ID NRFA_ECOLI Reviewed; 478 AA. AC P0ABK9; P32050; Q2M6N4; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 29-APR-2015, entry version 88. DE RecName: Full=Cytochrome c-552 {ECO:0000303|PubMed:7934939}; DE EC=1.7.2.2 {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:9593308}; DE AltName: Full=Ammonia-forming cytochrome c nitrite reductase; DE Short=Cytochrome c nitrite reductase {ECO:0000303|PubMed:11863430}; DE Flags: Precursor; GN Name=nrfA; OrderedLocusNames=b4070, JW4031; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-42 AND RP 150-167, FUNCTION, SUBCELLULAR LOCATION, COFACTOR, AND INDUCTION. RC STRAIN=K12; RX PubMed=7934939; DOI=10.1111/j.1365-2958.1993.tb01255.x; RA Darwin A., Hussain H.A., Griffiths L., Grove J., Sambongi Y., RA Busby S., Cole J.; RT "Regulation and sequence of the structural gene for cytochrome c552 RT from Escherichia coli: not a hexahaem but a 50 kDa tetrahaem nitrite RT reductase."; RL Mol. Microbiol. 9:1255-1265(1993). RN [2] 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., RA Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the RT region from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). 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., RA Mau B., 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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP CHARACTERIZATION AS A CYTOCHROME C. RX PubMed=8039676; DOI=10.1111/j.1574-6968.1994.tb06872.x; RA Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H., RA Pommier J., Mejean V., Cole J.A.; RT "A reassessment of the range of c-type cytochromes synthesized by RT Escherichia coli K-12."; RL FEMS Microbiol. Lett. 119:89-94(1994). RN [6] RP HEME-BINDING, COFACTOR, MASS SPECTROMETRY, MUTAGENESIS OF LYS-126, RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=9593308; DOI=10.1046/j.1365-2958.1998.00792.x; RA Eaves D.J., Grove J., Staudenmann W., James P., Poole R.K., RA White S.A., Griffiths I., Cole J.A.; RT "Involvement of products of the nrfEFG genes in the covalent RT attachment of haem c to a novel cysteine-lysine motif in the RT cytochrome c552 nitrite reductase from Escherichia coli."; RL Mol. Microbiol. 28:205-216(1998). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM AND RP HEME, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RP SUBCELLULAR LOCATION, MAGNETIC CIRCULAR DICHROISM, AND EPR RP SPECTROSCOPY. RX PubMed=11863430; DOI=10.1021/bi015765d; RA Bamford V.A., Angove H.C., Seward H.E., Thomson A.J., Cole J.A., RA Butt J.N., Hemmings A.M., Richardson D.J.; RT "Structure and spectroscopy of the periplasmic cytochrome c nitrite RT reductase from Escherichia coli."; RL Biochemistry 41:2921-2931(2002). RN [8] {ECO:0000244|PDB:2RDZ, ECO:0000244|PDB:2RF7} RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 27-478 IN COMPLEX WITH RP CALCIUM AND HEME, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF RP GLN-263. RX PubMed=18311941; DOI=10.1021/bi702175w; RA Clarke T.A., Kemp G.L., Van Wonderen J.H., Doyle R.M., Cole J.A., RA Tovell N., Cheesman M.R., Butt J.N., Richardson D.J., Hemmings A.M.; RT "Role of a conserved glutamine residue in tuning the catalytic RT activity of Escherichia coli cytochrome c nitrite reductase."; RL Biochemistry 47:3789-3799(2008). RN [9] {ECO:0000244|PDB:3L1T} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 27-478 IN COMPLEX WITH RP CALCIUM; HEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, FUNCTION, RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND COFACTOR. RX