BRD4_HUMAN
ID BRD4_HUMAN Reviewed; 1362 AA.
AC O60885; O60433; Q4G0X8; Q86YS8; Q96PD3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Bromodomain-containing protein 4;
DE AltName: Full=Protein HUNK1;
GN Name=BRD4; Synonyms=HUNK1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), DISEASE, AND CHROMOSOMAL
RP TRANSLOCATION WITH NUT.
RX PubMed=11733348; DOI=10.1016/s0002-9440(10)63049-0;
RA French C.A., Miyoshi I., Aster J.C., Kubonishi I., Kroll T.G., Dal Cin P.,
RA Vargas S.O., Perez-Atayde A.R., Fletcher J.A.;
RT "BRD4 bromodomain gene rearrangement in aggressive carcinoma with
RT translocation t(15;19).";
RL Am. J. Pathol. 159:1987-1992(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RC TISSUE=Placenta;
RA Weber B.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-719, DISEASE, CHROMOSOMAL TRANSLOCATION
RP WITH NUT, AND TISSUE SPECIFICITY.
RC TISSUE=Carcinoma;
RX PubMed=12543779;
RA French C.A., Miyoshi I., Kubonishi I., Grier H.E., Perez-Atayde A.R.,
RA Fletcher J.A.;
RT "BRD4-NUT fusion oncogene: a novel mechanism in aggressive carcinoma.";
RL Cancer Res. 63:304-307(2003).
RN [7]
RP FUNCTION, INTERACTION WITH CDK9 AND CCNT1, IDENTIFICATION IN THE P-TEFB
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16109376; DOI=10.1016/j.molcel.2005.06.027;
RA Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K.;
RT "The bromodomain protein Brd4 is a positive regulatory component of P-TEFb
RT and stimulates RNA polymerase II-dependent transcription.";
RL Mol. Cell 19:523-534(2005).
RN [8]
RP FUNCTION, INTERACTION WITH CDK9 AND CCNT1, AND IDENTIFICATION IN THE P-TEFB
RP COMPLEX.
RX PubMed=16109377; DOI=10.1016/j.molcel.2005.06.029;
RA Yang Z., Yik J.H., Chen R., He N., Jang M.K., Ozato K., Zhou Q.;
RT "Recruitment of P-TEFb for stimulation of transcriptional elongation by the
RT bromodomain protein Brd4.";
RL Mol. Cell 19:535-545(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP INTERACTION WITH KSHV PROTEIN LANA (MICROBIAL INFECTION).
RX PubMed=16940503; DOI=10.1128/jvi.00502-06;
RA You J., Srinivasan V., Denis G.V., Harrington W.J. Jr., Ballestas M.E.,
RA Kaye K.M., Howley P.M.;
RT "Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen
RT interacts with bromodomain protein Brd4 on host mitotic chromosomes.";
RL J. Virol. 80:8909-8919(2006).
RN [11]
RP INTERACTION WITH BOVINE PAPILLOMAVIRUS TYPE 1 REGULATORY PROTEIN E2.
RX PubMed=17189189; DOI=10.1016/j.molcel.2006.11.005;
RA Parish J.L., Bean A.M., Park R.B., Androphy E.J.;
RT "ChlR1 is required for loading papillomavirus E2 onto mitotic chromosomes
RT and viral genome maintenance.";
RL Mol. Cell 24:867-876(2006).
RN [12]
RP INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN EBNA1.
RX PubMed=18922874; DOI=10.1128/jvi.01680-08;
RA Lin A., Wang S., Nguyen T., Shire K., Frappier L.;
RT "The EBNA1 protein of Epstein-Barr virus functionally interacts with
RT Brd4.";
RL J. Virol. 82:12009-12019(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP FUNCTION.
RX PubMed=19596240; DOI=10.1016/j.cell.2009.05.047;
RA Hargreaves D.C., Horng T., Medzhitov R.;
RT "Control of inducible gene expression by signal-dependent transcriptional
RT elongation.";
RL Cell 138:129-145(2009).
RN [16]
RP FUNCTION, AND INTERACTION WITH RELA.
RX PubMed=19103749; DOI=10.1128/mcb.01365-08;
RA Huang B., Yang X.D., Zhou M.M., Ozato K., Chen L.F.;
RT "Brd4 coactivates transcriptional activation of NF-kappaB via specific
RT binding to acetylated RelA.";
RL Mol. Cell. Biol. 29:1375-1387(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-1117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH NSD3; JMJD6; CHD4; BICRA AND ATAD5.
RX PubMed=21555454; DOI=10.1128/mcb.01341-10;
RA Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W.,
RA Howley P.M.;
RT "The Brd4 extraterminal domain confers transcription activation independent
RT of pTEFb by recruiting multiple proteins, including NSD3.";
RL Mol. Cell. Biol. 31:2641-2652(2011).
RN [21]
RP SUBCELLULAR LOCATION.
RX PubMed=21890894; DOI=10.1093/nar/gkr698;
RA Ai N., Hu X., Ding F., Yu B., Wang H., Lu X., Zhang K., Li Y., Han A.,
RA Lin W., Liu R., Chen R.;
RT "Signal-induced Brd4 release from chromatin is essential for its role
RT transition from chromatin targeting to transcriptional regulation.";
RL Nucleic Acids Res. 39:9592-9604(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-1117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP FUNCTION.
RX PubMed=22334664; DOI=10.1074/jbc.m111.323493;
RA Wang R., Li Q., Helfer C.M., Jiao J., You J.;
RT "Bromodomain protein Brd4 associated with acetylated chromatin is important
RT for maintenance of higher-order chromatin structure.";
RL J. Biol. Chem. 287:10738-10752(2012).
RN [24]
RP FUNCTION.
RX PubMed=23086925; DOI=10.1074/jbc.m112.413047;
RA Zhang W., Prakash C., Sum C., Gong Y., Li Y., Kwok J.J., Thiessen N.,
RA Pettersson S., Jones S.J., Knapp S., Yang H., Chin K.C.;
RT "Bromodomain-containing protein 4 (BRD4) regulates RNA polymerase II serine
RT 2 phosphorylation in human CD4+ T cells.";
RL J. Biol. Chem. 287:43137-43155(2012).
RN [25]
RP FUNCTION.
RX PubMed=22509028; DOI=10.1073/pnas.1120422109;
RA Devaiah B.N., Lewis B.A., Cherman N., Hewitt M.C., Albrecht B.K.,
RA Robey P.G., Ozato K., Sims R.J. III, Singer D.S.;
RT "BRD4 is an atypical kinase that phosphorylates serine2 of the RNA
RT polymerase II carboxy-terminal domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6927-6932(2012).
RN [26]
RP FUNCTION, AND INTERACTION WITH JMJD6; CDK9 AND CCNT1.
RX PubMed=24360279; DOI=10.1016/j.cell.2013.10.056;
RA Liu W., Ma Q., Wong K., Li W., Ohgi K., Zhang J., Aggarwal A.,
RA Rosenfeld M.G.;
RT "Brd4 and JMJD6-associated anti-pause enhancers in regulation of
RT transcriptional pause release.";
RL Cell 155:1581-1595(2013).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-1126; SER-1201 AND
RP SER-1204, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [28]
RP FUNCTION, INTERACTION WITH TP53, PHOSPHORYLATION AT SER-484; SER-488;
RP SER-492; SER-494; SER-498; SER-499 AND SER-503, AND MUTAGENESIS OF
RP 492-SER--SER-494; 498-SER--THR-500 AND SER-503.
RX PubMed=23317504; DOI=10.1016/j.molcel.2012.12.006;
RA Wu S.Y., Lee A.Y., Lai H.T., Zhang H., Chiang C.M.;
RT "Phospho switch triggers Brd4 chromatin binding and activator recruitment
RT for gene-specific targeting.";
RL Mol. Cell 49:843-857(2013).
RN [29]
RP FUNCTION.
RX PubMed=23589332; DOI=10.1128/mcb.01180-12;
RA Patel M.C., Debrosse M., Smith M., Dey A., Huynh W., Sarai N.,
RA Heightman T.D., Tamura T., Ozato K.;
RT "BRD4 coordinates recruitment of pause release factor P-TEFb and the
RT pausing complex NELF/DSIF to regulate transcription elongation of
RT interferon-stimulated genes.";
RL Mol. Cell. Biol. 33:2497-2507(2013).
RN [30]
RP FUNCTION (ISOFORM B), SUBCELLULAR LOCATION (ISOFORM B), INTERACTION WITH
RP NCAPD3 AND SMC2, AND MUTAGENESIS OF ASN-140.
RX PubMed=23728299; DOI=10.1038/nature12147;
RA Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C., Cannell I.G.,
RA Bryson B.D., Rameseder J., Lee M.J., Blake E.J., Fydrych A., Ho R.,
RA Greenberger B.A., Chen G.C., Maffa A., Del Rosario A.M., Root D.E.,
RA Carpenter A.E., Hahn W.C., Sabatini D.M., Chen C.C., White F.M.,
RA Bradner J.E., Yaffe M.B.;
RT "The bromodomain protein Brd4 insulates chromatin from DNA damage
RT signalling.";
RL Nature 498:246-250(2013).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470 AND SER-1117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-694 AND LYS-1111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99; LYS-585; LYS-645; LYS-694;
RP LYS-1050; LYS-1111 AND LYS-1197, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [37]
RP INTERACTION WITH BICRA.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
RN [38]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-37; GLY-371; ASN-563; SER-598 AND
RP HIS-669.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [39]
RP STRUCTURE BY NMR OF 352-457.
RX PubMed=18500820; DOI=10.1021/bi8001659;
RA Liu Y., Wang X., Zhang J., Huang H., Ding B., Wu J., Shi Y.;
RT "Structural basis and binding properties of the second bromodomain of Brd4
RT with acetylated histone tails.";
RL Biochemistry 47:6403-6417(2008).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1
RP INHIBITOR, AND SUBCELLULAR LOCATION.
RX PubMed=20871596; DOI=10.1038/nature09504;
RA Filippakopoulos P., Qi J., Picaud S., Shen Y., Smith W.B., Fedorov O.,
RA Morse E.M., Keates T., Hickman T.T., Felletar I., Philpott M., Munro S.,
RA McKeown M.R., Wang Y., Christie A.L., West N., Cameron M.J., Schwartz B.,
RA Heightman T.D., La Thangue N., French C.A., Wiest O., Kung A.L., Knapp S.,
RA Bradner J.E.;
RT "Selective inhibition of BET bromodomains.";
RL Nature 468:1067-1073(2010).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH I-BET
RP INHIBITOR.
RX PubMed=21068722; DOI=10.1038/nature09589;
RA Nicodeme E., Jeffrey K.L., Schaefer U., Beinke S., Dewell S., Chung C.W.,
RA Chandwani R., Marazzi I., Wilson P., Coste H., White J., Kirilovsky J.,
RA Rice C.M., Lora J.M., Prinjha R.K., Lee K., Tarakhovsky A.;
RT "Suppression of inflammation by a synthetic histone mimic.";
RL Nature 468:1119-1123(2010).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 44-168, AND X-RAY CRYSTALLOGRAPHY
RP (2.3 ANGSTROMS) OF 333-460.
RX PubMed=21568322; DOI=10.1021/jm200108t;
RA Chung C.W., Coste H., White J.H., Mirguet O., Wilde J., Gosmini R.L.,
RA Delves C., Magny S.M., Woodward R., Hughes S.A., Boursier E.V., Flynn H.,
RA Bouillot A.M., Bamborough P., Brusq J.M., Gellibert F.J., Jones E.J.,
RA Riou A.M., Homes P., Martin S.L., Uings I.J., Toum J., Clement C.A.,
RA Boullay A.B., Grimley R.L., Blandel F.M., Prinjha R.K., Lee K.,
RA Kirilovsky J., Nicodeme E.;
RT "Discovery and characterization of small molecule inhibitors of the BET
RT family bromodomains.";
RL J. Med. Chem. 54:3827-3838(2011).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1
RP INHIBITOR.
