (3C-LIKE PROTEINASE NSP5), AND MUTAGENESIS OF CYS-3408.
RX   PubMed=35594856; DOI=10.1016/j.molcel.2022.04.033;
RG   COVID Human Genetic Effort;
RA   Planes R., Pinilla M., Santoni K., Hessel A., Passemar C., Lay K.,
RA   Paillette P., Valadao A.C., Robinson K.S., Bastard P., Lam N., Fadrique R.,
RA   Rossi I., Pericat D., Bagayoko S., Leon-Icaza S.A., Rombouts Y.,
RA   Perouzel E., Tiraby M., Zhang Q., Cicuta P., Jouanguy E., Neyrolles O.,
RA   Bryant C.E., Floto A.R., Goujon C., Lei F.Z., Martin-Blondel G., Silva S.,
RA   Casanova J.L., Cougoule C., Reversade B., Marcoux J., Ravet E., Meunier E.;
RT   "Human NLRP1 is a sensor of pathogenic coronavirus 3CL proteases in lung
RT   epithelial cells.";
RL   Mol. Cell 82:2385-2400(2022).
RN   [27]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 6), FUNCTION (NON-STRUCTURAL PROTEIN 3),
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4), SUBCELLULAR LOCATION (NON-STRUCTURAL
RP   PROTEIN 6), SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 3), SUBCELLULAR
RP   LOCATION (NON-STRUCTURAL PROTEIN 4), MUTAGENESIS OF 3675-SER--PHE-3677;
RP   PHE-3789 AND THR-3791, ACTIVITY REGULATION (NON-STRUCTURAL PROTEIN 6), AND
RP   INTERACTION WITH HOST ZFYVE1 (NON-STRUCTURAL PROTEIN 6).
RX   PubMed=35551511; DOI=10.1038/s41586-022-04835-6;
RA   Ricciardi S., Guarino A.M., Giaquinto L., Polishchuk E.V., Santoro M.,
RA   Di Tullio G., Wilson C., Panariello F., Soares V.C., Dias S.S.G.,
RA   Santos J.C., Souza T.M.L., Fusco G., Viscardi M., Brandi S., Bozza P.T.,
RA   Polishchuk R.S., Venditti R., De Matteis M.A.;
RT   "The role of NSP6 in the biogenesis of the SARS-CoV-2 replication
RT   organelle.";
RL   Nature 606:761-768(2022).
RN   [28]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 2), INTERACTION WITH HOST GIGYF2
RP   (NON-STRUCTURAL PROTEIN 2), SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   GLY-442.
RX   PubMed=35878012; DOI=10.1073/pnas.2204539119;
RA   Xu Z., Choi J.H., Dai D.L., Luo J., Ladak R.J., Li Q., Wang Y., Zhang C.,
RA   Wiebe S., Liu A.C.H., Ran X., Yang J., Naeli P., Garzia A., Zhou L.,
RA   Mahmood N., Deng Q., Elaish M., Lin R., Mahal L.K., Hobman T.C.,
RA   Pelletier J., Alain T., Vidal S.M., Duchaine T., Mazhab-Jafari M.T.,
RA   Mao X., Jafarnejad S.M., Sonenberg N.;
RT   "SARS-CoV-2 impairs interferon production via NSP2-induced repression of
RT   mRNA translation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 119:e2204539119-e2204539119(2022).
RN   [29]
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   [30]
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   [31]
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).
RN   [32]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.3 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP   7; NON-STRUCTURAL PROTEIN 8; NON-STRUCTURAL PROTEIN 9; NON-STRUCTURAL
RP   PROTEIN 10; RNA-DIRECTED RNA POLYMERASE NSP12 AND NON-STRUCTURAL PROTEIN
RP   13, SUBUNIT (NON-STRUCTURAL PROTEIN 8), SUBUNIT (NON-STRUCTURAL PROTEIN
RP   13), AND FUNCTION (NON-STRUCTURAL PROTEIN 13).
RX   PubMed=33232691; DOI=10.1016/j.cell.2020.11.016;
RA   Yan L., Ge J., Zheng L., Zhang Y., Gao Y., Wang T., Huang Y., Yang Y.,
RA   Gao S., Li M., Liu Z., Wang H., Li Y., Chen Y., Guddat L.W., Wang Q.,
RA   Rao Z., Lou Z.;
RT   "Cryo-EM Structure of an Extended SARS-CoV-2 Replication and Transcription
RT   Complex Reveals an Intermediate State in Cap Synthesis.";
RL   Cell 184:184-193(2021).
RN   [33] {ECO:0007744|PDB:7PKU}
RP   STRUCTURE BY NMR OF 834-929 (PAPAIN-LIKE PROTEASE NSP3), AND INTERACTION
RP   WITH N (PAPAIN-LIKE PROTEASE NSP3).
RX   PubMed=35044811; DOI=10.1126/sciadv.abm4034;
RA   Bessa L.M., Guseva S., Camacho-Zarco A.R., Salvi N., Maurin D., Perez L.M.,
RA   Botova M., Malki A., Nanao M., Jensen M.R., Ruigrok R.W.H., Blackledge M.;
RT   "The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex
RT   with its viral partner nsp3a.";
RL   Sci. Adv. 8:4034-4034(2022).
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]: Enhances mRNA repression of the
CC       4EHP-GYF2 complex in the host, thereby inhibiting the antiviral
CC       response and facilitating SARS-CoV-2 replication. Possibly acts in
CC       cooperation with nsp1, which induces ribosome stalling on host mRNA,
CC       triggering mRNA repression by the host 4EHP-GYF2 complex which is
CC       enhanced by nsp2. {ECO:0000269|PubMed:35878012}.
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
CC       (PubMed:35551511). Antagonizes innate immune induction of type I
CC       interferon by blocking the phosphorylation, dimerization and subsequent
CC       nuclear translocation of host IRF3 (PubMed:32733001). Prevents also
CC       host NF-kappa-B signaling (By similarity). In addition, PL-PRO
CC       possesses a deubiquitinating/deISGylating activity and processes both
CC       'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular
CC       substrates (PubMed:32726803). Cleaves preferentially ISG15 from
CC       antiviral protein IFIH1 (MDA5), but not RIGI (PubMed:33727702). Can
CC       play a role in host ADP-ribosylation by ADP-ribose (PubMed:32578982).
CC       Plays a role in the formation and maintenance of double membrane
CC       vesicles (DMVs) replication organelles (PubMed:35551511). DMVs are
CC       formed by nsp3 and nsp4, while nsp6 zippers ER membranes and connects
CC       to lipid droplets (PubMed:35551511). {ECO:0000250|UniProtKB:P0C6X7,
CC       ECO:0000269|PubMed:32578982, ECO:0000269|PubMed:32726803,
CC       ECO:0000269|PubMed:32733001, ECO:0000269|PubMed:33727702,
CC       ECO:0000269|PubMed:35551511}.
CC   -!- FUNCTION: [Non-structural protein 4]: Plays a role in the formation and
CC       maintenance of double membrane vesicles (DMVs) replication organelles
CC       (PubMed:35551511). DMVs are formed by nsp3 and nsp4, while nsp6 zippers
CC       ER membranes and connects to lipid droplets (PubMed:35551511).
CC       {ECO:0000269|PubMed:35551511}.
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). May cleave human NLRP1 in lung
CC       epithelial cells, thereby activating the NLRP1 inflammasome pathway
CC       (PubMed:35594856). May cleave human GSDMD, triggering alternative
CC       GSDME-mediated epithelial cell death upon activation of the NLRP1
CC       inflammasome, which may enhance the release interleukins 1B, 6, 16 and
CC       18 (PubMed:35594856). Also able to bind an ADP-ribose-1''-phosphate
CC       (ADRP) (PubMed:32198291, PubMed:32272481).
CC       {ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481,
CC       ECO:0000269|PubMed:32321856, ECO:0000269|PubMed:35594856}.
CC   -!- FUNCTION: [Non-structural protein 6]: Plays a role in the formation and
CC       maintenance of double membrane vesicles (DMVs) replication organelles
CC       (PubMed:35551511). DMVs are formed by nsp3 and nsp4, while nsp6 zippers
CC       ER membranes and connects to lipid droplets (PubMed:35551511). LDs are
CC       consumed during DMV formation (PubMed:35551511). Binds to host TBK1
CC       without affecting TBK1 phosphorylation; the interaction with TBK1
CC       decreases IRF3 phosphorylation, which leads to reduced IFN-beta
CC       production (PubMed:32979938). {ECO:0000269|PubMed:32979938,
CC       ECO:0000269|PubMed:35551511}.
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: [RNA-capping enzyme subunit nsp9]: Catalytic subunit of viral
CC       RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction
CC       for genomic and sub-genomic RNAs (PubMed:35944563). The kinase-like
CC       NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9,
CC       forming a covalent RNA-protein intermediate (PubMed:35944563).
CC       Subsequently, the NiRAN domain transfers RNA to GDP, forming the core
CC       cap structure GpppA-RNA (PubMed:35944563). The NSP14 and NSP16
CC       methyltransferases then add methyl groups to form functional cap
CC       structures (PubMed:35944563). Interacts with ribosome signal
CC       recognition particle RNA (SRP) (PubMed:33080218). Together with NSP8,
CC       suppress protein integration into the cell membrane, thereby disrupting
CC       host immune defenses (PubMed:33080218). {ECO:0000269|PubMed:33080218,
CC       ECO:0000269|PubMed:35944563}.
