HEADER MEMBRANE PROTEIN 02-JUL-25 9VOR TITLE CRYO-EM STRUCTURE OF HUMAN GPR158 BOUND TO NANOBODY NB20 CAVEAT 9VOR PEE A 812 HAS WRONG CHIRALITY AT ATOM C2 PIE B 810 HAS WRONG CAVEAT 2 9VOR CHIRALITY AT ATOM C1' COMPND MOL_ID: 1; COMPND 2 MOLECULE: METABOTROPIC GLYCINE RECEPTOR; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: MGLYR,G-PROTEIN COUPLED RECEPTOR 158; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NB20; COMPND 8 CHAIN: C, E; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: GPR158, KIAA1136; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 11 ORGANISM_TAXID: 9844; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG'; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 866768 KEYWDS GPCR, ORPHAN RECEPTOR, NANOBODY, RGS PROTEINS, SIGNALLING RECEPTOR, KEYWDS 2 MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR T.LABOUTE,S.ZUCCA,M.SIAL,M.SHARMA,G.BRUNORI,S.SINGH,A.SINGH, AUTHOR 2 K.MARTEMYANOV REVDAT 1 31-DEC-25 9VOR 0 JRNL AUTH T.LABOUTE,S.ZUCCA,M.SIAL,M.SHARMA,G.BRUNORI,S.SINGH,A.SINGH, JRNL AUTH 2 K.MARTEMYANOV JRNL TITL CRYO-EM STRUCTURE OF HUMAN GPR158 BOUND TO NANOBODY NB20 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.47 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.470 REMARK 3 NUMBER OF PARTICLES : 121523 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9VOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1300061121. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : 2D ARRAY REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : GPR158 COMPLEXED WITH NB20; REMARK 245 GPR158; NANOBODY REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.80 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 40 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4800.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 ALA A 3 REMARK 465 MET A 4 REMARK 465 ALA A 5 REMARK 465 TYR A 6 REMARK 465 PRO A 7 REMARK 465 LEU A 8 REMARK 465 LEU A 9 REMARK 465 LEU A 10 REMARK 465 CYS A 11 REMARK 465 LEU A 12 REMARK 465 LEU A 13 REMARK 465 LEU A 14 REMARK 465 ALA A 15 REMARK 465 GLN A 16 REMARK 465 LEU A 17 REMARK 465 GLY A 18 REMARK 465 LEU A 19 REMARK 465 GLY A 20 REMARK 465 ALA A 21 REMARK 465 VAL A 22 REMARK 465 GLY A 23 REMARK 465 ALA A 24 REMARK 465 SER A 25 REMARK 465 ARG A 26 REMARK 465 ASP A 27 REMARK 465 PRO A 28 REMARK 465 GLN A 29 REMARK 465 GLY A 30 REMARK 465 ARG A 31 REMARK 465 PRO A 32 REMARK 465 ASP A 33 REMARK 465 SER A 34 REMARK 465 PRO A 35 REMARK 465 ARG A 36 REMARK 465 GLU A 37 REMARK 465 ARG A 38 REMARK 465 THR A 39 REMARK 465 PRO A 40 REMARK 465 LYS A 41 REMARK 465 GLY A 42 REMARK 465 LYS A 43 REMARK 465 PRO A 44 REMARK 465 HIS A 45 REMARK 465 ALA A 46 REMARK 465 GLN A 47 REMARK 465 GLN A 48 REMARK 465 PRO A 49 REMARK 465 GLY A 50 REMARK 465 ARG A 51 REMARK 465 ALA A 52 REMARK 465 SER A 53 REMARK 465 ALA A 54 REMARK 465 SER A 55 REMARK 465 ASP A 56 REMARK 465 SER A 57 REMARK 465 SER A 58 REMARK 465 ALA A 59 REMARK 465 PRO A 60 REMARK 465 TRP A 61 REMARK 465 SER A 62 REMARK 465 ARG A 63 REMARK 465 SER A 64 REMARK 465 THR A 65 REMARK 465 ASP A 181 REMARK 465 SER A 182 REMARK 465 LEU A 183 REMARK 465 SER A 184 REMARK 465 ALA A 185 REMARK 465 PRO A 186 REMARK 465 LEU A 206 REMARK 465 SER A 207 REMARK 465 SER A 208 REMARK 465 SER A 209 REMARK 465 ALA A 210 REMARK 465 PRO A 211 REMARK 465 HIS A 212 REMARK 465 LEU A 213 REMARK 465 ALA A 214 REMARK 465 ASN A 215 REMARK 465 ALA A 216 REMARK 465 THR A 217 REMARK 465 LEU A 218 REMARK 465 GLU A 219 REMARK 465 THR A 220 REMARK 465 GLU A 221 REMARK 465 TRP A 222 REMARK 465 PHE A 223 REMARK 465 HIS A 224 REMARK 465 GLY A 225 REMARK 465 LEU A 226 REMARK 465 ARG A 227 REMARK 465 ARG A 228 REMARK 465 LYS A 229 REMARK 465 TRP A 230 REMARK 465 ARG A 231 REMARK 465 PRO A 232 REMARK 465 HIS A 233 REMARK 465 LEU A 234 REMARK 465 HIS A 235 REMARK 465 ARG A 236 REMARK 465 ARG A 237 REMARK 465 GLY A 238 REMARK 465 PRO A 239 REMARK 465 ASN A 240 REMARK 465 GLN A 241 REMARK 465 GLY A 242 REMARK 465 PRO A 243 REMARK 465 ARG A 244 REMARK 465 GLY A 245 REMARK 465 LEU A 246 REMARK 465 GLY A 247 REMARK 465 HIS A 248 REMARK 465 SER A 249 REMARK 465 TRP A 250 REMARK 465 ARG A 251 REMARK 465 ARG A 252 REMARK 465 LYS A 253 REMARK 465 