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Ribonucleoside-diphosphate reductase large chain 1 (EC 1.17.4.1) (Ribonucleotide reductase R1 subunit 1) (Ribonucleotide reductase large subunit 1)

 RIR1_YEAST              Reviewed;         888 AA.
P21524; D3DLX5;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
22-NOV-2017, entry version 177.
RecName: Full=Ribonucleoside-diphosphate reductase large chain 1;
EC=1.17.4.1;
AltName: Full=Ribonucleotide reductase R1 subunit 1;
AltName: Full=Ribonucleotide reductase large subunit 1;
Name=RNR1; Synonyms=CRT7, RIR1, SDS12; OrderedLocusNames=YER070W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100 AND 653-682, AND INDUCTION.
PubMed=2199320; DOI=10.1101/gad.4.5.740;
Elledge S.J., Davis R.W.;
"Two genes differentially regulated in the cell cycle and by DNA-
damaging agents encode alternative regulatory subunits of
ribonucleotide reductase.";
Genes Dev. 4:740-751(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-384 AND 546-590.
PubMed=8121398; DOI=10.1007/BF00281793;
Ozier-Kalogeropoulos O., Adeline M.-T., Yang W.-L., Carman G.M.,
Lacroute F.;
"Use of synthetic lethal mutants to clone and characterize a novel CTP
synthetase gene in Saccharomyces cerevisiae.";
Mol. Gen. Genet. 242:431-439(1994).
[5]
INTERACTION WITH SML1, AND ENZYME REGULATION.
PubMed=10593972; DOI=10.1074/jbc.274.51.36679;
Chabes A., Domkin V., Thelander L.;
"Yeast Sml1, a protein inhibitor of ribonucleotide reductase.";
J. Biol. Chem. 274:36679-36683(1999).
[6]
SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10716984; DOI=10.1073/pnas.97.6.2474;
Chabes A., Domkin V., Larsson G., Liu A., Graeslund A., Wijmenga S.,
Thelander L.;
"Yeast ribonucleotide reductase has a heterodimeric iron-radical-
containing subunit.";
Proc. Natl. Acad. Sci. U.S.A. 97:2474-2479(2000).
[7]
FUNCTION, AND MUTAGENESIS OF CYS-428.
PubMed=11893751; DOI=10.1074/jbc.M201553200;
Domkin V., Thelander L., Chabes A.;
"Yeast DNA damage-inducible Rnr3 has a very low catalytic activity
strongly stimulated after the formation of a cross-talking Rnr1/Rnr3
complex.";
J. Biol. Chem. 277:18574-18578(2002).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
SUBCELLULAR LOCATION.
PubMed=12732713; DOI=10.1073/pnas.1131932100;
Yao R., Zhang Z., An X., Bucci B., Perlstein D.L., Stubbe J.,
Huang M.;
"Subcellular localization of yeast ribonucleotide reductase regulated
by the DNA replication and damage checkpoint pathways.";
Proc. Natl. Acad. Sci. U.S.A. 100:6628-6633(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-837 AND
SER-887, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-387 AND LYS-853, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[13]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH CDP; UDP;
TTP; GDP; GTP; ADP AND AMPPNP, AND DISULFIDE BOND.
PubMed=16537479; DOI=10.1073/pnas.0600443103;
Xu H., Faber C., Uchiki T., Fairman J.W., Racca J., Dealwis C.;
"Structures of eukaryotic ribonucleotide reductase I provide insights
into dNTP regulation.";
Proc. Natl. Acad. Sci. U.S.A. 103:4022-4027(2006).
[14]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH GEMCITABINE
DIPHOSPHATE AND R2 PEPTIDES, AND SUBUNIT.
PubMed=16537480; DOI=10.1073/pnas.0600440103;
Xu H., Faber C., Uchiki T., Racca J., Dealwis C.;
"Structures of eukaryotic ribonucleotide reductase I define
gemcitabine diphosphate binding and subunit assembly.";
Proc. Natl. Acad. Sci. U.S.A. 103:4028-4033(2006).
[15]
X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH PEPTIDE
INHIBITORS, AND SUBUNIT.
