FDNG_ECOLI
ID FDNG_ECOLI Reviewed; 1015 AA.
AC P24183; P78261;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Formate dehydrogenase, nitrate-inducible, major subunit;
DE EC=1.17.5.3 {ECO:0000269|PubMed:11884747};
DE AltName: Full=Anaerobic formate dehydrogenase major subunit;
DE AltName: Full=Formate dehydrogenase-N subunit alpha;
DE Short=FDH-N subunit alpha;
DE Flags: Precursor;
GN Name=fdnG; OrderedLocusNames=b1474, JW1470;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SELENOCYSTEINE AT SEC-196.
RC STRAIN=K12;
RX PubMed=1834669; DOI=10.1016/s0021-9258(18)54583-x;
RA Berg B.L., Li J., Heider J., Stewart V.;
RT "Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I.
RT Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA)
RT encodes selenocysteine.";
RL J. Biol. Chem. 266:22380-22385(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP EXPORT VIA THE TAT-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [6]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=2168848; DOI=10.1093/genetics/125.4.691;
RA Berg B.L., Stewart V.;
RT "Structural genes for nitrate-inducible formate dehydrogenase in
RT Escherichia coli K-12.";
RL Genetics 125:691-702(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH BETA AND GAMMA
RP SUBUNITS; [4FE-4S] CLUSTER AND MO-BIS-MGD, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ELECTRON TRANSFER CHAIN, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11884747; DOI=10.1126/science.1068186;
RA Jormakka M., Tornroth S., Byrne B., Iwata S.;
RT "Molecular basis of proton motive force generation: structure of formate
RT dehydrogenase-N.";
RL Science 295:1863-1868(2002).
CC -!- FUNCTION: Formate dehydrogenase allows E.coli to use formate as major
CC electron donor during anaerobic respiration, when nitrate is used as
CC electron acceptor. The alpha subunit FdnG contains the formate
CC oxidation site. Electrons are transferred from formate to menaquinone
CC in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta
CC subunit (FdnH). Formate dehydrogenase-N is part of a system that
CC generates proton motive force, together with the dissimilatory nitrate
CC reductase (Nar). {ECO:0000269|PubMed:11884747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + formate + H(+) = a quinol + CO2;
CC Xref=Rhea:RHEA:48592, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124;
CC EC=1.17.5.3; Evidence={ECO:0000269|PubMed:11884747};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000269|PubMed:11884747};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:11884747};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:11884747};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:11884747};
CC -!- SUBUNIT: Trimer of heterotrimers, consisting of subunits alpha, beta
CC and gamma. {ECO:0000269|PubMed:11884747}.
CC -!- INTERACTION:
CC P24183; P13024: fdhE; NbExp=6; IntAct=EBI-550115, EBI-550129;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11884747}.
CC -!- INDUCTION: By nitrate under anaerobic conditions.
CC {ECO:0000269|PubMed:2168848}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; M75029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAD13438.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15123.1; -; Genomic_DNA.
DR PIR; E64900; JS0628.
DR RefSeq; NP_415991.1; NC_000913.3.
DR RefSeq; WP_010723100.1; NZ_LN832404.1.
DR PDB; 1KQF; X-ray; 1.60 A; A=1-1015.
DR PDB; 1KQG; X-ray; 2.80 A; A=1-1015.
DR PDBsum; 1KQF; -.
DR PDBsum; 1KQG; -.
DR SMR; P24183; -.
DR BioGRID; 4262900; 30.
DR BioGRID; 850396; 1.
DR ComplexPortal; CPX-1975; Formate dehydrogenase N complex.
DR DIP; DIP-9573N; -.
DR IntAct; P24183; 15.
DR STRING; 511145.b1474; -.
DR DrugBank; DB07918; 2-heptyl-4-hydroxyquinoline N-oxide.
DR TCDB; 5.A.3.2.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P24183; -.
DR PaxDb; P24183; -.
DR PRIDE; P24183; -.
DR GeneID; 946035; -.
DR KEGG; ecj:JW1470; -.
DR KEGG; eco:b1474; -.
DR PATRIC; fig|511145.12.peg.1540; -.
DR EchoBASE; EB1209; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR InParanoid; P24183; -.
DR OMA; SELWFFY; -.
DR PhylomeDB; P24183; -.
DR BioCyc; EcoCyc:FDNG-MON; -.
DR BioCyc; MetaCyc:FDNG-MON; -.
