ID RCEL_CERSP Reviewed; 282 AA. AC P0C0Y8; P02954; Q9RFB9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 103. DE RecName: Full=Reaction center protein L chain; DE AltName: Full=Photosynthetic reaction center L subunit; GN Name=pufL; OS Cereibacter sphaeroides (Rhodobacter sphaeroides). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Cereibacter. OX NCBI_TaxID=1063; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6095283; DOI=10.1073/pnas.81.23.7303; RA Williams J.C., Steiner L.A., Feher G., Simon M.I.; RT "Primary structure of the L subunit of the reaction center from RT Rhodopseudomonas sphaeroides."; RL Proc. Natl. Acad. Sci. U.S.A. 81:7303-7307(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Y; RX PubMed=2126457; DOI=10.1016/0300-9084(90)90116-x; RA Arnoux B., Ducruix A., Astier C., Picaud M., Roth M., Reiss-Husson F.; RT "Towards the understanding of the function of Rb sphaeroides Y wild type RT reaction center: gene cloning, protein and detergent structures in the RT three-dimensional crystals."; RL Biochimie 72:525-530(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). RX PubMed=2036404; DOI=10.1021/bi00236a005; RA Chang C.-H., El-Kabbani O., Tiede D., Norris J., Schiffer M.; RT "Structure of the membrane-bound protein photosynthetic reaction center RT from Rhodobacter sphaeroides."; RL Biochemistry 30:5352-5360(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RC STRAIN=R-26; RX PubMed=3054889; DOI=10.1073/pnas.85.22.8487; RA Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.; RT "Structure of the reaction center from Rhodobacter sphaeroides R-26: RT protein-cofactor (quinones and Fe2+) interactions."; RL Proc. Natl. Acad. Sci. U.S.A. 85:8487-8491(1988). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RC STRAIN=R-26; RX PubMed=2819866; DOI=10.1073/pnas.84.17.6162; RA Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.; RT "Structure of the reaction center from Rhodobacter sphaeroides R-26: the RT protein subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6162-6166(1987). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS). RX PubMed=9537989; DOI=10.1021/bi971717a; RA McAuley-Hecht K.E., Fyfe P.K., Ridge J.P., Prince S.M., Hunter C.N., RA Isaacs N.W., Cogdell R.J., Jones M.R.; RT "Structural studies of wild-type and mutant reaction centers from an RT antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical RT properties of the complex from bacterial cell to crystal."; RL Biochemistry 37:4740-4750(1998). RN [7] RP TOPOLOGY. RX PubMed=1645718; DOI=10.1016/s0021-9258(18)99114-3; RA Yun C.H., Van Doren S.R., Crofts A.R., Gennis R.B.; RT "The use of gene fusions to examine the membrane topology of the L-subunit RT of the photosynthetic reaction center and of the cytochrome b subunit of RT the bc1 complex from Rhodobacter sphaeroides."; RL J. Biol. Chem. 266:10967-10973(1991). CC -!