ID Q8WS26_TRYCR Unreviewed; 425 AA. AC Q8WS26; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 97. DE SubName: Full=Farnesyl diphosphate synthase {ECO:0000313|EMBL:AAL73357.1}; OS Trypanosoma cruzi. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum. OX NCBI_TaxID=5693 {ECO:0000313|EMBL:AAL73357.1}; RN [1] {ECO:0000313|EMBL:AAL73357.1} RP NUCLEOTIDE SEQUENCE. RA Ferella M.A., Bontempi E.J.; RT "Sequencing and characterization of a mitochondrial farnesyl diphosphate RT synthase of Trypanosoma cruzi."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:1YHK, ECO:0007829|PDB:1YHL} RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 64-425 IN COMPLEX WITH MG(2+). RX PubMed=16288456; DOI=10.1002/prot.20754; RA Gabelli S.B., McLellan J.S., Montalvetti A., Oldfield E., Docampo R., RA Amzel L.M.; RT "Structure and mechanism of the farnesyl diphosphate synthase from RT Trypanosoma cruzi: implications for drug design."; RL Proteins 62:80-88(2006). RN [3] {ECO:0007829|PDB:5QPD, ECO:0007829|PDB:5QPE} RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 64-425 IN COMPLEX WITH ZN(2+). RA Petrick J.K., Muenzker L., von Delft F., Jahnke W.; RT "PanDDA analysis group deposition - FPPS screened against the DSI Fragment RT Library."; RL Submitted (MAR-2019) to the PDB data bank. RN [4] {ECO:0007829|PDB:5QQC} RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 64-425 IN COMPLEX WITH MG(2+). RA Petrick J.K., Muenzker L., von Delft F., Jahnke W.; RT "PanDDA analysis group deposition of ground-state model - FPPS screened RT against the DSI Fragment Library."; RL Submitted (MAR-2019) to the PDB data bank. RN [5] {ECO:0007829|PDB:6SE2} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 64-425 IN COMPLEX WITH ZN(2+). RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase apo structure with zinc RT ions."; RL Submitted (JUL-2019) to the PDB data bank. RN [6] {ECO:0007829|PDB:6SDO} RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 64-425 IN COMPLEX WITH ZN(2+). RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase in complex with 3np."; RL Submitted (JUL-2019) to the PDB data bank. RN [7] {ECO:0007829|PDB:6SDQ} RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 64-425 IN COMPLEX WITH ZN(2+). RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase in complex with fragment RT 2m5n."; RL Submitted (JUL-2019) to the PDB data bank. RN [8] {ECO:0007829|PDB:6SDP} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 64-425 IN COMPLEX WITH ZN(2+). RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase in complex with fragment RT 4np."; RL Submitted (JUL-2019) to the PDB data bank. RN [9] {ECO:0007829|PDB:6SDN} RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 64-425 IN COMPLEX WITH ZN(2+). RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase in complex with fragment RT j82."; RL Submitted (JUL-2019) to the PDB data bank. RN [10] {ECO:0007829|PDB:6R04, ECO:0007829|PDB:6R05} RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 64-425 IN COMPLEX WITH ZN(2+). RA Petrick J.K., Jahnke W.; RT "Targeting farnesyl pyrophosphate synthase