CC   -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC       transcription by stimulating both nsp14 3'-5' exoribonuclease (By
CC       similarity) and nsp16 2'-O-methyltransferase activities
CC       (PubMed:35944563). Therefore plays an essential role in viral mRNAs cap
CC       methylation. {ECO:0000250|UniProtKB:P0C6X7,
CC       ECO:0000269|PubMed:35944563}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase nsp12]: RNA-directed RNA
CC       polymerase that catalyzes the transcription of viral genomic and
CC       subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both
CC       the minus and positive strands of genomic RNA (PubMed:32277040,
CC       PubMed:32358203, PubMed:32438371, PubMed:32526208). Subgenomic RNAs
CC       (sgRNAs) are formed by discontinuous transcription: The polymerase has
CC       the ability to pause at transcription-regulating sequences (TRS) and
CC       jump to the leader TRS, resulting in a major deletion
CC       (PubMed:35706445). This creates a series of subgenomic RNAs that are
CC       replicated, transcribed and translated (PubMed:35706445). In addition,
CC       Nsp12 is a subunit of the viral RNA capping enzyme that catalyzes the
CC       RNA guanylyltransferase reaction for genomic and sub-genomic RNAs
CC       (PubMed:35944563). The kinase-like NiRAN domain of NSP12 transfers RNA
CC       to the amino terminus of NSP9, forming a covalent RNA-protein
CC       intermediate (PubMed:35944563). Subsequently, the NiRAN domain
CC       transfers RNA to GDP, and forms the core cap structure GpppA-RNA
CC       (PubMed:35944563). {ECO:0000269|PubMed:35706445,
CC       ECO:0000269|PubMed:35944563, ECO:0000305|PubMed:32277040,
CC       ECO:0000305|PubMed:32358203, ECO:0000305|PubMed:32438371,
CC       ECO:0000305|PubMed:32526208}.
CC   -!- FUNCTION: [Helicase nsp13]: Plays a role in viral RNA synthesis
CC       (PubMed:33232691). Multi-functional protein with a zinc-binding domain
CC       in N-terminus displaying RNA and DNA duplex-unwinding activities with
CC       5' to 3' polarity. Activity of helicase is dependent on magnesium (By
CC       similarity). Binds to host TBK1 and inhibits TBK1 phosphorylation; the
CC       interaction with TBK1 decreases IRF3 phosphorylation, which leads to
CC       reduced IFN-beta production (PubMed:32979938).
CC       {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32979938,
CC       ECO:0000305|PubMed:33232691}.
CC   -!- FUNCTION: [Guanine-N7 methyltransferase nsp14]: Plays a role in viral
CC       RNA synthesis through two distinct activities. The N7-guanine
CC       methyltransferase activity plays a role in the formation of the cap
CC       structure GpppA-RNA (PubMed:35944563). The proofreading exoribonuclease
CC       reduces the sensitivity of the virus to RNA mutagens during replication
CC       (By similarity). This activity acts on both ssRNA and dsRNA in a 3'-5'
CC       direction (By similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC       ECO:0000269|PubMed:35944563}.
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). May bind genomic dsRNA in association with the
CC       replication-transcription complex (RTC), and play a role in nsp12
CC       discontinous transcription (PubMed:34562452, PubMed:35706445).
CC       {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:33504779,
CC       ECO:0000305|PubMed:34562452, ECO:0000305|PubMed:35706445}.
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 (PubMed:35944563). N7-methyl guanosine cap is a
CC       prerequisite for binding of nsp16 (PubMed:35944563). Therefore plays an
CC       essential role in viral mRNAs cap methylation which is essential to
CC       evade immune system (PubMed:35944563). May disrupt host mRNA splicing
CC       in nucleus by interacting with pre-mRNA Recognition Domains ofthe U1
CC       and U2 snRNAs (PubMed:33080218). {ECO:0000269|PubMed:33080218,
CC       ECO:0000269|PubMed:35944563}.
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: [3C-like proteinase nsp5]:
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   -!- CATALYTIC ACTIVITY: [RNA-capping enzyme subunit nsp9]:
CC       Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC         end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC         Evidence={ECO:0000269|PubMed:35944563};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67014;
CC         Evidence={ECO:0000269|PubMed:35944563};
CC   -!- CATALYTIC ACTIVITY: [Guanine-N7 methyltransferase nsp14]:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC         S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC         COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC         ChEBI:CHEBI:167617; EC=2.1.1.56;
CC         Evidence={ECO:0000269|PubMed:35944563};
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   -!- COFACTOR: [RNA-directed RNA polymerase nsp12]:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:35944563};
CC   -!- ACTIVITY REGULATION: [Papain-like protease nsp3]: Inhibited in vitro by
CC       GRL-0617. {ECO:0000269|PubMed:32726803}.
CC   -!- ACTIVITY REGULATION: [Non-structural protein 6]: Inhibited ex vivo by
CC       K22. It may shift NSP6 zippering activity towards the nuclear envelope,
CC       thereby impairing formation of the NSP6-compartment necessary for viral
CC       transcription/replication. {ECO:0000269|PubMed:35551511}.
CC   -!- ACTIVITY REGULATION: [Guanine-N7 methyltransferase 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 GIGYF2.
CC       {ECO:0000269|PubMed:35878012}.
CC   -!- SUBUNIT: [Papain-like protease nsp3]: May form homohexamers
CC       (PubMed:32763915). Interacts with N protein (PubMed:35044811).
CC       {ECO:0000269|PubMed:32763915, ECO:0000269|PubMed:35044811}.
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]: Forms homodimers
CC       (PubMed:35551511). Interacts with host ZFYVE1 (DFCP1)
CC       (PubMed:35551511), which leads to ER and DMVs binding to lipid
CC       droplets. Interacts with host TBK1; this interaction decreases IRF3
CC       phosphorylation by 57%, which leads to reduced IFN-beta production.
CC       {ECO:0000269|PubMed:32979938, ECO:0000269|PubMed:35551511}.
CC   -!- SUBUNIT: [Non-structural protein 7]: Interacts with nsp8 and nsp12 to
CC       form the replication-transcription complex (RTC): nsp12, nsp7, two
CC       subunits of nsp8, and up to two subunits of nsp13 (PubMed:32277040,
CC       PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452).
CC       Eight copies of nsp7 and eight copies of nsp8 assemble to form a
CC       heterohexadecamer dsRNA-encircling ring structure (By similarity).
CC       {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32277040,
CC       ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32438371,
CC       ECO:0000269|PubMed:32526208, ECO:0000305|PubMed:34562452}.
CC   -!- SUBUNIT: [Non-structural protein 8]: Interacts with nsp7, nsp13 and
CC       nsp12 (PubMed:33232691) to form the replication-transcription complex
CC       (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of
CC       nsp13 (PubMed:32277040, PubMed:32358203, PubMed:32438371,
CC       PubMed:32526208, PubMed:34562452). Eight copies of nsp7 and eight
CC       copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC       ring structure (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       ECO:0000269|PubMed:33232691, ECO:0000305|PubMed:34562452}.
CC   -!- SUBUNIT: [RNA-capping enzyme subunit nsp9]: Is a dimer (By similarity).
CC       Interacts with NSP12 (PubMed:35944563). {ECO:0000250|UniProtKB:P0C6X7,
CC       ECO:0000269|PubMed:35944563}.
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 to form the replication-transcription complex (RTC): nsp12, nsp7,
CC       two subunits of nsp8, and up to two subunits of nsp13 (PubMed:32277040,
CC       PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452).
CC       Interacts with nsp9 (PubMed:35944563). {ECO:0000269|PubMed:32277040,
CC       ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32438371,
CC       ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:35944563,
CC       ECO:0000305|PubMed:34562452}.
CC   -!- SUBUNIT: [Helicase nsp13]: Interacts with nsp8 to form the replication-
CC       transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC       to two subunits of nsp13 (PubMed:33232691, PubMed:34562452). Interacts
CC       with host TBK1; this interaction inhibits TBK1 phosphorylation and
CC       decreases by 75% IRF3 phosphorylation, which leads to reduced IFN-beta
CC       production (PubMed:32979938). {ECO:0000269|PubMed:32979938,
CC       ECO:0000269|PubMed:33232691, ECO:0000305|PubMed:34562452}.
CC   -!- SUBUNIT: [Guanine-N7 methyltransferase 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=6; IntAct=EBI-25475864, EBI-995350;
CC       PRO_0000449623; Q13283: G3BP1; Xeno; NbExp=5; IntAct=EBI-25475864, EBI-1047359;
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; Q15904: ATP6AP1; Xeno; NbExp=12; IntAct=EBI-25475868, EBI-714667;
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=20; 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, ECO:0000269|PubMed:35878012}. Host
CC       endosome {ECO:0000269|PubMed:33060197}.
CC   -!- SUBCELLULAR LOCATION: [Papain-like protease nsp3]: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:35551511}. Note=Localizes in virally-induced
CC       cytoplasmic double-membrane vesicles (DMV).
CC       {ECO:0000269|PubMed:35551511}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:35551511}. Note=Localizes in virally-induced
CC       cytoplasmic double-membrane vesicles (DMV).
CC       {ECO:0000269|PubMed:35551511}.
