ID RPOB_ECOLI Reviewed; 1342 AA. AC P0A8V2; P00575; P00576; P78242; Q2M8S3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 1. DT 27-MAR-2024, entry version 170. DE RecName: Full=DNA-directed RNA polymerase subunit beta; DE Short=RNAP subunit beta; DE EC=2.7.7.6; DE AltName: Full=RNA polymerase subunit beta; DE AltName: Full=Transcriptase subunit beta; GN Name=rpoB; Synonyms=groN, nitB, rif, ron, stl, stv, tabD; GN OrderedLocusNames=b3987, JW3950; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6266829; DOI=10.1111/j.1432-1033.1981.tb05381.x; RA Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Guryev S.O., RA Chertov O.Y., Modyanov N.N., Grinkevich V.A., Makarova I.A., RA Marchenko T.V., Polovnikova I.N., Lipkin V.M., Sverdlov E.D.; RT "The primary structure of Escherichia coli RNA polymerase. Nucleotide RT sequence of the rpoB gene and amino-acid sequence of the beta-subunit."; RL Eur. J. Biochem. 116:621-629(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B; RA Miller E.S., Shih G.C., Chung S.K., Ballard D.N.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8265357; DOI=10.1093/nar/21.23.5408; RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region RT from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-391. RX PubMed=7011900; DOI=10.1016/0378-1119(80)90076-1; RA Delcuve G., Downing W., Lewis H., Dennis P.P.; RT "Nucleotide sequence of the proximal portion of the RNA polymerase beta RT subunit gene of Escherichia coli."; RL Gene 11:367-373(1980). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188. RA Gurevich A.I., Avakov A.E., Kolosov M.N.; RT "The nucleotide sequence at the proximal end of rpoB gene of Escherichia RT coli."; RL Bioorg. Khim. 5:1735-1739(1979). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188. RA Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Lipkin V.M., Sverdlov E.D.; RT "Primary structure of RNA polymerase from E.coli: nucleotide sequence of RT the rpoB gene fragment and corresponding N-terminal amino acid sequence of RT the beta-subunit."; RL Bioorg. Khim. 6:1423-1426(1980). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. RX PubMed=377281; DOI=10.1073/pnas.76.4.1697; RA Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.; RT "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the RT gene for RNA polymerase subunit beta in Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979). RN [10] RP PROTEIN SEQUENCE OF 1-4. RC STRAIN=K12; RX PubMed=1095419; DOI=10.1016/0014-5793(75)81001-5; RA Fujiki H., Zurek G.; RT "The subunits of DNA-dependent RNA polymerase from E. coli: I. Amino acid RT analysis and primary structure of the N-terminal regions."; RL FEBS Lett. 55:242-244(1975). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-1144. RA Ovchinnikov Y.A., Sverdlov E.D., Lipkin V.M., Monastyrskaya G.S., RA Chertov O.Y., Gubanov V.V., Guryev S.O., Modyanov N.N., Grinkevich V.A., RA Makarova I.A., Marchenko T.V., Polovnikova I.N.; RT "Primary structure of RNA polymerase from E. coli; nucleotide sequence of RT EcoR1-C fragment of gene rpoB and amino acid sequence of the corresponding RT fragment of beta-subunit."; RL Bioorg. Khim. 6:655-665(1980). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-354. RA Sverdlov E.D., Lipkin V.M., Monastyrskaya G.S., Gubanov V.V., Guryev S.O., RA Chertov O.Y.; RT "The nucleotide sequence of strong RNA polymerase binding site within the RT E.coli rpoB structural gene."; RL Bioorg. Khim. 6:309-312(1980). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-669. RC STRAIN=ATCC 25290; RA Mollet C., Drancourt M., Raoult D.; RT "RNA polymerase beta-subunit."; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1143-1342. RA Gurevich A.I., Igoshin A.V., Kolosov M.N.; RT "Structure of a central part of E.coli operon rpoBC. Nucleotide sequence of RT the gene for beta subunit of RNA polymerase."; RL Bioorg. Khim. 6:1580-1584(1980). RN [15] RP FUNCTION IN TRANSCRIPTION, AND SUBUNIT. RX PubMed=1646077; DOI=10.1016/0092-8674(91)90553-b; RA Igarashi K., Ishihama A.; RT "Bipartite functional map of the E. coli RNA polymerase alpha subunit: RT involvement of the C-terminal region in transcription activation by cAMP- RT CRP."; RL Cell 65:1015-1022(1991). RN [16] RP MUTAGENESIS OF GLU-813. RX PubMed=2068078; DOI=10.1073/pnas.88.14.6018; RA Lee J., Kashlev M., Borukhov S., Goldfarb A.; RT "A beta subunit mutation disrupting the catalytic function of Escherichia RT coli RNA polymerase."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6018-6022(1991). RN [17] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [18] RP INTERACTION WITH ESCHERICHIA PHAGE LAMBDA ANTITERMINATION PROTEIN Q RP (MICROBIAL INFECTION). RX PubMed=18832144; DOI=10.1073/pnas.0805757105; RA Deighan P., Diez C.M., Leibman M., Hochschild A., Nickels B.E.; RT "The bacteriophage lambda Q antiterminator protein contacts the beta-flap RT domain of RNA polymerase."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15305-15310(2008). RN [19] RP INTERACTION WITH ESCHERICHIA PHAGE LAMBDA ANTITERMINATION PROTEIN Q RP (MICROBIAL INFECTION). RX PubMed=32313022; DOI=10.1038/s41598-020-63523-5; RA Dudenhoeffer B.R., Borggraefe J., Schweimer K., Knauer S.H.; RT "NusA directly interacts with antitermination factor Q from phage lambda."; RL Sci. Rep. 10:6607-6607(2020). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1022 AND LYS-1200, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [21] RP ACETYLATION. RX PubMed=21696463; DOI=10.1111/j.1365-2958.2011.07742.x; RA Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R., RA Wolfe A.J.; RT "Involvement of protein acetylation in glucose-induced transcription of a RT stress-responsive promoter."; RL Mol. Microbiol. 81:1190-1204(2011). RN [22] RP INTERACTION WITH CEDA. RX PubMed=28818726; DOI=10.1016/j.ijbiomac.2017.08.073; RA Sharma P., Tomar A.K., Kundu B.; RT "Identification of functional interactome of a key cell division regulatory RT protein CedA of E.coli."; RL Int. J. Biol. Macromol. 106:763-767(2018). RN [23] {ECO:0007744|PDB:3IYD} RP STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOA; RP RPOC; RPOD; RPOZ; CRP AND DNA, DNA-BINDING, AND SUBUNIT. RX PubMed=19903881; DOI=10.1073/pnas.0908782106; RA Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E., RA Ebright R.H., Lawson C.L.; RT "Three-dimensional EM structure of an intact activator-dependent RT transcription initiation complex."; RL Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009). RN [24] {ECO:0007744|PDB:3TBI} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 831-1057, AND INTERACTION WITH RP ENTEROBACTERIA PHAGE T4 RNA POLYMERASE COACTIVATOR (MICROBIAL INFECTION). RX PubMed=22135460; DOI=10.1073/pnas.1113328108; RA Twist K.A., Campbell E.A., Deighan P., Nechaev S., Jain V., RA Geiduschek E.P., Hochschild A., Darst S.A.; RT "Crystal structure of the bacteriophage T4 late-transcription coactivator RT gp33 with the beta-subunit flap domain of Escherichia coli RNA RT polymerase."; RL Proc. Natl. Acad. Sci. U.S.A. 108:19961-19966(2011). RN [25] {ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY} RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) IN COMPLEX WITH RPOA; RPOC; RPOD; RP RPOZ AND SALINAMIDE A, FUNCTION, SUBUNIT, BIOTECHNOLOGY, ANTIBIOTIC RP RESISTANCE, AND MUTAGENESIS OF ILE-561; ILE-569; ALA-665; ASP-675; ASN-677 RP AND LEU-680. RX PubMed=24843001; DOI=10.7554/elife.02451; RA Degen D., Feng Y., Zhang Y., Ebright K.Y., Ebright Y.W., Gigliotti M., RA Vahedian-Movahed H., Mandal S., Talaue M., Connell N., Arnold E., RA Fenical W., Ebright R.H.; RT "Transcription inhibition by the depsipeptide antibiotic salinamide A."; RL Elife 3:e02451-e02451(2014). RN [26] {ECO:0007744|PDB:6TQN, ECO:0007744|PDB:6TQO} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RRNA RP TRANSCRIPTION-ELONGATION-ANTITERMINATION COMPLEXES WITH AND WITHOUT S4, RP FUNCTION, AND SUBUNIT. RX PubMed=32871103; DOI=10.1016/j.molcel.2020.08.010; RA Huang Y.H., Hilal T., Loll B., Buerger J., Mielke T., Boettcher C., RA Said N., Wahl M.C.; RT "Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine RT Required for Ribosome Biosynthesis."; RL Mol. Cell 0:0-0(2020). CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the CC transcription of DNA into RNA using the four ribonucleoside CC triphosphates as substrates. {ECO:0000269|PubMed:1646077, CC ECO:0000269|PubMed:24843001}. CC -!- FUNCTION: Resistance to the antibiotics salinamide A, salinamide B, CC rifampicin, streptolydigin, CBR703, myxopyronin, and lipiarmycin can CC result from mutations in this protein. {ECO:0000269|PubMed:24843001, CC ECO:0000305|PubMed:24843001}. CC -!- FUNCTION: Part of the processive rRNA transcription and antitermination CC complex (rrnTAC). The complex forms an RNA-chaperone ring around the CC RNA exit tunnel of RNAP. It supports rapid transcription and CC antitermination of rRNA operons, cotranscriptional rRNA folding, and CC annealing of distal rRNA regions to allow correct ribosome biogenesis. CC {ECO:0000269|PubMed:32871103}. CC -!- CATALYTIC ACTIVITY: 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=2.7.7.6; CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' CC and 1 omega subunit. When a sigma factor is associated with the core CC the holoenzyme is formed, which can initiate transcription. The rRNA CC transcription and antitermination complex (rrnTAC) consists of RNAP, CC NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and CC precursor rRNA; S4 is more flexible than other subunits CC (PubMed:32871103). In pull-down experiments interacts with CedA CC (PubMed:28818726). {ECO:0000269|PubMed:1646077, CC ECO:0000269|PubMed:19903881, ECO:0000269|PubMed:24843001, CC ECO:0000269|PubMed:28818726, ECO:0000269|PubMed:32871103}. CC -!- SUBUNIT: (Microbial infection) Interacts (via flap domain) with CC Escherichia phage lambda antitermination protein Q; this interaction CC renders bacterial RNAP resistant to transcription pausing and allows it CC to read through termination signals. {ECO:0000269|PubMed:18832144, CC ECO:0000269|PubMed:32313022}. CC -!- SUBUNIT: (Microbial infection) Interacts (via flap domain) with the CC late transcription coactivator of enterobacteria phage T4. CC {ECO:0000269|PubMed:22135460}. CC -!- INTERACTION: CC P0A8V2; P60240: rapA; NbExp=5; IntAct=EBI-544996, EBI-551542; CC P0A8V2; P0A8T7: rpoC; NbExp=11; IntAct=EBI-544996, EBI-543604; CC P0A8V2; P00579: rpoD; NbExp=10; IntAct=EBI-544996, EBI-545104; CC P0A8V2; P13445: rpoS; NbExp=5; IntAct=EBI-544996, EBI-557581; CC P0A8V2; P03018: uvrD; NbExp=3; IntAct=EBI-544996, EBI-559573; CC P0A8V2; P13338: 33; Xeno; NbExp=5; IntAct=EBI-544996, EBI-15955782; CC P0A8V2; P32267: asiA; Xeno; NbExp=4; IntAct=EBI-544996, EBI-2124737; CC -!- PTM: Acetylated on several lysine residues in the presence of glucose. CC {ECO:0000269|PubMed:18723842, ECO:0000269|PubMed:21696463}. CC -!