PubMed=20629638; DOI=10.1042/BJ20100866; RA Kemp G.L., Clarke T.A., Marritt S.J., Lockwood C., Poock S.R., RA Hemmings A.M., Richardson D.J., Cheesman M.R., Butt J.N.; RT "Kinetic and thermodynamic resolution of the interactions between RT sulfite and the pentahaem cytochrome NrfA from Escherichia coli."; RL Biochem. J. 431:73-80(2010). RN [10] {ECO:0000244|PDB:3TOR} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 27-478 IN COMPLEX WITH RP CALCIUM AND HEME, AND COFACTOR. RX PubMed=22103542; DOI=10.1042/BST20110731; RA Lockwood C.W., Clarke T.A., Butt J.N., Hemmings A.M., Richardson D.J.; RT "Characterization of the active site and calcium binding in cytochrome RT c nitrite reductases."; RL Biochem. Soc. Trans. 39:1871-1875(2011). CC -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming CC six electrons in the process (PubMed:9593308, PubMed:11863430, CC PubMed:18311941, PubMed:20629638). Has very low activity toward CC hydroxylamine (PubMed:11863430). Has even lower activity toward CC sulfite (PubMed:20629638). Sulfite reductase activity is maximal CC at neutral pH (By similarity). {ECO:0000250|UniProtKB:L0DSL2, CC ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, CC ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:9593308, CC ECO:0000305|PubMed:7934939}. CC -!- CATALYTIC ACTIVITY: NH(3) + 2 H(2)O + 6 ferricytochrome c = CC nitrite + 6 ferrocytochrome c + 7 H(+). CC {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, CC ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:9593308}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:11863430, CC ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638, CC ECO:0000269|PubMed:22103542}; CC Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000269|PubMed:11863430, CC ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638, CC ECO:0000269|PubMed:22103542}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000269|PubMed:11863430, CC ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638, CC ECO:0000269|PubMed:22103542, ECO:0000269|PubMed:7934939, CC ECO:0000269|PubMed:9593308}; CC Note=Binds 5 heme groups covalently per monomer. CC {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, CC ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:22103542}; CC -!- ENZYME REGULATION: Subject to competitive inhibition by sulfite. CC {ECO:0000269|PubMed:20629638}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=28 uM for nitrite. {ECO:0000269|PubMed:11863430}; CC KM=30 uM for nitrite. {ECO:0000269|PubMed:18311941}; CC KM=22 uM for nitrite. {ECO:0000269|PubMed:20629638}; CC KM=70 uM for sulfite. {ECO:0000269|PubMed:20629638}; CC KM=30 mM for hydroxylamine. {ECO:0000269|PubMed:11863430}; CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). CC {ECO:0000305|PubMed:7934939}. CC -!- SUBUNIT: Homodimer (PubMed:11863430, PubMed:18311941). Component CC of a membrane-associated heterooligomeric complex (Probable). CC {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, CC ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11863430, CC ECO:0000269|PubMed:7934939}. CC -!- INDUCTION: Full induction attained in the presence of nitrite. CC Subject to glucose and nitrate repression. CC {ECO:0000269|PubMed:7934939}. CC -!- MASS SPECTROMETRY: Mass=53590; Method=MALDI; Range=27-478; CC Evidence={ECO:0000269|PubMed:9593308}; CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. {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; X72298; CAA51048.1; -; Genomic_DNA. DR EMBL; U00006; AAC43164.1; -; Genomic_DNA. DR EMBL; U00096; AAC77040.