RX PubMed=21964340; DOI=10.1038/nature10509;
RA Dawson M.A., Prinjha R.K., Dittmann A., Giotopoulos G., Bantscheff M.,
RA Chan W.I., Robson S.C., Chung C.W., Hopf C., Savitski M.M., Huthmacher C.,
RA Gudgin E., Lugo D., Beinke S., Chapman T.D., Roberts E.J., Soden P.E.,
RA Auger K.R., Mirguet O., Doehner K., Delwel R., Burnett A.K., Jeffrey P.,
RA Drewes G., Lee K., Huntly B.J., Kouzarides T.;
RT "Inhibition of BET recruitment to chromatin as an effective treatment for
RT MLL-fusion leukaemia.";
RL Nature 478:529-533(2011).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH
RP BENZODIAZEPINES AND BENZOTRIAZEPINES INHIBITORS.
RX PubMed=22137933; DOI=10.1016/j.bmc.2011.10.080;
RA Filippakopoulos P., Picaud S., Fedorov O., Keller M., Wrobel M.,
RA Morgenstern O., Bracher F., Knapp S.;
RT "Benzodiazepines and benzotriazepines as protein interaction inhibitors
RT targeting bromodomains of the BET family.";
RL Bioorg. Med. Chem. 20:1878-1886(2012).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 44-168, AND STRUCTURE BY NMR OF
RP 333-460.
RX PubMed=22645123; DOI=10.1074/jbc.m112.359505;
RA Zhang G., Liu R., Zhong Y., Plotnikov A.N., Zhang W., Zeng L., Rusinova E.,
RA Gerona-Nevarro G., Moshkina N., Joshua J., Chuang P.Y., Ohlmeyer M.,
RA He J.C., Zhou M.M.;
RT "Down-regulation of NF-kappaB transcriptional activity in HIV-associated
RT kidney disease by BRD4 inhibition.";
RL J. Biol. Chem. 287:28840-28851(2012).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH
RP BENZODIAZEPINES INHIBITORS.
RX PubMed=22136404; DOI=10.1021/jm201320w;
RA Chung C.W., Dean A.W., Woolven J.M., Bamborough P.;
RT "Fragment-based discovery of bromodomain inhibitors part 1: inhibitor
RT binding modes and implications for lead discovery.";
RL J. Med. Chem. 55:576-586(2012).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 44-168.
RX PubMed=23095041; DOI=10.1021/jm3010515;
RA Fish P.V., Filippakopoulos P., Bish G., Brennan P.E., Bunnage M.E.,
RA Cook A.S., Federov O., Gerstenberger B.S., Jones H., Knapp S., Marsden B.,
RA Nocka K., Owen D.R., Philpott M., Picaud S., Primiano M.J., Ralph M.J.,
RA Sciammetta N., Trzupek J.D.;
RT "Identification of a chemical probe for bromo and extra C-terminal
RT bromodomain inhibition through optimization of a fragment-derived hit.";
RL J. Med. Chem. 55:9831-9837(2012).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 44-168; 333-460 AND 1343-1362 IN
RP COMPLEX WITH ACETYLATED HISTONE, AND MUTAGENESIS OF ASN-140 AND ASN-433.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 44-168 IN COMPLEX WITH
RP 3,5-DIMETHYLISOXAZOLE INHIBITOR.
RX PubMed=23517011; DOI=10.1021/jm301588r;
RA Hewings D.S., Fedorov O., Filippakopoulos P., Martin S., Picaud S.,
RA Tumber A., Wells C., Olcina M.M., Freeman K., Gill A., Ritchie A.J.,
RA Sheppard D.W., Russell A.J., Hammond E.M., Knapp S., Brennan P.E.,
RA Conway S.J.;
RT "Optimization of 3,5-dimethylisoxazole derivatives as potent bromodomain
RT ligands.";
RL J. Med. Chem. 56:3217-3227(2013).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 44-167 IN COMPLEX WITH
RP 2-THIAZOLIDINONE INHIBITOR.
RX PubMed=23530754; DOI=10.1021/jm301793a;
RA Zhao L., Cao D., Chen T., Wang Y., Miao Z., Xu Y., Chen W., Wang X., Li Y.,
RA Du Z., Xiong B., Li J., Xu C., Zhang N., He J., Shen J.;
RT "Fragment-based drug discovery of 2-thiazolidinones as inhibitors of the
RT histone reader BRD4 bromodomain.";
RL J. Med. Chem. 56:3833-3851(2013).
RN [51] {ECO:0007744|PDB:6BNH}
RP STRUCTURE BY NMR OF 601-683 IN COMPLEX WITH JMJD6, INTERACTION WITH JMJD6
RP AND NSD3, MUTAGENESIS OF 651-GLU--GLU-653, AND SUBUNIT.
RX PubMed=29176719; DOI=10.1038/s41598-017-16588-8;
RA Konuma T., Yu D., Zhao C., Ju Y., Sharma R., Ren C., Zhang Q., Zhou M.M.,
RA Zeng L.;
RT "Structural Mechanism of the Oxygenase JMJD6 Recognition by the
RT Extraterminal (ET) Domain of BRD4.";
RL Sci. Rep. 7:16272-16272(2017).
CC -!- FUNCTION: Chromatin reader protein that recognizes and binds acetylated
CC histones and plays a key role in transmission of epigenetic memory
CC across cell divisions and transcription regulation. Remains associated
CC with acetylated chromatin throughout the entire cell cycle and provides
CC epigenetic memory for postmitotic G1 gene transcription by preserving
CC acetylated chromatin status and maintaining high-order chromatin
CC structure (PubMed:23589332, PubMed:23317504, PubMed:22334664). During
CC interphase, plays a key role in regulating the transcription of signal-
CC inducible genes by associating with the P-TEFb complex and recruiting
CC it to promoters. Also recruits P-TEFb complex to distal enhancers, so
CC called anti-pause enhancers in collaboration with JMJD6. BRD4 and JMJD6
CC are required to form the transcriptionally active P-TEFb complex by
CC displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from
CC P-TEFb, thereby transforming it into an active form that can then
CC phosphorylate the C-terminal domain (CTD) of RNA polymerase II
CC (PubMed:23589332, PubMed:19596240, PubMed:16109377, PubMed:16109376,
CC PubMed:24360279). Promotes phosphorylation of 'Ser-2' of the C-terminal
CC domain (CTD) of RNA polymerase II (PubMed:23086925). According to a
CC report, directly acts as an atypical protein kinase and mediates
CC phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA
CC polymerase II; these data however need additional evidences in vivo
CC (PubMed:22509028). In addition to acetylated histones, also recognizes
CC and binds acetylated RELA, leading to further recruitment of the P-TEFb
CC complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also
CC acts as a regulator of p53/TP53-mediated transcription: following
CC phosphorylation by CK2, recruited to p53/TP53 specific target promoters
CC (PubMed:23317504). {ECO:0000269|PubMed:16109376,
CC ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:19103749,
CC ECO:0000269|PubMed:19596240, ECO:0000269|PubMed:22334664,
CC ECO:0000269|PubMed:22509028, ECO:0000269|PubMed:23086925,
CC ECO:0000269|PubMed:23317504, ECO:0000269|PubMed:23589332,
CC ECO:0000269|PubMed:24360279}.
CC -!- FUNCTION: [Isoform B]: Acts as a chromatin insulator in the DNA damage
CC response pathway. Inhibits DNA damage response signaling by recruiting
CC the condensin-2 complex to acetylated histones, leading to chromatin
CC structure remodeling, insulating the region from DNA damage response by
CC limiting spreading of histone H2AX/H2A.x phosphorylation.
CC {ECO:0000269|PubMed:23728299}.
CC -!- SUBUNIT: Binds acetylated histone H4 (PubMed:29176719). Interacts with
CC p53/TP53; the interaction is direct (PubMed:23317504). Interacts (via
CC CTD region) with CDK9 and CCNT1, acting as an associated component of
CC P-TEFb complex (PubMed:16109376, PubMed:16109377, PubMed:23317504,
CC PubMed:24360279). Interacts with RELA (when acetylated at 'Lys-
CC 310')(PubMed:19103749). Interacts (via NET domain) with NSD3, CHD4,
CC BICRA and ATAD5 (PubMed:21555454,PubMed:29176719). The interaction with
CC BICRA bridges BRD4 to the GBAF complex (PubMed:29374058,
CC PubMed:16109376, PubMed:16109377, PubMed:19103749, PubMed:21555454,
CC PubMed:23317504). Interacts (via NET domain) with JMJD6 (via JmjC and
CC N-terminal domains); the interaction is stronger in presence of ssRNA
CC and recruits JMJD6 on distal enhancers (PubMed:24360279,
CC PubMed:21555454, PubMed:29176719). Interacts with NSD3
CC (PubMed:29176719). Isoform B: interacts with NCAPD3 and SMC2
CC (PubMed:23728299). {ECO:0000269|PubMed:16109376,
CC ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:19103749,
CC ECO:0000269|PubMed:21555454, ECO:0000269|PubMed:23317504,
CC ECO:0000269|PubMed:23728299, ECO:0000269|PubMed:24360279,
CC ECO:0000269|PubMed:29176719, ECO:0000269|PubMed:29374058}.
CC -!- SUBUNIT: (Microbial infection) Interacts with bovine papillomavirus
CC type 1 regulatory protein E2. This interactions may serve for the
CC tethering of viral genomes to host mitotic chromosomes allowing
CC successful partitioning of the viral genome during cell division.
CC {ECO:0000269|PubMed:17189189}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus (EBV)
CC protein EBNA1; this interaction facilitates transcriptional activation
CC by EBNA1. {ECO:0000269|PubMed:18922874}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus-8
CC (HHV-8) protein LANA. {ECO:0000269|PubMed:16940503}.
CC -!- INTERACTION:
CC O60885; Q86YD7: FAM90A1; NbExp=5; IntAct=EBI-723869, EBI-6658203;
CC O60885; P62993: GRB2; NbExp=2; IntAct=EBI-723869, EBI-401755;
CC O60885; Q6NYC1: JMJD6; NbExp=10; IntAct=EBI-723869, EBI-8464037;
CC O60885; P16333: NCK1; NbExp=2; IntAct=EBI-723869, EBI-389883;
CC O60885; Q04206: RELA; NbExp=8; IntAct=EBI-723869, EBI-73886;
CC O60885; A6NLX3: SPDYE4; NbExp=4; IntAct=EBI-723869, EBI-12047907;
CC O60885; Q15672: TWIST1; NbExp=7; IntAct=EBI-723869, EBI-1797287;
CC O60885; P03120: E2; Xeno; NbExp=4; IntAct=EBI-723869, EBI-1779322;
CC O60885; P04015: E2; Xeno; NbExp=3; IntAct=EBI-723869, EBI-7010556;
CC O60885; P06790: E2; Xeno; NbExp=2; IntAct=EBI-723869, EBI-7010629;
CC O60885; P17383: E2; Xeno; NbExp=2; IntAct=EBI-723869, EBI-7010529;
CC O60885-1; P10275: AR; NbExp=6; IntAct=EBI-9345088, EBI-608057;
CC O60885-1; O60563: CCNT1; NbExp=6; IntAct=EBI-9345088, EBI-2479671;
CC O60885-1; P50750: CDK9; NbExp=9; IntAct=EBI-9345088, EBI-1383449;
CC O60885-1; P62805: H4C9; NbExp=10; IntAct=EBI-9345088, EBI-302023;
CC O60885-1; Q15672: TWIST1; NbExp=9; IntAct=EBI-9345088, EBI-1797287;
CC O60885-1; P03120: E2; Xeno; NbExp=2; IntAct=EBI-9345088, EBI-1779322;
CC O60885-1; P03122: E2; Xeno; NbExp=2; IntAct=EBI-9345088, EBI-7028618;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16109376}. Chromosome
CC {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:21890894}.