- BIOTECHNOLOGY: Co-administration of salinamide and rifampicin or CC salinamide and myxopyronin suppresses the emergence of resistance to CC both antibiotics. {ECO:0000269|PubMed:24843001}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=Ref.7; Type=Miscellaneous discrepancy; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V00339; CAA23625.1; -; Genomic_DNA. DR EMBL; V00340; CAA23627.1; -; Genomic_DNA. DR EMBL; U76222; AAB18647.1; -; Genomic_DNA. DR EMBL; U00006; AAC43085.1; -; Genomic_DNA. DR EMBL; U00096; AAC76961.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77333.1; -; Genomic_DNA. DR EMBL; V00341; CAA23629.1; -; Genomic_DNA. DR EMBL; M38292; AAA24579.1; -; Genomic_DNA. DR EMBL; M38293; AAA24581.1; -; Genomic_DNA. DR EMBL; M38287; AAA24585.1; -; Genomic_DNA. DR EMBL; M38304; AAA24580.1; -; Genomic_DNA. DR EMBL; U77436; AAD09605.1; -; Genomic_DNA. DR EMBL; M38303; AAA24583.1; -; Genomic_DNA. DR PIR; F65205; RNECB. DR RefSeq; NP_418414.1; NC_000913.3. DR RefSeq; WP_000263098.1; NZ_STEB01000045.1. DR PDB; 3IYD; EM; -; C=1-1342. DR PDB; 3LTI; X-ray; 1.60 A; A=152-443. DR PDB; 3LU0; EM; -; C=1-1342. DR PDB; 3T72; X-ray; 4.33 A; o/q=896-910. DR PDB; 3TBI; X-ray; 3.00 A; B=831-1057. DR PDB; 4JK1; X-ray; 3.90 A; C/H=1-1342. DR PDB; 4JK2; X-ray; 4.20 A; C/H=1-1342. DR PDB; 4KMU; X-ray; 3.85 A; C/H=1-1342. DR PDB; 4KN4; X-ray; 3.96 A; C/H=1-1342. DR PDB; 4KN7; X-ray; 3.69 A; C/H=1-1342. DR PDB; 4MEX; X-ray; 3.90 A; C/I=1-1342. DR PDB; 4MEY; X-ray; 3.95 A; C/I=1-1342. DR PDB; 4S20; X-ray; 4.70 A; C/H=1-1342. DR PDB; 4XSX; X-ray; 3.71 A; C/I=1-1342. DR PDB; 4XSY; X-ray; 4.01 A; C/I=1-1342. DR PDB; 4XSZ; X-ray; 3.68 A; C/I=1-1342. DR PDB; 4YG2; X-ray; 3.70 A; C/I=1-1342. DR PDB; 4YLN; X-ray; 5.50 A; C/I/O=1-1342. DR PDB; 4YLO; X-ray; 6.00 A; C/I/O=1-1342. DR PDB; 4YLP; X-ray; 5.50 A; C/I/O=1-1342. DR PDB; 4ZH2; X-ray; 4.20 A; C/I=1-1342. DR PDB; 4ZH3; X-ray; 4.08 A; C/I=1-1342. DR PDB; 4ZH4; X-ray; 3.99 A; C/I=1-1342. DR PDB; 5EZK; X-ray; 8.50 A; C=1-1342. DR PDB; 5IPL; X-ray; 3.60 A; C=1-1342. DR PDB; 5IPM; X-ray; 4.20 A; C=1-1342. DR PDB; 5IPN; X-ray; 4.61 A; C=1-1342. DR PDB; 5MS0; EM; 9.80 A; C=1-1342. DR PDB; 5MY1; EM; 7.60 A; X=1-1342. DR PDB; 5NSR; EM; 3.80 A; C=1-1342. DR PDB; 5NSS; EM; 5.80 A; C=1-1342. DR PDB; 5NWT; X-ray; 3.76 A; C=1-1342. DR PDB; 5TBZ; X-ray; 7.00 A; C/H=1-1342. DR PDB; 5UAC; X-ray; 3.80 A; C/I=1-1342. DR PDB; 5UAG; X-ray; 3.40 A; C/I=1-1342. DR PDB; 5UAH; X-ray; 4.10 A; C/I=1-1342. DR PDB; 5UAJ; X-ray; 3.92 A; C/I=1-1342. DR PDB; 5UAL; X-ray; 3.89 A; C/I=1-1342. DR PDB; 5UAQ; X-ray; 3.60 A; C/I=1-1342. DR PDB; 5UI8; X-ray; 3.76 A; I=1-1342. DR PDB; 5VSW; X-ray; 4.29 A; C/I=1-1342. DR PDB; 5VT0; EM; 3.78 A; I=1-1342. DR PDB; 5W1S; X-ray; 3.81 A; C/I=1-1342. DR PDB; 5W1T; X-ray; 4.50 A; C/I=1-1342. DR PDB; 6ALF; EM; 4.10 A; I=1-1342. DR PDB; 6ALG; EM; 3.70 A; I=1-1342. DR PDB; 6ALH; EM; 4.40 A; I=1-1342. DR PDB; 6ASX; EM; 3.80 A; I=1-1342. DR PDB; 6AWB; EM; 6.70 A; 03=2-1341. DR PDB; 6AWC; EM; 7.90 A; 03=2-1341. DR PDB; 6AWD; EM; 8.10 A; 03=2-1341. DR PDB; 6B6H; EM; 3.90 A; C=1-1342. DR PDB; 6BJS; EM; 5.50 A; I=1-1342. DR PDB; 6BYU; X-ray; 3.60 A; C/I=1-1342. DR PDB; 6C6S; EM; 3.70 A; I=1-1342. DR PDB; 6C6T; EM; 3.50 A; I=1-1342. DR PDB; 6C6U; EM; 3.70 A; I=1-1342. DR PDB; 6C9Y; EM; 4.25 A; C=1-1342. DR PDB; 6CA0; EM; 5.75 A; C=1-1342. DR PDB; 6CUX; X-ray; 4.10 A; C/I=1-1342. DR PDB; 6FLP; EM; 4.10 A; C=1-1342. DR PDB; 6FLQ; EM; 4.10 A; C=1-1342. DR PDB; 6GFW; EM; 3.70 A; C=1-1342. DR PDB; 6GH5; EM; 3.40 A; C=1-1342. DR PDB; 6GH6; EM; 4.10 A; C=1-1342. DR PDB; 6GOV; EM; 3.70 A; X=1-1342. DR PDB; 6JBQ; EM; 4.02 A; C=1-1342. DR PDB; 6JNX; EM; 4.08 A; C=1-1342. DR PDB; 6K4Y; EM; 3.79 A; C=1-1342. DR PDB; 6KJ6; EM; 3.80 A; C=1-1342. DR PDB; 6LDI; EM; 3.69 A; C=1-1342. DR PDB; 6N4C; EM; 17.00 A; C=2-1342. DR PDB; 6N57; EM; 3.70 A; I=1-1342. DR PDB; 6N58; EM; 3.78 A; I=1-1342. DR PDB; 6N60; X-ray; 3.68 A; C=1-1342. DR PDB; 6N61; X-ray; 3.25 A; C=1-1342. DR PDB; 6N62; X-ray; 3.80 A; C=1-1342. DR PDB; 6OMF; EM; 3.26 A; C=1-1342. DR PDB; 6OUL; EM; 3.40 A; I=1-1342. DR PDB; 6P18; EM; 3.50 A; C=1-1342. DR PDB; 6P19; EM; 3.80 A; C=1-1342. DR PDB; 6P1K; EM; 4.05 A; I=1-1342. DR PDB; 6PB4; EM; 4.35 A; C=1-1342. DR PDB; 6PB5; EM; 4.52 A; C=1-1342. DR PDB; 6PB6; EM; 4.29 A; C=1-1342. DR PDB; 6PMI; EM; 3.86 A; C=1-1342. DR PDB; 6PMJ; EM; 3.91 A; C=1-1342. DR PDB; 6PSQ; EM; 3.40 A; I=1-1342. DR PDB; 6PSR; EM; 3.40 A; I=1-1342. DR PDB; 6PSS; EM; 3.50 A; I=1-1342. DR PDB; 6PST; EM; 3.00 A; I=1-1342. DR PDB; 6PSU; EM; 3.90 A; I=1-1342. DR PDB; 6PSV; EM; 3.50 A; I=1-1342. DR PDB; 6PSW; EM; 3.70 A; I=1-1342. DR PDB; 6R9B; EM; 3.80 A; C=1-1342. DR PDB; 6R9G; EM; 3.70 A; C=1-1342. DR PDB; 6RH3; EM; 3.60 A; C=1-1342. DR PDB; 6RI7; EM; 3.90 A; C=1-1342. DR PDB; 6RI9; EM; 3.70 A; C=1-1342. DR PDB; 6RIN; EM; 3.70 A; C=1-1342. DR PDB; 6RIP; EM; 3.40 A; C=1-1342. DR PDB; 6TQN; EM; 3.80 A; X=1-1342. DR PDB; 6TQO; EM; 4.00 A; X=1-1342. DR PDB; 6UTV; X-ray; 3.45 A; CCC=1-1342. DR PDB; 6UTW; X-ray; 3.85 A; CCC=1-1342. DR PDB; 6UTX; X-ray; 4.05 A; CCC=1-1342. DR PDB; 6UTY; X-ray; 4.15 A; CCC=1-1342. DR PDB; 6UTZ; X-ray; 3.80 A; CCC=1-1342. DR PDB; 6UU0; X-ray; 3.90 A; CCC=1-1342. DR PDB; 6UU1; X-ray; 4.10 A; CCC=1-1342. DR PDB; 6UU2; X-ray; 4.40 A; CCC=1-1342. DR PDB; 6UU3; X-ray; 4.00 A; CCC=1-1342. DR PDB; 6UU4; X-ray; 4.30 A; CCC=1-1342. DR PDB; 6UU5; X-ray; 5.40 A; CCC=1-1342. DR PDB; 6UU6; X-ray; 4.20 A; CCC=1-1342. DR PDB; 6UU7; X-ray; 4.40 A; CCC=1-1342. DR PDB; 6UU8; X-ray; 4.40 A; CCC=1-1342. DR