of Trypanosoma cruzi by RT fragment-based lead discovery."; RL Submitted (AUG-2019) to the PDB data bank. RN [11] {ECO:0007829|PDB:6SFA} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 64-425 IN COMPLEX WITH MN(2+). RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase apo structure with Mn RT ions."; RL Submitted (AUG-2019) to the PDB data bank. RN [12] {ECO:0007829|PDB:6SF8} RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 64-425. RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase in complex with fragment RT j51."; RL Submitted (AUG-2019) to the PDB data bank. RN [13] {ECO:0007829|PDB:6SF9} RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 64-425. RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase in complex with fragment RT j71."; RL Submitted (AUG-2019) to the PDB data bank. RN [14] {ECO:0007829|PDB:6T7N} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 64-425 IN COMPLEX WITH MN(2+). RA Magari F., Heine A., Klebe G.; RT "Trypanosoma cruzi farnesyl diphosphate synthase in complex with IPP and RT Mn."; RL Submitted (OCT-2019) to the PDB data bank. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000256|RuleBase:RU004466}. 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; AF386102; AAL73357.1; -; Genomic_DNA. DR PDB; 1YHK; X-ray; 2.10 A; A=64-425. DR PDB; 1YHL; X-ray; 1.95 A; A=64-425. DR PDB; 1YHM; X-ray; 2.50 A; A/B/C=64-425. DR PDB; 5QPD; X-ray; 1.93 A; A=64-425. DR PDB; 5QPE; X-ray; 1.77 A; A=64-425. DR PDB; 5QPF; X-ray; 1.50 A; A=64-425. DR PDB; 5QPG; X-ray; 1.58 A; A=64-425. DR PDB; 5QPH; X-ray; 1.86 A; A=64-425. DR PDB; 5QPI; X-ray; 1.67 A; A=64-425. DR PDB; 5QPJ; X-ray; 1.41 A; A=64-425. DR PDB; 5QPK; X-ray; 1.50 A; A=64-425. DR PDB; 5QPL; X-ray; 1.41 A; A=64-425. DR PDB; 5QPM; X-ray; 1.68 A; A=64-425. DR PDB; 5QPN; X-ray; 1.45 A; A=64-425. DR PDB; 5QPO; X-ray; 1.60 A; A=64-425. DR PDB; 5QPP; X-ray; 1.48 A; A=64-425. DR PDB; 5QPQ; X-ray; 1.49 A; A=64-425. DR PDB; 5QPR; X-ray; 1.67 A; A=64-425. DR PDB; 5QPS; X-ray; 1.61 A; A=64-425. DR PDB; 5QPT; X-ray; 1.46 A; A=64-425. DR PDB; 5QPU; X-ray; 1.44 A; A=64-425. DR PDB; 5QPV; X-ray; 1.60 A; A=64-425. DR PDB; 5QPW; X-ray; 1.72 A; A=64-425. DR PDB; 5QPX; X-ray; 1.67 A; A=64-425. DR PDB; 5QPY; X-ray; 1.67 A; A=64-425. DR PDB; 5QPZ; X-ray; 1.62 A; A=64-425. DR PDB; 5QQ0; X-ray; 1.60 A; A=64-425. DR PDB; 5QQ1; X-ray; 1.97 A; A=64-425. DR PDB; 5QQ2; X-ray; 1.73 A; A=64-425. DR PDB; 5QQ3; X-ray; 1.60 A; A=64-425. DR PDB; 5QQ4; X-ray; 1.58 A; A=64-425. DR PDB; 5QQ5; X-ray; 1.68 A; A=64-425. DR PDB; 5QQ6; X-ray; 1.94 A; A=64-425. DR PDB; 5QQ7; X-ray; 1.61 A; A=64-425. DR PDB; 5QQ8; X-ray; 1.62 A; A=64-425. DR PDB; 5QQ9; X-ray; 1.61 A; A=64-425. DR PDB; 5QQA; X-ray; 2.20 A; A=64-425. DR PDB; 5QQB; X-ray; 1.58 A; A=64-425. DR PDB; 5QQC; X-ray; 1.62 A; A=64-425. DR PDB; 6R04; X-ray; 1.47 A; A=64-425. DR PDB; 6R05; X-ray; 1.57 A; A=64-425. DR PDB; 6R06; X-ray; 1.56 A; A=64-425. DR PDB; 6R07; X-ray; 1.57 A; A=64-425. DR PDB; 6R08; X-ray; 1.44 A; A=64-425. DR PDB; 6R09; X-ray; 1.28 A; A=64-425. DR PDB; 6R0A; X-ray; 1.32 A; A=64-425. DR PDB; 6R0B; X-ray; 1.61 