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78072.1; -; Genomic_DNA. DR PIR; S39590; S39590. DR RefSeq; NP_418494.1; NC_000913.3. DR RefSeq; YP_492213.1; NC_007779.1. DR PDB; 1GU6; X-ray; 2.50 A; A/C/E/G=27-478. DR PDB; 2RDZ; X-ray; 1.74 A; A/B/C/D=27-478. DR PDB; 2RF7; X-ray; 2.04 A; A/B/C/D=37-477. DR PDB; 3L1T; X-ray; 2.30 A; A/B/C/D=27-478. DR PDB; 3TOR; X-ray; 2.00 A; A/B/C/D=27-478. DR PDB; 4WJY; X-ray; 2.15 A; A/B=27-478. DR PDBsum; 1GU6; -. DR PDBsum; 2RDZ; -. DR PDBsum; 2RF7; -. DR PDBsum; 3L1T; -. DR PDBsum; 3TOR; -. DR PDBsum; 4WJY; -. DR ProteinModelPortal; P0ABK9; -. DR SMR; P0ABK9; 37-477. DR DIP; DIP-36021N; -. DR IntAct; P0ABK9; 3. DR STRING; 511145.b4070; -. DR PaxDb; P0ABK9; -. DR PRIDE; P0ABK9; -. DR EnsemblBacteria; AAC77040; AAC77040; b4070. DR EnsemblBacteria; BAE78072; BAE78072; BAE78072. DR GeneID; 12930411; -. DR GeneID; 948571; -. DR KEGG; ecj:Y75_p3957; -. DR KEGG; eco:b4070; -. DR PATRIC; 32123689; VBIEscCol129921_4193. DR EchoBASE; EB1729; -. DR EcoGene; EG11781; nrfA. DR eggNOG; COG3303; -. DR HOGENOM; HOG000278511; -. DR InParanoid; P0ABK9; -. DR KO; K03385; -. DR OMA; CHEKGKS; -. DR OrthoDB; EOG6K3ZWZ; -. DR PhylomeDB; P0ABK9; -. DR BioCyc; EcoCyc:CYTOCHROMEC552-MONOMER; -. DR BioCyc; ECOL316407:JW4031-MONOMER; -. DR BioCyc; MetaCyc:CYTOCHROMEC552-MONOMER; -. DR BRENDA; 1.7.2.2; 2026. DR UniPathway; UPA00653; -. DR EvolutionaryTrace; P0ABK9; -. DR PRO; PR:P0ABK9; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR Genevestigator; P0ABK9; -. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0020037; F:heme binding; IDA:EcoCyc. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016966; F:nitric oxide reductase activity; IDA:CACAO. DR GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IDA:EcoCyc. DR GO; GO:0019645; P:anaerobic electron transport chain; IMP:EcoCyc. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.710.10; -; 1. DR HAMAP; MF_01182; Cytochrom_C552; 1. DR InterPro; IPR023155; Cyt_c-552/4. DR InterPro; IPR003321; Cyt_c552. DR InterPro; IPR017570; Cyt_c_NO2Rdtase_formate-dep. DR InterPro; IPR011031; Multihaem_cyt. DR Pfam; PF02335; Cytochrom_C552; 1. DR PIRSF; PIRSF000243; Cyt_c552; 1. DR TIGRFAMs; TIGR03152; cyto_c552_HCOOH; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Complete proteome; Direct protein sequencing; KW Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; KW Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 26 {ECO:0000269|PubMed:7934939}. FT CHAIN 27 478 Cytochrome c-552. FT /FTId=PRO_0000006578. FT METAL 94 94 Iron (heme 3 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 126 126 Iron (heme 1 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 164 164 Iron (heme 2 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 213 213 Iron (heme 3 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 215 215 Calcium. {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 216 216 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 261 261 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 263 263 Calcium. {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 275 275 Iron (heme 5 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 286 286 Iron (heme 4 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 301 301 Iron (heme 2 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 318 318 Iron (heme 5 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT METAL 393 393 Iron (heme 4 axial ligand). FT {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 