ASP A 254 REMARK 465 GLY A 255 REMARK 465 LEU A 256 REMARK 465 GLY A 257 REMARK 465 GLY A 258 REMARK 465 GLN A 293 REMARK 465 PRO A 294 REMARK 465 ASN A 295 REMARK 465 LEU A 296 REMARK 465 VAL A 297 REMARK 465 SER A 671 REMARK 465 ASN A 672 REMARK 465 ASN A 673 REMARK 465 PRO A 674 REMARK 465 ARG A 675 REMARK 465 ASP A 676 REMARK 465 ASP A 677 REMARK 465 ILE A 678 REMARK 465 ALA A 679 REMARK 465 THR A 680 REMARK 465 GLU A 681 REMARK 465 ALA A 682 REMARK 465 TYR A 683 REMARK 465 GLU A 684 REMARK 465 ASP A 685 REMARK 465 GLU A 686 REMARK 465 LEU A 687 REMARK 465 ASP A 688 REMARK 465 MET A 689 REMARK 465 GLY A 690 REMARK 465 ARG A 691 REMARK 465 SER A 692 REMARK 465 GLY A 693 REMARK 465 SER A 694 REMARK 465 TYR A 695 REMARK 465 LEU A 696 REMARK 465 ASN A 697 REMARK 465 SER A 698 REMARK 465 SER A 699 REMARK 465 ILE A 700 REMARK 465 ASN A 701 REMARK 465 SER A 702 REMARK 465 ALA A 703 REMARK 465 TRP A 704 REMARK 465 SER A 705 REMARK 465 GLU A 706 REMARK 465 HIS A 707 REMARK 465 SER A 708 REMARK 465 LEU A 709 REMARK 465 ASP A 710 REMARK 465 PRO A 711 REMARK 465 GLU A 712 REMARK 465 ASP A 713 REMARK 465 ILE A 714 REMARK 465 ARG A 715 REMARK 465 ASP A 716 REMARK 465 GLU A 717 REMARK 465 LEU A 718 REMARK 465 LYS A 719 REMARK 465 LYS A 720 REMARK 465 LEU A 721 REMARK 465 TYR A 722 REMARK 465 ALA A 723 REMARK 465 GLN A 724 REMARK 465 LEU A 725 REMARK 465 GLU A 726 REMARK 465 ILE A 727 REMARK 465 TYR A 728 REMARK 465 LYS A 729 REMARK 465 ARG A 730 REMARK 465 LYS A 731 REMARK 465 LYS A 732 REMARK 465 MET A 733 REMARK 465 ILE A 734 REMARK 465 THR A 735 REMARK 465 ASN A 736 REMARK 465 ASN A 737 REMARK 465 PRO A 738 REMARK 465 HIS A 739 REMARK 465 LEU A 740 REMARK 465 GLN A 741 REMARK 465 LYS A 742 REMARK 465 LYS A 743 REMARK 465 ARG A 744 REMARK 465 CYS A 745 REMARK 465 SER A 746 REMARK 465 LYS A 747 REMARK 465 LYS A 748 REMARK 465 GLY A 749 REMARK 465 LEU A 750 REMARK 465 GLY A 751 REMARK 465 ARG A 752 REMARK 465 SER A 753 REMARK 465 ILE A 754 REMARK 465 MET A 755 REMARK 465 ARG A 756 REMARK 465 ARG A 757 REMARK 465 ILE A 758 REMARK 465 THR A 759 REMARK 465 GLU A 760 REMARK 465 ILE A 761 REMARK 465 PRO A 762 REMARK 465 GLU A 763 REMARK 465 THR A 764 REMARK 465 VAL A 765 REMARK 465 SER A 766 REMARK 465 ARG A 767 REMARK 465 GLN A 768 REMARK 465 CYS A 769 REMARK 465 SER A 770 REMARK 465 LYS A 771 REMARK 465 GLU A 772 REMARK 465 ASP A 773 REMARK 465 LYS A 774 REMARK 465 GLU A 775 REMARK 465 LEU A 776 REMARK 465 GLU A 777 REMARK 465 VAL A 778 REMARK 465 LEU A 779 REMARK 465 PHE A 780 REMARK 465 GLN A 781 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 ALA B 3 REMARK 465 MET B 4 REMARK 465 ALA B 5 REMARK 465 TYR B 6 REMARK 465 PRO B 7 REMARK 465 LEU B 8 REMARK 465 LEU B 9 REMARK 465 LEU B 10 REMARK 465 CYS B 11 REMARK 465 LEU B 12 REMARK 465 LEU B 13 REMARK 465 LEU B 14 REMARK 465 ALA B 15 REMARK 465 GLN B 16 REMARK 465 LEU B 17 REMARK 465 GLY B 18 REMARK 465 LEU B 19 REMARK 465 GLY B 20 REMARK 465 ALA B 21 REMARK 465 VAL B 22 REMARK 465 GLY B 23 REMARK 465 ALA B 24 REMARK 465 SER B 25 REMARK 465 ARG B 26 REMARK 465 ASP B 27 REMARK 465 PRO B 28 REMARK 465 GLN B 29 REMARK 465 GLY B 30 REMARK 465 ARG B 31 REMARK 465 PRO B 32 REMARK 465 ASP B 33 REMARK 465 SER B 34 REMARK 465 PRO B 35 REMARK 465 ARG B 36 REMARK 465 GLU B 37 REMARK 465 ARG B 38 REMARK 465 THR B 39 REMARK 465 PRO B 40 REMARK 465 LYS B 41 REMARK 465 GLY B 42 REMARK 465 LYS B 43 REMARK 465 PRO B 44 REMARK 465 HIS B 45 REMARK 465 ALA B 46 REMARK 465 GLN B 47 REMARK 465 GLN B 48 REMARK 465 PRO B 49 REMARK 465 GLY B 50 REMARK 465 ARG B 51 REMARK 465 ALA B 52 REMARK 465 SER B 53 REMARK 465 ALA B 54 REMARK 465 SER B 55 REMARK 465 ASP B 56 REMARK 465 SER B 57 REMARK 465 SER B 58 REMARK 465 ALA B 59 REMARK 465 PRO B 60 REMARK 465 TRP B 61 REMARK 465 SER B 62 REMARK 465 ARG B 63 REMARK 465 SER B 64 REMARK 465 THR B 65 REMARK 465 ASP B 181 REMARK 465 SER B 182 REMARK 465 LEU B 183 REMARK 465 SER B 184 REMARK 465 ALA B 185 REMARK 465 PRO B 186 REMARK 465 LEU B 206 REMARK 465 SER B 207 REMARK 465 SER B 208 REMARK 465 SER B 209 REMARK 465 ALA B 210 REMARK 465 PRO B 211 REMARK 465 HIS B 212 REMARK 465 LEU B 213 REMARK 465 ALA B 214 REMARK 465 ASN B 215 REMARK 465 ALA B 216 REMARK 465 THR