- FUNCTION: The reaction center is a membrane-bound complex that mediates CC the initial photochemical event in the electron transfer process of CC photosynthesis. CC -!- SUBUNIT: Reaction center is composed of four bacteriochlorophylls, two CC bacteriopheophytins, two ubiquinones, one iron, and three highly CC hydrophobic polypeptide chains (designated L, M, and H). CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane; Multi-pass CC membrane protein. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. CC {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; M10206; AAA26177.1; -; Genomic_DNA. DR EMBL; X63404; CAA44999.1; -; Genomic_DNA. DR PIR; S24212; WNRFLS. DR RefSeq; WP_002720421.1; NZ_WTFI01000042.1. DR PDB; 1AIG; X-ray; 2.60 A; L/N=2-282. DR PDB; 1AIJ; X-ray; 2.20 A; L/R=2-282. DR PDB; 1DS8; X-ray; 2.50 A; L/R=2-282. DR PDB; 1DV3; X-ray; 2.50 A; L/R=2-282. DR PDB; 1DV6; X-ray; 2.50 A; L/R=2-282. DR PDB; 1E14; X-ray; 2.70 A; L=2-282. DR PDB; 1E6D; X-ray; 2.30 A; L=2-282. DR PDB; 1F6N; X-ray; 2.80 A; L=2-282. DR PDB; 1FNP; X-ray; 2.60 A; L=2-282. DR PDB; 1FNQ; X-ray; 2.60 A; L=2-282. DR PDB; 1JGW; X-ray; 2.80 A; L=2-282. DR PDB; 1JGX; X-ray; 3.01 A; L=2-282. DR PDB; 1JGY; X-ray; 2.70 A; L=2-282. DR PDB; 1JGZ; X-ray; 2.70 A; L=2-282. DR PDB; 1JH0; X-ray; 3.50 A; L=2-282. DR PDB; 1K6L; X-ray; 3.10 A; L=2-282. DR PDB; 1K6N; X-ray; 3.10 A; L=2-282. DR PDB; 1KBY; X-ray; 2.50 A; L=2-282. DR PDB; 1L9B; X-ray; 2.40 A; L=2-282. DR PDB; 1L9J; X-ray; 3.25 A; L/R=2-282. DR PDB; 1M3X; X-ray; 2.55 A; L=2-282. DR PDB; 1MPS; X-ray; 2.55 A; L=2-282. DR PDB; 1OGV; X-ray; 2.35 A; L=2-282. DR PDB; 1PCR; X-ray; 2.65 A; L=2-282. DR PDB; 1PSS; X-ray; 3.00 A; L=6-271. DR PDB; 1PST; X-ray; 3.00 A; L=6-271. DR PDB; 1QOV; X-ray; 2.10 A; L=2-282. DR PDB; 1RG5; X-ray; 2.50 A; L=2-282. DR PDB; 1RGN; X-ray; 2.80 A; L=2-282. DR PDB; 1RQK; X-ray; 2.70 A; L=2-282. DR PDB; 1RVJ; X-ray; 2.75 A; L=2-282. DR PDB; 1RY5; X-ray; 2.10 A; L=2-282. DR PDB; 1RZH; X-ray; 1.80 A; L=2-282. DR PDB; 1RZZ; X-ray; 2.40 A; L/R=2-282. DR PDB; 1S00; X-ray; 2.60 A; L/R=2-282. DR PDB; 1UMX; X-ray; 2.80 A; L=2-282. DR PDB; 1YF6; X-ray; 2.25 A; L=2-282. DR PDB; 1YST; X-ray; 3.00 A; L=2-274. DR PDB; 1Z9J; X-ray; 4.50 A; A=2-282. DR PDB; 1Z9K; X-ray; 4.60 A; A=2-282. DR PDB; 2BNP; X-ray; 2.70 A; A=2-282. DR PDB; 2BNS; X-ray; 2.50 A; A=2-282. DR PDB; 2BOZ; X-ray; 2.40 A; L=2-282. DR PDB; 2GMR; X-ray; 2.50 A; L=2-282. DR PDB; 2GNU; X-ray; 2.20 A; L=2-282. DR PDB; 2HG3; X-ray; 2.70 A; L=2-282. DR PDB; 2HG9; X-ray; 2.45 A; L=2-282. DR PDB; 2HH1; X-ray; 2.55 A; L=2-282. DR PDB; 2HHK; X-ray; 2.50 A; L=2-282. DR PDB; 2HIT; X-ray; 2.75 A; L=2-282. DR PDB; 2HJ6; X-ray; 3.00 A; L=2-282. DR PDB; 2J8C; X-ray; 1.87 A; L=2-282. DR PDB; 2J8D; X-ray; 2.07 A; L=2-282. DR PDB; 2JIY; X-ray; 2.20 A; L=2-282. DR PDB; 2JJ0; X-ray; 2.80 A; L=2-282. DR