CP51_MYCTU
ID CP51_MYCTU Reviewed; 451 AA.
AC P9WPP9; L0T4U1; P0A512; P77901;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Lanosterol 14-alpha demethylase;
DE EC=1.14.14.154 {ECO:0000269|PubMed:10430874};
DE AltName: Full=CYPLI;
DE AltName: Full=Cytochrome P450 51;
DE AltName: Full=Cytochrome P450-14DM;
DE AltName: Full=Cytochrome P450-LIA1;
DE AltName: Full=Sterol 14-alpha demethylase;
GN Name=cyp51; OrderedLocusNames=Rv0764c; ORFNames=MTCY369.09c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS A P450 CYTOCHROME, AND COFACTOR.
RX PubMed=9756611; DOI=10.1093/oxfordjournals.jbchem.a022167;
RA Aoyama Y., Horiuchi T., Gotoh O., Noshiro M., Yoshida Y.;
RT "CYP51-like gene of Mycobacterium tuberculosis actually encodes a P450
RT similar to eukaryotic CYP51.";
RL J. Biochem. 124:694-696(1998).
RN [3]
RP FUNCTION AS LANOSTEROL 14-ALPHA DEMETHYLASE, AND CATALYTIC ACTIVITY.
RX PubMed=10430874; DOI=10.1073/pnas.96.16.8937;
RA Bellamine A., Mangla A.T., Nes W.D., Waterman M.R.;
RT "Characterization and catalytic properties of the sterol 14 alpha-
RT demethylase from Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8937-8942(1999).
RN [4]
RP SUBSTRATE SPECIFICITY.
RX PubMed=11160374;
RA Bellamine A., Mangla A.T., Dennis A.L., Nes W.D., Waterman M.R.;
RT "Structural requirements for substrate recognition of Mycobacterium
RT tuberculosis 14alpha-demethylase: implications for sterol biosynthesis.";
RL J. Lipid Res. 42:128-136(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOGS.
RX PubMed=11248033; DOI=10.1073/pnas.061562898;
RA Podust L.M., Poulos T.L., Waterman M.R.;
RT "Crystal structure of cytochrome P450 14 alpha-sterol demethylase (CYP51)
RT from Mycobacterium tuberculosis in complex with azole inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3068-3073(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH HEME AND ESTRIOL.
RX PubMed=15530358; DOI=10.1016/j.str.2004.08.009;
RA Podust L.M., Yermalitskaya L.V., Lepesheva G.I., Podust V.N.,
RA Dalmasso E.A., Waterman M.R.;
RT "Estriol bound and ligand-free structures of sterol 14alpha-demethylase.";
RL Structure 12:1937-1945(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH HEME, AND
RP MUTAGENESIS.
RA Podust L.M., Yermalitskaya L.V., Kim Y., Waterman M.R.;
RT "Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51
RT from Mycobacterium tuberculosis.";
RL Submitted (JUL-2004) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOGS, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=17846131; DOI=10.1128/aac.00311-07;
RA Podust L.M., von Kries J.P., Eddine A.N., Kim Y., Yermalitskaya L.V.,
RA Kuehne R., Ouellet H., Warrier T., Altekoster M., Lee J.S., Rademann J.,
RA Oschkinat H., Kaufmann S.H., Waterman M.R.;
RT "Small-molecule scaffolds for CYP51 inhibitors identified by high-
RT throughput screening and defined by X-ray crystallography.";
RL Antimicrob. Agents Chemother. 51:3915-3923(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOGS.
RX PubMed=18367444; DOI=10.1074/jbc.m801145200;
RA Eddine A.N., von Kries J.P., Podust M.V., Warrier T., Kaufmann S.H.,
RA Podust L.M.;
RT "X-ray structure of 4,4'-dihydroxybenzophenone mimicking sterol substrate
RT in the active site of sterol 14alpha-demethylase (CYP51).";
RL J. Biol. Chem. 283:15152-15159(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOGS.