PDB; 6UU9; X-ray; 5.40 A; CCC=1-1342. DR PDB; 6UUA; X-ray; 4.00 A; CCC=1-1342. DR PDB; 6UUB; X-ray; 3.96 A; CCC=1-1342. DR PDB; 6UUC; X-ray; 4.10 A; CCC=1-1342. DR PDB; 6VJS; X-ray; 4.02 A; C/H=1-1342. DR PDB; 6VU3; EM; 3.70 A; AA=1-1342. DR PDB; 6VYQ; EM; 3.70 A; AA=2-1342. DR PDB; 6VYR; EM; 3.80 A; AA=1-1342. DR PDB; 6VYS; EM; 3.70 A; AA=1-1342. DR PDB; 6VYT; EM; 14.00 A; AA=1-1342. DR PDB; 6VYU; EM; 7.00 A; AA=1-1342. DR PDB; 6VYW; EM; 7.00 A; AA=1-1342. DR PDB; 6VYX; EM; 9.90 A; AA=1-1342. DR PDB; 6VYY; EM; 9.90 A; AA=1-1342. DR PDB; 6VYZ; EM; 9.90 A; AA=1-1342. DR PDB; 6VZ2; EM; 10.00 A; AA=1-1342. DR PDB; 6VZ3; EM; 8.90 A; AA=1-1342. DR PDB; 6VZ5; EM; 8.90 A; AA=1-1342. DR PDB; 6VZ7; EM; 7.00 A; AA=2-1342. DR PDB; 6VZJ; EM; 4.10 A; AA=1-1342. DR PDB; 6WMU; EM; 3.18 A; C=1-1342. DR PDB; 6X26; EM; 4.10 A; I=1-1342. DR PDB; 6X2F; EM; 4.00 A; I=1-1342. DR PDB; 6X2N; EM; 3.90 A; I=1-1342. DR PDB; 6X43; EM; 3.60 A; I=1-1342. DR PDB; 6X4W; EM; 3.80 A; I=1-1342. DR PDB; 6X4Y; EM; 3.60 A; I=1-1342. DR PDB; 6X50; EM; 3.30 A; I=1-1342. DR PDB; 6X6T; EM; 3.20 A; AA=1-1342. DR PDB; 6X7F; EM; 3.50 A; AA=1-1342. DR PDB; 6X7K; EM; 3.10 A; AA=1-1342. DR PDB; 6X9Q; EM; 4.80 A; AA=1-1342. DR PDB; 6XAS; EM; 3.80 A; I=1-1342. DR PDB; 6XAV; EM; 7.70 A; I=1-1342. DR PDB; 6XDQ; EM; 3.70 A; AA=1-1342. DR PDB; 6XDR; EM; 4.70 A; AA=1-1342. DR PDB; 6XGF; EM; 5.00 A; AA=1-1342. DR PDB; 6XH7; EM; 3.90 A; C=1-1342. DR PDB; 6XH8; EM; 4.10 A; C=1-1342. DR PDB; 6XII; EM; 7.00 A; AA=1-1342. DR PDB; 6XIJ; EM; 8.00 A; AA=1-1342. DR PDB; 6XL5; EM; 2.50 A; C=1-1342. DR PDB; 6XL9; EM; 2.50 A; C=1-1342. DR PDB; 6XLJ; EM; 2.70 A; C=1-1342. DR PDB; 6XLL; EM; 2.70 A; C=1-1342. DR PDB; 6XLM; EM; 3.20 A; C=1-1342. DR PDB; 6XLN; EM; 2.80 A; C=1-1342. DR PDB; 6Z9P; EM; 3.90 A; X=1-1342. DR PDB; 6Z9Q; EM; 5.70 A; X=1-1342. DR PDB; 6Z9R; EM; 4.10 A; X=1-1342. DR PDB; 6Z9S; EM; 4.40 A; X=1-1342. DR PDB; 6Z9T; EM; 4.10 A; X=1-1342. DR PDB; 6ZTJ; EM; 3.40 A; CC=1-1342. DR PDB; 6ZTL; EM; 3.50 A; CC=1-1342. DR PDB; 6ZTM; EM; 3.30 A; CC=1-1342. DR PDB; 6ZTN; EM; 3.90 A; CC=1-1342. DR PDB; 6ZTO; EM; 3.00 A; CC=1-1342. DR PDB; 6ZTP; EM; 3.00 A; CC=1-1342. DR PDB; 6ZU1; EM; 3.00 A; CC=1-1342. DR PDB; 7ADB; EM; 4.40 A; X=1-1342. DR PDB; 7ADC; EM; 4.00 A; X=1-1342. DR PDB; 7ADD; EM; 4.30 A; X=1-1342. DR PDB; 7ADE; EM; 4.20 A; X=1-1342. DR PDB; 7BEF; EM; 4.50 A; C=1-1342. DR PDB; 7BEG; EM; 4.20 A; C=1-1342. DR PDB; 7C17; EM; 4.22 A; C=1-1342. DR PDB; 7C97; EM; 3.68 A; C=1-1342. DR PDB; 7CHW; EM; 3.58 A; C=1-1342. DR PDB; 7DY6; EM; 3.68 A; C=1-1342. DR PDB; 7EGS; X-ray; 1.70 A; A=152-443. DR PDB; 7KHB; EM; 3.53 A; C=1-1342. DR PDB; 7KHC; EM; 4.14 A; C=1-1342. DR PDB; 7KHE; EM; 3.58 A; C=1-1342. DR PDB; 7KHI; EM; 3.62 A; C=1-1342. DR PDB; 7M8E; EM; 3.40 A; C=1-1342. DR PDB; 7MKD; EM; 3.20 A; I=1-1342. DR PDB; 7MKE; EM; 3.70 A; I=1-1342. DR PDB; 7MKI; EM; 3.50 A; I=1-1342. DR PDB; 7MKJ; EM; 2.90 A; I=1-1342. DR PDB; 7MKN; EM; 3.30 A; C=3-1342. DR PDB; 7MKO; EM; 3.15 A; C=3-1342. DR PDB; 7MKP; EM; 3.41 A; C=3-1342. DR PDB; 7MKQ; EM; 4.80 A; C=3-1342. DR PDB; 7N4E; EM; 3.80 A; C=1-1342. DR PDB; 7PY0; EM; 4.50 A; C=1-1342. DR PDB; 7PY1; EM; 3.80 A; C=1-1342. DR PDB; 7PY3; EM; 3.80 A; C=1-1342. DR PDB; 7PY5; EM; 3.90 A; C=1-1342. DR PDB; 7PY6; EM; 4.10 A; C=1-1342. DR PDB; 7PY7; EM; 4.10 A; C=1-1342. DR PDB; 7PY8; EM; 3.80 A; C=1-1342. DR PDB; 7PYJ; EM; 4.20 A; C=1-1342. DR PDB; 7PYK; EM; 4.10 A; C=1-1342. DR PDB; 7Q0J; EM; 4.30 A; C=1-1342. DR PDB; 7Q0K; EM; 4.00 A; C=1-1342. DR PDB; 7QV9; EM; 3.50 A; C=1-1342. DR PDB; 7QWP; EM; 3.40 A; C=1-1342. DR PDB; 7QXI; EM; 3.40 A; C=1-1342. DR PDB; 7SZJ; EM; 3.11 A; C=1-1342. DR PDB; 7SZK; EM; 2.94 A; C=1-1342. DR PDB; 7UBM; EM; 3.13 A; C=1-1342. DR PDB; 7UBN; EM; 3.36 A; C=1-1342. DR PDB; 7UWE; EM; 2.90 A; I=1-1342. DR PDB; 7UWH; EM; 3.10 A; I=1-1342. DR PDB; 7VWY; EM; 4.57 A; C=1-1342. DR PDB; 7VWZ; EM; 4.00 A; C=1-1342. DR PDB; 7W5W; EM; 4.55 A; C=1-1342. DR PDB; 7W5X; EM; 3.40 A; C=1-1342. DR PDB; 7W5Y; EM; 4.20 A; C=1-1342. DR PDB; 7XUE; EM; 3.17 A; I=1-1342. DR PDB; 7XUG; EM; 3.57 A; I=1-1342. DR PDB; 7XUI; EM; 3.61 A; I=1-1342. DR PDB; 7YP9; EM; 3.58 A; C=1-1342. DR PDB; 7YPA; EM; 3.05 A; C=1-1342. DR PDB; 7YPB; EM; 3.48 A; C=1-1342. DR PDB; 8ABY; EM; 3.70 A; C=1-1342. DR PDB; 8ABZ; EM; 3.40 A; C=1-1342. DR PDB; 8AC0; EM; 4.10 A; C=1-1342. DR PDB; 8AC1; EM; 4.06 A; C=1-1342. DR PDB; 8AC2; EM; 3.70 A; C=1-1342. DR PDB; 8ACP; EM; 4.50 A; C=1-1342. DR PDB; 8AD1; EM; 4.10 A; C=1-1342. DR PDB; 8E3F; EM; 6.50 A; A=1-1342. DR PDB; 8E5K; EM; 4.20 A; A=1-1342. DR PDB; 8E5O; EM; 4.40 A; A=1-1342. DR PDB; 8E6X; EM; 4.27 A; A=1-1342. DR PDB; 8E6Z; EM; 4.10 A; A=1-1342. DR PDB; 8EG7; EM; 3.20 A; I=1-1342. DR PDB; 8EG8; EM; 3.30 A; I=1-1342. DR PDB; 8EGB; EM; 3.80 A; I=1-1342. DR PDB; 8EH8; EM; 3.40 A; I=1-1342. DR PDB; 8EH9; EM; 3.90 A; I=1-1342. DR PDB; 8EHA; EM; 3.70 A; I=1-1342. DR PDB; 8EHF; EM; 3.30 A; I=1-1342. DR PDB; 8EHI; EM; 5.50 A; I=1-1342. DR PDB; 8F1I; EM; 3.00 A; I=1-1342. DR PDB; 8F1J; EM; 2.60 A; I=1-1342. DR PDB; 8F1K; EM; 2.80 A; I=1-1342. DR PDB; 8F3C; EM; 3.40 A; I=1-1342. DR PDB; 8FIX; EM; 3.90 A; C=1-1342. DR PDB; 8FIY; EM; 7.30 A; C=1-1342. DR PDB; 8FVR; EM; 2.42 A; F=1-1342. DR PDB; 8FVW; EM; 2.10 A; F=1-1342. DR PDB; 8G00; EM; 3.40 A; I=1-1342. DR PDB; 8G1S; EM; 3.70 A; I=1-1342. DR PDB; 8G7E; EM; 3.90 A; I=1-1341. DR PDB; 8HKC; EM; 2.49 A; C=2-1342. DR PDB; 8IGR; EM; 3.10 A; I=1-1342. DR PDB; 8IGS; EM; 3.40 A; I=1-1342. DR PDBsum; 3IYD; -. DR PDBsum; 3LTI; -. DR