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Ribonucleoside-diphosphate reductase 1 subunit alpha (EC 1.17.4.1) (Protein B1) (Ribonucleoside-diphosphate reductase 1 R1 subunit) (Ribonucleotide reductase 1)

 RIR1_ECOLI              Reviewed;         761 AA.
P00452; P78088; P78177;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
30-AUG-2017, entry version 179.
RecName: Full=Ribonucleoside-diphosphate reductase 1 subunit alpha;
EC=1.17.4.1;
AltName: Full=Protein B1;
AltName: Full=Ribonucleoside-diphosphate reductase 1 R1 subunit;
AltName: Full=Ribonucleotide reductase 1;
Name=nrdA; Synonyms=dnaF; OrderedLocusNames=b2234, JW2228;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6087316; DOI=10.1073/pnas.81.14.4294;
Carlson J., Fuchs J.A., Messing J.;
"Primary structure of the Escherichia coli ribonucleoside diphosphate
reductase operon.";
Proc. Natl. Acad. Sci. U.S.A. 81:4294-4297(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3287341; DOI=10.1093/nar/16.9.4174;
Nilsson O., Aaberg A., Lundqvist T., Sjoeberg B.-M.;
"Nucleotide sequence of the gene coding for the large subunit of
ribonucleotide reductase of Escherichia coli. Correction.";
Nucleic Acids Res. 16:4174-4174(1988).
[3]
SEQUENCE REVISION TO 526-527.
Sjoeberg B.-M.;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
PARTIAL PROTEIN SEQUENCE.
PubMed=3894026; DOI=10.1111/j.1432-1033.1985.tb09037.x;
Sjoeberg B.-M., Eriksson S., Joernvall H., Carlquist M., Eklund H.;
"Protein B1 of ribonucleotide reductase. Direct analytical data and
comparisons with data indirectly deduced from the nucleotide sequence
of the Escherichia coli nrdA gene.";
Eur. J. Biochem. 150:423-427(1985).
[8]
ACTIVE SITES.
PubMed=2663852;
Aaberg A., Hahne S., Karlsson M., Larsson A., Ormoe M., Aahgren A.,
Sjoeberg B.-M.;
"Evidence for two different classes of redox-active cysteines in
ribonucleotide reductase of Escherichia coli.";
J. Biol. Chem. 264:12249-12252(1989).
[9]
ACTIVE SITES, AND MUTAGENESIS OF TYR-730 AND TYR-731.
PubMed=8702814; DOI=10.1074/jbc.271.34.20655;
Ekberg M., Sahlin M., Eriksson M., Sjoberg B.M.;
"Two conserved tyrosine residues in protein R1 participate in an
intermolecular electron transfer in ribonucleotide reductase.";
J. Biol. Chem. 271:20655-20659(1996).
[10]
ENZYME REGULATION, AND INDUCTION BY HYDROXYUREA.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
Walker G.C.;
"Hydroxyurea induces hydroxyl radical-mediated cell death in
Escherichia coli.";
Mol. Cell 36:845-860(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8052308; DOI=10.1038/370533a0;
Uhlin U., Eklund H.;
"Structure of ribonucleotide reductase protein R1.";
Nature 370:533-539(1994).
[13]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF MUTANTS ALA-441; ASP-441 AND
GLN-441, DISULFIDE BOND, SUBUNIT, ACTIVE SITE, ENZYME REGULATION,
ENZYME MECHANISM, AND MUTAGENESIS OF GLU-441.
PubMed=9395490; DOI=10.1074/jbc.272.50.31533;
Persson A.L., Eriksson M., Katterle B., Potsch S., Sahlin M.,
Sjoberg B.M.;
"A new mechanism-based radical intermediate in a mutant R1 protein
affecting the catalytically essential Glu441 in Escherichia coli
ribonucleotide reductase.";
J. Biol. Chem. 272:31533-31541(1997).
[14]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEXES WITH ATP; GDP AND
TTP, DISULFIDE BOND, SUBUNIT, AND ENZYME REGULATION.
PubMed=9309223; DOI=10.1016/S0969-2126(97)00259-1;
Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnstroem K.,
Sjoeberg B.-M., Eklund H.;
"Binding of allosteric effectors to ribonucleotide reductase protein
R1: reduction of active-site cysteines promotes substrate binding.";
Structure 5:1077-1092(1997).
[15]
STRUCTURE BY NMR OF 737-761, AND BINDING SITES.