B 217 REMARK 465 LEU B 218 REMARK 465 GLU B 219 REMARK 465 THR B 220 REMARK 465 GLU B 221 REMARK 465 TRP B 222 REMARK 465 PHE B 223 REMARK 465 HIS B 224 REMARK 465 GLY B 225 REMARK 465 LEU B 226 REMARK 465 ARG B 227 REMARK 465 ARG B 228 REMARK 465 LYS B 229 REMARK 465 TRP B 230 REMARK 465 ARG B 231 REMARK 465 PRO B 232 REMARK 465 HIS B 233 REMARK 465 LEU B 234 REMARK 465 HIS B 235 REMARK 465 ARG B 236 REMARK 465 ARG B 237 REMARK 465 GLY B 238 REMARK 465 PRO B 239 REMARK 465 ASN B 240 REMARK 465 GLN B 241 REMARK 465 GLY B 242 REMARK 465 PRO B 243 REMARK 465 ARG B 244 REMARK 465 GLY B 245 REMARK 465 LEU B 246 REMARK 465 GLY B 247 REMARK 465 HIS B 248 REMARK 465 SER B 249 REMARK 465 TRP B 250 REMARK 465 ARG B 251 REMARK 465 ARG B 252 REMARK 465 LYS B 253 REMARK 465 ASP B 254 REMARK 465 GLY B 255 REMARK 465 LEU B 256 REMARK 465 GLY B 257 REMARK 465 GLY B 258 REMARK 465 ASP B 259 REMARK 465 LYS B 260 REMARK 465 PRO B 294 REMARK 465 ASN B 295 REMARK 465 LEU B 296 REMARK 465 VAL B 297 REMARK 465 SER B 671 REMARK 465 ASN B 672 REMARK 465 ASN B 673 REMARK 465 PRO B 674 REMARK 465 ARG B 675 REMARK 465 ASP B 676 REMARK 465 ASP B 677 REMARK 465 ILE B 678 REMARK 465 ALA B 679 REMARK 465 THR B 680 REMARK 465 GLU B 681 REMARK 465 ALA B 682 REMARK 465 TYR B 683 REMARK 465 GLU B 684 REMARK 465 ASP B 685 REMARK 465 GLU B 686 REMARK 465 LEU B 687 REMARK 465 ASP B 688 REMARK 465 MET B 689 REMARK 465 GLY B 690 REMARK 465 ARG B 691 REMARK 465 SER B 692 REMARK 465 GLY B 693 REMARK 465 SER B 694 REMARK 465 TYR B 695 REMARK 465 LEU B 696 REMARK 465 ASN B 697 REMARK 465 SER B 698 REMARK 465 SER B 699 REMARK 465 ILE B 700 REMARK 465 ASN B 701 REMARK 465 SER B 702 REMARK 465 ALA B 703 REMARK 465 TRP B 704 REMARK 465 SER B 705 REMARK 465 GLU B 706 REMARK 465 HIS B 707 REMARK 465 SER B 708 REMARK 465 LEU B 709 REMARK 465 ASP B 710 REMARK 465 PRO B 711 REMARK 465 GLU B 712 REMARK 465 ASP B 713 REMARK 465 ILE B 714 REMARK 465 ARG B 715 REMARK 465 ASP B 716 REMARK 465 GLU B 717 REMARK 465 LEU B 718 REMARK 465 LYS B 719 REMARK 465 LYS B 720 REMARK 465 LEU B 721 REMARK 465 TYR B 722 REMARK 465 ALA B 723 REMARK 465 GLN B 724 REMARK 465 LEU B 725 REMARK 465 GLU B 726 REMARK 465 ILE B 727 REMARK 465 TYR B 728 REMARK 465 LYS B 729 REMARK 465 ARG B 730 REMARK 465 LYS B 731 REMARK 465 LYS B 732 REMARK 465 MET B 733 REMARK 465 ILE B 734 REMARK 465 THR B 735 REMARK 465 ASN B 736 REMARK 465 ASN B 737 REMARK 465 PRO B 738 REMARK 465 HIS B 739 REMARK 465 LEU B 740 REMARK 465 GLN B 741 REMARK 465 LYS B 742 REMARK 465 LYS B 743 REMARK 465 ARG B 744 REMARK 465 CYS B 745 REMARK 465 SER B 746 REMARK 465 LYS B 747 REMARK 465 LYS B 748 REMARK 465 GLY B 749 REMARK 465 LEU B 750 REMARK 465 GLY B 751 REMARK 465 ARG B 752 REMARK 465 SER B 753 REMARK 465 ILE B 754 REMARK 465 MET B 755 REMARK 465 ARG B 756 REMARK 465 ARG B 757 REMARK 465 ILE B 758 REMARK 465 THR B 759 REMARK 465 GLU B 760 REMARK 465 ILE B 761 REMARK 465 PRO B 762 REMARK 465 GLU B 763 REMARK 465 THR B 764 REMARK 465 VAL B 765 REMARK 465 SER B 766 REMARK 465 ARG B 767 REMARK 465 GLN B 768 REMARK 465 CYS B 769 REMARK 465 SER B 770 REMARK 465 LYS B 771 REMARK 465 GLU B 772 REMARK 465 ASP B 773 REMARK 465 LYS B 774 REMARK 465 GLU B 775 REMARK 465 LEU B 776 REMARK 465 GLU B 777 REMARK 465 VAL B 778 REMARK 465 LEU B 779 REMARK 465 PHE B 780 REMARK 465 GLN B 781 REMARK 465 MET C -19 REMARK 465 GLY C -18 REMARK 465 SER C -17 REMARK 465 SER C -16 REMARK 465 HIS C -15 REMARK 465 HIS C -14 REMARK 465 HIS C -13 REMARK 465 HIS C -12 REMARK 465 HIS C -11 REMARK 465 HIS C -10 REMARK 465 HIS C -9 REMARK 465 HIS C -8 REMARK 465 LEU C -7 REMARK 465 GLU C -6 REMARK 465 VAL C -5 REMARK 465 LEU C -4 REMARK 465 PHE C -3 REMARK 465 GLN C -2 REMARK 465 GLY C -1 REMARK 465 PRO C 0 REMARK 465 ALA C 1 REMARK 465 GLU C 123 REMARK 465 PRO C 124 REMARK 465 LYS C 125 REMARK 465 THR C 126 REMARK 465 PRO C 127 REMARK 465 LYS C 128 REMARK 465 PRO C 129 REMARK 465 GLN C 130 REMARK 465 MET E -19 REMARK 465 GLY E -18 REMARK 465 SER E -17 REMARK 465 SER E -16 REMARK 465 HIS E -15 REMARK 465 HIS E -14 REMARK 465 HIS E -13 REMARK 465 HIS E -12 REMARK 465 HIS E -11 REMARK 465 HIS E -10 REMARK 465 HIS E -9 REMARK 465 HIS E -8 REMARK 465 LEU E -7 REMARK 