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Database: UniProt
Entry: P11349
LinkDB: P11349
Original site: P11349 
ID   NARH_ECOLI              Reviewed;         512 AA.
AC   P11349;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 3.
DT   10-APR-2019, entry version 182.
DE   RecName: Full=Respiratory nitrate reductase 1 beta chain;
DE            EC=1.7.5.1;
DE   AltName: Full=Nitrate reductase A subunit beta;
DE   AltName: Full=Quinol-nitrate oxidoreductase subunit beta;
GN   Name=narH; OrderedLocusNames=b1225, JW1216;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / TG1;
RX   PubMed=2674654; DOI=10.1007/BF00331275;
RA   Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.;
RT   "Nitrate reductase of Escherichia coli: completion of the nucleotide
RT   sequence of the nar operon and reassessment of the role of the alpha
RT   and beta subunits in iron binding and electron transfer.";
RL   Mol. Gen. Genet. 218:249-256(1989).
RN   [2]
RP   SEQUENCE REVISION TO 398-417.
RC   STRAIN=K12 / TG1;
RA   Blasco F.;
RL   Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-512.
RX   PubMed=2832376; DOI=10.1128/jb.170.4.1721-1729.1988;
RA   Sodergren E.J., Demoss J.A.;
RT   "narI region of the Escherichia coli nitrate reductase (nar) operon
RT   contains two genes.";
RL   J. Bacteriol. 170:1721-1729(1988).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-10.
RX   PubMed=3053688;
RA   Sodergren E.J., Hsu P.Y., Demoss J.A.;
RT   "Roles of the narJ and narI gene products in the expression of nitrate
RT   reductase in Escherichia coli.";
RL   J. Biol. Chem. 263:16156-16162(1988).
RN   [8]
RP   EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
RX   PubMed=1321049; DOI=10.1111/j.1432-1033.1992.tb17020.x;
RA   Guigliarelli B., Asso M., More C., Augier V., Blasco F., Pommier J.,
RA   Giordano G., Bertrand P.;
RT   "EPR and redox characterization of iron-sulfur centers in nitrate
RT   reductases A and Z from Escherichia coli. Evidence for a high-
RT   potential and a low-potential class and their relevance in the
RT   electron-transfer mechanism.";
RL   Eur. J. Biochem. 207:61-68(1992).
RN   [9]
RP   MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
RP   CLUSTERS.
RX   PubMed=8383531; DOI=10.1021/bi00059a018;
RA   Augier V., Guigliarelli B., Asso M., Bertrand P., Frixon C.,
RA   Giordano G., Chippaux M., Blasco F.;
RT   "Site-directed mutagenesis of conserved cysteine residues within the
RT   beta subunit of Escherichia coli nitrate reductase. Physiological,
RT   biochemical, and EPR characterization of the mutated enzymes.";
RL   Biochemistry 32:2013-2023(1993).
RN   [10]
RP   MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
RP   CLUSTERS.
RX   PubMed=8388253; DOI=10.1021/bi00070a018;
RA   Augier V., Asso M., Guigliarelli B., More C., Bertrand P.,
RA   Santini C.-L., Blasco F., Chippaux M., Giordano G.;
RT   "Removal of the high-potential [4Fe-4S] center of the beta-subunit
RT   from Escherichia coli nitrate reductase. Physiological, biochemical,
RT   and EPR characterization of site-directed mutated enzymes.";
RL   Biochemistry 32:5099-5108(1993).
RN   [11]
RP   MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
RP   CLUSTERS.
RX   PubMed=8664273; DOI=10.1021/bi952459p;
RA   Guigliarelli B., Magalon A., Asso M., Bertrand P., Frixon C.,
RA   Giordano G., Blasco F.;
RT   "Complete coordination of the four Fe-S centers of the beta subunit
RT   from Escherichia coli nitrate reductase. Physiological, biochemical,
RT   and EPR characterization of site-directed mutants lacking the highest
RT   or lowest potential [4Fe-4S] clusters.";
RL   Biochemistry 35:4828-4836(1996).
RN   [12]
RP   EPR SPECTROSCOPY, AND REDOX POTENTIOMETRY OF IRON-SULFUR CLUSTERS.