CC Note=Associates with acetylated chromatin (PubMed:21890894,
CC PubMed:16109376). Released from chromatin upon deacetylation of
CC histones that can be triggered by different signals such as activation
CC of the JNK pathway or nocodazole treatment (PubMed:21890894,
CC PubMed:16109376). Preferentially localizes to mitotic chromosomes,
CC while it does not localizes to meiotic chromosomes (PubMed:21890894,
CC PubMed:16109376). {ECO:0000269|PubMed:16109376,
CC ECO:0000269|PubMed:21890894}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Chromosome
CC {ECO:0000269|PubMed:23728299}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=Brd4L, Long;
CC IsoId=O60885-1; Sequence=Displayed;
CC Name=C; Synonyms=Brd4S, Short;
CC IsoId=O60885-2; Sequence=VSP_010902, VSP_010903;
CC Name=B;
CC IsoId=O60885-3; Sequence=VSP_047671;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12543779}.
CC -!- DOMAIN: The NET domain mediates interaction with a number of chromatin
CC proteins involved in transcription regulation (NSD3, JMJD6, CHD4,
CC GLTSCR1 and ATAD5). {ECO:0000269|PubMed:21555454}.
CC -!- DOMAIN: The C-terminal (CTD) region mediates interaction and
CC recruitment of CDK9 and CCNT1 subunits of the P-TEFb complex
CC (PubMed:16109376, PubMed:16109377). It is also required for maintenance
CC of higher-order chromatin structure (PubMed:22334664).
CC {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377,
CC ECO:0000269|PubMed:22334664}.
CC -!- DOMAIN: The 2 bromo domains mediate specific binding to acetylated
CC histones via Asn-140 and Asn-433, respectively (PubMed:20871596). The
CC exact combination of modified histone tails required to recruit BRD4 to
CC target genes is still unclear. The first bromo domain has high affinity
CC for acetylated histone H4 tail, whereas the second bromo domain
CC recognizes multiply acetylated marks in histone H3 (PubMed:22464331). A
CC number of specific inhibitors bind competitively to acetyl-lysine-
CC binding residues Asn-140 and Asn-433, promoting removal from acetylated
CC histones. Many of these inhibitors are benzodiazepine derivatives
CC (PubMed:22137933, PubMed:22136404, PubMed:23517011, PubMed:23530754).
CC {ECO:0000269|PubMed:20871596, ECO:0000269|PubMed:22136404,
CC ECO:0000269|PubMed:22137933, ECO:0000269|PubMed:22464331,
CC ECO:0000269|PubMed:23517011, ECO:0000269|PubMed:23530754}.
CC -!- PTM: Phosphorylation by CK2 disrupt the intramolecular binding between
CC the bromo domain 2 and the NPS region and promotes binding between the
CC NPS and the BID regions, leading to activate the protein and promote
CC binding to acetylated histones. In absence of phosphorylation, BRD4
CC does not localize to p53/TP53 target gene promoters, phosphorylation
CC promoting recruitment to p53/TP53 target promoters.
CC {ECO:0000269|PubMed:23317504}.
CC -!- DISEASE: Note=A chromosomal aberration involving BRD4 is found in a
CC rare, aggressive, and lethal carcinoma arising in midline organs of
CC young people. Translocation t(15;19)(q14;p13) with NUTM1 which produces
CC a BRD4-NUTM1 fusion protein. {ECO:0000269|PubMed:11733348,
CC ECO:0000269|PubMed:12543779}.
CC -!- MISCELLANEOUS: Some specific inhibitors of BRD4 that prevent binding to
CC acetylated histones by binding Asn-140 and Asn-433 are promising
CC therapeutic molecules for the treatment of leukemias. JQ1, a thieno-
CC triazolo-1,4-diazepine derivative, and I-BET, a benzodiazepine
CC derivative, have been tested on tumors with success (PubMed:20871596,
CC PubMed:21068722, PubMed:21964340). Treatment with GSK1210151A (I-
CC BET151, a I-BET derivative) has strong effets on mixed lineage leukemia
CC and promotes myeloid differentiation and leukemia stem-cell depletion
CC (PubMed:21964340). {ECO:0000305|PubMed:20871596,
CC ECO:0000305|PubMed:21068722, ECO:0000305|PubMed:21964340}.
CC -!- MISCELLANEOUS: [Isoform B]: Does not contain the C-terminal (CTD)
CC region required to recruit the P-TEFb complex. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27978.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BRD4ID837ch19p13.html";
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DR EMBL; AF386649; AAL26987.1; -; mRNA.
DR EMBL; Y12059; CAA72780.1; -; mRNA.
DR EMBL; AC004798; AAC27978.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC003111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84470.1; -; Genomic_DNA.
DR EMBL; BC035266; AAH35266.1; -; mRNA.
DR EMBL; AY166680; AAO22237.1; ALT_TERM; mRNA.
DR CCDS; CCDS12328.1; -. [O60885-1]
DR CCDS; CCDS46004.1; -. [O60885-2]
DR CCDS; CCDS82307.1; -. [O60885-3]
DR RefSeq; NP_001317313.1; NM_001330384.1. [O60885-3]
DR RefSeq; NP_055114.1; NM_014299.2. [O60885-2]
DR RefSeq; NP_490597.1; NM_058243.2. [O60885-1]
DR RefSeq; XP_011526156.1; XM_011527854.1.
DR RefSeq; XP_011526158.1; XM_011527856.2.
DR PDB; 2I8N; NMR; -; A=352-457.
DR PDB; 2LSP; NMR; -; B=333-460.
DR PDB; 2MJV; NMR; -; B=333-460.
DR PDB; 2N3K; NMR; -; A=600-678.
DR PDB; 2NCZ; NMR; -; A=601-683.
DR PDB; 2ND0; NMR; -; A=601-683.
DR PDB; 2ND1; NMR; -; A=601-683.
DR PDB; 2NNU; X-ray; 1.59 A; B=1343-1362.
DR PDB; 2OSS; X-ray; 1.35 A; A=44-168.
DR PDB; 2OUO; X-ray; 1.89 A; A=333-460.
DR PDB; 2YEL; X-ray; 1.65 A; A=44-168.
DR PDB; 2YEM; X-ray; 2.30 A; A/B=333-460.
DR PDB; 3MXF; X-ray; 1.60 A; A=42-168.
DR PDB; 3P5O; X-ray; 1.60 A; A=44-168.
DR PDB; 3SVF; X-ray; 1.98 A; A=44-168.
DR PDB; 3SVG; X-ray; 1.68 A; A=44-168.
DR PDB; 3U5J; X-ray; 1.60 A; A=44-168.
DR PDB; 3U5K; X-ray; 1.80 A; A/B/C/D=44-168.
DR PDB; 3U5L; X-ray; 1.39 A; A=44-168.
DR PDB; 3UVW; X-ray; 1.37 A; A=44-168.
DR PDB; 3UVX; X-ray; 1.91 A; A=44-168.
DR PDB; 3UVY; X-ray; 2.02 A; A=44-168.
DR PDB; 3UW9; X-ray; 2.30 A; A/B/C/D=44-168.
DR PDB; 3ZYU; X-ray; 1.50 A; A/B=44-168.
DR PDB; 4A9L; X-ray; 1.60 A; A=44-168.
DR PDB; 4BJX; X-ray; 1.59 A; A=44-168.
DR PDB; 4BW1; X-ray; 1.40 A; A=44-168.
DR PDB; 4BW2; X-ray; 1.92 A; A=44-168.
DR PDB; 4BW3; X-ray; 1.50 A; A=44-168.
DR PDB; 4BW4; X-ray; 1.67 A; A=44-168.
DR PDB; 4C66; X-ray; 1.87 A; A=44-167.
DR PDB; 4C67; X-ray; 1.55 A; A=44-168.
DR PDB; 4CFK; X-ray; 1.55 A; A=44-168.
DR PDB; 4CFL; X-ray; 1.32 A; A=44-168.
DR PDB; 4CL9; X-ray; 1.40 A; A=44-168.
DR PDB; 4CLB; X-ray; 1.60 A; A=44-168.
DR PDB; 4DON; X-ray; 1.52 A; A=44-166.
DR PDB; 4E96; X-ray; 1.92 A; A=44-168.
DR PDB; 4F3I; X-ray; 1.40 A; A=44-168.
DR PDB; 4GPJ; X-ray; 1.60 A; A=44-168.
DR PDB; 4HBV; X-ray; 1.63 A; A=42-168.
DR PDB; 4HBW; X-ray; 1.69 A; A=42-168.
DR PDB; 4HBX; X-ray; 1.62 A; A=42-168.
DR PDB; 4HBY; X-ray; 1.59 A; A=44-168.
DR PDB; 4HXK; X-ray; 1.61 A; A=44-167.
DR PDB; 4HXL; X-ray; 1.52 A; A=44-167.
DR PDB; 4HXM; X-ray; 1.50 A; A=44-166.
DR PDB; 4HXN; X-ray; 1.49 A; A=44-167.
DR PDB; 4HXO; X-ray; 1.76 A; A=44-167.
DR PDB; 4HXP; X-ray; 1.73 A; A=44-166.
DR PDB; 4HXR; X-ray; 1.53 A; A=44-167.
DR PDB; 4HXS; X-ray; 1.43 A; A=44-166.
DR PDB; 4IOO; X-ray; 1.25 A; A=44-168.
DR PDB; 4IOQ; X-ray; 1.50 A; A=44-168.
DR PDB; 4IOR; X-ray; 1.40 A; A=44-168.
DR PDB; 4J0R; X-ray; 1.72 A; A=44-168.
DR PDB; 4J0S; X-ray; 1.84 A; A=44-168.
DR PDB; 4J3I; X-ray; 1.24 A; A=44-168.
DR PDB; 4KV1; X-ray; 1.50 A; A/B=41-168.
DR PDB; 4KV4; X-ray; 2.00 A; A=351-459.
DR PDB; 4LR6; X-ray; 1.29 A; A=42-168.
DR PDB; 4LRG; X-ray; 2.21 A; A=42-168.
DR PDB; 4LYI; X-ray; 1.30 A; A=44-168.
DR PDB; 4LYS; X-ray; 1.83 A; A=44-168.
DR PDB; 4LYW; X-ray; 1.95 A; A=44-168.
DR PDB; 4LZR; X-ray; 1.85 A; A=44-168.
DR PDB; 4LZS; X-ray; 2.20 A; A=44-168.
DR PDB; 4MEN; X-ray; 1.81 A; A=44-168.
DR PDB; 4MEO; X-ray; 1.72 A; A=44-168.
DR PDB; 4MEP; X-ray; 1.85 A; A=44-168.
DR PDB; 4MEQ; X-ray; 1.77 A; A=44-168.
DR PDB; 4MR3; X-ray; 1.68 A; A=44-168.
DR PDB; 4MR4; X-ray; 1.66 A; A=44-168.
DR PDB; 4NQM; X-ray; 1.58 A; A=44-168.
DR PDB; 4NR8; X-ray; 1.64 A; A=44-168.
DR PDB; 4NUC; X-ray; 1.40 A; A=44-168.
DR PDB; 4NUD; X-ray; 1.20 A; A=44-168.
DR PDB; 4NUE; X-ray; 1.30 A; A=44-168.
DR PDB; 4O70; X-ray; 1.55 A; A/B=44-168.
DR PDB; 4O71; X-ray; 1.36 A; A/B=44-168.
DR PDB; 4O72; X-ray; 1.40 A; A=44-168.
DR PDB; 4O74; X-ray; 1.45 A; A/B=44-168.
DR PDB; 4O75; X-ray; 1.55 A; A=44-168.
DR PDB; 4O76; X-ray; 1.70 A; A/B/C/D=44-168.
DR PDB; 4O77; X-ray; 2.00 A; A/B=44-168.
DR PDB; 4O78; X-ray; 1.34 A; A=44-168.
DR PDB; 4O7A; X-ray; 1.34 A; A=44-168.
DR PDB; 4O7B; X-ray; 1.50 A; A=44-168.
