ID   RIR2_ECOLI              Reviewed;         376 AA.
AC   P69924; P00453;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Ribonucleoside-diphosphate reductase 1 subunit beta;
DE            EC=1.17.4.1;
DE   AltName: Full=Protein B2;
DE   AltName: Full=Protein R2;
DE   AltName: Full=Ribonucleotide reductase 1;
GN   Name=nrdB; Synonyms=ftsB; OrderedLocusNames=b2235, JW2229;
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=6087316; DOI=10.1073/pnas.81.14.4294;
RA   Carlson J., Fuchs J.A., Messing J.;
RT   "Primary structure of the Escherichia coli ribonucleoside diphosphate
RT   reductase operon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:4294-4297(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
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   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 2-21.
RX   PubMed=3511029; DOI=10.1128/jb.165.2.363-366.1986;
RA   Salowe S.P., Stubbe J.;
RT   "Cloning, overproduction, and purification of the B2 subunit of
RT   ribonucleoside-diphosphate reductase.";
RL   J. Bacteriol. 165:363-366(1986).
RN   [6]
RP   ACTIVITY REGULATION, AND INDUCTION BY HYDROXYUREA.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA   Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA   Walker G.C.;
RT   "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT   coli.";
RL   Mol. Cell 36:845-860(2009).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=2190093; DOI=10.1038/345593a0;
RA   Nordlund P., Sjoeberg B.-M., Eklund H.;
RT   "Three-dimensional structure of the free radical protein of ribonucleotide
RT   reductase.";
RL   Nature 345:593-598(1990).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=8331655; DOI=10.1006/jmbi.1993.1374;
RA   Nordlund P., Eklund H.;
RT   "Structure and function of the Escherichia coli ribonucleotide reductase
RT   protein R2.";
RL   J. Mol. Biol. 232:123-164(1993).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=8805591; DOI=10.1016/s0969-2126(96)00112-8;
RA   Logan D.T., Su X.-D., Aaberg A., Regnstroem K., Hajdu J., Eklund H.,
RA   Nordlund P.;
RT   "Crystal structure of reduced protein R2 of ribonucleotide reductase: the
RT   structural basis for oxygen activation at a dinuclear iron site.";
RL   Structure 4:1053-1064(1996).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX   PubMed=9309223; DOI=10.1016/s0969-2126(97)00259-1;
RA   Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnstroem K.,
RA   Sjoeberg B.-M., Eklund H.;
RT   "Binding of allosteric effectors to ribonucleotide reductase protein R1:
RT   reduction of active-site cysteines promotes substrate binding.";
RL   Structure 5:1077-1092(1997).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF MUTANT PHE-103.
RX   PubMed=9558317; DOI=10.1021/bi9728811;
RA   Tong W., Burdi D., Riggs-Gelasco P., Chen S., Edmondson D., Huynh B.H.,
RA   Stubbe J., Han S., Arvai A., Tainer J.;
RT   "Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase
RT   by time-resolved physical biochemical methods and X-ray crystallography.";
RL   Biochemistry 37:5840-5848(1998).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RX   PubMed=9692970; DOI=10.1021/bi9806403;
RA   Logan D.T., DeMare F., Persson B.O., Slaby A., Sjoeberg B.-M., Nordlund P.;
RT   "Crystal structures of two self-hydroxylating ribonucleotide reductase
RT   protein R2 mutants: structural basis for the oxygen-insertion step of
RT   hydroxylation reactions catalyzed by diiron proteins.";
RL   Biochemistry 37:10798-10807(1998).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS).
RX   PubMed=11315567; DOI=10.1007/s007750000205;
RA   Hogbom M., Andersson M.E., Nordlund P.;
RT   "Crystal structures of oxidized dinuclear manganese centres in Mn-
RT   substituted class I ribonucleotide reductase from Escherichia coli:
RT   carboxylate shifts with implications for O2 activation and radical
RT   generation.";
RL   J. Biol. Inorg. Chem. 6:315-323(2001).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. R2 contains the tyrosyl radical required
CC       for catalysis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10014};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 2 iron ions per subunit.;
CC   -!- ACTIVITY REGULATION: Inhibited by hydroxyurea, leads to dNTP depletion,
CC       replication fork arrest and genomic instability.