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 endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:35551511}. Note=Localizes at zppered ER membranes
CC       close to double-membrane vesicles (DMV). {ECO:0000269|PubMed:35551511}.
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: [RNA-capping enzyme subunit nsp9]: Host
CC       cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host
CC       cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}.
CC       Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7,
CC       nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely
CC       perinuclear. 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: [Guanine-N7 methyltransferase 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   -!- POLYMORPHISM: Variant Omicron/BQ.1.1 belongs to a lineage first
CC       isolated in Nigeria (November 2022). {ECO:0000305}.
CC   -!- POLYMORPHISM: Variant Omicron/XBB.1.5 belongs to a lineage first
CC       isolated in United States (November 2022). It is the result of
CC       recombination between omicron BJ.1 and BM.1.1. Moreover XBB.1.5 do not
CC       express ORF8. {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   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; 5SOI; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOJ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOK; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOL; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOM; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SON; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOO; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOP; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOQ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOR; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOS; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOT; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOU; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOV; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOW; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOX; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOY; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SOZ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SP0; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SP1; X-ray; 1.03 A; A/B=1025-1191.
DR   PDB; 5SP2; X-ray; 0.97 A; A/B=1025-1191.
DR   PDB; 5SP3; X-ray; 1.01 A; A/B=1025-1191.
DR   PDB; 5SP4; X-ray; 1.06 A; A/B=1025-1191.
DR   PDB; 5SP6; X-ray; 1.07 A; A/B=1025-1191.
DR   PDB; 5SP7; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SP8; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SP9; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPA; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPB; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPC; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPD; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPE; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPF; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPG; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPH; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPI; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPJ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPK; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPL; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPM; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPN; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPO; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPP; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPQ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPR; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPS; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPT; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPU; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPV; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPW; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPX; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPY; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SPZ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ0; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ1; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ2; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ3; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ4; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ5; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ6; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ7; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ8; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQ9; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQA; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQB; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQC; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQD; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQE; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQF; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQG; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQH; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQI; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQJ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQK; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQL; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQM; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQN; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQO; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQP; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQQ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQR; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQS; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQT; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQU; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQV; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQW; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQX; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQY; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SQZ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR0; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR1; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR2; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR3; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR4; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR5; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR6; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR7; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SR8; X-ray; 1.10 A; A/B=1025-1191.
DR   PDB; 5SR9; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRA; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRB; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRC; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRD; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRE; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRF; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRG; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRH; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRI; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRJ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRK; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRL; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRM; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRN; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRO; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRP; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRQ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRR; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRS; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRT; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRU; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRV; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRW; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRX; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRY; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SRZ; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 5SS0; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS1; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS2; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS3; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS4; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS5; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS6; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS7; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS8; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SS9; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSA; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSB; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSC; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSD; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSE; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSF; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSG; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSH; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSI; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSJ; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSK; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSL; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSM; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSN; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSO; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSP; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSQ; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 5SSR; X-ray; 1.15 A; A/B=1025-1191.
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; 7CYQ; EM; 2.83 A; A=4393-5324, B=3943-4140, C=3860-3942, G=5325-5925, I=4142-4253.
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; 7FR0; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 7FR1; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 7FR2; X-ray; 1.15 A; A/B=1025-1191.
DR   PDB; 7FR3; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FR4; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FR5; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FR6; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FR7; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FR8; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FR9; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FRA; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FRB; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FRC; X-ray; 1.00 A; A/B=1025-1191.
DR   PDB; 7FRD; X-ray; 1.00 A; A/B=1025-1191.
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; 7LCR; X-ray; 1.95 A; A/B=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; 7MAT; X-ray; 2.74 A; A/B=3264-3569.
DR   PDB; 7MAU; X-ray; 1.95 A; A/B=3264-3569.
DR   PDB; 7MAV; X-ray; 1.91 A; A/B=3264-3569.
DR   PDB; 7MAW; X-ray; 2.07 A; A/B=3264-3569.
DR   PDB; 7MAX; X-ray; 1.98 A; A/B=3264-3569.
DR   PDB; 7MAZ; X-ray; 1.70 A; A/B=3264-3569.
DR   PDB; 7MB0; X-ray; 1.54 A; A/B=3264-3569.
DR   PDB; 7MB1; X-ray; 1.43 A; A/B=3264-3569.
DR   PDB; 7MB2; X-ray; 1.89 A; A/B=3264-3569.
DR   PDB; 7MB3; X-ray; 1.81 A; A/B/C/D/E/F=3264-3569.
DR   PDB; 7MB6; X-ray; 2.21 A; A/B=3264-3569, C=3854-3859.
DR   PDB; 7MB7; X-ray; 2.02 A; A=3264-3569, B=3937-3942.
DR   PDB; 7MB8; X-ray; 1.62 A; A/B/C/D=3264-3569, E/F/G/H=4135-4140.
DR   PDB; 7MB9; X-ray; 1.81 A; A/B=3264-3569, C/D=4387-4392.
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; 7NIJ; X-ray; 1.58 A; A=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; 7P2G; X-ray; 2.50 A; A=3264-3569.
DR   PDB; 7P2O; NMR; -; A=1498-1561.
DR   PDB; 7PFL; X-ray; 1.80 A; A=3264-3569.
DR   PDB; 7PFM; X-ray; 2.00 A; A/B=3264-3569.
DR   PDB; 7PHZ; X-ray; 1.66 A; A/B=3264-3569.
DR   PDB; 7PKU; NMR; -; A=834-929.
DR   PDB; 7PXZ; X-ray; 1.75 A; A=3264-3569.
DR   PDB; 7PZQ; X-ray; 2.25 A; A/B=3264-3569.
DR   PDB; 7Q5E; X-ray; 1.67 A; A/B=3264-3569.
DR   PDB; 7Q5F; X-ray; 1.72 A; A/B=3264-3569.
DR   PDB; 7QBB; X-ray; 2.00 A; A=3264-3569.
DR   PDB; 7QG7; X-ray; 1.72 A; A/B=1025-1194.
DR   PDB; 7QGI; X-ray; 1.65 A; D=5932-6449.
DR   PDB; 7QIF; X-ray; 2.53 A; D=5932-6452.
DR   PDB; 7QKA; X-ray; 1.80 A; A=3264-3569.
DR   PDB; 7QT5; X-ray; 2.26 A; A=3264-3568.
DR   PDB; 7QT6; X-ray; 2.11 A; A=3264-3568.
DR   PDB; 7QT7; X-ray; 2.25 A; A=3264-3568.
DR   PDB; 7QT8; X-ray; 2.01 A; A/B=3264-3569.
DR   PDB; 7QT9; X-ray; 2.43 A; A=3264-3568.
DR   PDB; 7R1T; X-ray; 2.70 A; A=6798-7096, B=4263-4384.
DR   PDB; 7R1U; X-ray; 2.50 A; A=6798-7096, B=4263-4384.
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; 7RVM; X-ray; 1.95 A; A=3264-3569.
DR   PDB; 7RVN; X-ray; 1.63 A; A=3264-3569.
DR   PDB; 7RVO; X-ray; 1.80 A; A/B=3264-3569.
DR   PDB; 7RVP; X-ray; 1.90 A; A/B=3264-3569.
DR   PDB; 7RVQ; X-ray; 2.48 A; A=3264-3569.
DR   PDB; 7RVR; X-ray; 2.46 A; A=3264-3569.
DR   PDB; 7RVS; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7RVT; X-ray; 2.10 A; A/B=3264-3569.
DR   PDB; 7RVU; X-ray; 2.50 A; A=3264-3569.
DR   PDB; 7RVV; X-ray; 3.00 A; A=3264-3569.
DR   PDB; 7RVW; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7RVX; X-ray; 1.85 A; A/B=3264-3569.
DR   PDB; 7RVY; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7RVZ; X-ray; 1.90 A; A=3264-3569.
DR   PDB; 7RW0; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7RW1; X-ray; 2.50 A; A/B=3264-3569.
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; 7S6W; X-ray; 2.29 A; A/B=3264-3569.
DR   PDB; 7S6X; X-ray; 1.80 A; A=3264-3569.
DR   PDB; 7S6Y; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7S6Z; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7S70; X-ray; 2.60 A; A=3264-3569.
DR   PDB; 7S71; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7S72; X-ray; 2.50 A; A=3264-3569.
DR   PDB; 7S73; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7S74; X-ray; 1.70 A; A/B=3264-3569.
DR   PDB; 7S75; X-ray; 1.80 A; A=3264-3569.
DR   PDB; 7S82; EM; 3.50 A; A/B/C/D=3259-3569.
DR   PDB; 7SD9; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7SDA; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7SDC; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7SET; X-ray; 1.70 A; A=3264-3569.
DR   PDB; 7SF1; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7SF3; X-ray; 1.75 A; A=3264-3569.
DR   PDB; 7SFB; X-ray; 1.90 A; A=3264-3569.
DR   PDB; 7SFH; X-ray; 1.40 A; A=3264-3569.
DR   PDB; 7SFI; X-ray; 1.95 A; A=3264-3569.
DR   PDB; 7SGH; X-ray; 1.85 A; A/B/C/D=3264-3569.
DR   PDB; 7SI9; X-ray; 2.00 A; A=3264-3569.
DR   PDB; 7T2T; X-ray; 1.45 A; A=3264-3569.
DR   PDB; 7T2U; X-ray; 2.10 A; A/B/C/D=3263-3569.