465 GLU E -6 REMARK 465 VAL E -5 REMARK 465 LEU E -4 REMARK 465 PHE E -3 REMARK 465 GLN E -2 REMARK 465 GLY E -1 REMARK 465 PRO E 0 REMARK 465 ALA E 1 REMARK 465 GLU E 123 REMARK 465 PRO E 124 REMARK 465 LYS E 125 REMARK 465 THR E 126 REMARK 465 PRO E 127 REMARK 465 LYS E 128 REMARK 465 PRO E 129 REMARK 465 GLN E 130 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 95 CG CD CE NZ REMARK 470 ARG A 96 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 259 CG OD1 OD2 REMARK 470 HIS A 328 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 332 CG CD1 CD2 REMARK 470 ASN A 333 CG OD1 ND2 REMARK 470 ASN A 334 CG OD1 ND2 REMARK 470 SER A 335 OG REMARK 470 GLU A 336 CG CD OE1 OE2 REMARK 470 MET A 338 CG SD CE REMARK 470 ILE A 340 CG1 CG2 CD1 REMARK 470 LYS A 341 CG CD CE NZ REMARK 470 LEU A 343 CG CD1 CD2 REMARK 470 PHE A 345 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL A 346 CG1 CG2 REMARK 470 LEU A 347 CG CD1 CD2 REMARK 470 TYR A 350 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 351 CG CD OE1 OE2 REMARK 470 LYS A 355 CG CD CE NZ REMARK 470 TYR A 359 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS A 360 CG ND1 CD2 CE1 NE2 REMARK 470 VAL A 363 CG1 CG2 REMARK 470 LEU A 364 CG CD1 CD2 REMARK 470 VAL A 366 CG1 CG2 REMARK 470 ASN A 367 CG OD1 ND2 REMARK 470 ASN A 368 CG OD1 ND2 REMARK 470 PHE A 369 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 370 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 371 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 372 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 375 CG OD1 OD2 REMARK 470 GLN A 376 CG CD OE1 NE2 REMARK 470 HIS A 377 CG ND1 CD2 CE1 NE2 REMARK 470 ILE A 378 CG1 CG2 CD1 REMARK 470 SER A 381 OG REMARK 470 THR A 382 OG1 CG2 REMARK 470 LYS A 383 CG CD CE NZ REMARK 470 ASP A 384 CG OD1 OD2 REMARK 470 VAL A 385 CG1 CG2 REMARK 470 SER A 386 OG REMARK 470 GLU A 387 CG CD OE1 OE2 REMARK 470 GLU A 388 CG CD OE1 OE2 REMARK 470 TYR A 390 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL A 391 CG1 CG2 REMARK 470 LEU A 393 CG CD1 CD2 REMARK 470 PRO A 394 CG CD REMARK 470 ARG A 396 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 397 CG CD OE1 OE2 REMARK 470 MET A 529 CG SD CE REMARK 470 HIS A 567 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 95 CG CD CE NZ REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 293 CG CD OE1 NE2 REMARK 470 ASN B 334 CG OD1 ND2 REMARK 470 SER B 335 OG REMARK 470 GLU B 336 CG CD OE1 OE2 REMARK 470 MET B 338 CG SD CE REMARK 470 ILE B 340 CG1 CG2 CD1 REMARK 470 LYS B 341 CG CD CE NZ REMARK 470 LEU B 343 CG CD1 CD2 REMARK 470 PHE B 345 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL B 346 CG1 CG2 REMARK 470 LEU B 347 CG CD1 CD2 REMARK 470 TYR B 350 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU B 351 CG CD OE1 OE2 REMARK 470 ILE B 353 CG1 CG2 CD1 REMARK 470 LYS B 355 CG CD CE NZ REMARK 470 TYR B 359 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU B 364 CG CD1 CD2 REMARK 470 VAL B 366 CG1 CG2 REMARK 470 ASN B 367 CG OD1 ND2 REMARK 470 ASN B 368 CG OD1 ND2 REMARK 470 PHE B 369 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 370 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 371 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 372 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 375 CG OD1 OD2 REMARK 470 GLN B 376 CG CD OE1 NE2 REMARK 470 HIS B 377 CG ND1 CD2 CE1 NE2 REMARK 470 ILE B 378 CG1 CG2 CD1 REMARK 470 SER B 379 OG REMARK 470 SER B 381 OG REMARK 470 THR B 382 OG1 CG2 REMARK 470 LYS B 383 CG CD CE NZ REMARK 470 ASP B 384 CG OD1 OD2 REMARK 470 VAL B 385 CG1 CG2 REMARK 470 SER B 386 OG REMARK 470 GLU B 387 CG CD OE1 OE2 REMARK 470 GLU B 388 CG CD OE1 OE2 REMARK 470 TYR B 390 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL B 391 CG1 CG2 REMARK 470 LEU B 393 CG CD1 CD2 REMARK 470 PRO B 394 CG CD REMARK 470 ARG B 396 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 397 CG CD OE1 OE2 REMARK 470 ARG B 525 CG CD NE CZ NH1 NH2 REMARK 470 MET B 529 CG SD CE REMARK 470 HIS B 567 CG ND1 CD2 CE1 NE2 REMARK 470 GLU E 2 N REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 NH1 ARG A 525 O2P PEE A 812 2.