RX   PubMed=9516445; DOI=10.1074/jbc.273.13.7462;
RA   Rothery R.A., Magalon A., Giordano G., Guigliarelli B., Blasco F.,
RA   Weiner J.H.;
RT   "The molybdenum cofactor of Escherichia coli nitrate reductase A
RT   (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S]
RT   clusters.";
RL   J. Biol. Chem. 273:7462-7469(1998).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP   (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, AND SUBUNIT.
RX   PubMed=12910261; DOI=10.1038/nsb969;
RA   Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F.,
RA   Weiner J.H., Strynadka N.C.J.;
RT   "Insights into the respiratory electron transfer pathway from the
RT   structure of nitrate reductase A.";
RL   Nat. Struct. Biol. 10:681-687(2003).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP   (3FE-4S) AND IRON-SULFUR (4FE-4S), AND COFACTOR.
RX   PubMed=14725769; DOI=10.1016/j.str.2003.11.020;
RA   Jormakka M., Richardson D., Byrne B., Iwata S.;
RT   "Architecture of NarGH reveals a structural classification of Mo-
RT   bisMGD enzymes.";
RL   Structure 12:95-104(2004).
CC   -!- FUNCTION: The nitrate reductase enzyme complex allows E.coli to
CC       use nitrate as an electron acceptor during anaerobic growth. The
CC       beta chain is an electron transfer unit containing four cysteine
CC       clusters involved in the formation of iron-sulfur centers.
CC       Electrons are transferred from the gamma chain to the molybdenum
CC       cofactor of the alpha subunit.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC         Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC         ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124;
CC         EC=1.7.5.1;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:12910261,
CC         ECO:0000269|PubMed:14725769};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit.
CC       {ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000269|PubMed:12910261,
CC         ECO:0000269|PubMed:14725769};
CC       Note=Binds 1 [3Fe-4S] cluster per subunit.
CC       {ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769};
CC   -!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta
CC       and a gamma chain. Alpha and beta are catalytic chains; gamma
CC       chains are involved in binding the enzyme complex to the
CC       cytoplasmic membrane. {ECO:0000269|PubMed:12910261}.
CC   -!- INTERACTION:
CC       P42593:fadH; NbExp=3; IntAct=EBI-555067, EBI-561933;
CC       P09152:narG; NbExp=13; IntAct=EBI-555067, EBI-547248;
CC       P19317:narW; NbExp=3; IntAct=EBI-555067, EBI-555088;
CC       P19318:narY; NbExp=3; IntAct=EBI-555067, EBI-555059;
CC       P19319:narZ; NbExp=6; IntAct=EBI-555067, EBI-547262;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By nitrate.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="http://www.worthington-biochem.com/NAR/";
DR   EMBL; M20147; AAA24195.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74309.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA36095.1; -; Genomic_DNA.
DR   EMBL; X16181; CAA34304.1; -; Genomic_DNA.
DR   PIR; F64869; RDECNB.
DR   RefSeq; NP_415743.1; NC_000913.3.
DR   RefSeq; WP_000702650.1; NZ_LN832404.1.
DR   PDB; 1Q16; X-ray; 1.90 A; B=1-512.
DR   PDB; 1R27; X-ray; 2.00 A; B/D=1-512.
DR   PDB; 1SIW; X-ray; 2.20 A; B=1-512.
DR   PDB; 1Y4Z; X-ray; 2.00 A; B=1-512.
DR   PDB; 1Y5I; X-ray; 1.90 A; B=1-512.
DR   PDB; 1Y5L; X-ray; 2.50 A; B=1-512.
DR   PDB; 1Y5N; X-ray; 2.50 A; B=1-512.
DR   PDB; 3EGW; X-ray; 1.90 A; B=1-509.
DR   PDB; 3IR5; X-ray; 2.30 A; B=1-512.
DR   PDB; 3IR6; X-ray; 2.80 A; B=1-512.
DR   PDB; 3IR7; X-ray; 2.50 A; B=1-512.
DR   PDBsum; 1Q16; -.
DR   PDBsum; 1R27; -.
DR   PDBsum; 1SIW; -.
DR   PDBsum; 1Y4Z; -.
DR   PDBsum; 1Y5I; -.
DR   PDBsum; 1Y5L; -.
DR   PDBsum; 1Y5N; -.
DR   PDBsum; 3EGW; -.