DR PDB; 4O7C; X-ray; 1.55 A; A=44-168.
DR PDB; 4O7E; X-ray; 1.85 A; A/B=44-168.
DR PDB; 4O7F; X-ray; 1.80 A; A/B=44-168.
DR PDB; 4OGI; X-ray; 1.73 A; A/B=44-168.
DR PDB; 4OGJ; X-ray; 1.65 A; A/B=44-168.
DR PDB; 4PCE; X-ray; 1.29 A; A=44-168.
DR PDB; 4PCI; X-ray; 1.25 A; A=44-168.
DR PDB; 4PS5; X-ray; 1.40 A; A/B=44-168.
DR PDB; 4QB3; X-ray; 0.94 A; A=44-168.
DR PDB; 4QR3; X-ray; 1.37 A; A=44-166.
DR PDB; 4QR4; X-ray; 1.28 A; A=44-166.
DR PDB; 4QR5; X-ray; 1.41 A; A=44-166.
DR PDB; 4QZS; X-ray; 1.45 A; A=44-168.
DR PDB; 4UIX; X-ray; 1.58 A; A/B/C=44-168.
DR PDB; 4UIY; X-ray; 1.30 A; A=44-168.
DR PDB; 4UIZ; X-ray; 1.19 A; A=44-168.
DR PDB; 4UYD; X-ray; 1.37 A; A=44-183.
DR PDB; 4WHW; X-ray; 1.34 A; A=44-168.
DR PDB; 4WIV; X-ray; 1.56 A; A=44-168.
DR PDB; 4X2I; X-ray; 1.20 A; A=42-166.
DR PDB; 4XY9; X-ray; 1.83 A; A=42-168.
DR PDB; 4XYA; X-ray; 2.05 A; A=42-168.
DR PDB; 4YH3; X-ray; 1.60 A; A=44-170.
DR PDB; 4YH4; X-ray; 1.33 A; A=44-170.
DR PDB; 4Z1Q; X-ray; 1.40 A; A/B=42-167.
DR PDB; 4Z1S; X-ray; 1.06 A; A/B=42-166.
DR PDB; 4Z93; X-ray; 1.27 A; A=349-460.
DR PDB; 4ZC9; X-ray; 0.99 A; A=44-168.
DR PDB; 4ZW1; X-ray; 1.75 A; A=44-168.
DR PDB; 5A5S; X-ray; 1.36 A; A=44-168.
DR PDB; 5A85; X-ray; 1.72 A; A=44-168.
DR PDB; 5ACY; X-ray; 2.01 A; A/B=44-168.
DR PDB; 5AD2; X-ray; 2.01 A; A/B=44-168.
DR PDB; 5AD3; X-ray; 1.49 A; A/B=44-168.
DR PDB; 5BT4; X-ray; 1.50 A; A/B/C=44-168.
DR PDB; 5CFW; X-ray; 1.15 A; A=44-168.
DR PDB; 5COI; X-ray; 1.62 A; A=44-168.
DR PDB; 5CP5; X-ray; 1.79 A; A=44-168.
DR PDB; 5CPE; X-ray; 1.62 A; A=44-168.
DR PDB; 5CQT; X-ray; 1.60 A; A=44-168.
DR PDB; 5CRM; X-ray; 1.99 A; A=44-168.
DR PDB; 5CRZ; X-ray; 2.12 A; A=44-168.
DR PDB; 5CS8; X-ray; 1.62 A; A=44-168.
DR PDB; 5CTL; X-ray; 2.51 A; A=44-168.
DR PDB; 5CY9; X-ray; 1.55 A; A=44-168.
DR PDB; 5D0C; X-ray; 1.49 A; A=44-168.
DR PDB; 5D24; X-ray; 1.65 A; A=43-168.
DR PDB; 5D25; X-ray; 1.70 A; A=43-168.
DR PDB; 5D26; X-ray; 1.82 A; A=42-168.
DR PDB; 5D3H; X-ray; 1.70 A; A=44-168.
DR PDB; 5D3J; X-ray; 1.70 A; A=43-168.
DR PDB; 5D3L; X-ray; 1.50 A; A=42-168.
DR PDB; 5D3N; X-ray; 2.15 A; A=43-168.
DR PDB; 5D3P; X-ray; 1.95 A; A=42-168.
DR PDB; 5D3R; X-ray; 2.20 A; A=42-168.
DR PDB; 5D3S; X-ray; 1.75 A; A=44-168.
DR PDB; 5D3T; X-ray; 1.93 A; A=42-168.
DR PDB; 5DLX; X-ray; 1.90 A; A=44-168.
DR PDB; 5DLZ; X-ray; 1.70 A; A=44-168.
DR PDB; 5DW2; X-ray; 1.12 A; A=44-170.
DR PDB; 5DX4; X-ray; 2.30 A; A=44-168.
DR PDB; 5E0R; X-ray; 1.35 A; A=44-168.
DR PDB; 5EGU; X-ray; 2.21 A; A/B/C/D=44-168.
DR PDB; 5EI4; X-ray; 1.05 A; A=44-168.
DR PDB; 5EIS; X-ray; 1.60 A; A=44-168.
DR PDB; 5F5Z; X-ray; 1.76 A; A=44-168.
DR PDB; 5F60; X-ray; 1.35 A; A=44-168.
DR PDB; 5F61; X-ray; 1.45 A; A/B=44-168.
DR PDB; 5F62; X-ray; 1.35 A; A=44-168.
DR PDB; 5F63; X-ray; 1.45 A; A=44-168.
DR PDB; 5FBX; X-ray; 1.85 A; A=44-168.
DR PDB; 5H21; X-ray; 1.59 A; A=44-167.
DR PDB; 5HCL; X-ray; 1.50 A; A=44-168.
DR PDB; 5HLS; X-ray; 2.18 A; A=42-168.
DR PDB; 5HM0; X-ray; 1.40 A; A=42-168.
DR PDB; 5HQ5; X-ray; 1.60 A; A=44-168.
DR PDB; 5HQ6; X-ray; 1.95 A; A=44-166.
DR PDB; 5HQ7; X-ray; 1.90 A; A=44-167.
DR PDB; 5I80; X-ray; 1.45 A; A=42-167.
DR PDB; 5I88; X-ray; 1.40 A; A=42-167.
DR PDB; 5IGK; X-ray; 1.70 A; A=44-168.
DR PDB; 5JWM; X-ray; 1.71 A; A/B=333-460.
DR PDB; 5KDH; X-ray; 1.50 A; A=44-168.
DR PDB; 5KHM; X-ray; 1.48 A; A/B=44-168.
DR PDB; 5KJ0; X-ray; 1.51 A; A=44-168.
DR PDB; 5KU3; X-ray; 1.14 A; A=42-167.
DR PDB; 5LJ1; X-ray; 1.90 A; A=42-168.
DR PDB; 5LJ2; X-ray; 1.19 A; A=42-168.
DR PDB; 5LRQ; X-ray; 1.70 A; A=42-163.
DR PDB; 5LUU; X-ray; 1.61 A; A=44-168.
DR PDB; 5M39; X-ray; 1.38 A; A/B=42-168.
DR PDB; 5M3A; X-ray; 1.65 A; A=44-168.
DR PDB; 5MKZ; X-ray; 1.62 A; A=44-168.
DR PDB; 5MLI; X-ray; 1.63 A; A=42-168.
DR PDB; 5N2M; X-ray; 1.54 A; A=44-168.
DR PDB; 5NNC; X-ray; 2.22 A; A/B=44-168.
DR PDB; 5NND; X-ray; 1.82 A; A/B=44-168.
DR PDB; 5NNE; X-ray; 1.15 A; A=44-168.
DR PDB; 5NNF; X-ray; 1.15 A; A=44-168.
DR PDB; 5NNG; X-ray; 1.20 A; A=44-168.
DR PDB; 5O97; X-ray; 1.30 A; A=44-168.
DR PDB; 5OVB; X-ray; 1.95 A; A/B=44-168.
DR PDB; 5OWM; X-ray; 1.50 A; A=44-168.
DR PDB; 5OWW; X-ray; 1.50 A; A/B/C/D=44-168.
DR PDB; 5S9P; X-ray; 2.10 A; A/B/D/E=44-168.
DR PDB; 5S9Q; X-ray; 1.85 A; A/B/D/E=44-168.
DR PDB; 5S9R; X-ray; 1.85 A; A=44-168.
DR PDB; 5T35; X-ray; 2.70 A; A/E=333-460.
DR PDB; 5TI2; X-ray; 1.65 A; A=44-168.
DR PDB; 5TI3; X-ray; 1.70 A; A=44-168.
DR PDB; 5TI4; X-ray; 1.62 A; A=44-168.
DR PDB; 5TI5; X-ray; 1.83 A; A=44-168.
DR PDB; 5TI6; X-ray; 1.70 A; A=44-168.
DR PDB; 5TI7; X-ray; 1.65 A; A=44-168.
DR PDB; 5U28; X-ray; 1.80 A; A=44-180.
DR PDB; 5U2C; X-ray; 3.30 A; A/B=342-460.
DR PDB; 5U2E; X-ray; 1.99 A; A/B=42-180.
DR PDB; 5U2F; X-ray; 2.52 A; A/B=42-180.
DR PDB; 5UEO; X-ray; 1.85 A; A/B=352-457.
DR PDB; 5UEP; X-ray; 1.77 A; A=352-457.
DR PDB; 5UEQ; X-ray; 1.70 A; A=352-457.
DR PDB; 5UER; X-ray; 1.87 A; A=352-457.
DR PDB; 5UES; X-ray; 1.62 A; A=352-457.
DR PDB; 5UET; X-ray; 2.29 A; A=352-457.
DR PDB; 5UEU; X-ray; 2.26 A; A/B=352-457.
DR PDB; 5UEV; X-ray; 1.94 A; A=352-457.
DR PDB; 5UEX; X-ray; 2.29 A; A=352-457.
DR PDB; 5UEY; X-ray; 2.41 A; A=352-457.
DR PDB; 5UEZ; X-ray; 1.51 A; A=352-457.
DR PDB; 5UF0; X-ray; 1.35 A; A=352-457.
DR PDB; 5ULA; X-ray; 1.50 A; A/B=44-168.
DR PDB; 5UOO; X-ray; 1.69 A; A=333-460.
DR PDB; 5UVS; X-ray; 2.15 A; A=352-457.
DR PDB; 5UVT; X-ray; 1.67 A; A=352-457.
DR PDB; 5UVU; X-ray; 1.66 A; A=352-457.
DR PDB; 5UVV; X-ray; 1.99 A; A/B=352-457.
DR PDB; 5UVW; X-ray; 2.14 A; A/B/C=57-165.
DR PDB; 5UVX; X-ray; 1.53 A; A/B=352-457.
DR PDB; 5UVY; X-ray; 2.25 A; A=352-457.
DR PDB; 5UVZ; X-ray; 1.63 A; A=352-457.
DR PDB; 5V67; X-ray; 1.78 A; A=44-168.
DR PDB; 5VBO; X-ray; 1.30 A; A=44-168.
DR PDB; 5VBP; X-ray; 1.83 A; A/B=44-168.
DR PDB; 5VOM; X-ray; 1.67 A; A/B=44-168.
DR PDB; 5VZS; X-ray; 1.71 A; A/B=42-168.
DR PDB; 5W55; X-ray; 1.35 A; A=42-168.
DR PDB; 5WA5; X-ray; 1.17 A; A=42-168.
DR PDB; 5WMA; X-ray; 1.40 A; A=44-168.
DR PDB; 5WMD; X-ray; 1.27 A; A=44-168.
DR PDB; 5WMG; X-ray; 1.19 A; A=44-168.
DR PDB; 5WUU; X-ray; 1.72 A; A=44-167.
DR PDB; 5XHY; X-ray; 1.98 A; A=44-166.
DR PDB; 5XI2; X-ray; 1.91 A; A=44-166.
DR PDB; 5XI3; X-ray; 1.67 A; A=44-166.