PDBsum; 3LU0; -. DR PDBsum; 3T72; -. DR PDBsum; 3TBI; -. DR PDBsum; 4JK1; -. DR PDBsum; 4JK2; -. DR PDBsum; 4KMU; -. DR PDBsum; 4KN4; -. DR PDBsum; 4KN7; -. DR PDBsum; 4MEX; -. DR PDBsum; 4MEY; -. DR PDBsum; 4S20; -. DR PDBsum; 4XSX; -. DR PDBsum; 4XSY; -. DR PDBsum; 4XSZ; -. DR PDBsum; 4YG2; -. DR PDBsum; 4YLN; -. DR PDBsum; 4YLO; -. DR PDBsum; 4YLP; -. DR PDBsum; 4ZH2; -. DR PDBsum; 4ZH3; -. DR PDBsum; 4ZH4; -. DR PDBsum; 5EZK; -. DR PDBsum; 5IPL; -. DR PDBsum; 5IPM; -. DR PDBsum; 5IPN; -. DR PDBsum; 5MS0; -. DR PDBsum; 5MY1; -. DR PDBsum; 5NSR; -. DR PDBsum; 5NSS; -. DR PDBsum; 5NWT; -. DR PDBsum; 5TBZ; -. DR PDBsum; 5UAC; -. DR PDBsum; 5UAG; -. DR PDBsum; 5UAH; -. DR PDBsum; 5UAJ; -. DR PDBsum; 5UAL; -. DR PDBsum; 5UAQ; -. DR PDBsum; 5UI8; -. DR PDBsum; 5VSW; -. DR PDBsum; 5VT0; -. DR PDBsum; 5W1S; -. DR PDBsum; 5W1T; -. DR PDBsum; 6ALF; -. DR PDBsum; 6ALG; -. DR PDBsum; 6ALH; -. DR PDBsum; 6ASX; -. DR PDBsum; 6AWB; -. DR PDBsum; 6AWC; -. DR PDBsum; 6AWD; -. DR PDBsum; 6B6H; -. DR PDBsum; 6BJS; -. DR PDBsum; 6BYU; -. DR PDBsum; 6C6S; -. DR PDBsum; 6C6T; -. DR PDBsum; 6C6U; -. DR PDBsum; 6C9Y; -. DR PDBsum; 6CA0; -. DR PDBsum; 6CUX; -. DR PDBsum; 6FLP; -. DR PDBsum; 6FLQ; -. DR PDBsum; 6GFW; -. DR PDBsum; 6GH5; -. DR PDBsum; 6GH6; -. DR PDBsum; 6GOV; -. DR PDBsum; 6JBQ; -. DR PDBsum; 6JNX; -. DR PDBsum; 6K4Y; -. DR PDBsum; 6KJ6; -. DR PDBsum; 6LDI; -. DR PDBsum; 6N4C; -. DR PDBsum; 6N57; -. DR PDBsum; 6N58; -. DR PDBsum; 6N60; -. DR PDBsum; 6N61; -. DR PDBsum; 6N62; -. DR PDBsum; 6OMF; -. DR PDBsum; 6OUL; -. DR PDBsum; 6P18; -. DR PDBsum; 6P19; -. DR PDBsum; 6P1K; -. DR PDBsum; 6PB4; -. DR PDBsum; 6PB5; -. DR PDBsum; 6PB6; -. DR PDBsum; 6PMI; -. DR PDBsum; 6PMJ; -. DR PDBsum; 6PSQ; -. DR PDBsum; 6PSR; -. DR PDBsum; 6PSS; -. DR PDBsum; 6PST; -. DR PDBsum; 6PSU; -. DR PDBsum; 6PSV; -. DR PDBsum; 6PSW; -. DR PDBsum; 6R9B; -. DR PDBsum; 6R9G; -. DR PDBsum; 6RH3; -. DR PDBsum; 6RI7; -. DR PDBsum; 6RI9; -. DR PDBsum; 6RIN; -. DR PDBsum; 6RIP; -. DR PDBsum; 6TQN; -. DR PDBsum; 6TQO; -. DR PDBsum; 6UTV; -. DR PDBsum; 6UTW; -. DR PDBsum; 6UTX; -. DR PDBsum; 6UTY; -. DR PDBsum; 6UTZ; -. DR PDBsum; 6UU0; -. DR PDBsum; 6UU1; -. DR PDBsum; 6UU2; -. DR PDBsum; 6UU3; -. DR PDBsum; 6UU4; -. DR PDBsum; 6UU5; -. DR PDBsum; 6UU6; -. DR PDBsum; 6UU7; -. DR PDBsum; 6UU8; -. DR PDBsum; 6UU9; -. DR PDBsum; 6UUA; -. DR PDBsum; 6UUB; -. DR PDBsum; 6UUC; -. DR PDBsum; 6VJS; -. DR PDBsum; 6VU3; -. DR PDBsum; 6VYQ; -. DR PDBsum; 6VYR; -. DR PDBsum; 6VYS; -. DR PDBsum; 6VYT; -. DR PDBsum; 6VYU; -. DR PDBsum; 6VYW; -. DR PDBsum; 6VYX; -. DR PDBsum; 6VYY; -. DR PDBsum; 6VYZ; -. DR PDBsum; 6VZ2; -. DR PDBsum; 6VZ3; -. DR PDBsum; 6VZ5; -. DR PDBsum; 6VZ7; -. DR PDBsum; 6VZJ; -. DR PDBsum; 6WMU; -. DR PDBsum; 6X26; -. DR PDBsum; 6X2F; -. DR PDBsum; 6X2N; -. DR PDBsum; 6X43; -. DR PDBsum; 6X4W; -. DR PDBsum; 6X4Y; -. DR PDBsum; 6X50; -. DR PDBsum; 6X6T; -. DR PDBsum; 6X7F; -. DR PDBsum; 6X7K; -. DR PDBsum; 6X9Q; -. DR PDBsum; 6XAS; -. DR PDBsum; 6XAV; -. DR PDBsum; 6XDQ; -. DR PDBsum; 6XDR; -. DR PDBsum; 6XGF; -. DR PDBsum; 6XH7; -. DR PDBsum; 6XH8; -. DR PDBsum; 6XII; -. DR PDBsum; 6XIJ; -. DR PDBsum; 6XL5; -. DR PDBsum; 6XL9; -. DR PDBsum; 6XLJ; -. DR PDBsum; 6XLL; -. DR PDBsum; 6XLM; -. DR PDBsum; 6XLN; -. DR PDBsum; 6Z9P; -. DR PDBsum; 6Z9Q; -. DR PDBsum; 6Z9R; -. DR PDBsum; 6Z9S; -. DR PDBsum; 6Z9T; -. DR PDBsum; 6ZTJ; -. DR PDBsum; 6ZTL; -. DR PDBsum; 6ZTM; -. DR PDBsum; 6ZTN; -. DR PDBsum; 6ZTO; -. DR PDBsum; 6ZTP; -. DR PDBsum; 6ZU1; -. DR PDBsum; 7ADB; -. DR PDBsum; 7ADC; -. DR PDBsum; 7ADD; -. DR PDBsum; 7ADE; -. DR PDBsum; 7BEF; -. DR PDBsum; 7BEG; -. DR PDBsum; 7C17; -. DR PDBsum; 7C97; -. DR PDBsum; 7CHW; -. DR PDBsum; 7DY6; -. DR PDBsum; 7EGS; -. DR PDBsum; 7KHB; -. DR PDBsum; 7KHC; -. DR PDBsum; 7KHE; -. DR PDBsum; 7KHI; -. DR PDBsum; 7M8E; -. DR PDBsum; 7MKD; -. DR PDBsum; 7MKE; -. DR PDBsum; 7MKI; -. DR PDBsum; 7MKJ; -. DR PDBsum; 7MKN; -. DR PDBsum; 7MKO; -. DR PDBsum; 7MKP; -. DR PDBsum; 7MKQ; -. DR PDBsum; 7N4E; -. DR PDBsum; 7PY0; -. DR PDBsum; 7PY1; -. DR PDBsum; 7PY3; -. DR PDBsum; 7PY5; -. DR PDBsum; 7PY6; -. DR PDBsum; 7PY7; -. DR PDBsum; 7PY8; -. DR PDBsum; 7PYJ; -. DR PDBsum; 7PYK; -. DR PDBsum; 7Q0J; -. DR PDBsum; 7Q0K; -. DR PDBsum; 7QV9; -. DR PDBsum; 7QWP; -. DR PDBsum; 7QXI; -. DR PDBsum; 7SZJ; -. DR PDBsum; 7SZK; -. DR PDBsum; 7UBM; -. DR PDBsum; 7UBN; -. DR PDBsum; 7UWE; -. DR PDBsum; 7UWH; -. DR PDBsum; 7VWY; -. DR PDBsum; 7VWZ; -. DR PDBsum; 7W5W; -. DR PDBsum; 7W5X; -. DR PDBsum; 7W5Y; -. DR PDBsum; 7XUE; -. DR PDBsum; 7XUG; -. DR PDBsum; 7XUI; -. DR PDBsum; 7YP9; -. DR PDBsum; 7YPA; -. DR PDBsum; 7YPB; -. DR PDBsum; 8ABY; -. DR PDBsum; 8ABZ; -. DR PDBsum; 8AC0; -. DR PDBsum; 8AC1; -. DR PDBsum; 8AC2; -. DR PDBsum; 8ACP; -. DR PDBsum; 8AD1; -. DR PDBsum; 8E3F; -. DR PDBsum; 8E5K; -. DR PDBsum; 8E5O; -. DR PDBsum; 8E6X; -. DR PDBsum; 8E6Z; -. DR PDBsum; 8EG7; -. DR PDBsum; 8EG8; -. DR PDBsum; 8EGB; -. DR PDBsum; 8EH8; -. DR PDBsum; 8EH9; -. DR PDBsum; 8EHA; -. DR PDBsum; 8EHF; -. DR PDBsum; 8EHI; -. DR PDBsum; 8F1I; -. DR PDBsum; 8F1J; -. DR PDBsum; 8F1K; -. DR PDBsum; 8F3C; -. DR PDBsum; 8FIX; -. DR PDBsum; 8FIY; -. DR PDBsum; 8FVR; -. DR PDBsum; 8FVW; -. DR PDBsum; 8G00; -. DR PDBsum; 8G1S; -. DR PDBsum; 8G7E; -. DR PDBsum; 8HKC; -. DR PDBsum; 8IGR; -. DR PDBsum; 8IGS; -. DR AlphaFoldDB; P0A8V2; -. DR EMDB; EMD-11419; -. DR EMDB; EMD-14172; -. DR EMDB; EMD-15327; -. DR EMDB; EMD-15328; -. DR EMDB; EMD-15329; -. DR EMDB; EMD-15330; -. DR EMDB; EMD-15331; -. DR