122 122 Heme 1 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 125 125 Heme 1 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 160 160 Heme 2 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 163 163 Heme 2 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 209 209 Heme 3 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 212 212 Heme 3 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 216 216 Substrate. {ECO:0000305}. FT BINDING 264 264 Substrate. {ECO:0000305}. FT BINDING 282 282 Heme 4 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 285 285 Heme 4 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7}. FT BINDING 314 314 Heme 5 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7, FT ECO:0000244|PDB:3L1T, FT ECO:0000244|PDB:3TOR}. FT BINDING 317 317 Heme 5 (covalent). {ECO:0000244|PDB:1GU6, FT ECO:0000244|PDB:2RDZ, FT ECO:0000244|PDB:2RF7}. FT MUTAGEN 126 126 K->H,I,L: Almost complete loss of nitrite FT reductase activity. FT {ECO:0000269|PubMed:9593308}. FT MUTAGEN 263 263 Q->E: Increases affinity for nitrite FT without changing Vmax. FT {ECO:0000269|PubMed:18311941}. FT HELIX 42 45 {ECO:0000244|PDB:2RDZ}. FT TURN 46 48 {ECO:0000244|PDB:2RDZ}. FT HELIX 50 57 {ECO:0000244|PDB:2RDZ}. FT HELIX 58 61 {ECO:0000244|PDB:2RDZ}. FT HELIX 68 71 {ECO:0000244|PDB:2RDZ}. FT HELIX 74 78 {ECO:0000244|PDB:2RDZ}. FT TURN 79 81 {ECO:0000244|PDB:2RDZ}. FT HELIX 83 85 {ECO:0000244|PDB:2RDZ}. FT HELIX 94 96 {ECO:0000244|PDB:2RDZ}. FT HELIX 97 103 {ECO:0000244|PDB:2RDZ}. FT HELIX 105 107 {ECO:0000244|PDB:2RDZ}. FT STRAND 116 119 {ECO:0000244|PDB:2RDZ}. FT HELIX 120 123 {ECO:0000244|PDB:2RDZ}. FT TURN 124 126 {ECO:0000244|PDB:2RDZ}. FT HELIX 129 137 {ECO:0000244|PDB:2RDZ}. FT HELIX 139 143 {ECO:0000244|PDB:2RDZ}. FT STRAND 144 146 {ECO:0000244|PDB:2RDZ}. FT HELIX 147 150 {ECO:0000244|PDB:2RDZ}. FT TURN 151 153 {ECO:0000244|PDB:2RDZ}. FT HELIX 160 163 {ECO:0000244|PDB:2RDZ}. FT HELIX 169 172 {ECO:0000244|PDB:2RDZ}. FT HELIX 183 191 {ECO:0000244|PDB:2RDZ}. FT HELIX 196 198 {ECO:0000244|PDB:2RDZ}. FT HELIX 201 209 {ECO:0000244|PDB:2RDZ}. FT TURN 210 212 {ECO:0000244|PDB:2RDZ}. FT STRAND 217 219 {ECO:0000244|PDB:2RDZ}. FT TURN 220 223 {ECO:0000244|PDB:2RDZ}. FT STRAND 224 226 {ECO:0000244|PDB:2RDZ}. FT HELIX 235 244 {ECO:0000244|PDB:2RDZ}. FT STRAND 249 251 {ECO:0000244|PDB:2RDZ}. FT TURN 253 255 {ECO:0000244|PDB:2RDZ}. FT HELIX 266 272 {ECO:0000244|PDB:2RDZ}. FT HELIX 274 277 {ECO:0000244|PDB:2RDZ}. FT HELIX 282 286 {ECO:0000244|PDB:2RDZ}. FT STRAND 289 291 {ECO:0000244|PDB:2RDZ}. FT STRAND 297 299 {ECO:0000244|PDB:2RDZ}. FT HELIX 306 312 {ECO:0000244|PDB:2RDZ}. FT HELIX 314 316 {ECO:0000244|PDB:2RDZ}. FT HELIX 322 359 {ECO:0000244|PDB:2RDZ}. FT HELIX 364 385 {ECO:0000244|PDB:2RDZ}. FT HELIX 390 393 {ECO:0000244|PDB:2RDZ}. FT HELIX 395 422 {ECO:0000244|PDB:2RDZ}. FT HELIX 437 443 {ECO:0000244|PDB:2RDZ}. FT HELIX 448 472 {ECO:0000244|PDB:2RDZ}. SQ SEQUENCE 478 AA; 53703 MW; F965E986412A0456 CRC64; MTRIKINARR IFSLLIPFFF FTSVHAEQTA APAKPVTVEA KNETFAPQHP DQYLSWKATS EQSERVDALA EDPRLVILWA GYPFSRDYNK PRGHAFAVTD VRETLRTGAP KNAEDGPLPM ACWSCKSPDV ARLIQKDGED GYFHGKWARG GPEIVNNLGC ADCHNTASPE FAKGKPELTL SRPYAARAME AIGKPFEKAG RFDQQSMVCG QCHVEYYFDG KNKAVKFPWD DGMKVENMEQ YYDKIAFSDW TNSLSKTPML KAQHPEYETW TAGIHGKNNV TCIDCHMPKV QNAEGKLYTD HKIGNPFDNF AQTCANCHTQ DKAALQKVVA ERKQSINDLK IKVEDQLVHA HFEAKAALDA GATEAEMKPI QDDIRHAQWR WDLAIASHGI HMHAPEEGLR MLGTAMDKAA DARTKLARLL ATKGITHEIQ IPDISTKEKA QQAIGLNMEQ IKAEKQDFIK TVIPQWEEQA RKNGLLSQ //