PubMed=18610997; DOI=10.1021/jm800350u;
Xu H., Fairman J.W., Wijerathna S.R., Kreischer N.R., LaMacchia J.,
Helmbrecht E., Cooperman B.S., Dealwis C.;
"The structural basis for peptidomimetic inhibition of eukaryotic
ribonucleotide reductase: a conformationally flexible pharmacophore.";
J. Med. Chem. 51:4653-4659(2008).
-!- FUNCTION: Provides the precursors necessary for DNA synthesis.
Catalyzes the biosynthesis of deoxyribonucleotides from the
corresponding ribonucleotides. {ECO:0000269|PubMed:11893751}.
-!- 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 R1 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. Inhibited by SML1. {ECO:0000269|PubMed:10593972}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Vmax=2250 nmol/min/mg enzyme for cytidine 5'-diphosphate
{ECO:0000269|PubMed:10716984};
Temperature dependence:
Optimum temperature is 30 degrees Celsius.
{ECO:0000269|PubMed:10716984};
-!- PATHWAY: Genetic information processing; DNA replication.
-!- SUBUNIT: Heterotetramer of two large (R1) and two small (R2)
subunits. S.cerevisiae has two different R1 subunits (RNR1 and
RNR3) and two different R2 subunits (RNR2 and RNR4). The
functional form of the small subunits is a RNR2-RNR4 heterodimer,
where RNR2 provides the iron-radical center and RNR4 is required
for proper folding of RNR2 and assembly with the large subunits.
Under normal growth conditions, the active form of the large
subunits is a homodimer of the constitutively expressed RNR1. In
damaged cells or cells arrested for DNA synthesis, the reductase
consists of multiple species because of the association of the
small subunits (RNR2-RNR4) with either the RNR1 homodimer or a
heterodimer of RNR1 and the damage-inducible RNR3. RNR1 interacts
with the ribonucleotide reductase inhibitor SML1.
{ECO:0000269|PubMed:10593972, ECO:0000269|PubMed:10716984,
ECO:0000269|PubMed:16537480, ECO:0000269|PubMed:18610997}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-15234, EBI-15234;
P09938:RNR2; NbExp=5; IntAct=EBI-15234, EBI-15240;
P49723:RNR4; NbExp=5; IntAct=EBI-15234, EBI-15251;
Q04964:SML1; NbExp=4; IntAct=EBI-15234, EBI-27834;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12732713}.
-!- INDUCTION: Cell cycle-regulated with highest activity in S phase.
Moderately induced by DNA-damage. {ECO:0000269|PubMed:2199320}.
-!- MISCELLANEOUS: Two distinct regulatory sites have been defined:
the specificity site, which controls substrate specificity, and
the activity site which regulates overall catalytic activity. A
substrate-binding catalytic site, located on R1, is formed only in
the presence of the second subunit R2 (By similarity).
{ECO:0000250}.
-!- MISCELLANEOUS: Present with 293000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
large chain family. {ECO:0000305}.
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EMBL; U18813; AAB64606.1; -; Genomic_DNA.
EMBL; X69216; CAA49150.1; -; Genomic_DNA.
EMBL; X69217; CAA49151.1; -; Genomic_DNA.
EMBL; BK006939; DAA07729.1; -; Genomic_DNA.
PIR; S50573; S50573.
RefSeq; NP_010993.1; NM_001178961.1.
PDB; 1ZYZ; X-ray; 2.90 A; A/B=1-888.
PDB; 1ZZD; X-ray; 2.60 A; A=1-888.
PDB; 2CVS; X-ray; 2.60 A; A=1-888.
PDB; 2CVT; X-ray; 3.20 A; A=1-888.
PDB; 2CVU; X-ray; 2.90 A; A=1-888.
PDB; 2CVV; X-ray; 2.90 A; A=1-888.
PDB; 2CVW; X-ray; 2.40 A; A=1-888.
PDB; 2CVX; X-ray; 2.20 A; A=1-888.
PDB; 2CVY; X-ray; 2.40 A; A=1-888.
PDB; 2EUD; X-ray; 2.30 A; A=1-888.
PDB; 2ZLF; X-ray; 2.59 A; A=1-888.
PDB; 2ZLG; X-ray; 2.52 A; A=1-888.
PDB; 3K8T; X-ray; 2.10 A; A=1-888.
PDB; 3PAW; X-ray; 6.61 A; A/B/C/D=1-888.