EMDB; EMD-15352; -. DR EMDB; EMD-15357; -. DR EMDB; EMD-20203; -. DR EMDB; EMD-21879; -. DR EMDB; EMD-21881; -. DR EMDB; EMD-21883; -. DR EMDB; EMD-28845; -. DR EMDB; EMD-29212; -. DR EMDB; EMD-29213; -. DR EMDB; EMD-29491; -. DR EMDB; EMD-29494; -. DR EMDB; EMD-29640; -. DR EMDB; EMD-29676; -. DR EMDB; EMD-35438; -. DR EMDB; EMD-35439; -. DR EMDB; EMD-8584; -. DR EMDB; EMD-8586; -. DR SMR; P0A8V2; -. DR BioGRID; 4263472; 52. DR BioGRID; 852782; 2. DR ComplexPortal; CPX-4881; DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant. DR ComplexPortal; CPX-4883; DNA-directed RNA polymerase holoenzyme complex, SigmaS variant. DR ComplexPortal; CPX-4884; DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant. DR ComplexPortal; CPX-4885; DNA-directed RNA polymerase holoenzyme complex, SigmaE variant. DR ComplexPortal; CPX-4886; DNA-directed RNA polymerase holoenzyme complex, SigmaF variant. DR ComplexPortal; CPX-4887; DNA-directed RNA polymerase holoenzyme complex, SigmaH variant. DR ComplexPortal; CPX-4888; DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant. DR ComplexPortal; CPX-5674; Transcription elongation complex. DR ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex. DR DIP; DIP-35777N; -. DR IntAct; P0A8V2; 103. DR STRING; 511145.b3987; -. DR BindingDB; P0A8V2; -. DR ChEMBL; CHEMBL1852; -. DR DrugBank; DB00615; Rifabutin. DR DrugBank; DB04934; Rifalazil. DR DrugBank; DB01045; Rifampicin. DR DrugBank; DB11753; Rifamycin. DR DrugBank; DB01220; Rifaximin. DR DrugCentral; P0A8V2; -. DR CarbonylDB; P0A8V2; -. DR iPTMnet; P0A8V2; -. DR jPOST; P0A8V2; -. DR PaxDb; 511145-b3987; -. DR EnsemblBacteria; AAC76961; AAC76961; b3987. DR GeneID; 83578994; -. DR GeneID; 948488; -. DR KEGG; ecj:JW3950; -. DR KEGG; eco:b3987; -. DR PATRIC; fig|1411691.4.peg.2725; -. DR EchoBASE; EB0887; -. DR eggNOG; COG0085; Bacteria. DR HOGENOM; CLU_000524_4_3_6; -. DR InParanoid; P0A8V2; -. DR OMA; FMTWEGY; -. DR OrthoDB; 9803954at2; -. DR PhylomeDB; P0A8V2; -. DR BioCyc; EcoCyc:RPOB-MONOMER; -. DR BioCyc; MetaCyc:RPOB-MONOMER; -. DR BRENDA; 2.7.7.6; 2026. DR EvolutionaryTrace; P0A8V2; -. DR PRO; PR:P0A8V2; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0000345; C:cytosolic DNA-directed RNA polymerase complex; IPI:ComplexPortal. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0008023; C:transcription elongation factor complex; NAS:ComplexPortal. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0044780; P:bacterial-type flagellum assembly; NAS:ComplexPortal. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; NAS:ComplexPortal. DR GO; GO:0048870; P:cell motility; NAS:ComplexPortal. DR GO; GO:0036460; P:cellular response to cell envelope stress; NAS:ComplexPortal. DR GO; GO:0006352; P:DNA-templated transcription initiation; IDA:ComplexPortal. DR GO; GO:0006879; P:intracellular iron ion homeostasis; NAS:ComplexPortal. DR GO; GO:0042128; P:nitrate assimilation; NAS:ComplexPortal. DR GO; GO:0032784; P:regulation of DNA-templated transcription elongation; NAS:ComplexPortal. DR GO; GO:2000142; P:regulation of DNA-templated transcription initiation; IDA:ComplexPortal. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR GO; GO:0009408; P:response to heat; NAS:ComplexPortal. DR GO; GO:0090605; P:submerged biofilm formation; NAS:ComplexPortal. DR GO; GO:0031564; P:transcription antitermination; IDA:ComplexPortal. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.100; -; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1100.10; -; 2. DR Gene3D; 6.10.140.1670; -; 1. DR Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 1. DR HAMAP; MF_01321; RNApol_bact_RpoB; 1. DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf. DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom. DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf. DR InterPro; IPR010243; RNA_pol_bsu_bac. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR NCBIfam; TIGR02013; rpoB; 1. DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF20; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 2. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF10385; RNA_pol_Rpb2_45; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. DR SWISS-2DPAGE; P0A8V2; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Antibiotic resistance; KW Direct protein sequencing; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase. FT CHAIN 1..1342 FT /note="DNA-directed RNA polymerase subunit beta" FT /id="PRO_0000047892" FT MOD_RES 1022 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 1200 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MUTAGEN 561 FT /note="I->S: Resistant to antibiotics salinamide A and B." FT /evidence="ECO:0000269|PubMed:24843001" FT MUTAGEN 569 FT /note="I->S: Resistant to antibiotics salinamide A and B." FT /evidence="ECO:0000269|PubMed:24843001" FT MUTAGEN 665 FT /note="A->E: Resistant to antibiotics salinamide A and B." FT /evidence="ECO:0000269|PubMed:24843001" FT MUTAGEN 675 FT /note="D->A,G: Resistant to antibiotics salinamide A and FT B." FT /evidence="ECO:0000269|PubMed:24843001" FT MUTAGEN 677 FT /note="N->H,K: Resistant to antibiotics salinamide A and FT B." FT /evidence="ECO:0000269|PubMed:24843001" FT MUTAGEN 680 FT /note="L->M: Resistant to antibiotics salinamide A and B." FT /evidence="ECO:0000269|PubMed:24843001" FT MUTAGEN 813 FT /note="E->K: Disrupts the enzyme's active center." FT /evidence="ECO:0000269|PubMed:2068078" FT CONFLICT 4 FT /note="S -> R (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 106..107 FT /note="ER -> G (in Ref. 6; CAA23629)" FT /evidence="ECO:0000305" FT CONFLICT 384..391 FT /note="LFENLFFS -> CSRTCSSPT (in Ref. 6; CAA23629)" FT /evidence="ECO:0000305" FT CONFLICT 516 FT /note="D -> V (in Ref. 1; CAA23625/CAA23627 and 11; FT AAA24585)" FT /evidence="ECO:0000305" FT TURN 5..8 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 29..39 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:6XL5" FT HELIX 48..54 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 62..75 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 82..88 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 93..105 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:6X50" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 114..128 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:7XUE" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 141..145 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 172..177 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 184..188 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:8HKC" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:7SZK" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:6PSR" FT HELIX 207..212 FT /evidence="ECO:0007829|PDB:3LTI" FT HELIX 217..224 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 227..233 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 236..240 FT /evidence="ECO:0007829|PDB:3LTI" FT HELIX 243..246 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 250..253 FT /evidence="ECO:0007829|PDB:7MKJ" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 260..263 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:6XLL" FT HELIX 271..279 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:3LTI" FT HELIX 289..293 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:6XLN" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:6XLL" FT TURN 304..306 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 313..316 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 319..323 FT /evidence="ECO:0007829|PDB:3LTI" FT TURN 326..329 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 332..336 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:3LTI" FT HELIX 346..353 FT /evidence="ECO:0007829|PDB:3LTI" FT HELIX 359..370 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 371..374 FT /evidence="ECO:0007829|PDB:7UWE" FT HELIX 378..389 FT /evidence="ECO:0007829|PDB:3LTI" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:3LTI" FT HELIX 398..403 FT /evidence="ECO:0007829|PDB:3LTI" FT TURN 406..410 FT /evidence="ECO:0007829|PDB:3LTI" FT HELIX 424..429 FT /evidence="ECO:0007829|PDB:3LTI" FT HELIX 433..437 FT /evidence="ECO:0007829|PDB:3LTI" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:6PSV" FT STRAND 445..447 FT /evidence="ECO:0007829|PDB:6XL9" FT TURN 448..450 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 451..454 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 456..481 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 484..486 FT /evidence="ECO:0007829|PDB:6XL5" FT HELIX 489..492 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 496..508 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 512..514 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 520..528 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 529..532 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 534..537 FT /evidence="ECO:0007829|PDB:6PSS" FT TURN 540..542 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 545..548 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 552..554 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 555..557 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 567..571 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 572..575 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 583..585 FT /evidence="ECO:0007829|PDB:6XL5" FT STRAND 587..595 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 598..607 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 608..611 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 612..614 FT /evidence="ECO:0007829|PDB:6XLL" FT STRAND 619..622 FT /evidence="ECO:0007829|PDB:6N61" FT STRAND 627..640 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 642..645 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 647..649 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 652..655 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 659..661 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 663..666 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 668..670 FT /evidence="ECO:0007829|PDB:7YPA" FT HELIX 671..673 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 676..686 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 687..689 FT /evidence="ECO:0007829|PDB:7XUE" FT STRAND 692..694 FT /evidence="ECO:0007829|PDB:6XLN" FT STRAND 699..701 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 705..712 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 715..717 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 722..728 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 731..736 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 738..740 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 743..745 FT /evidence="ECO:0007829|PDB:6XL5" FT STRAND 748..752 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 756..758 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 762..765 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 