PubMed=10493864; DOI=10.1006/jmbi.1999.3067;
Berardi M.J., Bushweller J.H.;
"Binding specificity and mechanistic insight into glutaredoxin-
catalyzed protein disulfide reduction.";
J. Mol. Biol. 292:151-161(1999).
-!- FUNCTION: Provides the precursors necessary for DNA synthesis.
Catalyzes the biosynthesis of deoxyribonucleotides from the
corresponding ribonucleotides. R1 contains the binding sites for
both substrates and allosteric effectors and carries out the
actual reduction of the ribonucleotide. It also provides redox-
active cysteines.
-!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate +
thioredoxin disulfide + H(2)O = ribonucleoside diphosphate +
thioredoxin.
-!- ENZYME REGULATION: Under complex allosteric control mediated by
deoxynucleoside triphosphates and ATP binding to separate
specificity and activation sites on the alpha subunit. The type of
nucleotide bound at the specificity site determines substrate
preference. It seems probable that ATP makes the enzyme reduce CDP
and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction.
Stimulated by ATP and inhibited by dATP binding to the activity
site. In vitro, its activity is increased by dithiothreitol (DTT)
or thioredoxins (non-specific). Inhibited by hydroxyurea, leads to
dNTP depletion, replication fork arrest and genomic instability
(PubMed:20005847). {ECO:0000269|PubMed:9309223,
ECO:0000269|PubMed:9395490, ECO:0000305|PubMed:20005847}.
-!- PATHWAY: Genetic information processing; DNA replication.
-!- SUBUNIT: Tetramer of two alpha (R1) and two beta (R2) subunits.
The B1 protein is a dimer of alpha subunits. A radical transfer
pathway occurs between 'Tyr-122' of R2 and R1.
{ECO:0000269|PubMed:9309223, ECO:0000269|PubMed:9395490}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Alpha;
IsoId=P00452-1; Sequence=Displayed;
Name=Alpha';
IsoId=P00452-2; Sequence=VSP_018871, VSP_018872;
-!- INDUCTION: Induced 5-fold by hydroxyurea (at protein level).
{ECO:0000269|PubMed:20005847}.
-!- PTM: Binding of the substrate occurs primarily when the active-
site cysteines are reduced.
-!- MISCELLANEOUS: E.coli produces two separate class I enzymes. This
one is the functional enzyme during growth.
-!- MISCELLANEOUS: Two distinct regulatory sites have been defined:
one controls substrate specificity and the other regulates the
overall catalytic activity. A substrate-binding catalytic site,
located on R1, is formed only in the presence of the second
subunit R2.
-!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
large chain family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA24223.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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EMBL; K02672; AAA24223.1; ALT_SEQ; Genomic_DNA.
EMBL; X06999; CAA30056.2; -; Genomic_DNA.
EMBL; U00096; AAC75294.1; -; Genomic_DNA.
EMBL; AP009048; BAA16053.1; -; Genomic_DNA.
PIR; H64993; RDEC1R.
RefSeq; NP_416737.1; NC_000913.3.
RefSeq; WP_001075164.1; NZ_LN832404.1.
PDB; 1QFN; NMR; -; B=737-761.
PDB; 1R1R; X-ray; 2.90 A; A/B/C=1-761.
PDB; 1RLR; X-ray; 2.50 A; A=1-761.
PDB; 2R1R; X-ray; 3.00 A; A/B/C=1-761.
PDB; 2X0X; X-ray; 2.30 A; A/B/C=1-761.
PDB; 2XAK; X-ray; 2.80 A; A/B/C=1-761.
PDB; 2XAP; X-ray; 2.10 A; A/B/C=1-761.
PDB; 2XAV; X-ray; 2.80 A; A/B/C=1-761.
PDB; 2XAW; X-ray; 3.10 A; A/B/C=1-761.
PDB; 2XAX; X-ray; 2.75 A; A/B/C=1-761.
PDB; 2XAY; X-ray; 2.65 A; A/B/C=1-761.
PDB; 2XAZ; X-ray; 2.60 A; A/B/C=1-761.
PDB; 2XO4; X-ray; 2.50 A; A/B/C=1-761.
PDB; 2XO5; X-ray; 2.70 A; A/B/C=1-761.
PDB; 3R1R; X-ray; 3.00 A; A/B/C=1-761.
PDB; 3UUS; X-ray; 5.65 A; A/B/C/D=1-761.
PDB; 4ERM; X-ray; 3.95 A; A/B/C/D=1-761.
PDB; 4ERP; X-ray; 4.45 A; A/B/C/D=1-761.
PDB; 4R1R; X-ray; 3.20 A; A/B/C=1-761.
PDB; 5CNS; X-ray; 2.98 A; A/B/C/D=1-761.