A; A=64-425. DR PDB; 6SDN; X-ray; 1.51 A; A=64-425. DR PDB; 6SDO; X-ray; 1.68 A; A=64-425. DR PDB; 6SDP; X-ray; 1.45 A; A=64-425. DR PDB; 6SDQ; X-ray; 1.68 A; A=64-425. DR PDB; 6SE2; X-ray; 1.45 A; A=64-425. DR PDB; 6SF8; X-ray; 1.62 A; A=64-425. DR PDB; 6SF9; X-ray; 1.59 A; A=64-425. DR PDB; 6SFA; X-ray; 1.90 A; A=64-425. DR PDB; 6SHV; X-ray; 1.81 A; A=64-425. DR PDB; 6SI5; X-ray; 2.10 A; A=64-425. DR PDB; 6T7N; X-ray; 1.90 A; AAAA=64-425. DR PDBsum; 1YHK; -. DR PDBsum; 1YHL; -. DR PDBsum; 1YHM; -. DR PDBsum; 5QPD; -. DR PDBsum; 5QPE; -. DR PDBsum; 5QPF; -. DR PDBsum; 5QPG; -. DR PDBsum; 5QPH; -. DR PDBsum; 5QPI; -. DR PDBsum; 5QPJ; -. DR PDBsum; 5QPK; -. DR PDBsum; 5QPL; -. DR PDBsum; 5QPM; -. DR PDBsum; 5QPN; -. DR PDBsum; 5QPO; -. DR PDBsum; 5QPP; -. DR PDBsum; 5QPQ; -. DR PDBsum; 5QPR; -. DR PDBsum; 5QPS; -. DR PDBsum; 5QPT; -. DR PDBsum; 5QPU; -. DR PDBsum; 5QPV; -. DR PDBsum; 5QPW; -. DR PDBsum; 5QPX; -. DR PDBsum; 5QPY; -. DR PDBsum; 5QPZ; -. DR PDBsum; 5QQ0; -. DR PDBsum; 5QQ1; -. DR PDBsum; 5QQ2; -. DR PDBsum; 5QQ3; -. DR PDBsum; 5QQ4; -. DR PDBsum; 5QQ5; -. DR PDBsum; 5QQ6; -. DR PDBsum; 5QQ7; -. DR PDBsum; 5QQ8; -. DR PDBsum; 5QQ9; -. DR PDBsum; 5QQA; -. DR PDBsum; 5QQB; -. DR PDBsum; 5QQC; -. DR PDBsum; 6R04; -. DR PDBsum; 6R05; -. DR PDBsum; 6R06; -. DR PDBsum; 6R07; -. DR PDBsum; 6R08; -. DR PDBsum; 6R09; -. DR PDBsum; 6R0A; -. DR PDBsum; 6R0B; -. DR AlphaFoldDB; Q8WS26; -. DR SMR; Q8WS26; -. DR BindingDB; Q8WS26; -. DR ChEMBL; CHEMBL4752; -. DR DrugCentral; Q8WS26; -. DR VEuPathDB; TriTrypDB:BCY84_06991; -. DR VEuPathDB; TriTrypDB:C3747_92g62; -. DR VEuPathDB; TriTrypDB:C4B63_49g65; -. DR VEuPathDB; TriTrypDB:ECC02_007468; -. DR VEuPathDB; TriTrypDB:Tc_MARK_199; -. DR VEuPathDB; TriTrypDB:TcBrA4_0094470; -. DR VEuPathDB; TriTrypDB:TcCL_NonESM00446; -. DR VEuPathDB; TriTrypDB:TcCLB.508323.9; -. DR VEuPathDB; TriTrypDB:TcCLB.511823.70; -. DR VEuPathDB; TriTrypDB:TCDM_09927; -. DR VEuPathDB; TriTrypDB:TcG_08390; -. DR VEuPathDB; TriTrypDB:TCSYLVIO_001798; -. DR EvolutionaryTrace; Q8WS26; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR CDD; cd00685; Trans_IPPS_HT; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR InterPro; IPR039702; FPS1-like. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR033749; Polyprenyl_synt_CS. DR PANTHER; PTHR11525:SF0; FARNESYL PYROPHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR11525; FARNESYL-PYROPHOSPHATE SYNTHETASE; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1YHK, ECO:0007829|PDB:1YHL}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0007829|PDB:1YHL, ECO:0007829|PDB:1YHM}; KW Transferase {ECO:0000256|RuleBase:RU004466}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Zinc {ECO:0007829|PDB:5QPD, ECO:0007829|PDB:5QPE}. FT TRANSMEM 17..35 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 55..74 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 161 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1YHL, ECO:0007829|PDB:1YHM" FT BINDING 161 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:6T7N" FT BINDING 161 