DR PDB; 5XI4; X-ray; 1.49 A; A=44-166.
DR PDB; 5Y1Y; X-ray; 1.91 A; A=44-167.
DR PDB; 5Y8C; X-ray; 1.42 A; A=44-166.
DR PDB; 5Y8W; X-ray; 1.76 A; A=44-168.
DR PDB; 5Y8Y; X-ray; 1.87 A; A=44-168.
DR PDB; 5Y8Z; X-ray; 1.84 A; A=44-168.
DR PDB; 5Y93; X-ray; 1.62 A; A=44-168.
DR PDB; 5Y94; X-ray; 2.00 A; A=44-168.
DR PDB; 5YOU; X-ray; 1.50 A; A=42-168.
DR PDB; 5YOV; X-ray; 1.45 A; A=42-168.
DR PDB; 5YQX; X-ray; 1.82 A; A=44-167.
DR PDB; 5Z1R; X-ray; 1.62 A; A=44-168.
DR PDB; 5Z1S; X-ray; 1.42 A; A=44-168.
DR PDB; 5Z1T; X-ray; 1.42 A; A=44-168.
DR PDB; 5Z5T; X-ray; 1.99 A; A=44-167.
DR PDB; 5Z5U; X-ray; 1.63 A; A=44-167.
DR PDB; 5Z5V; X-ray; 1.66 A; A=44-167.
DR PDB; 5Z8G; X-ray; 1.70 A; A=44-168.
DR PDB; 5Z8R; X-ray; 2.00 A; A=44-168.
DR PDB; 5Z8Z; X-ray; 1.80 A; A=44-168.
DR PDB; 5Z90; X-ray; 1.80 A; A=44-168.
DR PDB; 5Z9C; NMR; -; A=53-168.
DR PDB; 5Z9K; X-ray; 1.89 A; A=44-168.
DR PDB; 6AFR; X-ray; 2.00 A; A=44-168.
DR PDB; 6AJV; X-ray; 1.45 A; A=42-168.
DR PDB; 6AJW; X-ray; 1.40 A; A=42-168.
DR PDB; 6AJX; X-ray; 1.89 A; A=42-168.
DR PDB; 6AJY; X-ray; 1.60 A; A=42-168.
DR PDB; 6AJZ; Other; 1.30 A; A=42-168.
DR PDB; 6BN7; X-ray; 3.50 A; C=42-168.
DR PDB; 6BN8; X-ray; 3.99 A; C=42-168.
DR PDB; 6BN9; X-ray; 4.38 A; C=42-168.
DR PDB; 6BNB; X-ray; 6.34 A; C=42-168.
DR PDB; 6BNH; NMR; -; A=601-683.
DR PDB; 6BOY; X-ray; 3.33 A; C=42-168.
DR PDB; 6C7Q; X-ray; 1.51 A; A=333-460.
DR PDB; 6C7R; X-ray; 1.50 A; A=44-165.
DR PDB; 6CD4; X-ray; 1.23 A; A=42-168.
DR PDB; 6CD5; X-ray; 1.58 A; A=44-168.
DR PDB; 6CIS; X-ray; 1.51 A; A=44-166.
DR PDB; 6CIY; X-ray; 1.68 A; A=44-168.
DR PDB; 6CJ1; X-ray; 1.53 A; A=44-166.
DR PDB; 6CJ2; X-ray; 1.47 A; A=42-166.
DR PDB; 6CKR; X-ray; 1.62 A; A/B=44-168.
DR PDB; 6CKS; X-ray; 1.72 A; A=44-168.
DR PDB; 6CZU; X-ray; 1.47 A; A=42-170.
DR PDB; 6CZV; X-ray; 1.88 A; A=42-170.
DR PDB; 6DJC; X-ray; 1.46 A; A/B=44-173.
DR PDB; 6DL2; X-ray; 1.47 A; A=44-168.
DR PDB; 6DMJ; X-ray; 1.15 A; A=44-168.
DR PDB; 6DML; X-ray; 1.50 A; A=44-168.
DR PDB; 6DNE; X-ray; 2.96 A; A/B=44-477.
DR PDB; 6DUV; X-ray; 1.80 A; A/B=347-458.
DR PDB; 6E4A; X-ray; 1.26 A; A/B=44-170.
DR PDB; 6FFD; X-ray; 1.83 A; A=347-463.
DR PDB; 6FNX; X-ray; 1.19 A; A=44-168.
DR PDB; 6FO5; X-ray; 0.95 A; A=44-168.
DR PDB; 6FSY; X-ray; 1.34 A; A=42-168.
DR PDB; 6FT3; X-ray; 1.28 A; A=42-168.
DR PDB; 6FT4; X-ray; 1.34 A; A=42-168.
DR PDB; 6G0D; X-ray; 1.31 A; A=42-168.
DR PDB; 6G0E; X-ray; 1.61 A; A=42-168.
DR PDB; 6G0F; X-ray; 1.62 A; A=42-168.
DR PDB; 6G0G; X-ray; 1.48 A; A=42-168.
DR PDB; 6G0H; X-ray; 1.91 A; A=42-168.
DR PDB; 6G0O; X-ray; 1.40 A; A=42-168.
DR PDB; 6G0P; X-ray; 1.30 A; A=42-168.
DR PDB; 6G0Q; X-ray; 1.40 A; A=42-168.
DR PDB; 6G0R; X-ray; 1.25 A; A=42-168.
DR PDB; 6G0S; X-ray; 1.48 A; A/B=42-168.
DR PDB; 6HDQ; X-ray; 1.70 A; A=44-168.
DR PDB; 6HOV; X-ray; 1.85 A; A=44-168.
DR PDB; 6I7X; X-ray; 1.20 A; A=44-168.
DR PDB; 6I7Y; X-ray; 1.00 A; A=44-168.
DR PDB; 6IN1; X-ray; 1.50 A; A=42-168.
DR PDB; 6JI3; X-ray; 2.20 A; A=44-166.
DR PDB; 6JI4; X-ray; 1.60 A; A=44-166.
DR PDB; 6JI5; X-ray; 2.00 A; A=44-166.
DR PDB; 6JJ3; X-ray; 1.72 A; A=44-167.
DR PDB; 6JJ5; X-ray; 1.20 A; A=44-167.
DR PDB; 6JJ6; X-ray; 1.40 A; A=44-167.
DR PDB; 6JJB; X-ray; 1.51 A; A=44-167.
DR PDB; 6KEC; X-ray; 1.35 A; A=44-168.
DR PDB; 6KED; X-ray; 2.55 A; A=44-168.
DR PDB; 6KEE; X-ray; 2.12 A; A=44-168.
DR PDB; 6KEF; X-ray; 2.44 A; A=44-168.
DR PDB; 6KEG; X-ray; 2.23 A; A=44-168.
DR PDB; 6KEH; X-ray; 1.55 A; A=44-168.
DR PDB; 6KEI; X-ray; 1.45 A; A=44-168.
DR PDB; 6KEJ; X-ray; 1.85 A; A=44-168.
DR PDB; 6KEK; X-ray; 1.55 A; A=44-168.
DR PDB; 6KO2; X-ray; 1.50 A; A=351-457.
DR PDB; 6LG4; X-ray; 1.85 A; A=44-167.
DR PDB; 6LG5; X-ray; 1.83 A; A=44-167.
DR PDB; 6LG6; X-ray; 1.98 A; A=44-167.
DR PDB; 6LG7; X-ray; 1.83 A; A=44-167.
DR PDB; 6LG8; X-ray; 1.58 A; A=44-167.
DR PDB; 6LG9; X-ray; 1.81 A; A=44-167.
DR PDB; 6LIH; X-ray; 1.62 A; A=44-166.
DR PDB; 6LIM; X-ray; 1.76 A; A=44-166.
DR PDB; 6MAU; X-ray; 2.11 A; A=44-170.
DR PDB; 6MH1; X-ray; 1.60 A; A/B=44-168.
DR PDB; 6MH7; X-ray; 1.74 A; A/B=44-168.
DR PDB; 6MNL; NMR; -; B=333-460.
DR PDB; 6P05; X-ray; 1.54 A; A=44-168.
DR PDB; 6PRT; X-ray; 1.30 A; A=43-168.
DR PDB; 6PS9; X-ray; 1.21 A; A=44-168.
DR PDB; 6PSB; X-ray; 1.59 A; A=44-168.
DR PDB; 6Q3Y; X-ray; 1.20 A; A/B=42-168.
DR PDB; 6Q3Z; X-ray; 2.00 A; A/B=44-168.
DR PDB; 6RWJ; X-ray; 1.40 A; A=44-168.
DR PDB; 6S25; X-ray; 1.10 A; A=44-168.
DR PDB; 6S4B; X-ray; 1.60 A; A=44-168.
DR PDB; 6S6K; X-ray; 1.40 A; A=44-168.
DR PDB; 6SA2; X-ray; 1.50 A; A=44-168.
DR PDB; 6SA3; X-ray; 1.80 A; A=44-168.
DR PDB; 6SAH; X-ray; 1.50 A; A=44-168.
DR PDB; 6SAJ; X-ray; 1.50 A; A=44-168.
DR PDB; 6SB8; X-ray; 1.50 A; A=44-168.
DR PDB; 6SE4; X-ray; 1.38 A; A=44-168.
DR PDB; 6SIS; X-ray; 3.50 A; A/E=333-460.
DR PDB; 6SWN; X-ray; 1.28 A; AAA=44-168.
DR PDB; 6SWQ; X-ray; 1.60 A; AAA=44-168.
DR PDB; 6TPX; X-ray; 1.48 A; AAA=44-168.
DR PDB; 6TPY; X-ray; 1.80 A; AAA=44-168.
DR PDB; 6TPZ; X-ray; 1.30 A; AAA=44-168.
DR PDB; 6U0D; X-ray; 1.43 A; A=44-168.
DR PDB; 6U6K; X-ray; 1.70 A; A=42-168.
DR PDB; 6U6L; X-ray; 2.60 A; A=347-464.
DR PDB; 6U72; X-ray; 2.30 A; A/B=42-168.
DR PDB; 6U74; X-ray; 1.85 A; A/B/C/D=42-168.
DR PDB; 6U8G; X-ray; 2.60 A; A/B/C/D=42-168.
DR PDB; 6U8I; X-ray; 2.50 A; A=347-464.
DR PDB; 6U8M; X-ray; 1.95 A; A/B=42-168.
DR PDB; 6ULS; X-ray; 1.50 A; A=42-168.
DR PDB; 6ULV; X-ray; 2.20 A; A/B/C/D=42-168.
DR PDB; 6UVJ; X-ray; 1.38 A; A=44-168.
DR PDB; 6UVM; X-ray; 1.51 A; A=44-168.
DR PDB; 6UWU; X-ray; 2.00 A; A=44-168.
DR PDB; 6UWX; X-ray; 1.31 A; A=44-168.
DR PDB; 6V0U; X-ray; 1.40 A; A=44-168.
DR PDB; 6V1K; X-ray; 1.75 A; A=44-168.
DR PDB; 6V1L; X-ray; 2.10 A; A=44-168.
DR PDB; 6V1U; X-ray; 1.73 A; A=44-168.
DR PDB; 6VIW; X-ray; 2.43 A; A/B/C=57-168.
DR PDB; 6VIX; X-ray; 2.12 A; A/B/C/D=352-457.
DR PDB; 6VIZ; X-ray; 2.39 A; A/B/C=57-168.
DR PDB; 6VUB; X-ray; 1.50 A; A=44-168.
DR PDB; 6VUC; X-ray; 1.55 A; A=44-168.
DR PDB; 6VUF; X-ray; 1.59 A; A/B=44-168.
DR PDB; 6VUJ; X-ray; 1.48 A; A=44-168.
DR PDB; 6WGX; X-ray; 1.53 A; A/B=44-168.
DR PDB; 6WVX; X-ray; 1.55 A; A/B=44-168.
DR PDB; 6WW8; X-ray; 2.30 A; A=43-180.