PDB; 3RSR; X-ray; 2.30 A; A=1-888.
PDB; 3S87; X-ray; 2.25 A; A=1-888.
PDB; 3S8A; X-ray; 2.90 A; A=1-888.
PDB; 3S8B; X-ray; 2.80 A; A=1-888.
PDB; 3S8C; X-ray; 2.77 A; A=1-888.
PDB; 3TB9; X-ray; 2.53 A; A=1-888.
PDB; 3TBA; X-ray; 2.80 A; A=1-888.
PDBsum; 1ZYZ; -.
PDBsum; 1ZZD; -.
PDBsum; 2CVS; -.
PDBsum; 2CVT; -.
PDBsum; 2CVU; -.
PDBsum; 2CVV; -.
PDBsum; 2CVW; -.
PDBsum; 2CVX; -.
PDBsum; 2CVY; -.
PDBsum; 2EUD; -.
PDBsum; 2ZLF; -.
PDBsum; 2ZLG; -.
PDBsum; 3K8T; -.
PDBsum; 3PAW; -.
PDBsum; 3RSR; -.
PDBsum; 3S87; -.
PDBsum; 3S8A; -.
PDBsum; 3S8B; -.
PDBsum; 3S8C; -.
PDBsum; 3TB9; -.
PDBsum; 3TBA; -.
ProteinModelPortal; P21524; -.
SMR; P21524; -.
BioGrid; 36813; 71.
DIP; DIP-6299N; -.
IntAct; P21524; 13.
MINT; MINT-680321; -.
STRING; 4932.YER070W; -.
iPTMnet; P21524; -.
MaxQB; P21524; -.
PRIDE; P21524; -.
EnsemblFungi; YER070W; YER070W; YER070W.
GeneID; 856801; -.
KEGG; sce:YER070W; -.
EuPathDB; FungiDB:YER070W; -.
SGD; S000000872; RNR1.
GeneTree; ENSGT00390000001372; -.
HOGENOM; HOG000057035; -.
InParanoid; P21524; -.
KO; K10807; -.
OMA; DRYFLHI; -.
OrthoDB; EOG092C0QYB; -.
BioCyc; MetaCyc:YER070W-MONOMER; -.
BioCyc; YEAST:YER070W-MONOMER; -.
BRENDA; 1.17.4.1; 984.
UniPathway; UPA00326; -.
EvolutionaryTrace; P21524; -.
PRO; PR:P21524; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000166; F:nucleotide binding; IDA:SGD.
GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:SGD.
GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:SGD.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
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; Allosteric enzyme; ATP-binding; Complete proteome;
Cytoplasm; Disulfide bond; DNA replication; Isopeptide bond;
Nucleotide-binding; Oxidoreductase; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 888 Ribonucleoside-diphosphate reductase
large chain 1.
/FTId=PRO_0000187203.
DOMAIN 1 92 ATP-cone. {ECO:0000255|PROSITE-
ProRule:PRU00492}.
REGION 11 17 Allosteric activator binding.
{ECO:0000250}.
REGION 217 218 Substrate binding.
REGION 285 288 Allosteric effector binding, determines
substrate specificity.
REGION 426 430 Substrate binding.
REGION 607 611 Substrate binding.
ACT_SITE 426 426 Proton acceptor.
ACT_SITE 428 428 Cysteine radical intermediate.
ACT_SITE 430 430 Proton acceptor.
BINDING 5 5 Allosteric activator. {ECO:0000250}.
BINDING 53 53 Allosteric activator. {ECO:0000250}.
BINDING 88 88 Allosteric activator. {ECO:0000250}.
BINDING 202 202 Substrate.
BINDING 247 247 Substrate; via amide nitrogen.
SITE 218 218 Important for hydrogen atom transfer.
{ECO:0000250}.
SITE 226 226 Allosteric effector binding, determines
substrate specificity.
SITE 256 256 Allosteric effector binding, determines
substrate specificity.
SITE 443 443 Important for hydrogen atom transfer.
{ECO:0000250}.
SITE 741 741 Important for electron transfer.
{ECO:0000250}.
SITE 742 742 Important for electron transfer.
{ECO:0000250}.
SITE 883 883 Interacts with thioredoxin/glutaredoxin.
{ECO:0000250}.