PDB; 5CNT; X-ray; 3.25 A; A/B/C/D=1-761.
PDB; 5CNU; X-ray; 3.40 A; A/B/C/D=1-761.
PDB; 5CNV; X-ray; 3.20 A; A/B/C/D=1-761.
PDB; 5R1R; X-ray; 3.10 A; A/B/C=1-761.
PDB; 6R1R; X-ray; 3.10 A; A/B/C=1-761.
PDB; 7R1R; X-ray; 3.10 A; A/B/C=1-761.
PDBsum; 1QFN; -.
PDBsum; 1R1R; -.
PDBsum; 1RLR; -.
PDBsum; 2R1R; -.
PDBsum; 2X0X; -.
PDBsum; 2XAK; -.
PDBsum; 2XAP; -.
PDBsum; 2XAV; -.
PDBsum; 2XAW; -.
PDBsum; 2XAX; -.
PDBsum; 2XAY; -.
PDBsum; 2XAZ; -.
PDBsum; 2XO4; -.
PDBsum; 2XO5; -.
PDBsum; 3R1R; -.
PDBsum; 3UUS; -.
PDBsum; 4ERM; -.
PDBsum; 4ERP; -.
PDBsum; 4R1R; -.
PDBsum; 5CNS; -.
PDBsum; 5CNT; -.
PDBsum; 5CNU; -.
PDBsum; 5CNV; -.
PDBsum; 5R1R; -.
PDBsum; 6R1R; -.
PDBsum; 7R1R; -.
ProteinModelPortal; P00452; -.
SMR; P00452; -.
BioGrid; 4262130; 181.
DIP; DIP-584N; -.
IntAct; P00452; 9.
MINT; MINT-1233906; -.
STRING; 316385.ECDH10B_2393; -.
PaxDb; P00452; -.
PRIDE; P00452; -.
EnsemblBacteria; AAC75294; AAC75294; b2234.
EnsemblBacteria; BAA16053; BAA16053; BAA16053.
GeneID; 946612; -.
KEGG; ecj:JW2228; -.
KEGG; eco:b2234; -.
PATRIC; fig|1411691.4.peg.1; -.
EchoBASE; EB0654; -.
EcoGene; EG10660; nrdA.
eggNOG; ENOG4105BZH; Bacteria.
eggNOG; COG0209; LUCA.
HOGENOM; HOG000278076; -.
InParanoid; P00452; -.
KO; K00525; -.
PhylomeDB; P00452; -.
BioCyc; EcoCyc:NRDA-MONOMER; -.
BioCyc; MetaCyc:NRDA-MONOMER; -.
BRENDA; 1.17.4.1; 2026.
SABIO-RK; P00452; -.
UniPathway; UPA00326; -.
EvolutionaryTrace; P00452; -.
PRO; PR:P00452; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:EcoliWiki.
GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:EcoCyc.
GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:EcoliWiki.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoliWiki.
InterPro; IPR005144; ATP-cone_dom.
InterPro; IPR013346; NrdE_NrdA.
InterPro; IPR000788; RNR_lg_C.
InterPro; IPR013509; RNR_lsu_N.
InterPro; IPR008926; RNR_R1-su_N.
Pfam; PF03477; ATP-cone; 1.
Pfam; PF02867; Ribonuc_red_lgC; 1.
Pfam; PF00317; Ribonuc_red_lgN; 1.
PRINTS; PR01183; RIBORDTASEM1.
SUPFAM; SSF48168; SSF48168; 1.
TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
PROSITE; PS51161; ATP_CONE; 1.
PROSITE; PS00089; RIBORED_LARGE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative initiation;
ATP-binding; Complete proteome; Direct protein sequencing;
Disulfide bond; DNA replication; Nucleotide-binding; Oxidoreductase;
Reference proteome.
CHAIN 1 761 Ribonucleoside-diphosphate reductase 1
subunit alpha.
/FTId=PRO_0000030596.
DOMAIN 5 95 ATP-cone. {ECO:0000255|PROSITE-
ProRule:PRU00492}.
REGION 15 21 Allosteric activator binding.
REGION 224 225 Substrate binding. {ECO:0000250}.
REGION 437 441 Substrate binding. {ECO:0000250}.
REGION 621 625 Substrate binding.
ACT_SITE 437 437 Proton acceptor.
ACT_SITE 439 439 Cysteine radical intermediate.
ACT_SITE 441 441 Proton acceptor.
BINDING 9 9 Allosteric activator.
BINDING 55 55 Allosteric activator.
BINDING 91 91 Allosteric activator.
BINDING 209 209 Substrate.