DR   PDB; 7T2V; X-ray; 2.47 A; A/B/C/D=3263-3569.
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; 7T70; X-ray; 2.35 A; A/B=3264-3569.
DR   PDB; 7T8M; X-ray; 1.60 A; A/B=3264-3569.
DR   PDB; 7T8R; X-ray; 1.74 A; A=3264-3569.
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; 7T9Y; X-ray; 2.18 A; A/B=3264-3569.
DR   PDB; 7TA4; X-ray; 1.78 A; A/B=3264-3569.
DR   PDB; 7TA7; X-ray; 2.28 A; A/B=3264-3569.
DR   PDB; 7TB2; X-ray; 1.80 A; A=3264-3569.
DR   PDB; 7TBT; X-ray; 2.45 A; A=3264-3569.
DR   PDB; 7TC4; X-ray; 1.94 A; A/B=3264-3569.
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; 7TEK; X-ray; 2.20 A; A=3264-3569.
DR   PDB; 7TEL; X-ray; 2.40 A; A=3264-3569.
DR   PDB; 7TFR; X-ray; 1.80 A; A=3264-3569.
DR   PDB; 7TGR; X-ray; 1.68 A; A=3264-3567.
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; 7TQ2; X-ray; 2.30 A; A/B=3264-3568.
DR   PDB; 7TQ3; X-ray; 2.00 A; A/B=3264-3568.
DR   PDB; 7TQ4; X-ray; 2.45 A; A=3264-3568.
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; 7TW7; X-ray; 1.62 A; A=6225-6452.
DR   PDB; 7TW8; X-ray; 1.55 A; A=6225-6452.
DR   PDB; 7TW9; X-ray; 1.41 A; A=6225-6452.
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; 7UKK; X-ray; 2.00 A; A=3264-3569.
DR   PDB; 7ULT; X-ray; 1.90 A; A/C=6799-7096, B/D=4254-4392.
DR   PDB; 7UU6; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7UU7; X-ray; 2.49 A; A=3264-3569.
DR   PDB; 7UU8; X-ray; 2.50 A; A=3264-3569.
DR   PDB; 7UU9; X-ray; 2.47 A; A=3264-3569.
DR   PDB; 7UUA; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7UUB; X-ray; 1.63 A; A=3264-3569.
DR   PDB; 7UUC; X-ray; 1.60 A; A=3264-3569.
DR   PDB; 7UUD; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7UUE; X-ray; 1.85 A; A=3264-3569.
DR   PDB; 7VAH; X-ray; 1.49 A; A=3264-3569.
DR   PDB; 7VVP; X-ray; 1.97 A; A/B=3266-3561.
DR   PDB; 7WHC; X-ray; 2.27 A; A/B/C/D=3264-3459.
DR   PDB; 7WOH; X-ray; 1.72 A; A/B=3264-3566.
DR   PDB; 7WQA; X-ray; 1.80 A; A=3264-3569.
DR   PDB; 7X6Y; X-ray; 1.39 A; B=3563-3569.
DR   PDB; 7X6Z; X-ray; 1.43 A; B=5319-5324.
DR   PDB; 7X70; X-ray; 1.25 A; B=4136-4140.
DR   PDB; 7YWR; NMR; -; A=3943-4026.
DR   PDB; 7Z2K; X-ray; 1.65 A; A/B=3264-3569.
DR   PDB; 7Z3U; X-ray; 1.72 A; A/B=3264-3569.
DR   PDB; 7Z59; X-ray; 2.00 A; A=3264-3568.
DR   PDB; 7ZB6; X-ray; 2.12 A; A/C=3264-3569.
DR   PDB; 7ZB7; X-ray; 1.63 A; A=3264-3569.
DR   PDB; 7ZB8; X-ray; 2.48 A; A/C=3264-3569.
DR   PDB; 7ZQV; X-ray; 2.26 A; A/B=3264-3569.
DR   PDB; 7ZV5; X-ray; 2.00 A; A=3264-3569.
DR   PDB; 7ZV7; X-ray; 1.34 A; A=3264-3569.
DR   PDB; 7ZV8; X-ray; 1.94 A; A/B=3264-3569.
DR   PDB; 8A4Q; X-ray; 1.75 A; A=3264-3569.
DR   PDB; 8A4T; X-ray; 2.50 A; A/B=3264-3568.
DR   PDB; 8A4Y; X-ray; 1.10 A; A=10-126.
DR   PDB; 8A55; X-ray; 0.99 A; A=10-126.
DR   PDB; 8ACD; X-ray; 1.39 A; A=3264-3569.
DR   PDB; 8ACL; X-ray; 1.40 A; A=3264-3569.
DR   PDB; 8AEB; X-ray; 1.83 A; A=3264-3569.
DR   PDB; 8AOU; NMR; -; A=1-180.
DR   PDB; 8AYW; X-ray; 1.10 A; B=10-126.
DR   PDB; 8AZ8; X-ray; 1.18 A; B=10-126.
DR   PDB; 8B2T; X-ray; 1.89 A; A=3264-3568.
DR   PDB; 8BSD; X-ray; 1.95 A; A=6799-7096, B=4254-4392.
DR   PDB; 8BZV; X-ray; 1.80 A; A=6799-7096, B=4254-4392.
DR   PDB; 8C19; X-ray; 1.95 A; A/B=1025-1191.
DR   PDB; 8C1A; X-ray; 1.90 A; A/B=1025-1191.
DR   PDB; 8C5M; X-ray; 1.90 A; A=6799-7096, B=4254-4392.
DR   PDB; 8CZW; X-ray; 1.70 A; A/B=3264-3568.
DR   PDB; 8CZX; X-ray; 1.65 A; A/B=3264-3568.
DR   PDB; 8D35; X-ray; 1.90 A; A/B=3264-3569.
DR   PDB; 8D4J; X-ray; 1.78 A; A/B=3264-3569.
DR   PDB; 8D4K; X-ray; 1.89 A; A=3264-3569.
DR   PDB; 8D4L; X-ray; 1.70 A; A/B=3264-3569.
DR   PDB; 8D4M; X-ray; 1.81 A; A=3264-3569.
DR   PDB; 8D4N; X-ray; 2.70 A; A/B=3264-3569.
DR   PDB; 8DCZ; X-ray; 2.38 A; A/B=3264-3569.
DR   PDB; 8DD1; X-ray; 2.03 A; A=3264-3569.
DR   PDB; 8DD9; X-ray; 2.04 A; A=3264-3569.
DR   PDB; 8DDI; X-ray; 2.80 A; A=3264-3569.
DR   PDB; 8DDM; X-ray; 2.78 A; A=3264-3569.
DR   PDB; 8DFE; X-ray; 1.89 A; A=3264-3569.
DR   PDB; 8DFN; X-ray; 2.04 A; A/B=3264-3569.
DR   PDB; 8DGB; X-ray; 2.87 A; A/B=3264-3569.
DR   PDB; 8DOX; X-ray; 1.46 A; A=3264-3565.
DR   PDB; 8DOY; X-ray; 1.59 A; A/B=3264-3564.
DR   PDB; 8DPR; X-ray; 2.00 A; A=3264-3569.
DR   PDB; 8DQU; X-ray; 2.45 A; C/F=4141-4253.
DR   PDB; 8DRR; X-ray; 2.00 A; A/B/C=3264-3563.
DR   PDB; 8DRS; X-ray; 1.80 A; A/B/C=3264-3563.
DR   PDB; 8DRT; X-ray; 1.50 A; A/B=3264-3563.
DR   PDB; 8DRU; X-ray; 2.31 A; A/B/C/D/E/F/G=3264-3569.
DR   PDB; 8DRV; X-ray; 2.40 A; A/B/C/D=3264-3569.
DR   PDB; 8DRW; X-ray; 2.67 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=3264-3569.
DR   PDB; 8DRX; X-ray; 1.50 A; A/B=3264-3563.
DR   PDB; 8DRY; X-ray; 2.49 A; A/B/C/D/E/F/G/H/I/J/K/L=3264-3569.
DR   PDB; 8DRZ; X-ray; 1.98 A; A/B/C/D/E/F/G=3264-3563.
DR   PDB; 8DS0; X-ray; 2.20 A; A/B=3264-3563.
DR   PDB; 8DS1; X-ray; 2.19 A; A/B/C/D/E/F/G/H/I/J/K/L=3264-3563.
DR   PDB; 8DS2; X-ray; 1.60 A; A/B=3264-3563.
DR   PDB; 8DSU; X-ray; 1.86 A; A/B=3264-3569.
DR   PDB; 8DZ0; X-ray; 2.29 A; A/B=3264-3569.
DR   PDB; 8DZ1; X-ray; 2.08 A; A/B=3264-3569.
DR   PDB; 8DZ2; X-ray; 2.13 A; A/B=3264-3569.
DR   PDB; 8DZ6; X-ray; 2.37 A; A/B=3264-3569.
DR   PDB; 8DZ9; X-ray; 1.66 A; A/B/C/D=3264-3569.
DR   PDB; 8DZA; X-ray; 1.96 A; A/B=3264-3569.
DR   PDB; 8E1Y; X-ray; 2.48 A; A/B=3264-3569.
DR   PDB; 8E25; X-ray; 1.87 A; A/B=3264-3569.
DR   PDB; 8E26; X-ray; 1.84 A; A/B=3264-3569.