RX PubMed=19190730; DOI=10.1371/journal.pntd.0000372;
RA Chen C.K., Doyle P.S., Yermalitskaya L.V., Mackey Z.B., Ang K.K.,
RA McKerrow J.H., Podust L.M.;
RT "Trypanosoma cruzi CYP51 inhibitor derived from a Mycobacterium
RT tuberculosis screen hit.";
RL PLoS Negl. Trop. Dis. 3:E372-E372(2009).
CC -!- FUNCTION: Its precise biological substrate is not known. Catalyzes C14-
CC demethylation of lanosterol, 24,25-dihydrolanosterol and obtusifoliol
CC which is critical for ergosterol biosynthesis. It transforms lanosterol
CC into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
CC {ECO:0000269|PubMed:10430874, ECO:0000269|PubMed:9756611}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--
CC hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4
CC H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154;
CC Evidence={ECO:0000269|PubMed:10430874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4
CC H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10430874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287;
CC Evidence={ECO:0000269|PubMed:10430874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=24,25-dihydrolanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein
CC reductase] = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 4
CC H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:45960, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:28113, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:78904;
CC Evidence={ECO:0000269|PubMed:10430874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45961;
CC Evidence={ECO:0000269|PubMed:10430874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 O2 + obtusifoliol + 3 reduced [NADPH--hemoprotein reductase]
CC = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate +
CC 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:14917, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17791, ChEBI:CHEBI:30109,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10430874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14918;
CC Evidence={ECO:0000269|PubMed:10430874};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:9756611};
CC -!- ACTIVITY REGULATION: Inhibited by alpha-ethyl-N-4-pyridinyl-
CC benzeneacetamide (EPBA) and 4,4'-dihydroxybenzophenone (DHBP).
CC {ECO:0000269|PubMed:17846131}.
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 1/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11248033,
CC ECO:0000269|PubMed:15530358, ECO:0000269|PubMed:17846131,
CC ECO:0000269|PubMed:18367444, ECO:0000269|PubMed:19190730,
CC ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 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; AL123456; CCP43511.1; -; Genomic_DNA.
DR PIR; G70706; G70706.
DR RefSeq; NP_215278.1; NC_000962.3.
DR RefSeq; WP_003898577.1; NZ_NVQJ01000035.1.
DR PDB; 1E9X; X-ray; 2.10 A; A=1-451.
DR PDB; 1EA1; X-ray; 2.21 A; A=1-451.
DR PDB; 1H5Z; X-ray; 2.05 A; A=1-451.
DR PDB; 1U13; X-ray; 2.01 A; A=1-451.
DR PDB; 1X8V; X-ray; 1.55 A; A=1-451.
DR PDB; 2BZ9; X-ray; 2.21 A; A/B=1-451.
DR PDB; 2CI0; X-ray; 1.53 A; A=1-451.
DR PDB; 2CIB; X-ray; 1.50 A; A=1-451.
DR PDB; 2VKU; X-ray; 1.95 A; A=1-451.
DR PDB; 2W09; X-ray; 1.57 A; A=1-451.
DR PDB; 2W0A; X-ray; 1.60 A; A=1-451.
DR PDB; 2W0B; X-ray; 1.56 A; A=1-451.
DR PDBsum; 1E9X; -.
DR PDBsum; 1EA1; -.
DR PDBsum; 1H5Z; -.
DR PDBsum; 1U13; -.
DR PDBsum; 1X8V; -.
DR PDBsum; 2BZ9; -.
DR PDBsum; 2CI0; -.
DR PDBsum; 2CIB; -.
DR PDBsum; 2VKU; -.
DR PDBsum; 2W09; -.
DR PDBsum; 2W0A; -.
DR PDBsum; 2W0B; -.
DR AlphaFoldDB; P9WPP9; -.
DR SMR; P9WPP9; -.
DR STRING; 83332.Rv0764c; -.
DR ChEMBL; CHEMBL5090; -.