BINDING 253 253 Substrate; via amide nitrogen.
{ECO:0000250}.
SITE 225 225 Important for hydrogen atom transfer.
SITE 232 232 Allosteric effector binding.
SITE 262 262 Allosteric effector binding.
SITE 462 462 Important for hydrogen atom transfer.
SITE 730 730 Important for electron transfer.
SITE 731 731 Important for electron transfer.
SITE 754 754 Interacts with thioredoxin/glutaredoxin.
SITE 759 759 Interacts with thioredoxin/glutaredoxin.
MOD_RES 283 283 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
DISULFID 225 462 Redox-active.
{ECO:0000269|PubMed:9309223,
ECO:0000269|PubMed:9395490}.
VAR_SEQ 1 25 Missing (in isoform Alpha').
{ECO:0000305}.
/FTId=VSP_018871.
VAR_SEQ 26 26 L -> M (in isoform Alpha').
{ECO:0000305}.
/FTId=VSP_018872.
VARIANT 1 2 Missing (in 15% of the chains).
VARIANT 1 1 Missing (in 30% of the chains).
MUTAGEN 441 441 E->A,Q: Loss of activity.
{ECO:0000269|PubMed:9395490}.
MUTAGEN 441 441 E->D: Decrease in activity.
{ECO:0000269|PubMed:9395490}.
MUTAGEN 730 730 Y->F: Loss of activity.
{ECO:0000269|PubMed:8702814}.
MUTAGEN 731 731 Y->F: Loss of activity.
{ECO:0000269|PubMed:8702814}.
STRAND 6 8 {ECO:0000244|PDB:2XAP}.
STRAND 10 12 {ECO:0000244|PDB:2XAP}.
STRAND 14 16 {ECO:0000244|PDB:2XAP}.
HELIX 19 30 {ECO:0000244|PDB:2XAP}.
HELIX 38 46 {ECO:0000244|PDB:2XAP}.
HELIX 55 68 {ECO:0000244|PDB:2XAP}.
STRAND 72 74 {ECO:0000244|PDB:2XAP}.
HELIX 77 94 {ECO:0000244|PDB:2XAP}.
STRAND 95 98 {ECO:0000244|PDB:2XAP}.
HELIX 102 111 {ECO:0000244|PDB:2XAP}.
HELIX 118 122 {ECO:0000244|PDB:2XAP}.
HELIX 125 134 {ECO:0000244|PDB:2XAP}.
HELIX 137 142 {ECO:0000244|PDB:2XAP}.
HELIX 145 154 {ECO:0000244|PDB:2XAP}.
TURN 160 162 {ECO:0000244|PDB:2XAP}.
HELIX 169 180 {ECO:0000244|PDB:2XAP}.
TURN 181 183 {ECO:0000244|PDB:2XAP}.
TURN 186 188 {ECO:0000244|PDB:2XAP}.
HELIX 189 201 {ECO:0000244|PDB:2XAP}.
STRAND 204 206 {ECO:0000244|PDB:2XAP}.
HELIX 209 214 {ECO:0000244|PDB:2XAP}.
STRAND 217 219 {ECO:0000244|PDB:5CNS}.
STRAND 225 229 {ECO:0000244|PDB:2XAP}.
HELIX 234 248 {ECO:0000244|PDB:2XAP}.
TURN 249 251 {ECO:0000244|PDB:2XAP}.
STRAND 253 257 {ECO:0000244|PDB:2XAP}.
STRAND 268 271 {ECO:0000244|PDB:1RLR}.
HELIX 274 276 {ECO:0000244|PDB:5R1R}.
HELIX 278 289 {ECO:0000244|PDB:2XAP}.
TURN 290 292 {ECO:0000244|PDB:2XAP}.
STRAND 296 299 {ECO:0000244|PDB:2XAP}.
STRAND 301 307 {ECO:0000244|PDB:2XAP}.
HELIX 313 317 {ECO:0000244|PDB:2XAP}.
TURN 318 320 {ECO:0000244|PDB:2XAP}.
STRAND 322 324 {ECO:0000244|PDB:2XAP}.
HELIX 326 328 {ECO:0000244|PDB:2XAP}.
STRAND 333 339 {ECO:0000244|PDB:2XAP}.
HELIX 341 349 {ECO:0000244|PDB:2XAP}.
STRAND 352 356 {ECO:0000244|PDB:2XAP}.
HELIX 358 360 {ECO:0000244|PDB:2XAP}.
HELIX 364 370 {ECO:0000244|PDB:2XAP}.
HELIX 372 384 {ECO:0000244|PDB:2XAP}.