DR   PDB; 8E4J; X-ray; 1.90 A; A/B=3258-3569.
DR   PDB; 8E4R; X-ray; 1.80 A; A/B=3258-3569.
DR   PDB; 8E5X; X-ray; 1.70 A; A/B=3264-3568.
DR   PDB; 8E5Z; X-ray; 1.80 A; A/B=3264-3568.
DR   PDB; 8E61; X-ray; 1.85 A; A/B=3264-3568.
DR   PDB; 8E63; X-ray; 1.75 A; A/B=3264-3568.
DR   PDB; 8E64; X-ray; 1.75 A; A/B=3264-3568.
DR   PDB; 8E65; X-ray; 1.80 A; A=3264-3568.
DR   PDB; 8E68; X-ray; 1.60 A; A/B=3264-3568.
DR   PDB; 8E69; X-ray; 2.26 A; A/B=3264-3568.
DR   PDB; 8E6A; X-ray; 2.05 A; A/B=3264-3568.
DR   PDB; 8EHJ; X-ray; 2.28 A; A/B=3264-3569.
DR   PDB; 8EHK; X-ray; 2.18 A; A=3264-3569.
DR   PDB; 8EHL; X-ray; 2.19 A; A=3264-3569.
DR   PDB; 8EHM; X-ray; 1.84 A; A/B=3264-3569.
DR   PDB; 8ERS; X-ray; 1.05 A; A/B=1025-1191.
DR   PDB; 8EY2; EM; 3.50 A; A/B/C/D=3259-3569.
DR   PDB; 8EYJ; X-ray; 1.74 A; A/B=3263-3569.
DR   PDB; 8F2E; X-ray; 2.43 A; A=2478-2763.
DR   PDB; 8F44; X-ray; 1.65 A; A/B=3264-3568.
DR   PDB; 8F45; X-ray; 1.65 A; A/B=3264-3568.
DR   PDB; 8F46; X-ray; 1.50 A; A/B=3264-3568.
DR   PDB; 8HDA; X-ray; 1.93 A; A/B=836-929.
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; 5SOI; -.
DR   PDBsum; 5SOJ; -.
DR   PDBsum; 5SOK; -.
DR   PDBsum; 5SOL; -.
DR   PDBsum; 5SOM; -.
DR   PDBsum; 5SON; -.
DR   PDBsum; 5SOO; -.
DR   PDBsum; 5SOP; -.
DR   PDBsum; 5SOQ; -.
DR   PDBsum; 5SOR; -.
DR   PDBsum; 5SOS; -.
DR   PDBsum; 5SOT; -.
DR   PDBsum; 5SOU; -.
DR   PDBsum; 5SOV; -.
DR   PDBsum; 5SOW; -.
DR   PDBsum; 5SOX; -.
DR   PDBsum; 5SOY; -.
DR   PDBsum; 5SOZ; -.
DR   PDBsum; 5SP0; -.
DR   PDBsum; 5SP1; -.
DR   PDBsum; 5SP2; -.
DR   PDBsum; 5SP3; -.
DR   PDBsum; 5SP4; -.
DR   PDBsum; 5SP6; -.
DR   PDBsum; 5SP7; -.
DR   PDBsum; 5SP8; -.
DR   PDBsum; 5SP9; -.
DR   PDBsum; 5SPA; -.
DR   PDBsum; 5SPB; -.
DR   PDBsum; 5SPC; -.
DR   PDBsum; 5SPD; -.
DR   PDBsum; 5SPE; -.
DR   PDBsum; 5SPF; -.
DR   PDBsum; 5SPG; -.
DR   PDBsum; 5SPH; -.
DR   PDBsum; 5SPI; -.
DR   PDBsum; 5SPJ; -.
DR   PDBsum; 5SPK; -.
DR   PDBsum; 5SPL; -.
DR   PDBsum; 5SPM; -.
DR   PDBsum; 5SPN; -.
DR   PDBsum; 5SPO; -.
DR   PDBsum; 5SPP; -.
DR   PDBsum; 5SPQ; -.
DR   PDBsum; 5SPR; -.
DR   PDBsum; 5SPS; -.
DR   PDBsum; 5SPT; -.
DR   PDBsum; 5SPU; -.
DR   PDBsum; 5SPV; -.
DR   PDBsum; 5SPW; -.
DR   PDBsum; 5SPX; -.
DR   PDBsum; 5SPY; -.
DR   PDBsum; 5SPZ; -.
DR   PDBsum; 5SQ0; -.
DR   PDBsum; 5SQ1; -.
DR   PDBsum; 5SQ2; -.
DR   PDBsum; 5SQ3; -.
DR   PDBsum; 5SQ4; -.
DR   PDBsum; 5SQ5; -.
DR   PDBsum; 5SQ6; -.
DR   PDBsum; 5SQ7; -.
DR   PDBsum; 5SQ8; -.
DR   PDBsum; 5SQ9; -.
DR   PDBsum; 5SQA; -.
DR   PDBsum; 5SQB; -.
DR   PDBsum; 5SQC; -.
DR   PDBsum; 5SQD; -.
DR   PDBsum; 5SQE; -.
DR   PDBsum; 5SQF; -.
DR   PDBsum; 5SQG; -.
DR   PDBsum; 5SQH; -.
DR   PDBsum; 5SQI; -.
DR   PDBsum; 5SQJ; -.
DR   PDBsum; 5SQK; -.
DR   PDBsum; 5SQL; -.
DR   PDBsum; 5SQM; -.
DR   PDBsum; 5SQN; -.
DR   PDBsum; 5SQO; -.
DR   PDBsum; 5SQP; -.
DR   PDBsum; 5SQQ; -.
DR   PDBsum; 5SQR; -.
DR   PDBsum; 5SQS; -.
DR   PDBsum; 5SQT; -.
DR   PDBsum; 5SQU; -.
DR   PDBsum; 5SQV; -.
DR   PDBsum; 5SQW; -.
DR   PDBsum; 5SQX; -.
DR   PDBsum; 5SQY; -.
DR   PDBsum; 5SQZ; -.
DR   PDBsum; 5SR0; -.
DR   PDBsum; 5SR1; -.
DR   PDBsum; 5SR2; -.
DR   PDBsum; 5SR3; -.
DR   PDBsum; 5SR4; -.
DR   PDBsum; 5SR5; -.
DR   PDBsum; 5SR6; -.
DR   PDBsum; 5SR7; -.
DR   PDBsum; 5SR8; -.
DR   PDBsum; 5SR9; -.
DR   PDBsum; 5SRA; -.
DR   PDBsum; 5SRB; -.
DR   PDBsum; 5SRC; -.
DR   PDBsum; 5SRD; -.
DR   PDBsum; 5SRE; -.
DR   PDBsum; 5SRF; -.
DR   PDBsum; 5SRG; -.
DR   PDBsum; 5SRH; -.
DR   PDBsum; 5SRI; -.
DR   PDBsum; 5SRJ; -.
DR   PDBsum; 5SRK; -.
DR   PDBsum; 5SRL; -.
DR   PDBsum; 5SRM; -.
DR   PDBsum; 5SRN; -.
DR   PDBsum; 5SRO; -.
DR   PDBsum; 5SRP; -.
DR   PDBsum; 5SRQ; -.
DR   PDBsum; 5SRR; -.
DR   PDBsum; 5SRS; -.
DR   PDBsum; 5SRT; -.
DR   PDBsum; 5SRU; -.
DR   PDBsum; 5SRV; -.
DR   PDBsum; 5SRW; -.
DR   PDBsum; 5SRX; -.
DR   PDBsum; 5SRY; -.
DR   PDBsum; 5SRZ; -.
DR   PDBsum; 5SS0; -.
DR   PDBsum; 5SS1; -.
DR   PDBsum; 5SS2; -.
DR   PDBsum; 5SS3; -.
DR   PDBsum; 5SS4; -.
DR   PDBsum; 5SS5; -.
DR   PDBsum; 5SS6; -.
DR   PDBsum; 5SS7; -.
DR   PDBsum; 5SS8; -.
DR   PDBsum; 5SS9; -.
DR   PDBsum; 5SSA; -.
DR   PDBsum; 5SSB; -.
DR   PDBsum; 5SSC; -.
DR   PDBsum; 5SSD; -.
DR   PDBsum; 5SSE; -.
DR   PDBsum; 5SSF; -.
DR   PDBsum; 5SSG; -.
DR   PDBsum; 5SSH; -.
DR   PDBsum; 5SSI; -.
DR   PDBsum; 5SSJ; -.
DR   PDBsum; 5SSK; -.
DR   PDBsum; 5SSL; -.
DR   PDBsum; 5SSM; -.
DR   PDBsum; 5SSN; -.
DR   PDBsum; 5SSO; -.
DR   PDBsum; 5SSP; -.
DR   PDBsum; 5SSQ; -.
DR   PDBsum; 5SSR; -.
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; 7CYQ; -.
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; 7FR0; -.
DR   PDBsum; 7FR1; -.
DR   PDBsum; 7FR2; -.
DR   PDBsum; 7FR3; -.
DR   PDBsum; 7FR4; -.
DR   PDBsum; 7FR5; -.
DR   PDBsum; 7FR6; -.
DR   PDBsum; 7FR7; -.
DR   PDBsum; 7FR8; -.
DR   PDBsum; 7FR9; -.