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 MET A 80 -7.50 74.95 REMARK 500 ARG A 96 -165.75 -127.41 REMARK 500 ALA A 97 71.45 63.11 REMARK 500 SER A 100 -165.49 -78.33 REMARK 500 ALA A 116 177.55 -59.15 REMARK 500 ALA A 118 21.94 -76.88 REMARK 500 HIS A 119 157.72 72.04 REMARK 500 VAL A 138 -57.77 -134.04 REMARK 500 LYS A 144 13.12 59.79 REMARK 500 SER A 145 51.64 -92.21 REMARK 500 GLU A 147 -168.33 54.61 REMARK 500 PRO A 169 1.69 -68.79 REMARK 500 SER A 172 -163.81 -79.35 REMARK 500 SER A 179 98.46 -64.71 REMARK 500 GLU A 197 -5.71 72.38 REMARK 500 GLU A 273 -108.72 40.40 REMARK 500 TYR A 277 169.44 60.72 REMARK 500 GLU A 299 -155.83 60.44 REMARK 500 CYS A 318 14.13 55.51 REMARK 500 SER A 320 -165.11 -78.23 REMARK 500 ASN A 334 -101.00 55.89 REMARK 500 MET A 338 -51.06 175.38 REMARK 500 LEU A 347 -60.33 -95.48 REMARK 500 CYS A 354 -62.02 -101.04 REMARK 500 ALA A 356 -134.62 54.30 REMARK 500 TYR A 359 -169.72 -169.06 REMARK 500 LEU A 364 70.21 61.94 REMARK 500 ARG A 372 -4.17 71.71 REMARK 500 ILE A 378 -151.21 53.87 REMARK 500 SER A 386 -148.78 73.50 REMARK 500 TYR A 390 -167.38 -167.18 REMARK 500 ASP A 404 -155.63 117.57 REMARK 500 CYS A 408 -76.15 75.32 REMARK 500 SER A 477 -166.81 -76.25 REMARK 500 TYR A 496 47.17 -91.00 REMARK 500 GLN A 516 59.63 35.63 REMARK 500 ARG A 517 135.28 -171.13 REMARK 500 THR A 522 -169.69 -70.17 REMARK 500 CYS A 549 46.55 -90.10 REMARK 500 GLN A 550 -35.21 -130.51 REMARK 500 ARG A 577 -7.08 72.92 REMARK 500 PRO A 665 46.26 -77.34 REMARK 500 ASP B 90 -73.95 63.48 REMARK 500 LEU B 94 115.95 -161.65 REMARK 500 CYS B 99 94.88 -68.32 REMARK 500 TYR B 103 135.82 -170.26 REMARK 500 ALA B 106 -105.40 54.43 REMARK 500 PRO B 109 44.31 -82.35 REMARK 500 ALA B 116 -8.48 81.00 REMARK 500 HIS B 119 147.25 64.62 REMARK 500 REMARK 500 THIS ENTRY HAS 107 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PEE A 812 REMARK 610 PIE B 810 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-65225 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HUMAN GPR158 BOUND TO NANOBODY NB20 DBREF 9VOR A 1 775 UNP Q5T848 MGLYR_HUMAN 1 775 DBREF 9VOR B 1 775 UNP Q5T848 MGLYR_HUMAN 1 775 DBREF 9VOR C -19 130 PDB 9VOR 9VOR -19 130 DBREF 9VOR E -19 130 PDB 9VOR 9VOR -19 130 SEQADV 9VOR LEU A 776 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR GLU A 777 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR VAL A 778 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR LEU A 779 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR PHE A 780 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR GLN A 781 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR LEU B 776 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR GLU B 777 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR VAL B 778 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR LEU B 779 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR PHE B 780 UNP Q5T848 EXPRESSION TAG SEQADV 9VOR GLN B 781 UNP Q5T848 EXPRESSION TAG SEQRES 1 A 781 MET GLY ALA MET ALA TYR PRO LEU LEU LEU CYS LEU LEU SEQRES 2 A 781 LEU ALA GLN LEU GLY LEU GLY ALA VAL GLY ALA SER ARG SEQRES 3 A 781 ASP PRO GLN GLY ARG PRO ASP SER PRO ARG GLU ARG THR SEQRES 4 A 781 PRO LYS GLY LYS PRO HIS ALA GLN GLN PRO GLY ARG ALA SEQRES 5 A 781 SER ALA SER ASP SER SER ALA PRO TRP SER ARG SER THR SEQRES 6 A 781 ASP GLY THR ILE LEU ALA GLN LYS LEU ALA GLU GLU VAL SEQRES 7 A 781 PRO MET ASP VAL ALA SER TYR LEU TYR THR GLY ASP SER SEQRES 8 A 781 HIS GLN LEU LYS ARG ALA ASN CYS SER GLY ARG TYR GLU SEQRES 9 A 781 LEU ALA GLY LEU PRO GLY LYS TRP PRO ALA LEU ALA SER SEQRES 10 A 781 ALA HIS PRO SER LEU HIS ARG ALA LEU ASP THR LEU THR SEQRES 11 A 781 HIS ALA THR ASN PHE LEU ASN VAL MET LEU GLN SER ASN SEQRES 12 A 781 LYS SER ARG GLU GLN ASN LEU GLN ASP ASP LEU ASP TRP SEQRES 13 A 781 TYR GLN ALA LEU VAL TRP SER LEU LEU GLU GLY GLU PRO SEQRES 14 A 781 SER ILE SER ARG ALA ALA ILE THR PHE SER THR ASP SER SEQRES 15 A 781 LEU SER ALA PRO ALA PRO GLN VAL PHE LEU GLN ALA THR SEQRES 16 A 781 ARG GLU GLU SER ARG ILE LEU LEU GLN ASP LEU SER SER SEQRES 17 A 781 SER ALA PRO HIS LEU ALA ASN ALA THR LEU GLU THR GLU SEQRES 18 A 781 TRP PHE HIS GLY LEU ARG ARG LYS TRP ARG PRO HIS LEU SEQRES 19 A 781 HIS ARG ARG GLY PRO ASN GLN GLY PRO