SITE 886 886 Interacts with thioredoxin/glutaredoxin.
{ECO:0000250}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 816 816 Phosphoserine.
{ECO:0000250|UniProtKB:P21672}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 887 887 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
DISULFID 218 443 Redox-active.
{ECO:0000269|PubMed:16537479}.
CROSSLNK 387 387 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 853 853 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 428 428 C->A: Completely abolishes reductase
activity. {ECO:0000269|PubMed:11893751}.
CONFLICT 329 329 F -> L (in Ref. 4; CAA49151).
{ECO:0000305}.
CONFLICT 587 589 TLR -> NLK (in Ref. 4; CAA49150).
{ECO:0000305}.
CONFLICT 666 666 Q -> E (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 679 679 E -> Q (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
HELIX 19 23 {ECO:0000244|PDB:1ZYZ}.
TURN 31 33 {ECO:0000244|PDB:1ZYZ}.
HELIX 36 41 {ECO:0000244|PDB:1ZYZ}.
HELIX 53 66 {ECO:0000244|PDB:1ZYZ}.
TURN 67 70 {ECO:0000244|PDB:1ZYZ}.
HELIX 79 89 {ECO:0000244|PDB:2CVX}.
HELIX 94 102 {ECO:0000244|PDB:3K8T}.
TURN 107 110 {ECO:0000244|PDB:3K8T}.
HELIX 118 126 {ECO:0000244|PDB:3K8T}.
HELIX 128 132 {ECO:0000244|PDB:3K8T}.
HELIX 137 142 {ECO:0000244|PDB:3K8T}.
HELIX 145 154 {ECO:0000244|PDB:3K8T}.
STRAND 158 163 {ECO:0000244|PDB:2CVX}.
HELIX 167 179 {ECO:0000244|PDB:3K8T}.
HELIX 183 194 {ECO:0000244|PDB:3K8T}.
STRAND 197 200 {ECO:0000244|PDB:3K8T}.
HELIX 202 207 {ECO:0000244|PDB:3K8T}.
STRAND 210 212 {ECO:0000244|PDB:3K8T}.
STRAND 218 222 {ECO:0000244|PDB:3K8T}.
HELIX 228 242 {ECO:0000244|PDB:3K8T}.
TURN 243 245 {ECO:0000244|PDB:3S8A}.
STRAND 247 251 {ECO:0000244|PDB:3K8T}.
TURN 263 266 {ECO:0000244|PDB:3K8T}.
HELIX 272 285 {ECO:0000244|PDB:3K8T}.
TURN 288 291 {ECO:0000244|PDB:2CVX}.
STRAND 297 301 {ECO:0000244|PDB:3K8T}.
HELIX 308 311 {ECO:0000244|PDB:3K8T}.
TURN 312 315 {ECO:0000244|PDB:3K8T}.
STRAND 317 319 {ECO:0000244|PDB:3K8T}.
HELIX 321 323 {ECO:0000244|PDB:2CVX}.
STRAND 328 334 {ECO:0000244|PDB:3K8T}.
HELIX 336 343 {ECO:0000244|PDB:3K8T}.
STRAND 347 351 {ECO:0000244|PDB:3K8T}.
TURN 353 355 {ECO:0000244|PDB:3K8T}.
HELIX 359 361 {ECO:0000244|PDB:3K8T}.
HELIX 364 376 {ECO:0000244|PDB:3K8T}.
STRAND 380 384 {ECO:0000244|PDB:3K8T}.
HELIX 385 399 {ECO:0000244|PDB:3K8T}.
STRAND 403 406 {ECO:0000244|PDB:3K8T}.
HELIX 407 412 {ECO:0000244|PDB:3K8T}.
TURN 415 419 {ECO:0000244|PDB:3K8T}.
STRAND 427 429 {ECO:0000244|PDB:1ZYZ}.
STRAND 441 443 {ECO:0000244|PDB:3K8T}.
STRAND 445 449 {ECO:0000244|PDB:3K8T}.
HELIX 450 453 {ECO:0000244|PDB:3K8T}.
STRAND 454 456 {ECO:0000244|PDB:2CVX}.
STRAND 458 462 {ECO:0000244|PDB:2EUD}.
STRAND 463 465 {ECO:0000244|PDB:2CVX}.
HELIX 467 487 {ECO:0000244|PDB:3K8T}.
