ID NIFK_AZOVI Reviewed; 523 AA. AC P07329; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 138. DE RecName: Full=Nitrogenase molybdenum-iron protein beta chain; DE EC=1.18.6.1; DE AltName: Full=Dinitrogenase; DE AltName: Full=Nitrogenase component I; GN Name=nifK; OS Azotobacter vinelandii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW; RX PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989; RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S., RA Cash V.L., Beynon J., Newton W.E., Dean D.R.; RT "Physical and genetic map of the major nif gene cluster from Azotobacter RT vinelandii."; RL J. Bacteriol. 171:1017-1027(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW; RX PubMed=3863780; DOI=10.1016/0378-1119(85)90255-0; RA Brigle K.E., Newton W.E., Dean D.R.; RT "Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase RT structural gene cluster."; RL Gene 37:37-44(1985). RN [3] RP PROTEIN SEQUENCE OF 2-20 AND 521-523. RX PubMed=649581; DOI=10.1016/s0021-9258(17)34817-2; RA Lundell D.J., Howard J.B.; RT "Isolation and partial characterization of two different subunits from the RT molybdenum-iron protein of Azotobacter vinelandii nitrogenase."; RL J. Biol. Chem. 253:3422-3426(1978). RN [4] RP ACTIVITY REGULATION, AND INDUCTION. RC STRAIN=CA; RX PubMed=7830548; DOI=10.1111/j.1365-2958.1994.tb01270.x; RA Moshiri F., Kim J.W., Fu C., Maier R.J.; RT "The FeSII protein of Azotobacter vinelandii is not essential for aerobic RT nitrogen fixation, but confers significant protection to oxygen-mediated RT inactivation of nitrogenase in vitro and in vivo."; RL Mol. Microbiol. 14:101-114(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RA Kim J., Rees D.C.; RT "Crystallographic structure and functional implications of the nitrogenase RT molybdenum-iron protein from Azotobacter vinelandii."; RL Nature 360:553-560(1992). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=9163420; DOI=10.1038/387370a0; RA Schindelin H., Kisker C., Schlessman J.L., Howard J.B., Rees D.C.; RT "Structure of ADP x [AlF(4)](-)-stabilized nitrogenase complex and its RT implications for signal transduction."; RL Nature 387:370-376(1997). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=9063865; DOI=10.1021/bi9626665; RA Peters J.W., Stowell M.H.B., Soltis S.M., Finnegan M.G., Johnson M.K., RA Rees D.C.; RT "Redox-dependent structural changes in the nitrogenase P-cluster."; RL Biochemistry 36:1181-1187(1997). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=11170380; DOI=10.1021/bi001645e; RA Chiu H.-J., Peters J.W., Lanzilotta W.N., Ryle M.J., Seefeldt L.C., RA Howard J.B., Rees D.C.; RT "MgATP-bound and nucleotide-free structures of a nitrogenase protein RT complex between the Leu 127Delta-Fe-protein and the MoFe-protein."; RL Biochemistry 40:641-650(2001). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-195. RX PubMed=11327812; DOI=10.1021/bi0013997; RA Soerlie M., Christiansen J., Lemon B.J., Peters J.W., Dean D.R., RA Hales B.J.; RT "Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe RT protein."; RL Biochemistry 40:1540-1549(2001). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CROSS-LINKED HETERODIMER WITH RP FE-PROTEIN. RX PubMed=12501184; DOI=10.1021/bi026642b; RA Schmid B., Einsle O., Chiu H.J., Willing A., Yoshida M., Howard J.B., RA Rees D.C.; RT "Biochemical and structural characterization of the cross-linked complex of RT nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure."; RL Biochemistry 41:15557-15565(2002). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=11951047; DOI=10.1126/science.1070010; RA Schmid B., Ribbe M.W., Einsle O., Yoshida M., Thomas L.M., Dean D.R., RA Rees D.C., Burgess B.K.; RT "Structure of a cofactor-deficient nitrogenase MoFe protein."; RL Science 296:352-356(2002). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS). RX PubMed=12215645; DOI=10.1126/science.1073877; RA Einsle O., Tezcan F.A., Andrade S.L.A., Schmid B., Yoshida M., Howard J.B., RA Rees D.C.; RT "Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the RT FeMo-cofactor."; RL Science 297:1696-1700(2002). CC -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase CC complex that catalyzes the key enzymatic reactions in nitrogen CC fixation. CC -!- CATALYTIC ACTIVITY: CC Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 CC ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 CC phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA- CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997, CC ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456216; EC=1.18.6.1; CC -!- COFACTOR: CC Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; CC Note=Binds 1 [8Fe-7S] cluster per heterodimer.; CC -!- ACTIVITY REGULATION: Nitrogenase holoenzyme is subject to CC 'conformational protection' by FeSII; under oxidizing conditions FeSII CC binds to the holoenzyme and reversibly protects it from oxidation CC (PubMed:7830548). {ECO:0000269|PubMed:7830548}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with CC the iron protein (nitrogenase component 2). CC -!- INDUCTION: Constitutively expressed during log and stationary phase in CC sucrose-limited cultures, its levels decrease during stationary phase CC (at protein level). {ECO:0000269|PubMed:7830548}. CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN 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; M20568; AAA64711.1; -; Genomic_DNA. DR EMBL; M11579; AAA22144.1; -; Genomic_DNA. DR PIR; B43049; NIAVMB. DR RefSeq; WP_012698833.1; NZ_FPKM01000020.1. DR PDB; 1FP4; X-ray; 2.50 A; B/D=1-523. DR PDB; 1G20; X-ray; 2.20 A; B/D=1-523. DR PDB; 1G21; X-ray; 3.00 A; B/D=1-523. DR PDB; 1L5H; X-ray; 2.30 A; B=2-523. DR PDB; 1M1N; X-ray; 1.16 A; B/D/F/H=2-523. DR PDB; 1M1Y; X-ray; 3.20 A; B/D/J/L=2-523. DR PDB; 1M34; X-ray; 2.30 A; B/D/J/L=2-523. DR PDB; 1N2C; X-ray; 3.00 A; B/D=2-523. DR PDB; 2AFH; X-ray; 2.10 A; B/D=2-523. DR PDB; 2AFI; X-ray; 3.10 A; B/D/J/L=2-523. DR PDB; 2MIN; X-ray; 2.03 A; B/D=2-523. DR PDB; 3K1A; X-ray; 2.23 A; B/D=2-523. DR PDB; 3MIN; X-ray; 2.03 A; B/D=2-523. DR PDB; 3U7Q; X-ray; 1.00 A; B/D=1-523. DR PDB; 4ND8; X-ray; 2.00 A; B/D=1-523. DR PDB; 4TKU; X-ray; 1.43 A; B/D=1-523. DR PDB; 4TKV; X-ray; 1.50 A; B/D=1-523. DR PDB; 4WNA; X-ray; 2.00 A; B/D=1-523. DR PDB; 4WZA; X-ray; 1.90 A; B/D=2-523. DR PDB; 4WZB; X-ray; 2.30 A; B/D=2-523. DR PDB; 4XPI; X-ray; 1.97 A; B/D=2-523. DR PDB; 5BVG; X-ray; 1.60 A; B/D=1-523. DR PDB; 5BVH; X-ray; 1.53 A; B/D=1-523. DR PDB; 5CX1; X-ray; 1.75 A; B/D/F/H/J/L/N/P=1-523. DR PDB; 5VQ4; X-ray; 2.30 A; B/D=1-523. DR PDB; 6BBL; X-ray; 1.68 A; B/D=1-523. DR PDB; 6CDK; X-ray; 2.10 A; B/D=1-523. DR PDB; 6O7L; X-ray; 2.26 A; B/D=1-523. DR PDB; 6O7M; X-ray; 1.40 A; B/D=1-523. DR PDB; 6O7N; X-ray; 1.75 A; B/D=1-523. DR PDB; 6O7O; X-ray; 1.89 A; B/D=1-523. DR PDB; 6O7P; X-ray; 1.70 A; B/D=1-523. DR PDB; 6O7Q; X-ray; 2.00 A; B/D=1-523. DR PDB; 6O7R; X-ray; 2.27 A; B/D=1-523. DR PDB; 6O7S; X-ray; 2.27 A; B/D=1-523. DR PDB; 6OP1; X-ray; 1.70 A; B/D=2-523. DR PDB; 6OP2; X-ray; 1.90 A; B/D=2-523. DR PDB; 6OP3; X-ray; 1.60 A; B/D=2-523. DR PDB; 6OP4; X-ray; 2.30 A; B/D=2-523. DR PDB; 6UG0; X-ray; 1.83 