CC       {ECO:0000305|PubMed:20005847}.
CC   -!- SUBUNIT: Tetramer of two alpha (R1) and two beta (R2) subunits. The B1
CC       protein is a dimer of alpha subunits. A radical transfer pathway occurs
CC       between Tyr-123 of R2 and R1.
CC   -!- INTERACTION:
CC       P69924; P0A6Y8: dnaK; NbExp=2; IntAct=EBI-555196, EBI-542092;
CC       P69924; P00452: nrdA; NbExp=11; IntAct=EBI-555196, EBI-370018;
CC       P69924; P69924: nrdB; NbExp=5; IntAct=EBI-555196, EBI-555196;
CC   -!- INDUCTION: Induced 4.2-fold by hydroxyurea (at protein level).
CC       {ECO:0000269|PubMed:20005847}.
CC   -!- MISCELLANEOUS: E.coli produces two separate class I enzymes. This one
CC       is the functional enzyme during growth.
CC   -!- MISCELLANEOUS: A substrate-binding catalytic site, located on R1, is
CC       formed only in the presence of the second subunit R2.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
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DR   EMBL; K02672; AAA24224.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75295.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16054.1; -; Genomic_DNA.
DR   PIR; A00527; RDEC2R.
DR   RefSeq; NP_416738.1; NC_000913.3.
DR   RefSeq; WP_000332037.1; NZ_STEB01000002.1.
DR   PDB; 1AV8; X-ray; 2.80 A; A/B=2-341.
DR   PDB; 1BIQ; X-ray; 2.05 A; A/B=2-376.
DR   PDB; 1JPR; X-ray; 1.88 A; A/B=2-376.
DR   PDB; 1JQC; X-ray; 1.61 A; A/B=2-376.
DR   PDB; 1MRR; X-ray; 2.50 A; A/B=2-376.
DR   PDB; 1MXR; X-ray; 1.42 A; A/B=2-376.
DR   PDB; 1PFR; X-ray; 2.20 A; A/B=2-341.
DR   PDB; 1PIM; X-ray; 2.00 A; A/B=2-376.
DR   PDB; 1PIU; X-ray; 2.20 A; A/B=2-376.
DR   PDB; 1PIY; X-ray; 1.68 A; A/B=2-376.
DR   PDB; 1PIZ; X-ray; 1.90 A; A/B=2-376.
DR   PDB; 1PJ0; X-ray; 1.90 A; A/B=2-376.
DR   PDB; 1PJ1; X-ray; 1.95 A; A/B=2-376.
DR   PDB; 1PM2; X-ray; 1.80 A; A/B=2-340.
DR   PDB; 1R1R; X-ray; 2.90 A; D/E/F/P=357-376.
DR   PDB; 1R65; X-ray; 1.95 A; A/B=2-376.
DR   PDB; 1RIB; X-ray; 2.20 A; A/B=2-376.
DR   PDB; 1RNR; X-ray; 2.50 A; A/B=2-376.
DR   PDB; 1RSR; X-ray; 2.00 A; A/B=2-376.
DR   PDB; 1RSV; X-ray; 2.20 A; A/B=2-376.
DR   PDB; 1XIK; X-ray; 1.70 A; A/B=2-376.
DR   PDB; 1YFD; X-ray; 1.90 A; A/B=2-376.
DR   PDB; 2ALX; X-ray; 2.60 A; A=1-340.
DR   PDB; 2AV8; X-ray; 2.46 A; A/B=2-341.
DR   PDB; 2R1R; X-ray; 3.00 A; D/E/F/P=357-376.
DR   PDB; 2X0X; X-ray; 2.30 A; D/E/F/P=357-376.
DR   PDB; 2XAK; X-ray; 2.80 A; D/E/F/P=357-376.
DR   PDB; 2XAP; X-ray; 2.10 A; D/E/F/P=357-376.
DR   PDB; 2XAV; X-ray; 2.80 A; D/E/F/P=357-376.
DR   PDB; 2XAW; X-ray; 3.10 A; D/E/F/P=357-376.
DR   PDB; 2XAX; X-ray; 2.75 A; D/E/F/P=357-376.
