KSHA_MYCTU
ID KSHA_MYCTU Reviewed; 386 AA.
AC P71875; L0TCS9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=3-ketosteroid-9-alpha-monooxygenase, oxygenase component {ECO:0000303|PubMed:19234303};
DE AltName: Full=3-ketosteroid-9-alpha-hydroxylase, oxygenase component {ECO:0000303|PubMed:19234303};
DE Short=KSH {ECO:0000303|PubMed:19234303};
DE AltName: Full=Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase {ECO:0000303|PubMed:19234303};
DE EC=1.14.15.30 {ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:21987574};
DE AltName: Full=Rieske-type oxygenase {ECO:0000303|PubMed:19234303};
DE Short=RO {ECO:0000303|PubMed:19234303};
GN Name=kshA; OrderedLocusNames=Rv3526;
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 INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17635188; DOI=10.1111/j.1365-2958.2007.05827.x;
RA Kendall S.L., Withers M., Soffair C.N., Moreland N.J., Gurcha S.,
RA Sidders B., Frita R., Ten Bokum A., Besra G.S., Lott J.S., Stoker N.G.;
RT "A highly conserved transcriptional repressor controls a large regulon
RT involved in lipid degradation in Mycobacterium smegmatis and Mycobacterium
RT tuberculosis.";
RL Mol. Microbiol. 65:684-699(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=21987574; DOI=10.1074/jbc.m111.289975;
RA Capyk J.K., Casabon I., Gruninger R., Strynadka N.C., Eltis L.D.;
RT "Activity of 3-ketosteroid 9alpha-hydroxylase (KshAB) indicates cholesterol
RT side chain and ring degradation occur simultaneously in Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 286:40717-40724(2011).
RN [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH IRON ION AND
RP IRON-SULFUR (2FE-2S), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, PATHWAY, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19234303; DOI=10.1074/jbc.m900719200;
RA Capyk J.K., D'Angelo I., Strynadka N.C., Eltis L.D.;
RT "Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a Rieske oxygenase
RT in the cholesterol degradation pathway of Mycobacterium tuberculosis.";
RL J. Biol. Chem. 284:9937-9946(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) IN COMPLEX WITH IRON ION AND
RP IRON-SULFUR (2FE-2S), AND COFACTOR.
RX PubMed=25049233; DOI=10.1074/jbc.m114.575886;
RA Penfield J.S., Worrall L.J., Strynadka N.C., Eltis L.D.;
RT "Substrate specificities and conformational flexibility of 3-ketosteroid
RT 9alpha-hydroxylases.";
RL J. Biol. Chem. 289:25523-25536(2014).
CC -!- FUNCTION: Involved in the degradation of cholesterol. Catalyzes the
CC introduction of a 9a-hydroxyl moiety into 1,4-androstadiene-3,17-dione
CC (ADD) to yield the 9alpha-hydroxy-1,4-androstadiene-3,17-dione (9OHADD)
CC intermediate which spontaneously form 3-hydroxy-9,10-seconandrost-
CC 1,3,5(10)-triene-9,17-dione (HSA) via the meta-cleavage of ring B with
CC concomitant aromatization of ring A. KSH is also able to use 4-
CC androstene-3,17-dione (AD), 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-
CC BNC), 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate (1,4-BNC), 3-oxo-
CC 23,24-bisnorcholesta-4-en-22-oyl-coenzyme A thioester (4-BNC-CoA) and
CC 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-
CC BNC-CoA) as substrates. {ECO:0000269|PubMed:19234303,
CC ECO:0000269|PubMed:21987574}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-
CC 2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O
CC + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:32199, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:40799, ChEBI:CHEBI:63641;
CC EC=1.14.15.30; Evidence={ECO:0000269|PubMed:19234303,
CC ECO:0000269|PubMed:21987574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32200;
CC Evidence={ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:21987574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-4-ene-3,17-dione + H(+) + NADH + O2 = 9alpha-hydroxy-