HELIX 493 502 {ECO:0000244|PDB:3K8T}.
STRAND 506 510 {ECO:0000244|PDB:3K8T}.
HELIX 512 519 {ECO:0000244|PDB:3K8T}.
HELIX 526 554 {ECO:0000244|PDB:3K8T}.
HELIX 564 567 {ECO:0000244|PDB:3K8T}.
HELIX 571 574 {ECO:0000244|PDB:3K8T}.
STRAND 581 583 {ECO:0000244|PDB:2ZLG}.
HELIX 585 595 {ECO:0000244|PDB:3K8T}.
HELIX 611 615 {ECO:0000244|PDB:3K8T}.
STRAND 619 622 {ECO:0000244|PDB:2CVS}.
STRAND 627 629 {ECO:0000244|PDB:2CVX}.
STRAND 634 636 {ECO:0000244|PDB:1ZYZ}.
STRAND 638 641 {ECO:0000244|PDB:1ZYZ}.
HELIX 643 651 {ECO:0000244|PDB:3K8T}.
HELIX 657 664 {ECO:0000244|PDB:3K8T}.
TURN 665 668 {ECO:0000244|PDB:3K8T}.
HELIX 678 683 {ECO:0000244|PDB:3K8T}.
HELIX 687 689 {ECO:0000244|PDB:3K8T}.
HELIX 692 703 {ECO:0000244|PDB:3K8T}.
STRAND 714 718 {ECO:0000244|PDB:2CVX}.
HELIX 721 734 {ECO:0000244|PDB:3K8T}.
STRAND 737 741 {ECO:0000244|PDB:3K8T}.
STRAND 743 745 {ECO:0000244|PDB:2CVX}.
TURN 748 751 {ECO:0000244|PDB:1ZYZ}.
HELIX 760 763 {ECO:0000244|PDB:1ZYZ}.
HELIX 764 766 {ECO:0000244|PDB:1ZYZ}.
TURN 789 791 {ECO:0000244|PDB:1ZYZ}.
SEQUENCE 888 AA; 99561 MW; 56BE1B077916E419 CRC64;
MYVYKRDGRK EPVQFDKITA RISRLCYGLD PKHIDAVKVT QRIISGVYEG VTTIELDNLA
AETCAYMTTV HPDYATLAAR IAISNLHKQT TKQFSKVVED LYRYVNAATG KPAPMISDDV
YNIVMENKDK LNSAIVYDRD FQYSYFGFKT LERSYLLRIN GQVAERPQHL IMRVALGIHG
RDIEAALETY NLMSLKYFTH ASPTLFNAGT PKPQMSSCFL VAMKEDSIEG IYDTLKECAL
ISKTAGGIGL HIHNIRSTGS YIAGTNGTSN GLIPMIRVFN NTARYVDQGG NKRPGAFALY
LEPWHADIFD FIDIRKNHGK EEIRARDLFP ALWIPDLFMK RVEENGTWTL FSPTSAPGLS
DCYGDEFEAL YTRYEKEGRG KTIKAQKLWY SILEAQTETG TPFVVYKDAC NRKSNQKNLG
VIKSSNLCCE IVEYSAPDET AVCNLASVAL PAFIETSEDG KTSTYNFKKL HEIAKVVTRN
LNRVIDRNYY PVEEARKSNM RHRPIALGVQ GLADTFMLLR LPFDSEEARL LNIQIFETIY
HASMEASCEL AQKDGPYETF QGSPASQGIL QFDMWDQKPY GMWDWDTLRK DIMKHGVRNS
LTMAPMPTAS TSQILGYNEC FEPVTSNMYS RRVLSGEFQV VNPYLLRDLV DLGIWDEGMK
QYLITQNGSI QGLPNVPQEL KDLYKTVWEI SQKTIINMAA DRSVYIDQSH SLNLFLRAPT
MGKLTSMHFY GWKKGLKTGM YYLRTQAASA AIQFTIDQKI ADQATENVAD ISNLKRPSYM
PSSASYAASD FVPAAVTANA TIPSLDSSSE ASREASPAPT GSHSLTKGMA ELNVQESKVE
VPEVPAPTKN EEKAAPIVDD EETEFDIYNS KVIACAIDNP EACEMCSG


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