DR PDB; 6X7B; X-ray; 1.95 A; A/B=44-176.
DR PDB; 6X7C; X-ray; 2.70 A; A=44-176.
DR PDB; 6X7D; X-ray; 2.50 A; A/B=44-176.
DR PDB; 6XUZ; X-ray; 1.07 A; A=44-168.
DR PDB; 6XV3; X-ray; 1.47 A; A/B/C/D=44-168.
DR PDB; 6XV7; X-ray; 1.67 A; A=44-168.
DR PDB; 6XVC; X-ray; 1.10 A; B=44-168.
DR PDB; 6YIN; X-ray; 1.53 A; A=44-168.
DR PDB; 6YQN; X-ray; 1.05 A; A=44-168.
DR PDB; 6YQO; X-ray; 1.07 A; A=44-168.
DR PDB; 6YQP; X-ray; 1.25 A; A=44-168.
DR PDB; 6YQZ; X-ray; 1.39 A; A=44-168.
DR PDB; 6Z7G; X-ray; 1.59 A; AAA=44-168.
DR PDB; 6Z7L; X-ray; 1.62 A; AAA=44-168.
DR PDB; 6Z7M; X-ray; 1.26 A; AAA=44-168.
DR PDB; 6ZB3; X-ray; 1.42 A; AAA=44-168.
DR PDB; 6ZCI; X-ray; 1.98 A; A=44-168.
DR PDB; 6ZED; X-ray; 1.08 A; AAA=44-168.
DR PDB; 6ZEL; X-ray; 1.12 A; AAA=44-168.
DR PDB; 6ZF9; X-ray; 1.20 A; AAA=44-168.
DR PDB; 7A9U; X-ray; 1.44 A; AAA=44-168.
DR PDB; 7AJN; X-ray; 1.48 A; A=44-168.
DR PDB; 7AQT; NMR; -; A=351-459.
DR PDB; 7AXR; X-ray; 1.50 A; A=44-168.
DR PDB; 7C2Z; X-ray; 1.30 A; A=44-168.
DR PDB; 7C6P; X-ray; 1.73 A; A=352-457.
DR PDB; 7DHS; X-ray; 1.76 A; A/B=44-168.
DR PDB; 7EHW; X-ray; 1.65 A; A=44-167.
DR PDB; 7EHY; X-ray; 1.51 A; A=44-167.
DR PDB; 7EIG; X-ray; 1.30 A; A=44-167.
DR PDB; 7EIK; X-ray; 1.70 A; A=44-167.
DR PDB; 7EIL; X-ray; 1.70 A; A=44-167.
DR PDB; 7JKW; X-ray; 1.20 A; A=44-168.
DR PDB; 7JKX; X-ray; 1.20 A; A=44-168.
DR PDB; 7JKY; X-ray; 1.16 A; A=44-168.
DR PDB; 7JKZ; X-ray; 2.49 A; A=333-460.
DR PDB; 7K6G; X-ray; 1.70 A; A/B=44-168.
DR PDB; 7K6H; X-ray; 1.50 A; A=44-168.
DR PDB; 7KHH; X-ray; 2.28 A; D=44-168.
DR PDB; 7KHL; X-ray; 1.29 A; A/B=44-168.
DR PDB; 7KO0; X-ray; 1.90 A; A=349-460.
DR PDB; 7L9M; X-ray; 1.45 A; A/B=44-168.
DR PDB; 7LA9; X-ray; 2.20 A; A/B/C/D/E/F=44-168.
DR PDB; 7M16; X-ray; 1.42 A; A=44-168.
DR PDB; 7MCE; X-ray; 1.76 A; A=44-168.
DR PDB; 7MCF; X-ray; 2.19 A; A/B=44-168.
DR PDB; 7MLQ; X-ray; 1.32 A; A=44-168.
DR PDB; 7MLR; X-ray; 1.20 A; A=44-168.
DR PDB; 7MLS; X-ray; 1.26 A; A=44-168.
DR PDB; 7O18; X-ray; 1.70 A; AAA=44-168.
DR PDB; 7OEO; X-ray; 1.51 A; AAA=347-463.
DR PDB; 7P6V; X-ray; 1.17 A; AAA=44-168.
DR PDB; 7P6W; X-ray; 1.31 A; AAA=44-168.
DR PDB; 7P6Y; X-ray; 1.88 A; AAA/BBB=44-168.
DR PDB; 7R9C; X-ray; 1.50 A; A=44-168.
DR PDB; 7REK; X-ray; 1.20 A; A/B=44-168.
DR PDB; 7REL; X-ray; 1.55 A; A=44-168.
DR PDB; 7REM; X-ray; 1.80 A; A=44-168.
DR PDB; 7RXR; X-ray; 1.41 A; A/B=44-168.
DR PDB; 7RXS; X-ray; 1.43 A; A=44-168.
DR PDB; 7RXT; X-ray; 1.68 A; A=44-168.
DR PDBsum; 2I8N; -.
DR PDBsum; 2LSP; -.
DR PDBsum; 2MJV; -.
DR PDBsum; 2N3K; -.
DR PDBsum; 2NCZ; -.
DR PDBsum; 2ND0; -.
DR PDBsum; 2ND1; -.
DR PDBsum; 2NNU; -.
DR PDBsum; 2OSS; -.
DR PDBsum; 2OUO; -.
DR PDBsum; 2YEL; -.
DR PDBsum; 2YEM; -.
DR PDBsum; 3MXF; -.
DR PDBsum; 3P5O; -.
DR PDBsum; 3SVF; -.
DR PDBsum; 3SVG; -.
DR PDBsum; 3U5J; -.
DR PDBsum; 3U5K; -.
DR PDBsum; 3U5L; -.
DR PDBsum; 3UVW; -.
DR PDBsum; 3UVX; -.
DR PDBsum; 3UVY; -.
DR PDBsum; 3UW9; -.
DR PDBsum; 3ZYU; -.
DR PDBsum; 4A9L; -.
DR PDBsum; 4BJX; -.
DR PDBsum; 4BW1; -.
DR PDBsum; 4BW2; -.
DR PDBsum; 4BW3; -.
DR PDBsum; 4BW4; -.
DR PDBsum; 4C66; -.
DR PDBsum; 4C67; -.
DR PDBsum; 4CFK; -.
DR PDBsum; 4CFL; -.
DR PDBsum; 4CL9; -.
DR PDBsum; 4CLB; -.
DR PDBsum; 4DON; -.
DR PDBsum; 4E96; -.
DR PDBsum; 4F3I; -.
DR PDBsum; 4GPJ; -.
DR PDBsum; 4HBV; -.
DR PDBsum; 4HBW; -.
DR PDBsum; 4HBX; -.
DR PDBsum; 4HBY; -.
DR PDBsum; 4HXK; -.
DR PDBsum; 4HXL; -.
DR PDBsum; 4HXM; -.
DR PDBsum; 4HXN; -.
DR PDBsum; 4HXO; -.
DR PDBsum; 4HXP; -.
DR PDBsum; 4HXR; -.
DR PDBsum; 4HXS; -.
DR PDBsum; 4IOO; -.
DR PDBsum; 4IOQ; -.
DR PDBsum; 4IOR; -.
DR PDBsum; 4J0R; -.
DR PDBsum; 4J0S; -.
DR PDBsum; 4J3I; -.
DR PDBsum; 4KV1; -.
DR PDBsum; 4KV4; -.
DR PDBsum; 4LR6; -.
DR PDBsum; 4LRG; -.
DR PDBsum; 4LYI; -.
DR PDBsum; 4LYS; -.
DR PDBsum; 4LYW; -.
DR PDBsum; 4LZR; -.
DR PDBsum; 4LZS; -.
DR PDBsum; 4MEN; -.
DR PDBsum; 4MEO; -.
DR PDBsum; 4MEP; -.
DR PDBsum; 4MEQ; -.
DR PDBsum; 4MR3; -.
DR PDBsum; 4MR4; -.
DR PDBsum; 4NQM; -.
DR PDBsum; 4NR8; -.
DR PDBsum; 4NUC; -.
DR PDBsum; 4NUD; -.
DR PDBsum; 4NUE; -.
DR PDBsum; 4O70; -.
DR PDBsum; 4O71; -.
DR PDBsum; 4O72; -.
DR PDBsum; 4O74; -.
DR PDBsum; 4O75; -.
DR PDBsum; 4O76; -.
DR PDBsum; 4O77; -.
DR PDBsum; 4O78; -.
DR PDBsum; 4O7A; -.
DR PDBsum; 4O7B; -.
DR PDBsum; 4O7C; -.
DR PDBsum; 4O7E; -.
DR PDBsum; 4O7F; -.
DR PDBsum; 4OGI; -.
DR PDBsum; 4OGJ; -.
DR PDBsum; 4PCE; -.
DR PDBsum; 4PCI; -.
DR PDBsum; 4PS5; -.
DR PDBsum; 4QB3; -.
DR PDBsum; 4QR3; -.
DR PDBsum; 4QR4; -.
DR PDBsum; 4QR5; -.
DR PDBsum; 4QZS; -.
DR PDBsum; 4UIX; -.
DR PDBsum; 4UIY; -.
DR PDBsum; 4UIZ; -.
DR PDBsum; 4UYD; -.
DR PDBsum; 4WHW; -.
DR PDBsum; 4WIV; -.
DR PDBsum; 4X2I; -.
DR PDBsum; 4XY9; -.
DR PDBsum; 4XYA; -.
DR PDBsum; 4YH3; -.
DR PDBsum; 4YH4; -.
DR PDBsum; 4Z1Q; -.
DR PDBsum; 4Z1S; -.
DR PDBsum; 4Z93; -.
DR PDBsum; 4ZC9; -.
DR PDBsum; 4ZW1; -.
DR PDBsum; 5A5S; -.
DR PDBsum; 5A85; -.
DR PDBsum; 5ACY; -.
DR PDBsum; 5AD2; -.
DR PDBsum; 5AD3; -.
DR PDBsum; 5BT4; -.
DR PDBsum; 5CFW; -.
DR PDBsum; 5COI; -.
DR PDBsum; 5CP5; -.
DR PDBsum; 5CPE; -.
DR PDBsum; 5CQT; -.
DR PDBsum; 5CRM; -.
DR PDBsum; 5CRZ; -.
DR PDBsum; 5CS8; -.
DR PDBsum; 5CTL; -.
DR PDBsum; 5CY9; -.
DR PDBsum; 5D0C; -.
DR PDBsum; 5D24; -.
DR PDBsum; 5D25; -.
DR PDBsum; 5D26; -.
DR PDBsum; 5D3H; -.
DR PDBsum; 5D3J; -.
DR PDBsum; 5D3L; -.
DR PDBsum; 5D3N; -.
DR PDBsum; 5D3P; -.
DR PDBsum; 5D3R; -.
DR PDBsum; 5D3S; -.
DR PDBsum; 5D3T; -.
DR PDBsum; 5DLX; -.
DR PDBsum; 5DLZ; -.
DR PDBsum; 5DW2; -.
DR PDBsum; 5DX4; -.
DR PDBsum; 5E0R; -.
DR PDBsum; 5EGU; -.
DR PDBsum; 5EI4; -.
DR PDBsum; 5EIS; -.
DR PDBsum; 5F5Z; -.
DR PDBsum; 5F60; -.
DR PDBsum; 5F61; -.
DR PDBsum; 5F62; -.
DR PDBsum; 5F63; -.
DR PDBsum; 5FBX; -.
DR PDBsum; 5H21; -.
DR PDBsum; 5HCL; -.
DR PDBsum; 5HLS; -.
DR PDBsum; 5HM0; -.
DR PDBsum; 5HQ5; -.
DR PDBsum; 5HQ6; -.
DR PDBsum; 5HQ7; -.
DR PDBsum; 5I80; -.
DR PDBsum; 5I88; -.
DR PDBsum; 5IGK; -.
DR PDBsum; 5JWM; -.
DR PDBsum; 5KDH; -.