768..770 FT /evidence="ECO:0007829|PDB:7QWP" FT STRAND 782..785 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 789..794 FT /evidence="ECO:0007829|PDB:6XL9" FT STRAND 797..805 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 808..811 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 812..814 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 816..819 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 820..824 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 825..828 FT /evidence="ECO:0007829|PDB:8HKC" FT STRAND 830..842 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 844..846 FT /evidence="ECO:0007829|PDB:7YPA" FT STRAND 849..852 FT /evidence="ECO:0007829|PDB:3TBI" FT STRAND 855..857 FT /evidence="ECO:0007829|PDB:6XLN" FT HELIX 860..862 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 863..865 FT /evidence="ECO:0007829|PDB:8FVR" FT STRAND 869..871 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 876..878 FT /evidence="ECO:0007829|PDB:6XL9" FT STRAND 882..884 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 886..888 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 892..894 FT /evidence="ECO:0007829|PDB:3TBI" FT HELIX 897..906 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 907..910 FT /evidence="ECO:0007829|PDB:6GH5" FT STRAND 912..915 FT /evidence="ECO:0007829|PDB:8HKC" FT STRAND 926..935 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 937..939 FT /evidence="ECO:0007829|PDB:7YPA" FT HELIX 943..959 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 962..979 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 980..982 FT /evidence="ECO:0007829|PDB:8FVR" FT HELIX 987..990 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 996..999 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1003..1005 FT /evidence="ECO:0007829|PDB:7SZK" FT HELIX 1006..1009 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1011..1021 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 1022..1028 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1029..1037 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1046..1058 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1065..1067 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1069..1071 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1073..1080 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1082..1084 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1095..1098 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1100..1102 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 1103..1107 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1110..1133 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1138..1150 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1152..1154 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1161..1163 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1166..1176 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1186..1188 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1192..1201 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1202..1204 FT /evidence="ECO:0007829|PDB:7UWE" FT STRAND 1208..1210 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 1215..1217 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1225..1236 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1239..1242 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1244..1248 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1253..1255 FT /evidence="ECO:0007829|PDB:8FVW" FT TURN 1262..1265 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1268..1270 FT /evidence="ECO:0007829|PDB:8HKC" FT HELIX 1272..1281 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1284..1291 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1292..1296 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1298..1310 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 1321..1332 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 1335..1339 FT /evidence="ECO:0007829|PDB:8FVW" SQ SEQUENCE 1342 AA; 150632 MW; F9E95344C54AB118 CRC64; MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE AAFRSVFPIQ SYSGNSELQY VSYRLGEPVF DVQECQIRGV TYSAPLRVKL RLVIYEREAP EGTVKDIKEQ EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR GSWLDFEFDP KDNLFVRIDR RRKLPATIIL RALNYTTEQI LDLFFEKVIF EIRDNKLQME LVPERLRGET ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVKLIEVPVE YIAGKVVAKD YIDESTGELI CAANMELSLD LLAKLSQSGH KRIETLFTND LDHGPYISET LRVDPTNDRL SALVEIYRMM RPGEPPTREA AESLFENLFF SEDRYDLSAV GRMKFNRSLL REEIEGSGIL SKDDIIDVMK KLIDIRNGKG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS LGDLDTLMPQ DMINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR ERAGFEVRDV HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRKVTDGVVT DEIHYLSAIE EGNYVIAQAN SNLDEEGHFV EDLVTCRSKG ESSLFSRDQV DYMDVSTQQV VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV GTGMERAVAV DSGVTAVAKR GGVVQYVDAS RIVIKVNEDE MYPGEAGIDI YNLTKYTRSN QNTCINQMPC VSLGEPVERG DVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELACVS RDTKLGPEEI TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE MQLKQAKKDL SEELQILEAG LFSRIRAVLV AGGVEAEKLD KLPRDRWLEL GLTDEEKQNQ LEQLAEQYDE LKHEFEKKLE AKRRKITQGD DLAPGVLKIV KVYLAVKRRI QPGDKMAGRH GNKGVISKIN PIEDMPYDEN GTPVDIVLNP LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK LREFIQRAYD LGADVRQKVD LSTFSDEEVM RLAENLRKGM PIATPVFDGA KEAEIKELLK LGDLPTSGQI RLYDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GNHQMEPGMP ESFNVLLKEI RSLGINIELE DE //