DR   PDB; 2XAY; X-ray; 2.65 A; D/E/F/P=357-376.
DR   PDB; 2XAZ; X-ray; 2.60 A; D/E/F/P=357-376.
DR   PDB; 2XO4; X-ray; 2.50 A; D/E/F/P=357-376.
DR   PDB; 2XO5; X-ray; 2.70 A; D/E/F/P=357-376.
DR   PDB; 2XOF; X-ray; 2.20 A; A/B=2-376.
DR   PDB; 3R1R; X-ray; 3.00 A; D/E/F/P=357-376.
DR   PDB; 3UUS; X-ray; 5.65 A; E/F/G/H=2-376.
DR   PDB; 4ERM; X-ray; 3.95 A; E/F/G/H=2-376.
DR   PDB; 4ERP; X-ray; 4.45 A; E/F/G/H=2-376.
DR   PDB; 4R1R; X-ray; 3.20 A; D/E/F/P=357-376.
DR   PDB; 5CI2; X-ray; 2.25 A; A=2-376.
DR   PDB; 5CI3; X-ray; 2.40 A; A=2-376.
DR   PDB; 5CNS; X-ray; 2.98 A; E/F/G/H=2-376.
DR   PDB; 5CNT; X-ray; 3.25 A; E/F/G/H=2-376.
DR   PDB; 5CNU; X-ray; 3.40 A; E/F/G/H=2-376.
DR   PDB; 5CNV; X-ray; 3.20 A; E/F/G/H=2-376.
DR   PDB; 5R1R; X-ray; 3.10 A; D/E/F/P=357-376.
DR   PDB; 6R1R; X-ray; 3.10 A; D/E/F/P=357-376.
DR   PDB; 6W4X; EM; 3.60 A; C/D=1-376.
DR   PDB; 7AI8; X-ray; 2.10 A; A=1-376.
DR   PDB; 7AI9; X-ray; 2.00 A; A=1-376.
DR   PDB; 7BET; X-ray; 2.30 A; A=1-376.
DR   PDB; 7R1R; X-ray; 3.10 A; D/E/F/P=357-376.
DR   PDBsum; 1AV8; -.
DR   PDBsum; 1BIQ; -.
DR   PDBsum; 1JPR; -.
DR   PDBsum; 1JQC; -.
DR   PDBsum; 1MRR; -.
DR   PDBsum; 1MXR; -.
DR   PDBsum; 1PFR; -.
DR   PDBsum; 1PIM; -.
DR   PDBsum; 1PIU; -.
DR   PDBsum; 1PIY; -.
DR   PDBsum; 1PIZ; -.
DR   PDBsum; 1PJ0; -.
DR   PDBsum; 1PJ1; -.
DR   PDBsum; 1PM2; -.
DR   PDBsum; 1R1R; -.
DR   PDBsum; 1R65; -.
DR   PDBsum; 1RIB; -.
DR   PDBsum; 1RNR; -.
DR   PDBsum; 1RSR; -.
DR   PDBsum; 1RSV; -.
DR   PDBsum; 1XIK; -.
DR   PDBsum; 1YFD; -.
DR   PDBsum; 2ALX; -.
DR   PDBsum; 2AV8; -.
DR   PDBsum; 2R1R; -.
DR   PDBsum; 2X0X; -.
DR   PDBsum; 2XAK; -.
DR   PDBsum; 2XAP; -.
DR   PDBsum; 2XAV; -.
DR   PDBsum; 2XAW; -.
DR   PDBsum; 2XAX; -.
DR   PDBsum; 2XAY; -.
DR   PDBsum; 2XAZ; -.
DR   PDBsum; 2XO4; -.
DR   PDBsum; 2XO5; -.
DR   PDBsum; 2XOF; -.
DR   PDBsum; 3R1R; -.
DR   PDBsum; 3UUS; -.
DR   PDBsum; 4ERM; -.
DR   PDBsum; 4ERP; -.
DR   PDBsum; 4R1R; -.
DR   PDBsum; 5CI2; -.
DR   PDBsum; 5CI3; -.
DR   PDBsum; 5CNS; -.
DR   PDBsum; 5CNT; -.
DR   PDBsum; 5CNU; -.
DR   PDBsum; 5CNV; -.