ARG GLY LEU GLY SEQRES 20 A 781 HIS SER TRP ARG ARG LYS ASP GLY LEU GLY GLY ASP LYS SEQRES 21 A 781 SER HIS PHE LYS TRP SER PRO PRO TYR LEU GLU CYS GLU SEQRES 22 A 781 ASN GLY SER TYR LYS PRO GLY TRP LEU VAL THR LEU SER SEQRES 23 A 781 SER ALA ILE TYR GLY LEU GLN PRO ASN LEU VAL PRO GLU SEQRES 24 A 781 PHE ARG GLY VAL MET LYS VAL ASP ILE ASN LEU GLN LYS SEQRES 25 A 781 VAL ASP ILE ASP GLN CYS SER SER ASP GLY TRP PHE SER SEQRES 26 A 781 GLY THR HIS LYS CYS HIS LEU ASN ASN SER GLU CYS MET SEQRES 27 A 781 PRO ILE LYS GLY LEU GLY PHE VAL LEU GLY ALA TYR GLU SEQRES 28 A 781 CYS ILE CYS LYS ALA GLY PHE TYR HIS PRO GLY VAL LEU SEQRES 29 A 781 PRO VAL ASN ASN PHE ARG ARG ARG GLY PRO ASP GLN HIS SEQRES 30 A 781 ILE SER GLY SER THR LYS ASP VAL SER GLU GLU ALA TYR SEQRES 31 A 781 VAL CYS LEU PRO CYS ARG GLU GLY CYS PRO PHE CYS ALA SEQRES 32 A 781 ASP ASP SER PRO CYS PHE VAL GLN GLU ASP LYS TYR LEU SEQRES 33 A 781 ARG LEU ALA ILE ILE SER PHE GLN ALA LEU CYS MET LEU SEQRES 34 A 781 LEU ASP PHE VAL SER MET LEU VAL VAL TYR HIS PHE ARG SEQRES 35 A 781 LYS ALA LYS SER ILE ARG ALA SER GLY LEU ILE LEU LEU SEQRES 36 A 781 GLU THR ILE LEU PHE GLY SER LEU LEU LEU TYR PHE PRO SEQRES 37 A 781 VAL VAL ILE LEU TYR PHE GLU PRO SER THR PHE ARG CYS SEQRES 38 A 781 ILE LEU LEU ARG TRP ALA ARG LEU LEU GLY PHE ALA THR SEQRES 39 A 781 VAL TYR GLY THR VAL THR LEU LYS LEU HIS ARG VAL LEU SEQRES 40 A 781 LYS VAL PHE LEU SER ARG THR ALA GLN ARG ILE PRO TYR SEQRES 41 A 781 MET THR GLY GLY ARG VAL MET ARG MET LEU ALA VAL ILE SEQRES 42 A 781 LEU LEU VAL VAL PHE TRP PHE LEU ILE GLY TRP THR SER SEQRES 43 A 781 SER VAL CYS GLN ASN LEU GLU LYS GLN ILE SER LEU ILE SEQRES 44 A 781 GLY GLN GLY LYS THR SER ASP HIS LEU ILE PHE ASN MET SEQRES 45 A 781 CYS LEU ILE ASP ARG TRP ASP TYR MET THR ALA VAL ALA SEQRES 46 A 781 GLU PHE LEU PHE LEU LEU TRP GLY VAL TYR LEU CYS TYR SEQRES 47 A 781 ALA VAL ARG THR VAL PRO SER ALA PHE HIS GLU PRO ARG SEQRES 48 A 781 TYR MET ALA VAL ALA VAL HIS ASN GLU LEU ILE ILE SER SEQRES 49 A 781 ALA ILE PHE HIS THR ILE ARG PHE VAL LEU ALA SER ARG SEQRES 50 A 781 LEU GLN SER ASP TRP MET LEU MET LEU TYR PHE ALA HIS SEQRES 51 A 781 THR HIS LEU THR VAL THR VAL THR ILE GLY LEU LEU LEU SEQRES 52 A 781 ILE PRO LYS PHE SER HIS SER SER ASN ASN PRO ARG ASP SEQRES 53 A 781 ASP ILE ALA THR GLU ALA TYR GLU ASP GLU LEU ASP MET SEQRES 54 A 781 GLY ARG SER GLY SER TYR LEU ASN SER SER ILE ASN SER SEQRES 55 A 781 ALA TRP SER GLU HIS SER LEU ASP PRO GLU ASP ILE ARG SEQRES 56 A 781 ASP GLU LEU LYS LYS LEU TYR ALA GLN LEU GLU ILE TYR SEQRES 57 A 781 LYS ARG LYS LYS MET ILE THR ASN ASN PRO HIS LEU GLN SEQRES 58 A 781 LYS LYS ARG CYS SER LYS LYS GLY LEU GLY ARG SER ILE SEQRES 59 A 781 MET ARG ARG ILE THR GLU ILE PRO GLU THR VAL SER ARG SEQRES 60 A 781 GLN CYS SER LYS GLU ASP LYS GLU LEU GLU VAL LEU PHE SEQRES 61 A 781 GLN SEQRES 1 B 781 MET GLY ALA MET ALA TYR PRO LEU LEU LEU CYS LEU LEU SEQRES 2 B 781 LEU ALA GLN LEU GLY LEU GLY ALA VAL GLY ALA SER ARG SEQRES 3 B 781 ASP PRO GLN GLY ARG PRO ASP SER PRO ARG GLU ARG THR SEQRES 4 B 781 PRO LYS GLY LYS PRO HIS ALA GLN GLN PRO GLY ARG ALA SEQRES 5 B 781 SER ALA SER ASP SER SER ALA PRO TRP SER ARG SER THR SEQRES 6 B 781 ASP GLY THR ILE LEU ALA GLN LYS LEU ALA GLU GLU VAL SEQRES 7 B 781 PRO MET ASP VAL ALA SER TYR LEU TYR THR GLY ASP SER SEQRES 8 B 781 HIS GLN LEU LYS ARG ALA ASN CYS SER GLY ARG TYR GLU SEQRES 9 B 781 LEU ALA GLY LEU PRO GLY LYS TRP PRO ALA LEU ALA SER SEQRES 10 B 781 ALA HIS PRO SER LEU HIS ARG ALA LEU ASP THR LEU THR SEQRES 11 B 781 HIS ALA THR ASN PHE LEU ASN VAL MET LEU GLN SER ASN SEQRES 12 B 781 LYS SER ARG GLU GLN ASN LEU GLN ASP ASP LEU ASP TRP SEQRES 13 B 781 TYR GLN ALA LEU VAL TRP SER LEU LEU GLU GLY GLU PRO SEQRES 14 B 781 SER ILE SER ARG ALA ALA ILE THR PHE SER THR ASP SER SEQRES 15 B 781 LEU SER ALA PRO ALA PRO GLN VAL PHE LEU GLN ALA THR SEQRES 16 B 781 ARG GLU GLU SER ARG ILE LEU LEU GLN ASP LEU SER SER SEQRES 17 B 781 SER ALA PRO HIS LEU ALA ASN ALA THR LEU GLU THR GLU SEQRES 18 B 781 TRP PHE HIS GLY LEU ARG ARG LYS TRP ARG PRO HIS LEU SEQRES 19 B 781 HIS ARG ARG GLY PRO ASN GLN GLY PRO ARG GLY LEU GLY SEQRES 20 B 781 HIS SER TRP ARG ARG LYS ASP GLY LEU GLY GLY ASP LYS SEQRES 21 B 781 SER HIS