DR   PDBsum; 3IR5; -.
DR   PDBsum; 3IR6; -.
DR   PDBsum; 3IR7; -.
DR   ProteinModelPortal; P11349; -.
DR   SMR; P11349; -.
DR   BioGrid; 4262231; 28.
DR   ComplexPortal; CPX-1974; Nitrate reductase A complex.
DR   DIP; DIP-10312N; -.
DR   IntAct; P11349; 15.
DR   STRING; 511145.b1225; -.
DR   DrugBank; DB04464; N-Formylmethionine.
DR   TCDB; 5.A.3.1.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   jPOST; P11349; -.
DR   PaxDb; P11349; -.
DR   PRIDE; P11349; -.
DR   EnsemblBacteria; AAC74309; AAC74309; b1225.
DR   EnsemblBacteria; BAA36095; BAA36095; BAA36095.
DR   GeneID; 945780; -.
DR   KEGG; ecj:JW1216; -.
DR   KEGG; eco:b1225; -.
DR   PATRIC; fig|1411691.4.peg.1056; -.
DR   EchoBASE; EB0633; -.
DR   EcoGene; EG10639; narH.
DR   eggNOG; ENOG4108IUE; Bacteria.
DR   eggNOG; COG1140; LUCA.
DR   HOGENOM; HOG000237353; -.
DR   InParanoid; P11349; -.
DR   KO; K00371; -.
DR   PhylomeDB; P11349; -.
DR   BioCyc; EcoCyc:NARH-MONOMER; -.
DR   BioCyc; ECOL316407:JW1216-MONOMER; -.
DR   BioCyc; MetaCyc:NARH-MONOMER; -.
DR   BRENDA; 1.7.5.1; 2026.
DR   EvolutionaryTrace; P11349; -.
DR   PRO; PR:P11349; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0031224; C:intrinsic component of membrane; IDA:EcoCyc.
DR   GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0044799; C:NarGHI complex; IDA:EcoCyc.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008940; F:nitrate reductase activity; IMP:EcoCyc.
DR   GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0042126; P:nitrate metabolic process; IMP:EcoCyc.
DR   CDD; cd10557; NarH_beta-like; 1.
DR   Gene3D; 1.10.3650.10; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR029263; Nitr_red_bet_C.
DR   InterPro; IPR038262; Nitr_red_bet_C_sf.
DR   InterPro; IPR006547; NO3_Rdtase_bsu.
DR   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF14711; Nitr_red_bet_C; 1.
DR   TIGRFAMs; TIGR01660; narH; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; 3Fe-4S; 4Fe-4S; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN         1    512       Respiratory nitrate reductase 1 beta
FT                                chain.
FT                                /FTId=PRO_0000096720.
FT   DOMAIN        7     35       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      175    206       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      208    237       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        16     16       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL        19     19       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL        22     22       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL        26     26       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       184    184       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       187    187       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       192    192       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       196    196       Iron-sulfur 4 (3Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       217    217       Iron-sulfur 4 (3Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       223    223       Iron-sulfur 4 (3Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       227    227       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       244    244       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       247    247       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       259    259       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   METAL       263    263       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:12910261,
FT                                ECO:0000269|PubMed:14725769}.
FT   CONFLICT    398    417       DTKPVLRALKRMLAMRHYKR -> EYQTGTARTETYAGDAS
FT                                LQT (in Ref. 6; AAA24195). {ECO:0000305}.
FT   STRAND        3     12       {ECO:0000244|PDB:1Q16}.
FT   TURN         13     15       {ECO:0000244|PDB:1Q16}.
FT   HELIX        21     30       {ECO:0000244|PDB:1Q16}.
FT   STRAND       41     49       {ECO:0000244|PDB:1Q16}.
FT   TURN         51     57       {ECO:0000244|PDB:1Q16}.
FT   HELIX        59     62       {ECO:0000244|PDB:1Q16}.
FT   STRAND       65     68       {ECO:0000244|PDB:1Q16}.
FT   STRAND       74     76       {ECO:0000244|PDB:1Q16}.
FT   HELIX        81     85       {ECO:0000244|PDB:1Q16}.
FT   TURN         86     89       {ECO:0000244|PDB:1Q16}.