STRAND 386 388 {ECO:0000244|PDB:2XAX}.
STRAND 391 394 {ECO:0000244|PDB:2XAP}.
HELIX 395 409 {ECO:0000244|PDB:2XAP}.
STRAND 412 416 {ECO:0000244|PDB:2XAP}.
HELIX 419 422 {ECO:0000244|PDB:2XAP}.
STRAND 423 426 {ECO:0000244|PDB:2XAP}.
TURN 428 430 {ECO:0000244|PDB:2XAP}.
STRAND 438 440 {ECO:0000244|PDB:5CNS}.
STRAND 463 468 {ECO:0000244|PDB:2XAP}.
TURN 469 471 {ECO:0000244|PDB:2XAP}.
HELIX 475 477 {ECO:0000244|PDB:2XAP}.
HELIX 478 495 {ECO:0000244|PDB:2XAP}.
HELIX 501 510 {ECO:0000244|PDB:2XAP}.
STRAND 513 518 {ECO:0000244|PDB:2XAP}.
HELIX 520 526 {ECO:0000244|PDB:2XAP}.
STRAND 531 534 {ECO:0000244|PDB:2X0X}.
HELIX 537 562 {ECO:0000244|PDB:2XAP}.
HELIX 568 570 {ECO:0000244|PDB:2XAP}.
HELIX 573 575 {ECO:0000244|PDB:2XAP}.
HELIX 579 582 {ECO:0000244|PDB:2XAP}.
HELIX 585 589 {ECO:0000244|PDB:2XAP}.
HELIX 599 609 {ECO:0000244|PDB:2XAP}.
STRAND 612 614 {ECO:0000244|PDB:2XO5}.
HELIX 624 628 {ECO:0000244|PDB:2XAP}.
STRAND 639 645 {ECO:0000244|PDB:2XAP}.
STRAND 648 650 {ECO:0000244|PDB:5CNS}.
STRAND 652 655 {ECO:0000244|PDB:2XAP}.
HELIX 659 662 {ECO:0000244|PDB:2XAP}.
TURN 663 665 {ECO:0000244|PDB:2XAP}.
HELIX 669 671 {ECO:0000244|PDB:2XAP}.
STRAND 672 675 {ECO:0000244|PDB:2XAK}.
HELIX 676 686 {ECO:0000244|PDB:2XAP}.
STRAND 697 699 {ECO:0000244|PDB:2XAP}.
HELIX 701 703 {ECO:0000244|PDB:2XAP}.
HELIX 705 707 {ECO:0000244|PDB:2XAP}.
HELIX 711 723 {ECO:0000244|PDB:2XAP}.
STRAND 732 734 {ECO:0000244|PDB:2XAP}.
HELIX 738 741 {ECO:0000244|PDB:1RLR}.
SEQUENCE 761 AA; 85775 MW; 7E034F154567C3FC CRC64;
MNQNLLVTKR DGSTERINLD KIHRVLDWAA EGLHNVSISQ VELRSHIQFY DGIKTSDIHE
TIIKAAADLI SRDAPDYQYL AARLAIFHLR KKAYGQFEPP ALYDHVVKMV EMGKYDNHLL
EDYTEEEFKQ MDTFIDHDRD MTFSYAAVKQ LEGKYLVQNR VTGEIYESAQ FLYILVAACL
FSNYPRETRL QYVKRFYDAV STFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT
SSAIVKYVSQ RAGIGINAGR IRALGSPIRG GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG
AATLFYPMWH LEVESLLVLK NNRGVEGNRV RHMDYGVQIN KLMYTRLLKG EDITLFSPSD
VPGLYDAFFA DQEEFERLYT KYEKDDSIRK QRVKAVELFS LMMQERASTG RIYIQNVDHC
NTHSPFDPAI APVRQSNLCL EIALPTKPLN DVNDENGEIA LCTLSAFNLG AINNLDELEE
LAILAVRALD ALLDYQDYPI PAAKRGAMGR RTLGIGVINF AYYLAKHGKR YSDGSANNLT
HKTFEAIQYY LLKASNELAK EQGACPWFNE TTYAKGILPI DTYKKDLDTI ANEPLHYDWE
ALRESIKTHG LRNSTLSALM PSETSSQISN ATNGIEPPRG YVSIKASKDG ILRQVVPDYE
HLHDAYELLW EMPGNDGYLQ LVGIMQKFID QSISANTNYD PSRFPSGKVP MQQLLKDLLT
AYKFGVKTLY YQNTRDGAED AQDDLVPSIQ DDGCESGACK I


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