CC androst-4-ene-3,17-dione + H2O + NAD(+); Xref=Rhea:RHEA:45968,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16422, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:85549; Evidence={ECO:0000269|PubMed:19234303,
CC ECO:0000269|PubMed:21987574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45969;
CC Evidence={ECO:0000269|PubMed:21987574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxochol-4-en-22-oate + H(+) + NADH + O2 = 9alpha-hydroxy-3-
CC oxochol-4-en-22-oate + H2O + NAD(+); Xref=Rhea:RHEA:45972,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83777,
CC ChEBI:CHEBI:85550; Evidence={ECO:0000269|PubMed:21987574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45973;
CC Evidence={ECO:0000269|PubMed:21987574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxochola-1,4-dien-22-oate + H(+) + NADH + O2 = 9alpha-
CC hydroxy-3-oxochola-1,4-dien-22-oate + H2O + NAD(+);
CC Xref=Rhea:RHEA:45976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:85551, ChEBI:CHEBI:85553;
CC Evidence={ECO:0000269|PubMed:21987574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45977;
CC Evidence={ECO:0000269|PubMed:21987574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxochol-4-en-22-oyl-CoA + H(+) + NADH + O2 = 9alpha-hydroxy-
CC 3-oxochol-4-en-22-oyl-CoA + H2O + NAD(+); Xref=Rhea:RHEA:45980,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83792,
CC ChEBI:CHEBI:85548; Evidence={ECO:0000269|PubMed:21987574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45981;
CC Evidence={ECO:0000269|PubMed:21987574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxochola-1,4-dien-22-oyl-CoA + H(+) + NADH + O2 = 9alpha-
CC hydroxy-3-oxochola-1,4-dien-22-oyl-CoA + H2O + NAD(+);
CC Xref=Rhea:RHEA:45984, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:83793, ChEBI:CHEBI:85547;
CC Evidence={ECO:0000269|PubMed:21987574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45985;
CC Evidence={ECO:0000269|PubMed:21987574};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628,
CC ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628, ECO:0000269|PubMed:19234303,
CC ECO:0000269|PubMed:25049233};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233};
CC Note=Binds 1 Fe cation. {ECO:0000269|PubMed:19234303,
CC ECO:0000269|PubMed:25049233};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for 4-BNC (at pH 7 and at 22 degrees Celsius)
CC {ECO:0000269|PubMed:21987574};
CC KM=6.8 uM for 4-BNC-CoA (at pH 7 and at 22 degrees Celsius)
CC {ECO:0000269|PubMed:21987574};
CC KM=17 uM for 1,4-BNC-CoA (at pH 7 and at 22 degrees Celsius)
CC {ECO:0000269|PubMed:21987574};
CC KM=24 uM for AD (at pH 7 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:19234303};
CC KM=70 uM for 1,4-BNC (at pH 7 and at 22 degrees Celsius)
CC {ECO:0000269|PubMed:21987574};
CC KM=110 uM for ADD (at pH 7 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:19234303};
CC Note=kcat is 2.7 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7 and at
CC 22 degrees Celsius) (PubMed:21987574). kcat is 0.8 sec(-1) for ADD as
CC substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303). kcat
CC is 0.61 sec(-1) for 4-BNC-CoA as substrate (at pH 7 and at 22 degrees
CC Celsius) (PubMed:21987574). kcat is 0.25 sec(-1) for 1,4-BNC as
CC substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574). kcat
CC is 0.08 sec(-1) for 4-BNC as substrate (at pH 7 and at 22 degrees
CC Celsius) (PubMed:21987574). kcat is 0.07 sec(-1) for AD as substrate
CC (at pH 7 and at 25 degrees Celsius) (PubMed:19234303).
CC {ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:21987574};
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC {ECO:0000305|PubMed:19234303}.
CC -!- SUBUNIT: Homotrimer (PubMed:19234303). The two-component system 3-
CC ketosteroid-9-alpha-monooxygenase is composed of an oxygenase component
CC KshA and a reductase component KshB (PubMed:21987574).