DR   PDBsum; 7FRA; -.
DR   PDBsum; 7FRB; -.
DR   PDBsum; 7FRC; -.
DR   PDBsum; 7FRD; -.
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; 7LCR; -.
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; 7MAT; -.
DR   PDBsum; 7MAU; -.
DR   PDBsum; 7MAV; -.
DR   PDBsum; 7MAW; -.
DR   PDBsum; 7MAX; -.
DR   PDBsum; 7MAZ; -.
DR   PDBsum; 7MB0; -.
DR   PDBsum; 7MB1; -.
DR   PDBsum; 7MB2; -.
DR   PDBsum; 7MB3; -.
DR   PDBsum; 7MB6; -.
DR   PDBsum; 7MB7; -.
DR   PDBsum; 7MB8; -.
DR   PDBsum; 7MB9; -.
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; 7NIJ; -.
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; 7P2G; -.
DR   PDBsum; 7P2O; -.
DR   PDBsum; 7PFL; -.
DR   PDBsum; 7PFM; -.
DR   PDBsum; 7PHZ; -.
DR   PDBsum; 7PKU; -.
DR   PDBsum; 7PXZ; -.
DR   PDBsum; 7PZQ; -.
DR   PDBsum; 7Q5E; -.
DR   PDBsum; 7Q5F; -.
DR   PDBsum; 7QBB; -.
DR   PDBsum; 7QG7; -.
DR   PDBsum; 7QGI; -.
DR   PDBsum; 7QIF; -.
DR   PDBsum; 7QKA; -.
DR   PDBsum; 7QT5; -.
DR   PDBsum; 7QT6; -.
DR   PDBsum; 7QT7; -.
DR   PDBsum; 7QT8; -.
DR   PDBsum; 7QT9; -.
DR   PDBsum; 7R1T; -.
DR   PDBsum; 7R1U; -.
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; 7RVM; -.
DR   PDBsum; 7RVN; -.
DR   PDBsum; 7RVO; -.
DR   PDBsum; 7RVP; -.
DR   PDBsum; 7RVQ; -.
DR   PDBsum; 7RVR; -.
DR   PDBsum; 7RVS; -.
DR   PDBsum; 7RVT; -.
DR   PDBsum; 7RVU; -.
DR   PDBsum; 7RVV; -.
DR   PDBsum; 7RVW; -.
DR   PDBsum; 7RVX; -.
DR   PDBsum; 7RVY; -.
DR   PDBsum; 7RVZ; -.
DR   PDBsum; 7RW0; -.
DR   PDBsum; 7RW1; -.
DR   PDBsum; 7S3K; -.
DR   PDBsum; 7S3S; -.
DR   PDBsum; 7S4B; -.
DR   PDBsum; 7S6W; -.
DR   PDBsum; 7S6X; -.
DR   PDBsum; 7S6Y; -.
DR   PDBsum; 7S6Z; -.
DR   PDBsum; 7S70; -.
DR   PDBsum; 7S71; -.
DR   PDBsum; 7S72; -.
DR   PDBsum; 7S73; -.
DR   PDBsum; 7S74; -.
DR   PDBsum; 7S75; -.
DR   PDBsum; 7S82; -.
DR   PDBsum; 7SD9; -.
DR   PDBsum; 7SDA; -.
DR   PDBsum; 7SDC; -.
DR   PDBsum; 7SET; -.
DR   PDBsum; 7SF1; -.
DR   PDBsum; 7SF3; -.
DR   PDBsum; 7SFB; -.
DR   PDBsum; 7SFH; -.
DR   PDBsum; 7SFI; -.
DR   PDBsum; 7SGH; -.
DR   PDBsum; 7SI9; -.
DR   PDBsum; 7T2T; -.
DR   PDBsum; 7T2U; -.
DR   PDBsum; 7T2V; -.
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; 7T70; -.
DR   PDBsum; 7T8M; -.
DR   PDBsum; 7T8R; -.
DR   PDBsum; 7T9W; -.
DR   PDBsum; 7T9Y; -.
DR   PDBsum; 7TA4; -.
DR   PDBsum; 7TA7; -.
DR   PDBsum; 7TB2; -.
DR   PDBsum; 7TBT; -.
DR   PDBsum; 7TC4; -.
DR   PDBsum; 7TDU; -.
DR   PDBsum; 7TE0; -.
DR   PDBsum; 7TEH; -.
DR   PDBsum; 7TEK; -.
DR   PDBsum; 7TEL; -.
DR   PDBsum; 7TFR; -.
DR   PDBsum; 7TGR; -.
DR   PDBsum; 7THH; -.
DR   PDBsum; 7TI9; -.
DR   PDBsum; 7TJ2; -.
DR   PDBsum; 7TQ2; -.
DR   PDBsum; 7TQ3; -.
DR   PDBsum; 7TQ4; -.
DR   PDBsum; 7TQ5; -.
DR   PDBsum; 7TQ6; -.
DR   PDBsum; 7TQV; -.
DR   PDBsum; 7TW7; -.
DR   PDBsum; 7TW8; -.
DR   PDBsum; 7TW9; -.
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; 7UKK; -.
DR   PDBsum; 7ULT; -.
DR   PDBsum; 7UU6; -.
DR   PDBsum; 7UU7; -.
DR   PDBsum; 7UU8; -.
DR   PDBsum; 7UU9; -.
DR   PDBsum; 7UUA; -.
DR   PDBsum; 7UUB; -.
DR   PDBsum; 7UUC; -.
DR   PDBsum; 7UUD; -.
DR   PDBsum; 7UUE; -.
DR   PDBsum; 7VAH; -.
DR   PDBsum; 7VVP; -.
DR   PDBsum; 7WHC; -.
DR   PDBsum; 7WOH; -.
DR   PDBsum; 7WQA; -.
DR   PDBsum; 7X6Y; -.
DR   PDBsum; 7X6Z; -.
DR   PDBsum; 7X70; -.
DR   PDBsum; 7YWR; -.
DR   PDBsum; 7Z2K; -.
DR   PDBsum; 7Z3U; -.
DR   PDBsum; 7Z59; -.
DR   PDBsum; 7ZB6; -.
DR   PDBsum; 7ZB7; -.
DR   PDBsum; 7ZB8; -.
DR   PDBsum; 7ZQV; -.
DR   PDBsum; 7ZV5; -.
DR   PDBsum; 7ZV7; -.
DR   PDBsum; 7ZV8; -.
DR   PDBsum; 8A4Q; -.
DR   PDBsum; 8A4T; -.
DR   PDBsum; 8A4Y; -.
DR   PDBsum; 8A55; -.
DR   PDBsum; 8ACD; -.
DR   PDBsum; 8ACL; -.
DR   PDBsum; 8AEB; -.
DR   PDBsum; 8AOU; -.
DR   PDBsum; 8AYW; -.
DR   PDBsum; 8AZ8; -.
DR   PDBsum; 8B2T; -.
DR   PDBsum; 8BSD; -.
DR   PDBsum; 8BZV; -.
DR   PDBsum; 8C19; -.
DR   PDBsum; 8C1A; -.
DR   PDBsum; 8C5M; -.
DR   PDBsum; 8CZW; -.
DR   PDBsum; 8CZX; -.
DR   PDBsum; 8D35; -.
DR   PDBsum; 8D4J; -.
DR   PDBsum; 8D4K; -.
DR   PDBsum; 8D4L; -.
DR   PDBsum; 8D4M; -.
DR   PDBsum; 8D4N; -.
DR   PDBsum; 8DCZ; -.
DR   PDBsum; 8DD1; -.
DR   PDBsum; 8DD9; -.
DR   PDBsum; 8DDI; -.
DR   PDBsum; 8DDM; -.
DR   PDBsum; 8DFE; -.
DR   PDBsum; 8DFN; -.
DR   PDBsum; 8DGB; -.
DR   PDBsum; 8DOX; -.
DR   PDBsum; 8DOY; -.
DR   PDBsum; 8DPR; -.
DR   PDBsum; 8DQU; -.
DR   PDBsum; 8DRR; -.
DR   PDBsum; 8DRS; -.
DR   PDBsum; 8DRT; -.
DR   PDBsum; 8DRU; -.
DR   PDBsum; 8DRV; -.
DR   PDBsum; 8DRW; -.
DR   PDBsum; 8DRX; -.
DR   PDBsum; 8DRY; -.
DR   PDBsum; 8DRZ; -.
DR   PDBsum; 8DS0; -.
DR   PDBsum; 8DS1; -.
DR   PDBsum; 8DS2; -.
DR   PDBsum; 8DSU; -.
DR   PDBsum; 8DZ0; -.
DR   PDBsum; 8DZ1; -.
DR   PDBsum; 8DZ2; -.
DR   PDBsum; 8DZ6; -.
DR   PDBsum; 8DZ9; -.
DR   PDBsum; 8DZA; -.
DR   PDBsum; 8E1Y; -.
DR   PDBsum; 8E25; -.
DR   PDBsum; 8E26; -.
DR   PDBsum; 8E4J; -.
DR   PDBsum; 8E4R; -.
DR   PDBsum; 8E5X; -.
DR   PDBsum; 8E5Z; -.
DR   PDBsum; 8E61; -.
DR   PDBsum; 8E63; -.
DR   PDBsum; 8E64; -.
DR   PDBsum; 8E65; -.
DR   PDBsum; 8E68; -.