PDB; 2RCR; X-ray; 3.10 A; L=2-282. DR PDB; 2UWS; X-ray; 2.90 A; L=2-282. DR PDB; 2UWT; X-ray; 2.50 A; L=2-282. DR PDB; 2UWU; X-ray; 2.04 A; L=2-282. DR PDB; 2UWV; X-ray; 2.13 A; L=2-282. DR PDB; 2UWW; X-ray; 2.05 A; L=2-282. DR PDB; 2UX3; X-ray; 2.50 A; L=2-282. DR PDB; 2UX4; X-ray; 2.51 A; L=2-282. DR PDB; 2UX5; X-ray; 2.21 A; L=2-282. DR PDB; 2UXJ; X-ray; 2.25 A; L=2-282. DR PDB; 2UXK; X-ray; 2.31 A; L=2-282. DR PDB; 2UXL; X-ray; 2.88 A; L=2-282. DR PDB; 2UXM; X-ray; 2.70 A; L=2-282. DR PDB; 3DSY; X-ray; 3.00 A; L=2-282. DR PDB; 3DTA; X-ray; 3.20 A; L=2-282. DR PDB; 3DTR; X-ray; 3.10 A; L=2-282. DR PDB; 3DTS; X-ray; 3.10 A; L=2-282. DR PDB; 3DU2; X-ray; 3.10 A; L=2-282. DR PDB; 3DU3; X-ray; 2.80 A; L=2-282. DR PDB; 3DUQ; X-ray; 2.70 A; L=2-282. DR PDB; 3I4D; X-ray; 2.01 A; L=2-282. DR PDB; 3V3Y; X-ray; 2.80 A; L=2-282. DR PDB; 3V3Z; X-ray; 2.90 A; L=2-282. DR PDB; 3ZUM; X-ray; 2.50 A; L=2-282. DR PDB; 3ZUW; X-ray; 2.31 A; L=2-282. DR PDB; 4H99; X-ray; 2.97 A; L=2-282. DR PDB; 4H9L; X-ray; 2.77 A; L=2-282. DR PDB; 4HBH; X-ray; 2.93 A; L=2-282. DR PDB; 4HBJ; X-ray; 2.74 A; L=2-282. DR PDB; 4IN7; X-ray; 2.85 A; L=2-282. DR PDB; 4LWY; X-ray; 2.90 A; L=1-282. DR PDB; 4N7K; X-ray; 2.85 A; L=2-282. DR PDB; 4RCR; X-ray; 2.80 A; L=2-282. DR PDB; 4TQQ; X-ray; 2.50 A; L=2-282. DR PDB; 4V9G; X-ray; 7.78 A; AL/BL=1-282. DR PDB; 5LSE; X-ray; 2.50 A; L=2-282. DR PDB; 5V33; X-ray; 3.49 A; L=2-282. DR PDB; 6Z02; X-ray; 2.10 A; L=2-282. DR PDB; 6Z1J; X-ray; 2.10 A; L=2-282. DR PDB; 6Z27; X-ray; 2.10 A; L=2-282. DR PDB; 7MH3; X-ray; 2.30 A; L=1-282. DR PDB; 7MH4; X-ray; 2.48 A; L=1-282. DR PDB; 7MH5; X-ray; 2.85 A; L=1-282. DR PDB; 7MH8; X-ray; 2.75 A; L=1-282. DR PDB; 7MH9; X-ray; 3.10 A; L=1-282. DR PDB; 7MHA; X-ray; 2.79 A; L=1-282. DR PDB; 7OD5; X-ray; 2.10 A; L=2-282. DR PDB; 7P0Q; X-ray; 1.73 A; L=2-282. DR PDB; 7P17; X-ray; 2.22 A; L=2-282. DR PDB; 7Q7F; X-ray; 2.75 A; L=2-282. DR PDB; 7Q7G; X-ray; 2.69 A; L=2-282. DR PDB; 7Q7H; X-ray; 2.49 A; L=2-282. DR PDB; 7Q7J; X-ray; 2.69 A; L=2-282. DR PDB; 7Q7M; X-ray; 2.55 A; L=2-282. DR PDB; 7Q7N; X-ray; 2.87 A; L=2-282. DR PDB; 7Q7O; X-ray; 2.65 A; L=2-282. DR PDB; 7Z8D; X-ray; 2.14 A; L=2-282. DR PDB; 8C3F; X-ray; 2.60 A; L=2-282. DR PDB; 8C5X; X-ray; 2.60 A; L=2-282. DR PDB; 8C6K; X-ray; 2.86 A; L=2-282. DR PDB; 8C7C; X-ray; 2.60 A; L=2-282. DR PDB; 8C87; X-ray; 2.45 A; L=2-282. DR PDB; 8C88; X-ray; 2.75 A; L=2-282. DR PDBsum; 1AIG; -. DR PDBsum; 1AIJ; -. DR PDBsum; 1DS8; -. DR PDBsum; 1DV3; -. DR PDBsum; 1DV6; -. DR PDBsum; 1E14; -. DR PDBsum; 1E6D; -. DR PDBsum; 1F6N; -. DR PDBsum; 1FNP; -. DR PDBsum; 1FNQ; -. DR PDBsum; 1JGW; -. DR PDBsum; 1JGX; -. DR PDBsum; 1JGY; -. DR PDBsum; 1JGZ; -. DR PDBsum; 1JH0; -. DR PDBsum; 1K6L; -. DR PDBsum; 1K6N; -. DR PDBsum; 1KBY; -. DR PDBsum; 1L9B; -. DR PDBsum; 1L9J; -. DR PDBsum; 1M3X; -. DR PDBsum; 1MPS; -. DR PDBsum; 1OGV; -. DR