PHE LYS TRP SER PRO PRO TYR LEU GLU CYS GLU SEQRES 22 B 781 ASN GLY SER TYR LYS PRO GLY TRP LEU VAL THR LEU SER SEQRES 23 B 781 SER ALA ILE TYR GLY LEU GLN PRO ASN LEU VAL PRO GLU SEQRES 24 B 781 PHE ARG GLY VAL MET LYS VAL ASP ILE ASN LEU GLN LYS SEQRES 25 B 781 VAL ASP ILE ASP GLN CYS SER SER ASP GLY TRP PHE SER SEQRES 26 B 781 GLY THR HIS LYS CYS HIS LEU ASN ASN SER GLU CYS MET SEQRES 27 B 781 PRO ILE LYS GLY LEU GLY PHE VAL LEU GLY ALA TYR GLU SEQRES 28 B 781 CYS ILE CYS LYS ALA GLY PHE TYR HIS PRO GLY VAL LEU SEQRES 29 B 781 PRO VAL ASN ASN PHE ARG ARG ARG GLY PRO ASP GLN HIS SEQRES 30 B 781 ILE SER GLY SER THR LYS ASP VAL SER GLU GLU ALA TYR SEQRES 31 B 781 VAL CYS LEU PRO CYS ARG GLU GLY CYS PRO PHE CYS ALA SEQRES 32 B 781 ASP ASP SER PRO CYS PHE VAL GLN GLU ASP LYS TYR LEU SEQRES 33 B 781 ARG LEU ALA ILE ILE SER PHE GLN ALA LEU CYS MET LEU SEQRES 34 B 781 LEU ASP PHE VAL SER MET LEU VAL VAL TYR HIS PHE ARG SEQRES 35 B 781 LYS ALA LYS SER ILE ARG ALA SER GLY LEU ILE LEU LEU SEQRES 36 B 781 GLU THR ILE LEU PHE GLY SER LEU LEU LEU TYR PHE PRO SEQRES 37 B 781 VAL VAL ILE LEU TYR PHE GLU PRO SER THR PHE ARG CYS SEQRES 38 B 781 ILE LEU LEU ARG TRP ALA ARG LEU LEU GLY PHE ALA THR SEQRES 39 B 781 VAL TYR GLY THR VAL THR LEU LYS LEU HIS ARG VAL LEU SEQRES 40 B 781 LYS VAL PHE LEU SER ARG THR ALA GLN ARG ILE PRO TYR SEQRES 41 B 781 MET THR GLY GLY ARG VAL MET ARG MET LEU ALA VAL ILE SEQRES 42 B 781 LEU LEU VAL VAL PHE TRP PHE LEU ILE GLY TRP THR SER SEQRES 43 B 781 SER VAL CYS GLN ASN LEU GLU LYS GLN ILE SER LEU ILE SEQRES 44 B 781 GLY GLN GLY LYS THR SER ASP HIS LEU ILE PHE ASN MET SEQRES 45 B 781 CYS LEU ILE ASP ARG TRP ASP TYR MET THR ALA VAL ALA SEQRES 46 B 781 GLU PHE LEU PHE LEU LEU TRP GLY VAL TYR LEU CYS TYR SEQRES 47 B 781 ALA VAL ARG THR VAL PRO SER ALA PHE HIS GLU PRO ARG SEQRES 48 B 781 TYR MET ALA VAL ALA VAL HIS ASN GLU LEU ILE ILE SER SEQRES 49 B 781 ALA ILE PHE HIS THR ILE ARG PHE VAL LEU ALA SER ARG SEQRES 50 B 781 LEU GLN SER ASP TRP MET LEU MET LEU TYR PHE ALA HIS SEQRES 51 B 781 THR HIS LEU THR VAL THR VAL THR ILE GLY LEU LEU LEU SEQRES 52 B 781 ILE PRO LYS PHE SER HIS SER SER ASN ASN PRO ARG ASP SEQRES 53 B 781 ASP ILE ALA THR GLU ALA TYR GLU ASP GLU LEU ASP MET SEQRES 54 B 781 GLY ARG SER GLY SER TYR LEU ASN SER SER ILE ASN SER SEQRES 55 B 781 ALA TRP SER GLU HIS SER LEU ASP PRO GLU ASP ILE ARG SEQRES 56 B 781 ASP GLU LEU LYS LYS LEU TYR ALA GLN LEU GLU ILE TYR SEQRES 57 B 781 LYS ARG LYS LYS MET ILE THR ASN ASN PRO HIS LEU GLN SEQRES 58 B 781 LYS LYS ARG CYS SER LYS LYS GLY LEU GLY ARG SER ILE SEQRES 59 B 781 MET ARG ARG ILE THR GLU ILE PRO GLU THR VAL SER ARG SEQRES 60 B 781 GLN CYS SER LYS GLU ASP LYS GLU LEU GLU VAL LEU PHE SEQRES 61 B 781 GLN SEQRES 1 C 150 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS HIS LEU SEQRES 2 C 150 GLU VAL LEU PHE GLN GLY PRO ALA GLU VAL GLN LEU GLN SEQRES 3 C 150 GLU SER GLY GLY GLY LEU VAL GLN ALA GLY GLY SER LEU SEQRES 4 C 150 ARG LEU SER CYS ALA ALA SER GLY SER ILE GLY ASN ILE SEQRES 5 C 150 TYR ILE MET GLY TRP TYR ARG GLN THR PRO GLY PRO GLN SEQRES 6 C 150 ARG GLU LEU VAL ALA THR ILE ARG THR VAL ARG TRP THR SEQRES 7 C 150 LYS TYR GLU ASP TYR ALA ASP SER VAL LYS GLY ARG PHE SEQRES 8 C 150 THR ILE SER ASP ASP ASP ALA LYS ASN THR VAL TYR LEU SEQRES 9 C 150 GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 10 C 150 TYR CYS ASN TYR LYS ASP TYR ASN ALA PRO SER ASP GLY SEQRES 11 C 150 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLU SEQRES 12 C 150 PRO LYS THR PRO LYS PRO GLN SEQRES 1 E 150 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS HIS LEU SEQRES 2 E 150 GLU VAL LEU PHE GLN GLY PRO ALA GLU VAL GLN LEU GLN SEQRES 3 E 150 GLU SER GLY GLY GLY LEU VAL GLN ALA GLY GLY SER LEU SEQRES 4 E 150 ARG LEU SER CYS ALA ALA SER GLY SER ILE GLY ASN ILE SEQRES 5 E 150 TYR ILE MET GLY TRP TYR ARG GLN THR PRO GLY PRO GLN SEQRES 6 E 150 ARG GLU LEU VAL ALA THR ILE ARG THR VAL ARG TRP THR SEQRES 7 E 150 LYS TYR GLU ASP TYR ALA ASP SER VAL LYS GLY ARG PHE SEQRES 8 E 150 THR ILE SER ASP ASP ASP ALA LYS ASN THR VAL TYR LEU SEQRES 9 E 150 GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 10 E 150 TYR CYS ASN TYR LYS ASP TYR ASN ALA PRO SER ASP GLY SEQRES 11 