DR   PDBsum; 8E69; -.
DR   PDBsum; 8E6A; -.
DR   PDBsum; 8EHJ; -.
DR   PDBsum; 8EHK; -.
DR   PDBsum; 8EHL; -.
DR   PDBsum; 8EHM; -.
DR   PDBsum; 8ERS; -.
DR   PDBsum; 8EY2; -.
DR   PDBsum; 8EYJ; -.
DR   PDBsum; 8F2E; -.
DR   PDBsum; 8F44; -.
DR   PDBsum; 8F45; -.
DR   PDBsum; 8F46; -.
DR   PDBsum; 8HDA; -.
DR   SASBDB; P0DTD1; -.
DR   SMR; P0DTD1; -.
DR   BioGRID; 4383849; 81.
DR   BioGRID; 4383850; 283.
DR   BioGRID; 4383851; 553.
DR   BioGRID; 4383852; 614.
DR   BioGRID; 4383853; 1490.
DR   BioGRID; 4383854; 413.
DR   BioGRID; 4383855; 1306.
DR   BioGRID; 4383856; 549.
DR   BioGRID; 4383857; 381.
DR   BioGRID; 4383858; 538.
DR   BioGRID; 4383859; 221.
DR   BioGRID; 4383860; 439.
DR   BioGRID; 4383861; 621.
DR   BioGRID; 4383862; 523.
DR   BioGRID; 4383863; 486.
DR   BioGRID; 4383864; 760.
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   iPTMnet; P0DTD1; -.
DR   DNASU; 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:0044167; C:host cell endoplasmic reticulum membrane; 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:0016020; C:membrane; IEA:UniProtKB-KW.
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'-RNA exonuclease 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:0005507; F:copper ion binding; IMP:DisProt.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
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:0008289; F:lipid binding; IDA:DisProt.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; TAS:Reactome.
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:0044600; F:protein guanylyltransferase activity; TAS:Reactome.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:DisProt.
DR   GO; GO:0016892; F:RNA endonuclease activity, producing 3'-phosphomonoesters; TAS:Reactome.
DR   GO; GO:0003968; F:RNA-dependent 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:0006351; P:DNA-templated transcription; IEA:InterPro.
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:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR   GO; GO:0039519; P:modulation by virus of host autophagy; ISS:UniProtKB.
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:0001172; P:RNA-templated transcription; 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:0039527; P:suppression by virus of host TRAF-mediated signal transduction; 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:0019082; P:viral protein processing; IEA:InterPro.
DR   GO; GO:0046786; P:viral replication complex formation and maintenance; NAS: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; cd21901; alpha_betaCoV_Nsp10; 1.
DR   CDD; cd21560; betaCoV-Nsp6; 1.
DR   CDD; cd21722; betaCoV_Nsp13-helicase; 1.
DR   CDD; cd21659; betaCoV_Nsp14; 1.
DR   CDD; cd21516; betaCoV_Nsp2_SARS-like; 1.
DR   CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR   CDD; cd21827; betaCoV_Nsp7; 1.
DR   CDD; cd21831; betaCoV_Nsp8; 1.
DR   CDD; cd21898; betaCoV_Nsp9; 1.
DR   CDD; cd21732; betaCoV_PLPro; 1.
DR   CDD; cd20762; capping_2-OMTase_Nidovirales; 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_betaCoV_Nsp15-like; 1.
DR   CDD; cd22662; SARS-CoV-like_Nsp1_C; 1.
DR   CDD; cd21796; SARS-CoV-like_Nsp1_N; 1.
DR   CDD; cd21814; SARS-CoV-like_Nsp3_betaSM; 1.
DR   CDD; cd21822; SARS-CoV-like_Nsp3_NAB; 1.
DR   CDD; cd21591; SARS-CoV-like_RdRp; 1.
DR   CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR   CDD; cd21525; SUD_C_SARS-CoV_Nsp3; 1.
DR   CDD; cd21717; TM_Y_SARS-CoV-like_Nsp3_C; 1.
DR   CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR   CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR   DisProt; DP02925; -.
DR   Gene3D; 1.10.8.1190; -; 1.
DR   Gene3D; 2.60.120.1680; -; 1.
DR   Gene3D; 3.10.20.350; -; 1.
DR   Gene3D; 3.10.20.540; -; 1.
DR   Gene3D; 3.40.50.11580; -; 1.
DR   Gene3D; 6.10.140.2090; -; 1.
DR   Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR   Gene3D; 3.40.30.150; Coronavirus polyprotein cleavage domain; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR   Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR   Gene3D; 3.40.220.20; Nsp3, SUD-M subdomain; 1.
DR   Gene3D; 3.40.220.30; Nsp3, SUD-N subdomain; 1.
DR   Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR   Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR   Gene3D; 3.40.50.11020; Replicase polyprotein, nucleic acid-binding domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR046443; a/bCoV_NSP1_glob.
DR   InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR   InterPro; IPR046442; bCoV_NSP1_C.
DR   InterPro; IPR046435; COV_N7_MTASE.
DR   InterPro; IPR043608; CoV_NSP15_M.
DR   InterPro; IPR043606; CoV_NSP15_N.
DR   InterPro; IPR043613; CoV_NSP2_C.
DR   InterPro; IPR047573; CoV_NSP2_M.
DR   InterPro; IPR043611; CoV_NSP3_C.
DR   InterPro; IPR047566; CoV_NSP3_Y3.
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; IPR046438; NIV_2_O_MTASE.
DR   InterPro; IPR046436; NIV_EXON.
DR   InterPro; IPR036333; NSP10_sf_CoV.
DR   InterPro; IPR047570; NSP12_IF_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_glob_bCoV.
DR   InterPro; IPR038030; NSP1_glob_sf_bCoV.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR044389; NSP2_SARS-CoV-like.
DR   InterPro; IPR024375; NSP3_bCoV.
DR   InterPro; IPR047567; NSP3_G2M_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; IPR046441; RdRp_CoV.
DR   InterPro; IPR009469; RdRp_N_CoV.
DR   InterPro; IPR044351; RdRp_SARS-CoV-like.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43788:SF16; AAA_12 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF16251; bCoV_NAB; 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; SSF144246; Coronavirus NSP10-like; 1.
DR   SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR   SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF142877; EndoU-like; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF159936; NSP3A-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF101816; Replicase NSP9; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF160099; SARS Nsp1-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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; PS51993; COV_3ECTO; 1.
DR   PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR   PROSITE; PS51954; COV_N7_MTASE; 1.
DR   PROSITE; PS51962; COV_NSP1; 1.
DR   PROSITE; PS52000; COV_NSP12_IF; 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_Y; 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; Disulfide bond; 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="RNA-capping enzyme subunit nsp9"
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="Guanine-N7 methyltransferase 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|PubMed:35551511"
FT   TRANSMEM        3587..3607
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3608
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:35551511"
FT   TRANSMEM        3609..3629
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3630..3634
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:35551511"
FT   TRANSMEM        3635..3655
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3656..3673
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:35551511"
FT   TRANSMEM        3674..3694
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3695..3729
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:35551511"
FT   TRANSMEM        3730..3750
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3751..3778
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:35551511"
FT   TRANSMEM        3779..3799
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3800..7096
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:35551511"
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          2247..2317
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2395..2763
FT                   /note="CoV Nsp3 Y"
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          4658..4756
FT                   /note="Nsp12 Interface"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
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          1..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000305|PubMed:35108439"
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          2395..2485
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2399..2412
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2445..2455
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2486..2763
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2486..2580
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2581..2662
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2663..2763
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          3931..4020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000305|PubMed:35108439"
FT   REGION          4759..4973
FT                   /note="RdRp Fingers N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4937..4947
FT                   /note="Interaction with RMP Remdesivir"
FT                   /evidence="ECO:0000269|PubMed:32358203"
FT   REGION          4974..5012
FT                   /note="RdRp Palm N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5013..5071
FT                   /note="RdRp Fingers C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5072..5207
FT                   /note="RdRp Palm C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          5208..5324
FT                   /note="RdRp Thumb"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
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 PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444,
FT                   ECO:0000269|PubMed:32726803"
FT   ACT_SITE        1835
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1849
FT                   /note="For PL-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         1752
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1755
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1787
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1789
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2409
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2445
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2448
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2452
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2455
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4327
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4370
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4601
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:33232691,
FT                   ECO:0007744|PDB:7CYQ"
FT   BINDING         4610
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:33232691,
FT                   ECO:0007744|PDB:7CYQ"
FT   BINDING         4687
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344,
FT                   ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         4693
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344,
FT                   ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         4698
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344,
FT                   ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         4702
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344,
FT                   ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         4879
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293,
FT                   ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5034
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293,
FT                   ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5037
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293,
FT                   ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208,
FT                   ECO:0000269|PubMed:33232691"
FT   BINDING         5038
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293,
FT                   ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5340
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5363
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5374
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5379
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5396
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
FT   BINDING         5399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986,
FT                   ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ"
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="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         6204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="15"
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="16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6409
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="16"
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   DISULFID        2263..2291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2282..2288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   VARIANT         47
FT                   /note="K -> R (in strain: Omicron/XBB.1.5)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         135
FT                   /note="S -> R (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT                   Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
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         556
FT                   /note="Q -> K (in strain: Omicron/BQ.1.1)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         842
FT                   /note="T -> I (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT                   Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
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         1221
FT                   /note="S -> L (in strain: Omicron/BA.2.75)"
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.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
FT                   /evidence="ECO:0000305"
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         1640
FT                   /note="P -> S (in strain: Omicron/BA.2.75)"
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.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         3090
FT                   /note="T -> I (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT                   Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         3201
FT                   /note="L -> F (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT                   Omicron/BA.2.75, Omicron/XBB.1.5)"
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.2.75,
FT                   Omicron/BA.4, Omicron/BA.5, Omicron/BQ.1.1, Omicron/
FT                   XBB.1.5)"
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.2.75, Omicron/BA.4, Omicron/
FT                   BA.5, Omicron/BQ.1.1, Omicron/XBB.1.5)"
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.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
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         3829
FT                   /note="L -> F (in strain: Omicron/BQ.1.1)"
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         4060
FT                   /note="N -> S (in strain: Omicron/BA.2.75)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         4665
FT                   /note="Y -> H (in strain: Omicron/BQ.1.1)"
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.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         5063
FT                   /note="G -> S (in strain: Delta/B.1.617.2, Omicron/BA.2.75,
FT                   Omicron/BQ.1.1, Omicron/XBB.1.5)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         5360
FT                   /note="S -> P (in strain: Omicron/BQ.1.1, Omicron/XBB.1.5)"
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         5557
FT                   /note="M -> I (in strain: Omicron/BQ.1.1)"
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         5592
FT                   /note="N -> S (in strain: Omicron/BQ.1.1)"
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.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
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.2.75, Omicron/BA.4, Omicron/
FT                   BA.5, Omicron/BQ.1.1, Omicron/XBB.1.5)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         6564
FT                   /note="T -> I (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT                   Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT                   BQ.1.1, Omicron/XBB.1.5)"
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         442
FT                   /note="G->V: Significant loss of GIGYF2-mediated mRNA
FT                   repression."