DR DrugCentral; P9WPP9; -.
DR SwissLipids; SLP:000001161; -.
DR PaxDb; P9WPP9; -.
DR GeneID; 888819; -.
DR KEGG; mtu:Rv0764c; -.
DR TubercuList; Rv0764c; -.
DR eggNOG; COG2124; Bacteria.
DR OMA; AWTLIEL; -.
DR PhylomeDB; P9WPP9; -.
DR BRENDA; 1.14.14.154; 3445.
DR BRENDA; 1.14.15.36; 3445.
DR UniPathway; UPA00770; UER00754.
DR PRO; PR:P9WPP9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:MTBBASE.
DR GO; GO:0020037; F:heme binding; IDA:MTBBASE.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008398; F:sterol 14-demethylase activity; IDA:MTBBASE.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IDA:MTBBASE.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism.
FT CHAIN 1..451
FT /note="Lanosterol 14-alpha demethylase"
FT /id="PRO_0000052017"
FT BINDING 72
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:11248033,
FT ECO:0000269|PubMed:15530358, ECO:0000269|PubMed:17846131,
FT ECO:0000269|PubMed:18367444, ECO:0000269|PubMed:19190730,
FT ECO:0000269|Ref.8"
FT BINDING 76
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:11248033,
FT ECO:0000269|PubMed:15530358, ECO:0000269|PubMed:17846131,
FT ECO:0000269|PubMed:18367444, ECO:0000269|PubMed:19190730,
FT ECO:0000269|Ref.8"
FT BINDING 97
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:11248033,
FT ECO:0000269|PubMed:15530358, ECO:0000269|PubMed:17846131,
FT ECO:0000269|PubMed:18367444, ECO:0000269|PubMed:19190730,
FT ECO:0000269|Ref.8"
FT BINDING 259
FT /ligand="substrate"
FT BINDING 326
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:11248033,
FT ECO:0000269|PubMed:15530358, ECO:0000269|PubMed:17846131,
FT ECO:0000269|PubMed:18367444, ECO:0000269|PubMed:19190730,
FT ECO:0000269|Ref.8"
FT BINDING 392
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:11248033,
FT ECO:0000269|PubMed:15530358, ECO:0000269|PubMed:17846131,
FT ECO:0000269|PubMed:18367444, ECO:0000269|PubMed:19190730,
FT ECO:0000269|Ref.8"
FT BINDING 394
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 433
FT /ligand="substrate"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:2CIB"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2W09"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2W09"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:1X8V"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1X8V"
FT HELIX 107..125
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 189..214
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2VKU"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 243..274
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 305..317
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:2CIB"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:2CIB"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:2CIB"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 397..414
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:2CIB"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:2CIB"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:2CIB"
SQ SEQUENCE 451 AA; 50878 MW; B3D671EA9542A57B CRC64;
MSAVALPRVS GGHDEHGHLE EFRTDPIGLM QRVRDECGDV GTFQLAGKQV VLLSGSHANE
FFFRAGDDDL DQAKAYPFMT PIFGEGVVFD ASPERRKEML HNAALRGEQM KGHAATIEDQ
VRRMIADWGE AGEIDLLDFF AELTIYTSSA CLIGKKFRDQ LDGRFAKLYH ELERGTDPLA
YVDPYLPIES FRRRDEARNG LVALVADIMN GRIANPPTDK SDRDMLDVLI AVKAETGTPR
FSADEITGMF ISMMFAGHHT SSGTASWTLI ELMRHRDAYA AVIDELDELY GDGRSVSFHA
LRQIPQLENV LKETLRLHPP LIILMRVAKG EFEVQGHRIH EGDLVAASPA ISNRIPEDFP
DPHDFVPARY EQPRQEDLLN RWTWIPFGAG RHRCVGAAFA IMQIKAIFSV LLREYEFEMA
QPPESYRNDH SKMVVQLAQP ACVRYRRRTG V