FT   HELIX        97    100       {ECO:0000244|PDB:1Q16}.
FT   STRAND      104    106       {ECO:0000244|PDB:1Q16}.
FT   HELIX       109    113       {ECO:0000244|PDB:1Q16}.
FT   STRAND      126    128       {ECO:0000244|PDB:1Q16}.
FT   TURN        129    131       {ECO:0000244|PDB:1Q16}.
FT   TURN        142    148       {ECO:0000244|PDB:1Q16}.
FT   HELIX       152    155       {ECO:0000244|PDB:1Q16}.
FT   HELIX       159    161       {ECO:0000244|PDB:1Q16}.
FT   HELIX       167    170       {ECO:0000244|PDB:1Q16}.
FT   HELIX       172    174       {ECO:0000244|PDB:1Q16}.
FT   STRAND      178    182       {ECO:0000244|PDB:1Q16}.
FT   HELIX       191    194       {ECO:0000244|PDB:1Q16}.
FT   STRAND      201    204       {ECO:0000244|PDB:1Q16}.
FT   TURN        205    207       {ECO:0000244|PDB:1Q16}.
FT   STRAND      210    212       {ECO:0000244|PDB:1Q16}.
FT   TURN        214    216       {ECO:0000244|PDB:1Q16}.
FT   HELIX       223    226       {ECO:0000244|PDB:1Q16}.
FT   STRAND      232    235       {ECO:0000244|PDB:1Q16}.
FT   TURN        236    239       {ECO:0000244|PDB:1Q16}.
FT   STRAND      240    243       {ECO:0000244|PDB:1Q16}.
FT   HELIX       248    251       {ECO:0000244|PDB:1Q16}.
FT   TURN        252    254       {ECO:0000244|PDB:1Q16}.
FT   HELIX       258    261       {ECO:0000244|PDB:1Q16}.
FT   STRAND      268    276       {ECO:0000244|PDB:1Q16}.
FT   HELIX       277    279       {ECO:0000244|PDB:1Q16}.
FT   HELIX       280    284       {ECO:0000244|PDB:1Q16}.
FT   HELIX       289    291       {ECO:0000244|PDB:1Q16}.
FT   HELIX       292    297       {ECO:0000244|PDB:1Q16}.
FT   HELIX       306    314       {ECO:0000244|PDB:1Q16}.
FT   HELIX       319    325       {ECO:0000244|PDB:1Q16}.
FT   HELIX       329    334       {ECO:0000244|PDB:1Q16}.
FT   STRAND      341    343       {ECO:0000244|PDB:1Q16}.
FT   HELIX       345    347       {ECO:0000244|PDB:1Q16}.
FT   STRAND      352    356       {ECO:0000244|PDB:1Q16}.
FT   STRAND      366    368       {ECO:0000244|PDB:1Q16}.
FT   HELIX       380    382       {ECO:0000244|PDB:1Q16}.
FT   STRAND      383    385       {ECO:0000244|PDB:1Q16}.
FT   HELIX       387    394       {ECO:0000244|PDB:1Q16}.
FT   HELIX       399    420       {ECO:0000244|PDB:1Q16}.
FT   HELIX       428    432       {ECO:0000244|PDB:1Q16}.
FT   HELIX       437    447       {ECO:0000244|PDB:1Q16}.
FT   HELIX       452    455       {ECO:0000244|PDB:1Q16}.
FT   TURN        463    466       {ECO:0000244|PDB:1Q16}.
FT   HELIX       469    475       {ECO:0000244|PDB:1Q16}.
SQ   SEQUENCE   512 AA;  58066 MW;  2E7719C8D078BAEA CRC64;
     MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ GFPTDWENQE
     KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY YEPFDFDYQN LHTAPEGSKS
     QPIARPRSLI TGERMAKIEK GPNWEDDLGG EFDKLAKDKN FDNIQKAMYS QFENTFMMYL
     PRLCEHCLNP ACVATCPSGA IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK
     SEKCIFCYPR IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF
     LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL PMVWYVPPLS
     PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK PVLRALKRML AMRHYKRAET
     VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA NYEDRFVVPS SHRELAREAF PEKNGCGFTF
     GDGCHGSDTK FNLFNSRRID AIDVTSKTEP HP
//
DBGET integrated database retrieval system