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5QPD, ECO:0007829|PDB:5QPG" FT BINDING 161 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5QPE, ECO:0007829|PDB:5QPF" FT BINDING 165 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5QQC" FT BINDING 165 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1YHL, ECO:0007829|PDB:1YHM" FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6SFA" FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:6T7N" FT BINDING 165 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:5QPV, ECO:0007829|PDB:5QQ9" FT BINDING 165 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5QPD, ECO:0007829|PDB:5QPG" FT BINDING 165 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:6R0B" FT BINDING 165 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5QPE, ECO:0007829|PDB:5QPF" FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1YHL, ECO:0007829|PDB:1YHM" FT BINDING 233 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:6T7N" FT BINDING 233 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6SFA" FT BINDING 233 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:6R0B" FT BINDING 233 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5QPE, ECO:0007829|PDB:5QPF" FT BINDING 299 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:5QQ3" FT BINDING 313 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1YHL" FT BINDING 313 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:1YHM, ECO:0007829|PDB:5QQC" FT BINDING 313 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:6SFA" FT BINDING 313 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:6T7N" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="9" FT /evidence="ECO:0007829|PDB:5QPL, ECO:0007829|PDB:5QQ3" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0007829|PDB:5QPH, ECO:0007829|PDB:5QPJ" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0007829|PDB:5QPD, ECO:0007829|PDB:5QPI" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0007829|PDB:5QPF, ECO:0007829|PDB:5QPG" FT BINDING 317 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:1YHM, ECO:0007829|PDB:5QQC" FT BINDING 317 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:6T7N" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0007829|PDB:5QPD, ECO:0007829|PDB:5QPI" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0007829|PDB:5QPH, ECO:0007829|PDB:5QPJ" FT BINDING 331 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="9" FT /evidence="ECO:0007829|PDB:5QPL, ECO:0007829|PDB:5QQ3" FT BINDING 331 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0007829|PDB:5QPD, ECO:0007829|PDB:5QPI" SQ SEQUENCE 425 AA; 48829 MW; CCBD1343BE591FB1 CRC64; MTAFACFPHS LFYSTRLPFF FFFFCVCVHC CLRYLCLLKC AYCCSDKNYF RPLNYFFYCL YLAMASMERF LSVYDEVQAF LLDQLQSKYE IDPNRARYLR IMMDTTCLGG KYFRGMTVVN VAEGFLAVTQ HDEATKERIL HDACVGGWMI EFLQAHYLVE DDIMDGSVMR RGKPCWYRFP GVTTQCAIND GIILKSWTQI MAWHYFADRP FLKDLLCLFQ KVDYATAVGQ MYDVTSMCDS NKLDPEVAQP MTTDFAEFTP AIYKRIVKYK TTFYTYLLPL VMGLLVSEAA ASVEMNLVER VAHLIGEYFQ VQDDVMDCFT PPEQLGKVGT DIEDAKCSWL AVTFLGKANA AQVAEFKANY GEKDPAKVAV VKRLYSKANL QADFAAYEAE VVREVESLIE QLKVKSPTFA ESVAVVWEKT HKRKK //