PDBsum; 1PCR; -. DR PDBsum; 1PSS; -. DR PDBsum; 1PST; -. DR PDBsum; 1QOV; -. DR PDBsum; 1RG5; -. DR PDBsum; 1RGN; -. DR PDBsum; 1RQK; -. DR PDBsum; 1RVJ; -. DR PDBsum; 1RY5; -. DR PDBsum; 1RZH; -. DR PDBsum; 1RZZ; -. DR PDBsum; 1S00; -. DR PDBsum; 1UMX; -. DR PDBsum; 1YF6; -. DR PDBsum; 1YST; -. DR PDBsum; 1Z9J; -. DR PDBsum; 1Z9K; -. DR PDBsum; 2BNP; -. DR PDBsum; 2BNS; -. DR PDBsum; 2BOZ; -. DR PDBsum; 2GMR; -. DR PDBsum; 2GNU; -. DR PDBsum; 2HG3; -. DR PDBsum; 2HG9; -. DR PDBsum; 2HH1; -. DR PDBsum; 2HHK; -. DR PDBsum; 2HIT; -. DR PDBsum; 2HJ6; -. DR PDBsum; 2J8C; -. DR PDBsum; 2J8D; -. DR PDBsum; 2JIY; -. DR PDBsum; 2JJ0; -. DR PDBsum; 2RCR; -. DR PDBsum; 2UWS; -. DR PDBsum; 2UWT; -. DR PDBsum; 2UWU; -. DR PDBsum; 2UWV; -. DR PDBsum; 2UWW; -. DR PDBsum; 2UX3; -. DR PDBsum; 2UX4; -. DR PDBsum; 2UX5; -. DR PDBsum; 2UXJ; -. DR PDBsum; 2UXK; -. DR PDBsum; 2UXL; -. DR PDBsum; 2UXM; -. DR PDBsum; 3DSY; -. DR PDBsum; 3DTA; -. DR PDBsum; 3DTR; -. DR PDBsum; 3DTS; -. DR PDBsum; 3DU2; -. DR PDBsum; 3DU3; -. DR PDBsum; 3DUQ; -. DR PDBsum; 3I4D; -. DR PDBsum; 3V3Y; -. DR PDBsum; 3V3Z; -. DR PDBsum; 3ZUM; -. DR PDBsum; 3ZUW; -. DR PDBsum; 4H99; -. DR PDBsum; 4H9L; -. DR PDBsum; 4HBH; -. DR PDBsum; 4HBJ; -. DR PDBsum; 4IN7; -. DR PDBsum; 4LWY; -. DR PDBsum; 4N7K; -. DR PDBsum; 4RCR; -. DR PDBsum; 4TQQ; -. DR PDBsum; 4V9G; -. DR PDBsum; 5LSE; -. DR PDBsum; 5V33; -. DR PDBsum; 6Z02; -. DR PDBsum; 6Z1J; -. DR PDBsum; 6Z27; -. DR PDBsum; 7MH3; -. DR PDBsum; 7MH4; -. DR PDBsum; 7MH5; -. DR PDBsum; 7MH8; -. DR PDBsum; 7MH9; -. DR PDBsum; 7MHA; -. DR PDBsum; 7OD5; -. DR PDBsum; 7P0Q; -. DR PDBsum; 7P17; -. DR PDBsum; 7Q7F; -. DR PDBsum; 7Q7G; -. DR PDBsum; 7Q7H; -. DR PDBsum; 7Q7J; -. DR PDBsum; 7Q7M; -. DR PDBsum; 7Q7N; -. DR PDBsum; 7Q7O; -. DR PDBsum; 7Z8D; -. DR PDBsum; 8C3F; -. DR PDBsum; 8C5X; -. DR PDBsum; 8C6K; -. DR PDBsum; 8C7C; -. DR PDBsum; 8C87; -. DR PDBsum; 8C88; -. DR AlphaFoldDB; P0C0Y8; -. DR SMR; P0C0Y8; -. DR DIP; DIP-60489N; -. DR IntAct; P0C0Y8; 1. DR DrugBank; DB04147; Dodecyldimethylamine N-oxide. DR DrugBank; DB08215; Terbutryn. DR DrugBank; DB08690; Ubiquinone Q2. DR TCDB; 3.E.2.1.1; the photosynthetic reaction center (prc) family. DR GeneID; 67446990; -. DR OMA; WGHGFPY; -. DR EvolutionaryTrace; P0C0Y8; -. DR GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro. DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042314; F:bacteriochlorophyll binding; IEA:UniProtKB-KW. DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro. DR CDD; cd09290; Photo-RC_L; 1. DR Gene3D; 1.20.85.10; Photosystem II protein D1-like; 2. DR InterPro; IPR036854; Photo_II_D1/D2_sf. DR InterPro; IPR005871; Photo_RC_L. DR InterPro; IPR000484; Photo_RC_L/M. DR NCBIfam; TIGR01157; pufL; 1. DR Pfam; PF00124; Photo_RC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Bacteriochlorophyll; Chlorophyll; Chromophore; KW Electron transport; Iron; Magnesium; Membrane; Metal-binding; KW Photosynthesis; Reaction center; Transmembrane; Transmembrane helix; KW Transport. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..282 FT /note="Reaction center protein L chain" FT /id="PRO_0000090407" FT TOPO_DOM 2..32 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:1645718" FT TRANSMEM 33..56 FT /note="Helical" FT TOPO_DOM 57..83 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:1645718" FT TRANSMEM 84..112 FT /note="Helical" FT TOPO_DOM 113..116 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:1645718" FT TRANSMEM 117..139 FT /note="Helical" FT TOPO_DOM 140..171 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:1645718" FT TRANSMEM 172..199 FT /note="Helical" FT TOPO_DOM 200..225 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:1645718" FT TRANSMEM 226..251 FT /note="Helical" FT TOPO_DOM 252..282 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:1645718" FT BINDING 154 FT /ligand="(7R,8Z)-bacteriochlorophyll b" FT /ligand_id="ChEBI:CHEBI:30034" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT BINDING 174 FT /ligand="(7R,8Z)-bacteriochlorophyll b" FT /ligand_id="ChEBI:CHEBI:30034" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT BINDING 191 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 217 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT BINDING 231 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT TURN 5..7 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:7P0Q" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:7P0Q" FT TURN 20..23 FT /evidence="ECO:0007829|PDB:7P0Q" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:1KBY" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:1KBY" FT HELIX 33..57 FT /evidence="ECO:0007829|PDB:7P0Q" FT TURN 62..64 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 85..112 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 117..133 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 135..140 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 172..199 FT /evidence="ECO:0007829|PDB:7P0Q" FT STRAND 202..205 FT /evidence="ECO:0007829|PDB:1PCR" FT HELIX 210..221 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 227..250 FT /evidence="ECO:0007829|PDB:7P0Q" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:7P0Q" FT HELIX 261..268 FT /evidence="ECO:0007829|PDB:7P0Q" FT TURN 271..275 FT /evidence="ECO:0007829|PDB:7P0Q" FT STRAND 277..280 FT /evidence="ECO:0007829|PDB:7P0Q" SQ SEQUENCE 282 AA; 31457 MW; 044F4D3AF085B136 CRC64; MALLSFERKY RVPGGTLVGG NLFDFWVGPF YVGFFGVATF FFAALGIILI AWSAVLQGTW NPQLISVYPP ALEYGLGGAP LAKGGLWQII TICATGAFVS WALREVEICR KLGIGYHIPF AFAFAILAYL TLVLFRPVMM GAWGYAFPYG IWTHLDWVSN TGYTYGNFHY NPAHMIAISF FFTNALALAL HGALVLSAAN PEKGKEMRTP DHEDTFFRDL VGYSIGTLGI HRLGLLLSLS AVFFSALCMI ITGTIWFDQW VDWWQWWVKL PWWANIPGGI NG //