DR PDBsum; 5KHM; -.
DR PDBsum; 5KJ0; -.
DR PDBsum; 5KU3; -.
DR PDBsum; 5LJ1; -.
DR PDBsum; 5LJ2; -.
DR PDBsum; 5LRQ; -.
DR PDBsum; 5LUU; -.
DR PDBsum; 5M39; -.
DR PDBsum; 5M3A; -.
DR PDBsum; 5MKZ; -.
DR PDBsum; 5MLI; -.
DR PDBsum; 5N2M; -.
DR PDBsum; 5NNC; -.
DR PDBsum; 5NND; -.
DR PDBsum; 5NNE; -.
DR PDBsum; 5NNF; -.
DR PDBsum; 5NNG; -.
DR PDBsum; 5O97; -.
DR PDBsum; 5OVB; -.
DR PDBsum; 5OWM; -.
DR PDBsum; 5OWW; -.
DR PDBsum; 5S9P; -.
DR PDBsum; 5S9Q; -.
DR PDBsum; 5S9R; -.
DR PDBsum; 5T35; -.
DR PDBsum; 5TI2; -.
DR PDBsum; 5TI3; -.
DR PDBsum; 5TI4; -.
DR PDBsum; 5TI5; -.
DR PDBsum; 5TI6; -.
DR PDBsum; 5TI7; -.
DR PDBsum; 5U28; -.
DR PDBsum; 5U2C; -.
DR PDBsum; 5U2E; -.
DR PDBsum; 5U2F; -.
DR PDBsum; 5UEO; -.
DR PDBsum; 5UEP; -.
DR PDBsum; 5UEQ; -.
DR PDBsum; 5UER; -.
DR PDBsum; 5UES; -.
DR PDBsum; 5UET; -.
DR PDBsum; 5UEU; -.
DR PDBsum; 5UEV; -.
DR PDBsum; 5UEX; -.
DR PDBsum; 5UEY; -.
DR PDBsum; 5UEZ; -.
DR PDBsum; 5UF0; -.
DR PDBsum; 5ULA; -.
DR PDBsum; 5UOO; -.
DR PDBsum; 5UVS; -.
DR PDBsum; 5UVT; -.
DR PDBsum; 5UVU; -.
DR PDBsum; 5UVV; -.
DR PDBsum; 5UVW; -.
DR PDBsum; 5UVX; -.
DR PDBsum; 5UVY; -.
DR PDBsum; 5UVZ; -.
DR PDBsum; 5V67; -.
DR PDBsum; 5VBO; -.
DR PDBsum; 5VBP; -.
DR PDBsum; 5VOM; -.
DR PDBsum; 5VZS; -.
DR PDBsum; 5W55; -.
DR PDBsum; 5WA5; -.
DR PDBsum; 5WMA; -.
DR PDBsum; 5WMD; -.
DR PDBsum; 5WMG; -.
DR PDBsum; 5WUU; -.
DR PDBsum; 5XHY; -.
DR PDBsum; 5XI2; -.
DR PDBsum; 5XI3; -.
DR PDBsum; 5XI4; -.
DR PDBsum; 5Y1Y; -.
DR PDBsum; 5Y8C; -.
DR PDBsum; 5Y8W; -.
DR PDBsum; 5Y8Y; -.
DR PDBsum; 5Y8Z; -.
DR PDBsum; 5Y93; -.
DR PDBsum; 5Y94; -.
DR PDBsum; 5YOU; -.
DR PDBsum; 5YOV; -.
DR PDBsum; 5YQX; -.
DR PDBsum; 5Z1R; -.
DR PDBsum; 5Z1S; -.
DR PDBsum; 5Z1T; -.
DR PDBsum; 5Z5T; -.
DR PDBsum; 5Z5U; -.
DR PDBsum; 5Z5V; -.
DR PDBsum; 5Z8G; -.
DR PDBsum; 5Z8R; -.
DR PDBsum; 5Z8Z; -.
DR PDBsum; 5Z90; -.
DR PDBsum; 5Z9C; -.
DR PDBsum; 5Z9K; -.
DR PDBsum; 6AFR; -.
DR PDBsum; 6AJV; -.
DR PDBsum; 6AJW; -.
DR PDBsum; 6AJX; -.
DR PDBsum; 6AJY; -.
DR PDBsum; 6AJZ; -.
DR PDBsum; 6BN7; -.
DR PDBsum; 6BN8; -.
DR PDBsum; 6BN9; -.
DR PDBsum; 6BNB; -.
DR PDBsum; 6BNH; -.
DR PDBsum; 6BOY; -.
DR PDBsum; 6C7Q; -.
DR PDBsum; 6C7R; -.
DR PDBsum; 6CD4; -.
DR PDBsum; 6CD5; -.
DR PDBsum; 6CIS; -.
DR PDBsum; 6CIY; -.
DR PDBsum; 6CJ1; -.
DR PDBsum; 6CJ2; -.
DR PDBsum; 6CKR; -.
DR PDBsum; 6CKS; -.
DR PDBsum; 6CZU; -.
DR PDBsum; 6CZV; -.
DR PDBsum; 6DJC; -.
DR PDBsum; 6DL2; -.
DR PDBsum; 6DMJ; -.
DR PDBsum; 6DML; -.
DR PDBsum; 6DNE; -.
DR PDBsum; 6DUV; -.
DR PDBsum; 6E4A; -.
DR PDBsum; 6FFD; -.
DR PDBsum; 6FNX; -.
DR PDBsum; 6FO5; -.
DR PDBsum; 6FSY; -.
DR PDBsum; 6FT3; -.
DR PDBsum; 6FT4; -.
DR PDBsum; 6G0D; -.
DR PDBsum; 6G0E; -.
DR PDBsum; 6G0F; -.
DR PDBsum; 6G0G; -.
DR PDBsum; 6G0H; -.
DR PDBsum; 6G0O; -.
DR PDBsum; 6G0P; -.
DR PDBsum; 6G0Q; -.
DR PDBsum; 6G0R; -.
DR PDBsum; 6G0S; -.
DR PDBsum; 6HDQ; -.
DR PDBsum; 6HOV; -.
DR PDBsum; 6I7X; -.
DR PDBsum; 6I7Y; -.
DR PDBsum; 6IN1; -.
DR PDBsum; 6JI3; -.
DR PDBsum; 6JI4; -.
DR PDBsum; 6JI5; -.
DR PDBsum; 6JJ3; -.
DR PDBsum; 6JJ5; -.
DR PDBsum; 6JJ6; -.
DR PDBsum; 6JJB; -.
DR PDBsum; 6KEC; -.
DR PDBsum; 6KED; -.
DR PDBsum; 6KEE; -.
DR PDBsum; 6KEF; -.
DR PDBsum; 6KEG; -.
DR PDBsum; 6KEH; -.
DR PDBsum; 6KEI; -.
DR PDBsum; 6KEJ; -.
DR PDBsum; 6KEK; -.
DR PDBsum; 6KO2; -.
DR PDBsum; 6LG4; -.
DR PDBsum; 6LG5; -.
DR PDBsum; 6LG6; -.
DR PDBsum; 6LG7; -.
DR PDBsum; 6LG8; -.
DR PDBsum; 6LG9; -.
DR PDBsum; 6LIH; -.
DR PDBsum; 6LIM; -.
DR PDBsum; 6MAU; -.
DR PDBsum; 6MH1; -.
DR PDBsum; 6MH7; -.
DR PDBsum; 6MNL; -.
DR PDBsum; 6P05; -.
DR PDBsum; 6PRT; -.
DR PDBsum; 6PS9; -.
DR PDBsum; 6PSB; -.
DR PDBsum; 6Q3Y; -.
DR PDBsum; 6Q3Z; -.
DR PDBsum; 6RWJ; -.
DR PDBsum; 6S25; -.
DR PDBsum; 6S4B; -.
DR PDBsum; 6S6K; -.
DR PDBsum; 6SA2; -.
DR PDBsum; 6SA3; -.
DR PDBsum; 6SAH; -.
DR PDBsum; 6SAJ; -.
DR PDBsum; 6SB8; -.
DR PDBsum; 6SE4; -.
DR PDBsum; 6SIS; -.
DR PDBsum; 6SWN; -.
DR PDBsum; 6SWQ; -.
DR PDBsum; 6TPX; -.
DR PDBsum; 6TPY; -.
DR PDBsum; 6TPZ; -.
DR PDBsum; 6U0D; -.
DR PDBsum; 6U6K; -.
DR PDBsum; 6U6L; -.
DR PDBsum; 6U72; -.
DR PDBsum; 6U74; -.
DR PDBsum; 6U8G; -.
DR PDBsum; 6U8I; -.
DR PDBsum; 6U8M; -.
DR PDBsum; 6ULS; -.
DR PDBsum; 6ULV; -.
DR PDBsum; 6UVJ; -.
DR PDBsum; 6UVM; -.
DR PDBsum; 6UWU; -.
DR PDBsum; 6UWX; -.
DR PDBsum; 6V0U; -.
DR PDBsum; 6V1K; -.
DR PDBsum; 6V1L; -.
DR PDBsum; 6V1U; -.
DR PDBsum; 6VIW; -.
DR PDBsum; 6VIX; -.
DR PDBsum; 6VIZ; -.
DR PDBsum; 6VUB; -.
DR PDBsum; 6VUC; -.
DR PDBsum; 6VUF; -.
DR PDBsum; 6VUJ; -.
DR PDBsum; 6WGX; -.
DR PDBsum; 6WVX; -.
DR PDBsum; 6WW8; -.
DR PDBsum; 6X7B; -.
DR PDBsum; 6X7C; -.
DR PDBsum; 6X7D; -.
DR PDBsum; 6XUZ; -.
DR PDBsum; 6XV3; -.
DR PDBsum; 6XV7; -.
DR PDBsum; 6XVC; -.
DR PDBsum; 6YIN; -.
DR PDBsum; 6YQN; -.
DR PDBsum; 6YQO; -.
DR PDBsum; 6YQP; -.
DR PDBsum; 6YQZ; -.
DR PDBsum; 6Z7G; -.
DR PDBsum; 6Z7L; -.
DR PDBsum; 6Z7M; -.
DR PDBsum; 6ZB3; -.
DR PDBsum; 6ZCI; -.
DR PDBsum; 6ZED; -.
DR PDBsum; 6ZEL; -.
DR PDBsum; 6ZF9; -.
DR PDBsum; 7A9U; -.
DR PDBsum; 7AJN; -.
DR PDBsum; 7AQT; -.
DR PDBsum; 7AXR; -.
DR PDBsum; 7C2Z; -.
DR PDBsum; 7C6P; -.
DR PDBsum; 7DHS; -.
DR PDBsum; 7EHW; -.
DR PDBsum; 7EHY; -.
DR PDBsum; 7EIG; -.
DR PDBsum; 7EIK; -.
DR PDBsum; 7EIL; -.
DR PDBsum; 7JKW; -.
DR PDBsum; 7JKX; -.
DR PDBsum; 7JKY; -.
DR PDBsum; 7JKZ; -.
DR PDBsum; 7K6G; -.
DR PDBsum; 7K6H; -.
DR PDBsum; 7KHH; -.
DR PDBsum; 7KHL; -.
DR PDBsum; 7KO0; -.
DR PDBsum; 7L9M; -.
DR PDBsum; 7LA9; -.
DR PDBsum; 7M16; -.
DR PDBsum; 7MCE; -.
DR PDBsum; 7MCF; -.
DR PDBsum; 7MLQ; -.
DR PDBsum; 7MLR; -.
DR PDBsum; 7MLS; -.
DR PDBsum; 7O18; -.
DR PDBsum; 7OEO; -.
DR PDBsum; 7P6V; -.
DR PDBsum; 7P6W; -.
DR PDBsum; 7P6Y; -.
DR PDBsum; 7R9C; -.
DR PDBsum; 7REK; -.
DR PDBsum; 7REL; -.
DR PDBsum; 7REM; -.
DR PDBsum; 7RXR; -.