DR   PDBsum; 5R1R; -.
DR   PDBsum; 6R1R; -.
DR   PDBsum; 6W4X; -.
DR   PDBsum; 7AI8; -.
DR   PDBsum; 7AI9; -.
DR   PDBsum; 7BET; -.
DR   PDBsum; 7R1R; -.
DR   AlphaFoldDB; P69924; -.
DR   EMDB; EMD-21540; -.
DR   SMR; P69924; -.
DR   BioGRID; 4260492; 56.
DR   ComplexPortal; CPX-1075; Ribonucleoside-diphosphate reductase 1 complex.
DR   DIP; DIP-36213N; -.
DR   IntAct; P69924; 13.
DR   STRING; 511145.b2235; -.
DR   DrugBank; DB09462; Glycerin.
DR   jPOST; P69924; -.
DR   PaxDb; 511145-b2235; -.
DR   EnsemblBacteria; AAC75295; AAC75295; b2235.
DR   GeneID; 75058011; -.
DR   GeneID; 946732; -.
DR   KEGG; ecj:JW2229; -.
DR   KEGG; eco:b2235; -.
DR   PATRIC; fig|511145.12.peg.2324; -.
DR   EchoBASE; EB0655; -.
DR   eggNOG; COG0208; Bacteria.
DR   HOGENOM; CLU_062403_0_0_6; -.
DR   InParanoid; P69924; -.
DR   OMA; LEPMFLG; -.
DR   OrthoDB; 9765051at2; -.
DR   PhylomeDB; P69924; -.
DR   BioCyc; EcoCyc:NRDB-MONOMER; -.
DR   BioCyc; MetaCyc:NRDB-MONOMER; -.
DR   BRENDA; 1.17.4.1; 2026.
DR   SABIO-RK; P69924; -.
DR   EvolutionaryTrace; P69924; -.
DR   PRO; PR:P69924; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:EcoliWiki.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IDA:ComplexPortal.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:EcoliWiki.
DR   GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoliWiki.
DR   GO; GO:0009185; P:ribonucleoside diphosphate metabolic process; IDA:ComplexPortal.
DR   CDD; cd01049; RNRR2; 1.
DR   DisProt; DP00107; -.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR030475; RNR_small_AS.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Deoxyribonucleotide synthesis; Direct protein sequencing;
KW   Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3511029"
FT   CHAIN           2..376
FT                   /note="Ribonucleoside-diphosphate reductase 1 subunit beta"
FT                   /id="PRO_0000190476"
FT   ACT_SITE        123
FT   BINDING         85
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         116
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         116
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         119
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         239
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         242
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:1JQC"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           35..46
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           59..64
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           68..95
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           103..128
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           134..143
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           145..151
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           154..171
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           187..206
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           208..221
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           226..255
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:1PJ1"
FT   HELIX           260..268
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           270..291
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   TURN            292..294
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           302..319
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   HELIX           334..338
FT                   /evidence="ECO:0007829|PDB:1MXR"
FT   STRAND          343..345
FT                   /evidence="ECO:0007829|PDB:5CI2"
FT   HELIX           368..371
FT                   /evidence="ECO:0007829|PDB:2XAP"
SQ   SEQUENCE   376 AA;  43517 MW;  BF2D9A49B643E84A CRC64;
     MAYTTFSQTK NDQLKEPMFF GQPVNVARYD QQKYDIFEKL IEKQLSFFWR PEEVDVSRDR
     IDYQALPEHE KHIFISNLKY QTLLDSIQGR SPNVALLPLI SIPELETWVE TWAFSETIHS
     RSYTHIIRNI VNDPSVVFDD IVTNEQIQKR AEGISSYYDE LIEMTSYWHL LGEGTHTVNG
     KTVTVSLREL KKKLYLCLMS VNALEAIRFY VSFACSFAFA ERELMEGNAK IIRLIARDEA
     LHLTGTQHML NLLRSGADDP EMAEIAEECK QECYDLFVQA AQQEKDWADY LFRDGSMIGL
     NKDILCQYVE YITNIRMQAV GLDLPFQTRS NPIPWINTWL VSDNVQVAPQ EVEVSSYLVG
     QIDSEVDTDD LSNFQL
//