CC {ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:21987574}.
CC -!- INDUCTION: Induced by KstR. {ECO:0000269|PubMed:17635188}.
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DR EMBL; AL123456; CCP46348.1; -; Genomic_DNA.
DR PIR; G70674; G70674.
DR RefSeq; NP_218043.1; NC_000962.3.
DR RefSeq; WP_003419211.1; NZ_NVQJ01000014.1.
DR PDB; 2ZYL; X-ray; 2.30 A; A=1-386.
DR PDB; 4QCK; X-ray; 2.46 A; A=1-386.
DR PDBsum; 2ZYL; -.
DR PDBsum; 4QCK; -.
DR AlphaFoldDB; P71875; -.
DR SMR; P71875; -.
DR STRING; 83332.Rv3526; -.
DR SwissLipids; SLP:000001163; -.
DR PaxDb; P71875; -.
DR GeneID; 888268; -.
DR KEGG; mtu:Rv3526; -.
DR TubercuList; Rv3526; -.
DR eggNOG; COG4638; Bacteria.
DR InParanoid; P71875; -.
DR OMA; AVYQMRR; -.
DR PhylomeDB; P71875; -.
DR BioCyc; MetaCyc:G185E-7803-MON; -.
DR BRENDA; 1.14.15.30; 3445.
DR UniPathway; UPA00062; -.
DR EvolutionaryTrace; P71875; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:MTBBASE.
DR GO; GO:0036200; F:3-ketosteroid 9-alpha-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:MTBBASE.
DR GO; GO:0047086; F:ketosteroid monooxygenase activity; IDA:MTBBASE.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006707; P:cholesterol catabolic process; IDA:MTBBASE.
DR GO; GO:0070207; P:protein homotrimerization; IPI:MTBBASE.
DR GO; GO:0070723; P:response to cholesterol; IEP:MTBBASE.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR045605; KshA-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF19298; KshA_C; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cholesterol metabolism; Iron; Iron-sulfur;
KW Lipid degradation; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Reference proteome; Steroid metabolism; Sterol metabolism; Virulence.
FT CHAIN 1..386
FT /note="3-ketosteroid-9-alpha-monooxygenase, oxygenase
FT component"
FT /id="PRO_0000404098"
FT DOMAIN 26..128
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 67
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233"
FT BINDING 89
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:F1CMY8"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:19234303,
FT ECO:0000269|PubMed:25049233"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:19234303,
FT ECO:0000269|PubMed:25049233"
FT BINDING 304
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:19234303,
FT ECO:0000269|PubMed:25049233"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2ZYL"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2ZYL"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 224..246
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 249..263
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 266..276
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:4QCK"
FT HELIX 287..308
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:2ZYL"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2ZYL"
FT HELIX 358..372
FT /evidence="ECO:0007829|PDB:2ZYL"
SQ SEQUENCE 386 AA; 44268 MW; 510F89D334D230B4 CRC64;
MSTDTSGVGV REIDAGALPT RYARGWHCLG VAKDYLEGKP HGVEAFGTKL VVFADSHGDL
KVLDGYCRHM GGDLSEGTVK GDEVACPFHD WRWGGDGRCK LVPYARRTPR MARTRSWTTD
VRSGLLFVWH DHEGNPPDPA VRIPEIPEAA SDEWTDWRWN RILIEGSNCR DIIDNVTDMA
HFFYIHFGLP TYFKNVFEGH IASQYLHNVG RPDVDDLGTS YGEAHLDSEA SYFGPSFMIN
WLHNRYGNYK SESILINCHY PVTQNSFVLQ WGVIVEKPKG MSEEMTDKLS RVFTEGVSKG
FLQDVEIWKH KTRIDNPLLV EEDGAVYQLR RWYEQFYVDV ADIKPEMVER FEIEVDTKRA
NEFWNAEVEK NLKSREVSDD VPAEQH