A; B/D=1-523. DR PDB; 6VXT; X-ray; 1.74 A; B/D=1-523. DR PDB; 7JRF; X-ray; 1.33 A; B/D=1-523. DR PDB; 7MCI; X-ray; 1.65 A; B/D=1-523. DR PDB; 7UT6; EM; 1.91 A; B/D=1-523. DR PDB; 7UT7; EM; 1.91 A; B/D=1-523. DR PDB; 7UT8; EM; 2.43 A; B/D=1-523. DR PDB; 7UT9; EM; 2.44 A; B/D=1-523. DR PDB; 7UTA; EM; 2.40 A; B/D=1-523. DR PDB; 8BTS; X-ray; 3.03 A; B/D/I/L=1-523. DR PDB; 8CRS; EM; 2.04 A; B/D=2-523. DR PDB; 8DBX; EM; 1.92 A; B/D=1-523. DR PDB; 8DBY; EM; 2.26 A; B/D=1-523. DR PDB; 8DFC; EM; 2.48 A; B/D=1-523. DR PDB; 8DFD; EM; 2.12 A; B/D=1-523. DR PDB; 8DPN; EM; 2.49 A; B/D=1-523. DR PDB; 8E3T; X-ray; 2.20 A; B/D=1-523. DR PDB; 8E3U; X-ray; 1.99 A; B/D=1-523. DR PDB; 8E3V; X-ray; 2.00 A; B/D=1-523. DR PDB; 8ENL; EM; 2.37 A; B/D=2-523. DR PDB; 8ENM; EM; 2.14 A; B/D=1-523. DR PDB; 8ENN; EM; 2.58 A; B/D=2-523. DR PDB; 8ENO; EM; 2.71 A; B/D=2-523. DR PDBsum; 1FP4; -. DR PDBsum; 1G20; -. DR PDBsum; 1G21; -. DR PDBsum; 1L5H; -. DR PDBsum; 1M1N; -. DR PDBsum; 1M1Y; -. DR PDBsum; 1M34; -. DR PDBsum; 1N2C; -. DR PDBsum; 2AFH; -. DR PDBsum; 2AFI; -. DR PDBsum; 2MIN; -. DR PDBsum; 3K1A; -. DR PDBsum; 3MIN; -. DR PDBsum; 3U7Q; -. DR PDBsum; 4ND8; -. DR PDBsum; 4TKU; -. DR PDBsum; 4TKV; -. DR PDBsum; 4WNA; -. DR PDBsum; 4WZA; -. DR PDBsum; 4WZB; -. DR PDBsum; 4XPI; -. DR PDBsum; 5BVG; -. DR PDBsum; 5BVH; -. DR PDBsum; 5CX1; -. DR PDBsum; 5VQ4; -. DR PDBsum; 6BBL; -. DR PDBsum; 6CDK; -. DR PDBsum; 6O7L; -. DR PDBsum; 6O7M; -. DR PDBsum; 6O7N; -. DR PDBsum; 6O7O; -. DR PDBsum; 6O7P; -. DR PDBsum; 6O7Q; -. DR PDBsum; 6O7R; -. DR PDBsum; 6O7S; -. DR PDBsum; 6OP1; -. DR PDBsum; 6OP2; -. DR PDBsum; 6OP3; -. DR PDBsum; 6OP4; -. DR PDBsum; 6UG0; -. DR PDBsum; 6VXT; -. DR PDBsum; 7JRF; -. DR PDBsum; 7MCI; -. DR PDBsum; 7UT6; -. DR PDBsum; 7UT7; -. DR PDBsum; 7UT8; -. DR PDBsum; 7UT9; -. DR PDBsum; 7UTA; -. DR PDBsum; 8BTS; -. DR PDBsum; 8CRS; -. DR PDBsum; 8DBX; -. DR PDBsum; 8DBY; -. DR PDBsum; 8DFC; -. DR PDBsum; 8DFD; -. DR PDBsum; 8DPN; -. DR PDBsum; 8E3T; -. DR PDBsum; 8E3U; -. DR PDBsum; 8E3V; -. DR PDBsum; 8ENL; -. DR PDBsum; 8ENM; -. DR PDBsum; 8ENN; -. DR PDBsum; 8ENO; -. DR AlphaFoldDB; P07329; -. DR EMDB; EMD-26957; -. DR EMDB; EMD-27316; -. DR EMDB; EMD-27317; -. DR EMDB; EMD-27404; -. DR EMDB; EMD-27405; -. DR EMDB; EMD-28272; -. DR EMDB; EMD-28273; -. DR SMR; P07329; -. DR OMA; CCAYHRS; -. DR BioCyc; MetaCyc:MONOMER-19494; -. DR BRENDA; 1.18.6.1; 49. DR EvolutionaryTrace; P07329; -. DR GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0009399; P:nitrogen fixation; IMP:CACAO. DR CDD; cd01974; Nitrogenase_MoFe_beta; 1. DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3. DR Gene3D; 1.20.89.10; Nitrogenase Molybdenum-iron Protein, subunit B, domain 4; 1. DR InterPro; IPR000510; Nase/OxRdtase_comp1. DR InterPro; IPR000318; Nase_comp1_CS. DR InterPro; IPR005976; Nase_Mo-Fe_CF_bsu. DR InterPro; IPR024564; Nase_Mo-Fe_CF_bsu_N. DR NCBIfam; TIGR01286; nifK; 1. DR PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1. DR PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1. DR Pfam; PF11844; DUF3364; 1. DR Pfam; PF00148; Oxidored_nitro; 1. DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1. DR PROSITE; PS00699; NITROGENASE_1_1; 1. DR PROSITE; PS00090; NITROGENASE_1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Direct protein sequencing; Iron; Iron-sulfur; KW Metal-binding; Nitrogen fixation; Nucleotide-binding; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:649581" FT CHAIN 2..523 FT /note="Nitrogenase molybdenum-iron protein beta chain" FT /id="PRO_0000153091" FT BINDING 70 FT /ligand="[8Fe-7S] cluster" FT /ligand_id="ChEBI:CHEBI:21143" FT /ligand_note="ligand shared with alpha chain" FT BINDING 95 FT /ligand="[8Fe-7S] cluster" FT /ligand_id="ChEBI:CHEBI:21143" FT /ligand_note="ligand shared with alpha chain" FT BINDING 153 FT /ligand="[8Fe-7S] cluster" FT /ligand_id="ChEBI:CHEBI:21143" FT /ligand_note="ligand shared with alpha chain" FT BINDING 188 FT /ligand="[8Fe-7S] cluster" FT /ligand_id="ChEBI:CHEBI:21143" FT /ligand_note="ligand shared with alpha chain" FT CONFLICT 103 FT /note="F -> L (in Ref. 2; AAA22144)" FT /evidence="ECO:0000305" FT STRAND 5..7 FT /evidence="ECO:0007829|PDB:7UT8" FT HELIX 11..14 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 18..31 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 37..46 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 50..57 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 71..80 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 93..107 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:1G21" FT HELIX 120..123 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 128..142 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 162..171 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:1L5H" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:2AFI" FT HELIX 193..209 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 210..215 FT /evidence="ECO:0007829|PDB:3U7Q" FT TURN 218..221 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 234..246 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 251..255 FT /evidence="ECO:0007829|PDB:3U7Q" FT TURN 258..261 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 266..268 FT /evidence="ECO:0007829|PDB:6O7M" FT HELIX 278..283 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 287..294 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 299..307 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 321..336 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 342..362 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 366..370 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 373..385 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 389..395 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 400..411 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 414..416 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 420..424 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 427..436 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 440..444 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 448..458 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 460..462 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 466..468 FT /evidence="ECO:0007829|PDB:3U7Q" FT STRAND 475..478 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 479..481 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 486..508 FT /evidence="ECO:0007829|PDB:3U7Q" FT TURN 512..515 FT /evidence="ECO:0007829|PDB:3U7Q" FT HELIX 516..518 FT /evidence="ECO:0007829|PDB:3U7Q" SQ SEQUENCE 523 AA; 59460 MW; B6ECD633A24998F2 CRC64; MSQQVDKIKA SYPLFLDQDY KDMLAKKRDG FEEKYPQDKI DEVFQWTTTK EYQELNFQRE ALTVNPAKAC QPLGAVLCAL GFEKTMPYVH GSQGCVAYFR SYFNRHFREP VSCVSDSMTE DAAVFGGQQN MKDGLQNCKA TYKPDMIAVS TTCMAEVIGD DLNAFINNSK KEGFIPDEFP VPFAHTPSFV GSHVTGWDNM FEGIARYFTL KSMDDKVVGS NKKINIVPGF ETYLGNFRVI KRMLSEMGVG YSLLSDPEEV LDTPADGQFR MYAGGTTQEE MKDAPNALNT VLLQPWHLEK TKKFVEGTWK HEVPKLNIPM GLDWTDEFLM KVSEISGQPI PASLTKERGR LVDMMTDSHT WLHGKRFALW GDPDFVMGLV KFLLELGCEP VHILCHNGNK RWKKAVDAIL AASPYGKNAT VYIGKDLWHL RSLVFTDKPD FMIGNSYGKF IQRDTLHKGK EFEVPLIRIG FPIFDRHHLH RSTTLGYEGA MQILTTLVNS ILERLDEETR GMQATDYNHD LVR //