FT                   /evidence="ECO:0000269|PubMed:35878012"
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         3408
FT                   /note="C->A: Complete loss of 3C-like proteinase nsp5
FT                   cleavage."
FT                   /evidence="ECO:0000269|PubMed:35594856"
FT   MUTAGEN         3675..3677
FT                   /note="Missing: Faster formation of double membrane
FT                   vesicles."
FT                   /evidence="ECO:0000269|PubMed:35551511"
FT   MUTAGEN         3789
FT                   /note="F->Q: Complete loss of ER zippering."
FT                   /evidence="ECO:0000269|PubMed:35551511"
FT   MUTAGEN         3791
FT                   /note="T->W: Complete loss of ER zippering."
FT                   /evidence="ECO:0000269|PubMed:35551511"
FT   MUTAGEN         4141
FT                   /note="N->A,D: Complete loss of RNA guanylyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:35944563"
FT   MUTAGEN         4142
FT                   /note="N->A: Complete loss of RNA guanylyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:35944563"
FT   MUTAGEN         5125
FT                   /note="R->A: Complete loss of RNA guanylyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:35944563"
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            3403..3406
FT                   /evidence="ECO:0007829|PDB:7NIJ"
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           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:7ZB7"
FT   STRAND          3544..3546
FT                   /evidence="ECO:0007829|PDB:7VVP"
FT   STRAND          3547..3549
FT                   /evidence="ECO:0007829|PDB:7K3T"
FT   HELIX           3556..3564
FT                   /evidence="ECO:0007829|PDB:7K3T"
FT   HELIX           3566..3568
FT                   /evidence="ECO:0007829|PDB:7X6Y"
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   TURN            3947..3950
FT                   /evidence="ECO:0007829|PDB:7YWR"
FT   HELIX           3952..3970
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   HELIX           3974..3982
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   HELIX           3984..3986
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   TURN            3988..3991
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   TURN            3994..3997
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   HELIX           3998..4000
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   TURN            4011..4013
FT                   /evidence="ECO:0007829|PDB:7BTF"
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   HELIX           4137..4139
FT                   /evidence="ECO:0007829|PDB:7X70"
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           4398..4403
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   STRAND          4411..4416
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   STRAND          4424..4430
FT                   /evidence="ECO:0007829|PDB:7BV2"
FT   STRAND          4435..4441
FT                   /evidence="ECO:0007829|PDB:7BV2"
FT   STRAND          4444..4451
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   HELIX           4453..4455
FT                   /evidence="ECO:0007829|PDB:7C2K"
FT   STRAND          4457..4466
FT                   /evidence="ECO:0007829|PDB:7CYQ"
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          4491..4500
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   STRAND          4502..4511
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   STRAND          4513..4515
FT                   /evidence="ECO:0007829|PDB:7CYQ"
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..4605
FT                   /evidence="ECO:0007829|PDB:7CYQ"
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           5305..5308
FT                   /evidence="ECO:0007829|PDB:7CYQ"
FT   HELIX           5310..5314
FT                   /evidence="ECO:0007829|PDB:7BV2"
FT   HELIX           5315..5317
FT                   /evidence="ECO:0007829|PDB:7BV2"
FT   TURN            5320..5323
FT                   /evidence="ECO:0007829|PDB:7X6Z"
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   STRAND          5376..5378
FT                   /evidence="ECO:0007829|PDB:7CYQ"
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   TURN            5726..5728
FT                   /evidence="ECO:0007829|PDB:7CYQ"
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   TURN            5782..5784
FT                   /evidence="ECO:0007829|PDB:7CYQ"
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:5SLD"
FT   TURN            5964..5966
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          5968..5970
FT                   /evidence="ECO:0007829|PDB:7N0C"
FT   STRAND          5972..5975
FT                   /evidence="ECO:0007829|PDB:7R2V"
FT   HELIX           5976..5982
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           5990..5992
FT                   /evidence="ECO:0007829|PDB:7R2V"
FT   HELIX           6001..6006
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6008..6010
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6011..6018
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6023..6025
FT                   /evidence="ECO:0007829|PDB:7N0D"
FT   STRAND          6032..6036
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6039..6045
FT                   /evidence="ECO:0007829|PDB:5SLD"
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:5SLD"
FT   TURN            6100..6102
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6107..6110
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6115..6119
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6120..6122
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6124..6126
FT                   /evidence="ECO:0007829|PDB:7MC5"
FT   STRAND          6133..6138
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6141..6143
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   TURN            6144..6147
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6148..6150
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6152..6154
FT                   /evidence="ECO:0007829|PDB:5SMK"
FT   STRAND          6160..6163
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6165..6168
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6169..6172
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6178..6183
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6187..6189
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6195..6211
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6227..6249
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   STRAND          6252..6257
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   STRAND          6265..6267
FT                   /evidence="ECO:0007829|PDB:7N0D"
FT   STRAND          6269..6279
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   TURN            6282..6284
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   HELIX           6285..6287
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   STRAND          6288..6290
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   TURN            6292..6294
FT                   /evidence="ECO:0007829|PDB:5SLX"
FT   HELIX           6295..6298
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   TURN            6299..6301
FT                   /evidence="ECO:0007829|PDB:7N0C"
FT   STRAND          6304..6311
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   STRAND          6314..6316
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   STRAND          6319..6326
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   STRAND          6333..6337
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6339..6341
FT                   /evidence="ECO:0007829|PDB:7R2V"
FT   STRAND          6343..6353
FT                   /evidence="ECO:0007829|PDB:5SLD"
FT   HELIX           6359..6361
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   STRAND          6364..6366
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   STRAND          6371..6373
FT                   /evidence="ECO:0007829|PDB:5SLW"
FT   TURN            6387..6389
FT                   /evidence="ECO:0007829|PDB:5SLP"
FT   STRAND          6398..6400
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   HELIX           6401..6403
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   TURN            6404..6406
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   HELIX           6410..6428
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   STRAND          6431..6436
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   HELIX           6442..6445
FT                   /evidence="ECO:0007829|PDB:7TW9"
FT   HELIX           6446..6448
FT                   /evidence="ECO:0007829|PDB:7TW8"
FT   HELIX           6454..6464
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6476..6479
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6482..6487
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6490..6496
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6499..6501
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   HELIX           6503..6511
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   HELIX           6521..6526
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6531..6536
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   TURN            6540..6543
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6544..6548
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6550..6553
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   TURN            6555..6557
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6558..6562
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   HELIX           6566..6568
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6569..6571
FT                   /evidence="ECO:0007829|PDB:6X1B"
FT   STRAND          6573..6576
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6577..6579
FT                   /evidence="ECO:0007829|PDB:7TJ2"
FT   HELIX           6582..6588
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6590..6598
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6612..6614
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6617..6619
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6622..6624
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6629..6634
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6637..6639
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6652..6654
FT                   /evidence="ECO:0007829|PDB:7KEG"
FT   HELIX           6660..6667
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   HELIX           6670..6676
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   TURN            6680..6683
FT                   /evidence="ECO:0007829|PDB:6X4I"
FT   HELIX           6684..6687
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6689..6691
FT                   /evidence="ECO:0007829|PDB:7KEG"
FT   STRAND          6693..6696
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   HELIX           6703..6712
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6715..6718
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6726..6734
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   TURN            6735..6737
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6740..6747
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   HELIX           6751..6759
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6765..6774
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6777..6786
FT                   /evidence="ECO:0007829|PDB:5SBF"
FT   STRAND          6789..6795
FT                   /evidence="ECO:0007829|PDB:5SBF"
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
//