DR BRENDA; 1.17.5.3; 2026.
DR EvolutionaryTrace; P24183; -.
DR PRO; PR:P24183; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; 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:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0036397; F:formate dehydrogenase (quinone) activity; IDA:EcoCyc.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:EcoCyc.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008430; F:selenium binding; IDA:EcoCyc.
DR GO; GO:0019645; P:anaerobic electron transport chain; IC:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0015944; P:formate oxidation; IDA:EcoCyc.
DR GO; GO:0006788; P:heme oxidation; IC:ComplexPortal.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01553; formate-DH-alph; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
KW Oxidoreductase; Periplasm; Reference proteome; Selenocysteine; Signal.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 34..1015
FT /note="Formate dehydrogenase, nitrate-inducible, major
FT subunit"
FT /id="PRO_0000063222"
FT DOMAIN 43..106
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 196
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT NON_STD 196
FT /note="Selenocysteine"
FT CONFLICT 96
FT /note="A -> P (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 484..491
FT /note="ANTPKATL -> GEHAERRRW (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="S -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 85..89
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 126..144
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1KQG"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 360..368
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 373..380
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 451..456
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 478..485
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 501..513
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 519..527
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 537..545
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 559..562
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 566..573
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 577..585
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 588..593
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 597..600
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 624..627
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 649..667
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 672..677
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 690..698
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 728..733
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 749..751
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 767..770
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 771..774
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 780..783
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:1KQG"
FT STRAND 798..800
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 802..809
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 856..859
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 876..879
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 885..887
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 890..895
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 902..904
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 905..907
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 909..914
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 919..922
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 924..930
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 937..941
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 946..953
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 960..962
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 969..973
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 978..982
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 988..990
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 998..1000
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 1007..1014
FT /evidence="ECO:0007829|PDB:1KQF"
SQ SEQUENCE 1015 AA; 112963 MW; E4B9449D6B2407DA CRC64;
MDVSRRQFFK ICAGGMAGTT VAALGFAPKQ ALAQARNYKL LRAKEIRNTC TYCSVGCGLL
MYSLGDGAKN AREAIYHIEG DPDHPVSRGA LCPKGAGLLD YVNSENRLRY PEYRAPGSDK
WQRISWEEAF SRIAKLMKAD RDANFIEKNE QGVTVNRWLS TGMLCASGAS NETGMLTQKF
ARSLGMLAVD NQARVUHGPT VASLAPTFGR GAMTNHWVDI KNANVVMVMG GNAAEAHPVG
FRWAMEAKNN NDATLIVVDP RFTRTASVAD IYAPIRSGTD ITFLSGVLRY LIENNKINAE
YVKHYTNASL LVRDDFAFED GLFSGYDAEK RQYDKSSWNY QLDENGYAKR DETLTHPRCV
WNLLKEHVSR YTPDVVENIC GTPKADFLKV CEVLASTSAP DRTTTFLYAL GWTQHTVGAQ
NIRTMAMIQL LLGNMGMAGG GVNALRGHSN IQGLTDLGLL STSLPGYLTL PSEKQVDLQS
YLEANTPKAT LADQVNYWSN YPKFFVSLMK SFYGDAAQKE NNWGYDWLPK WDQTYDVIKY
FNMMDEGKVT GYFCQGFNPV ASFPDKNKVV SCLSKLKYMV VIDPLVTETS TFWQNHGESN
DVDPASIQTE VFRLPSTCFA EEDGSIANSG RWLQWHWKGQ DAPGEARNDG EILAGIYHHL
RELYQSEGGK GVEPLMKMSW NYKQPHEPQS DEVAKENNGY ALEDLYDANG VLIAKKGQLL
SSFAHLRDDG TTASSCWIYT GSWTEQGNQM ANRDNSDPSG LGNTLGWAWA WPLNRRVLYN
RASADINGKP WDPKRMLIQW NGSKWTGNDI PDFGNAAPGT PTGPFIMQPE GMGRLFAINK
MAEGPFPEHY EPIETPLGTN PLHPNVVSNP VVRLYEQDAL RMGKKEQFPY VGTTYRLTEH
FHTWTKHALL NAIAQPEQFV EISETLAAAK GINNGDRVTV SSKRGFIRAV AVVTRRLKPL
NVNGQQVETV GIPIHWGFEG VARKGYIANT LTPNVGDANS QTPEYKAFLV NIEKA