DR PDBsum; 7RXS; -.
DR PDBsum; 7RXT; -.
DR AlphaFoldDB; O60885; -.
DR BMRB; O60885; -.
DR SASBDB; O60885; -.
DR SMR; O60885; -.
DR BioGRID; 117036; 1531.
DR CORUM; O60885; -.
DR DIP; DIP-39776N; -.
DR IntAct; O60885; 63.
DR MINT; O60885; -.
DR STRING; 9606.ENSP00000263377; -.
DR BindingDB; O60885; -.
DR ChEMBL; CHEMBL1163125; -.
DR DrugCentral; O60885; -.
DR GuidetoPHARMACOLOGY; 1945; -.
DR GlyGen; O60885; 8 sites, 2 O-linked glycans (8 sites).
DR iPTMnet; O60885; -.
DR MetOSite; O60885; -.
DR PhosphoSitePlus; O60885; -.
DR SwissPalm; O60885; -.
DR BioMuta; BRD4; -.
DR EPD; O60885; -.
DR jPOST; O60885; -.
DR MassIVE; O60885; -.
DR MaxQB; O60885; -.
DR PaxDb; O60885; -.
DR PeptideAtlas; O60885; -.
DR PRIDE; O60885; -.
DR ProteomicsDB; 49651; -. [O60885-1]
DR ProteomicsDB; 49652; -. [O60885-2]
DR ProteomicsDB; 62139; -.
DR ABCD; O60885; 4 sequenced antibodies.
DR Antibodypedia; 13956; 446 antibodies from 38 providers.
DR DNASU; 23476; -.
DR Ensembl; ENST00000263377.6; ENSP00000263377.1; ENSG00000141867.19. [O60885-1]
DR Ensembl; ENST00000360016.9; ENSP00000353112.4; ENSG00000141867.19. [O60885-3]
DR Ensembl; ENST00000371835.8; ENSP00000360901.3; ENSG00000141867.19. [O60885-2]
DR Ensembl; ENST00000679869.1; ENSP00000506350.1; ENSG00000141867.19. [O60885-1]
DR GeneID; 23476; -.
DR KEGG; hsa:23476; -.
DR MANE-Select; ENST00000679869.1; ENSP00000506350.1; NM_001379291.1; NP_001366220.1.
DR UCSC; uc002nar.4; human. [O60885-1]
DR CTD; 23476; -.
DR DisGeNET; 23476; -.
DR GeneCards; BRD4; -.
DR GeneReviews; BRD4; -.
DR HGNC; HGNC:13575; BRD4.
DR HPA; ENSG00000141867; Low tissue specificity.
DR MalaCards; BRD4; -.
DR MIM; 608749; gene.
DR neXtProt; NX_O60885; -.
DR OpenTargets; ENSG00000141867; -.
DR Orphanet; 199; Cornelia de Lange syndrome.
DR Orphanet; 443167; NUT midline carcinoma.
DR PharmGKB; PA25416; -.
DR VEuPathDB; HostDB:ENSG00000141867; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000154549; -.
DR HOGENOM; CLU_001499_0_3_1; -.
DR InParanoid; O60885; -.
DR OMA; YKIIRSP; -.
DR OrthoDB; 619848at2759; -.
DR PhylomeDB; O60885; -.
DR TreeFam; TF317345; -.
DR PathwayCommons; O60885; -.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; O60885; -.
DR SIGNOR; O60885; -.
DR BioGRID-ORCS; 23476; 698 hits in 1128 CRISPR screens.
DR ChiTaRS; BRD4; human.
DR EvolutionaryTrace; O60885; -.
DR GeneWiki; BRD4; -.
DR GenomeRNAi; 23476; -.
DR Pharos; O60885; Tchem.
DR PRO; PR:O60885; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O60885; protein.
DR Bgee; ENSG00000141867; Expressed in buccal mucosa cell and 211 other tissues.
DR ExpressionAtlas; O60885; baseline and differential.
DR Genevisible; O60885; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0106140; F:P-TEFb complex binding; IDA:FlyBase.
DR GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IDA:MGI.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IMP:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:FlyBase.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; IDA:UniProtKB.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd05497; Bromo_Brdt_I_like; 1.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR DisProt; DP01898; -.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR IDEAL; IID00111; -.
DR InterPro; IPR031354; BRD4_CDT.
DR InterPro; IPR043508; Bromo_Brdt_I.
DR InterPro; IPR043509; Bromo_Brdt_II.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF17105; BRD4_CDT; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Bromodomain;
KW Chromatin regulator; Chromosomal rearrangement; Chromosome; DNA damage;
KW Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1362
FT /note="Bromodomain-containing protein 4"
FT /id="PRO_0000211183"
FT DOMAIN 75..147
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 368..440
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 600..682
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..503
FT /note="NPS region"
FT REGION 524..579
FT /note="BID region"
FT REGION 674..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1362
FT /note="C-terminal (CTD) region"
FT REGION 1116..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..274
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..745
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..847
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1036
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 140
FT /note="Acetylated histone binding"
FT /evidence="ECO:0000269|PubMed:22464331"
FT SITE 433
FT /note="Acetylated histone binding"
FT /evidence="ECO:0000269|PubMed:22464331"
FT SITE 719..720
FT /note="Breakpoint for translocation to form BDR4-NUTM1
FT fusion protein"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 484
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23317504"
FT MOD_RES 488
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23317504"
FT MOD_RES 492
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23317504"
FT MOD_RES 494
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23317504"
FT MOD_RES 498
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23317504"
FT MOD_RES 499
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23317504"
FT MOD_RES 503
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23317504"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1111
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 585
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 694
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1050
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 720..1362
FT /note="EMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQ
FT QQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHL
FT PQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPA
FT VSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSV
FT KVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTH
FT IQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPL
FT MIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPF
FT SPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEP
FT KTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKA
FT QAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAA
FT AVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENL
FT F -> AFCTSGDFVSPGPSPYHSHVQCGRFREMLRWFLVDVEQTAAGQPHRQSAAGPAI
FT TWAPAIAYPSPECARCCVGCS (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047671"
FT VAR_SEQ 720..722
FT /note="EMA -> GPA (in isoform C)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010902"
FT VAR_SEQ 723..1362
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010903"
FT VARIANT 37
FT /note="P -> S (in dbSNP:rs35177876)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041919"
FT VARIANT 371
FT /note="A -> G (in dbSNP:rs55805532)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041920"
FT VARIANT 563
FT /note="S -> N (in dbSNP:rs55970906)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041921"
FT VARIANT 598
FT /note="T -> S (in dbSNP:rs34362023)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041922"
FT VARIANT 669
FT /note="R -> H (in dbSNP:rs35824241)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041923"
FT VARIANT 1097
FT /note="R -> H (in dbSNP:rs35676845)"
FT /id="VAR_048427"
FT MUTAGEN 140
FT /note="N->A: Abolishes binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:22464331,
FT ECO:0000269|PubMed:23728299"
FT MUTAGEN 433
FT /note="N->A: Abolishes binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:22464331"
FT MUTAGEN 492..494
FT /note="SSS->ASA: Impaired phosphorylation by CK2 and
FT binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:23317504"
FT MUTAGEN 498..500
FT /note="SST->AAA: Impaired phosphorylation by CK2 and
FT binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:23317504"
FT MUTAGEN 503
FT /note="S->A: Impaired phosphorylation by CK2 and binding to
FT acetylated histones."
FT /evidence="ECO:0000269|PubMed:23317504"
FT MUTAGEN 651..653
FT /note="EIE->AIA: Decreases interaction with JMJD6 and
FT NSD3.No effect on interaction with histone 4 acetylated."
FT /evidence="ECO:0000269|PubMed:29176719"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4WHW"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6X7B"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:4QB3"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:4QB3"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4QB3"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5Z1S"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:4QB3"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:4QB3"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:4QB3"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6X7D"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:4QB3"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:4QB3"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:6X7B"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:2LSP"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:4Z93"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:4Z93"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:4Z93"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:4Z93"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:4Z93"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:4Z93"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:4Z93"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2MJV"
FT HELIX 415..432
FT /evidence="ECO:0007829|PDB:4Z93"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:2I8N"
FT HELIX 438..454
FT /evidence="ECO:0007829|PDB:4Z93"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:2NCZ"
FT HELIX 612..624
FT /evidence="ECO:0007829|PDB:2N3K"
FT HELIX 627..640
FT /evidence="ECO:0007829|PDB:2N3K"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:2NCZ"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:2N3K"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:2N3K"
FT HELIX 661..675
FT /evidence="ECO:0007829|PDB:2N3K"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:6BNH"
FT HELIX 1345..1354
FT /evidence="ECO:0007829|PDB:2NNU"
FT TURN 1355..1357
FT /evidence="ECO:0007829|PDB:2NNU"
SQ SEQUENCE 1362 AA; 152219 MW; D52EFE1CF9960907 CRC64;
MSAESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET SNPNKPKRQT
NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI IKTPMDMGTI KKRLENNYYW
NAQECIQDFN TMFTNCYIYN KPGDDIVLMA EALEKLFLQK INELPTEETE IMIVQAKGRG
RGRKETGTAK PGVSTVPNTT QASTPPQTQT PQPNPPPVQA TPHPFPAVTP DLIVQTPVMT
VVPPQPLQTP PPVPPQPQPP PAPAPQPVQS HPPIIAATPQ PVKTKKGVKR KADTTTPTTI
DPIHEPPSLP PEPKTTKLGQ RRESSRPVKP PKKDVPDSQQ HPAPEKSSKV SEQLKCCSGI
LKEMFAKKHA AYAWPFYKPV DVEALGLHDY CDIIKHPMDM STIKSKLEAR EYRDAQEFGA
DVRLMFSNCY KYNPPDHEVV AMARKLQDVF EMRFAKMPDE PEEPVVAVSS PAVPPPTKVV
APPSSSDSSS DSSSDSDSST DDSEEERAQR LAELQEQLKA VHEQLAALSQ PQQNKPKKKE
KDKKEKKKEK HKRKEEVEEN KKSKAKEPPP KKTKKNNSSN SNVSKKEPAP MKSKPPPTYE
SEEEDKCKPM SYEEKRQLSL DINKLPGEKL GRVVHIIQSR EPSLKNSNPD EIEIDFETLK
PSTLRELERY VTSCLRKKRK PQAEKVDVIA GSSKMKGFSS SESESSSESS SSDSEDSETE
MAPKSKKKGH PGREQKKHHH HHHQQMQQAP APVPQQPPPP PQQPPPPPPP QQQQQPPPPP
PPPSMPQQAA PAMKSSPPPF IATQVPVLEP QLPGSVFDPI GHFTQPILHL PQPELPPHLP
QPPEHSTPPH LNQHAVVSPP ALHNALPQQP SRPSNRAAAL PPKPARPPAV SPALTQTPLL
PQPPMAQPPQ VLLEDEEPPA PPLTSMQMQL YLQQLQKVQP PTPLLPSVKV QSQPPPPLPP
PPHPSVQQQL QQQPPPPPPP QPQPPPQQQH QPPPRPVHLQ PMQFSTHIQQ PPPPQGQQPP
HPPPGQQPPP PQPAKPQQVI QHHHSPRHHK SDPYSTGHLR EAPSPLMIHS PQMSQFQSLT
HQSPPQQNVQ PKKQELRAAS VVQPQPLVVV KEEKIHSPII RSEPFSPSLR PEPPKHPESI
KAPVHLPQRP EMKPVDVGRP VIRPPEQNAP PPGAPDKDKQ KQEPKTPVAP KKDLKIKNMG
SWASLVQKHP TTPSSTAKSS SDSFEQFRRA AREKEEREKA LKAQAEHAEK EKERLRQERM
RSREDEDALE QARRAHEEAR RRQEQQQQQR QEQQQQQQQQ AAAVAAAATP QAQSSQPQSM
LDQQRELARK REQERRRREA MAATIDMNFQ SDLLSIFEEN LF