E 150 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLU SEQRES 12 E 150 PRO LYS THR PRO LYS PRO GLN HET CLR A 801 28 HET CLR A 802 28 HET CLR A 803 28 HET CLR A 804 28 HET CLR A 805 28 HET CLR A 806 28 HET CLR A 807 28 HET CLR A 808 28 HET CLR A 809 28 HET CLR A 810 28 HET CLR A 811 28 HET PEE A 812 47 HET CLR B 801 28 HET CLR B 802 28 HET CLR B 803 28 HET CLR B 804 28 HET CLR B 805 28 HET CLR B 806 28 HET CLR B 807 28 HET CLR B 808 28 HET CLR B 809 28 HET PIE B 810 54 HETNAM CLR CHOLESTEROL HETNAM PEE 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE HETNAM PIE 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-PHOSPHOINOSITOL HETSYN PEE DOPE FORMUL 5 CLR 20(C27 H46 O) FORMUL 16 PEE C41 H78 N O8 P FORMUL 26 PIE C43 H80 O13 P 1- HELIX 1 AA1 ASP A 66 ALA A 75 1 10 HELIX 2 AA2 GLU A 76 VAL A 78 5 3 HELIX 3 AA3 MET A 80 TYR A 87 1 8 HELIX 4 AA4 THR A 88 LEU A 94 5 7 HELIX 5 AA5 ALA A 118 ASN A 137 1 20 HELIX 6 AA6 LEU A 150 GLY A 167 1 18 HELIX 7 AA7 LEU A 418 PHE A 441 1 24 HELIX 8 AA8 ALA A 444 GLY A 451 1 8 HELIX 9 AA9 GLY A 451 TYR A 466 1 16 HELIX 10 AB1 VAL A 470 PHE A 474 5 5 HELIX 11 AB2 SER A 477 VAL A 495 1 19 HELIX 12 AB3 THR A 498 THR A 514 1 17 HELIX 13 AB4 ARG A 525 CYS A 549 1 25 HELIX 14 AB5 GLN A 550 LYS A 554 5 5 HELIX 15 AB6 TRP A 578 VAL A 600 1 23 HELIX 16 AB7 HIS A 608 LEU A 634 1 27 HELIX 17 AB8 GLN A 639 ILE A 664 1 26 HELIX 18 AB9 PRO A 665 PHE A 667 5 3 HELIX 19 AC1 GLY B 67 GLU B 76 1 10 HELIX 20 AC2 ASP B 81 TYR B 87 1 7 HELIX 21 AC3 ALA B 118 MET B 139 1 22 HELIX 22 AC4 LEU B 150 LEU B 164 1 15 HELIX 23 AC5 LEU B 418 HIS B 440 1 23 HELIX 24 AC6 GLY B 451 TYR B 466 1 16 HELIX 25 AC7 VAL B 470 PHE B 474 5 5 HELIX 26 AC8 SER B 477 THR B 514 1 38 HELIX 27 AC9 ARG B 525 CYS B 549 1 25 HELIX 28 AD1 GLN B 550 LYS B 554 5 5 HELIX 29 AD2 TRP B 578 VAL B 600 1 23 HELIX 30 AD3 HIS B 608 LEU B 634 1 27 HELIX 31 AD4 GLN B 639 LEU B 662 1 24 HELIX 32 AD5 LEU B 663 SER B 668 5 6 HELIX 33 AD6 LYS C 90 THR C 94 5 5 HELIX 34 AD7 LYS E 90 THR E 94 5 5 SHEET 1 AA1 6 LEU A 202 LEU A 203 0 SHEET 2 AA1 6 PHE A 191 LEU A 192 -1 N LEU A 192 O LEU A 202 SHEET 3 AA1 6 ILE A 171 ILE A 176 -1 N ILE A 176 O PHE A 191 SHEET 4 AA1 6 VAL A 303 ASN A 309 -1 O ASP A 307 N SER A 172 SHEET 5 AA1 6 TRP A 281 ALA A 288 -1 N LEU A 285 O VAL A 306 SHEET 6 AA1 6 PRO A 268 LEU A 270 -1 N TYR A 269 O LEU A 282 SHEET 1 AA2 2 ILE A 559 GLY A 562 0 SHEET 2 AA2 2 PHE A 570 CYS A 573 -1 O MET A 572 N GLY A 560 SHEET 1 AA3 5 LEU B 202 LEU B 203 0 SHEET 2 AA3 5 PHE B 191 LEU B 192 -1 N LEU B 192 O LEU B 202 SHEET 3 AA3 5 SER B 172 ILE B 176 -1 N ILE B 176 O PHE B 191 SHEET 4 AA3 5 GLY B 302 ASP B 307 -1 O ASP B 307 N SER B 172 SHEET 5 AA3 5 SER B 286 ILE B 289 -1 N SER B 287 O MET B 304 SHEET 1 AA4 2 ILE B 559 GLY B 562 0 SHEET 2 AA4 2 PHE B 570 CYS B 573 -1 O MET B 572 N GLY B 560 SHEET 1 AA5 2 LEU C 5 GLN C 6 0 SHEET 2 AA5 2 ALA C 24 ALA C 25 -1 O ALA C 24 N GLN C 6 SHEET 1 AA6 2 LEU C 12 VAL C 13 0 SHEET 2 AA6 2 THR C 119 VAL C 120 1 O THR C 119 N VAL C 13 SHEET 1 AA7 2 THR C 72 SER C 74 0 SHEET 2 AA7 2 TYR C 83 GLN C 85 -1 O GLN C 85 N THR C 72 SHEET 1 AA8 2 VAL C 96 TYR C 97 0 SHEET 2 AA8 2 THR C 116 GLN C 117 -1 O THR C 116 N TYR C 97 SHEET 1 AA9 2 VAL E 13 GLN E 14 0 SHEET 2 AA9 2 VAL E 120 SER E 121 1 O SER E 121 N VAL E 13 SHEET 1 AB1 2 ARG E 20 CYS E 23 0 SHEET 2 AB1 2 VAL E 82 GLN E 85 -1 O VAL E 82 N CYS E 23 SHEET 1 AB2 3 TYR E 38 ARG E 39 0 SHEET 2 AB2 3 ALA E 95 TYR E 98 -1 O TYR E 98 N TYR E 38 SHEET 3 AB2 3 THR E 116 VAL E 118 -1 O VAL E 118 N ALA E 95 SHEET 1 AB3 2 THR E 51 ILE E 52 0 SHEET 2 AB3 2 GLU E 61 ASP E 62 -1 O ASP E 62 N THR E 51 SSBOND 1 CYS A 99 CYS A 272 1555 1555 2.04 SSBOND 2 CYS A 318 CYS A 354 1555 1555 2.03 SSBOND 3 CYS A 330 CYS A 352 1555 1555 2.04 SSBOND 4 CYS A 337 CYS A 392 1555 1555 2.03 SSBOND 5 CYS A 395 CYS A 402 1555 1555 2.03 SSBOND 6 CYS A 399 CYS A 408 1555 1555 2.03 SSBOND 7 CYS A 481 CYS A 573 1555 1555 2.03 SSBOND 8 CYS B 99 CYS B 272 1555 1555 2.03 SSBOND 9 CYS B 318 CYS B 354 1555 1555 2.03 SSBOND 10 CYS B 330 CYS B 352 1555 1555 2.03 SSBOND 11 CYS B 337 CYS B 392 1555 1555 2.03 SSBOND 12 CYS B 395 CYS B 402 1555 1555 2.03 SSBOND 13 CYS B 399 CYS B 408 1555 1555 2.03 SSBOND 14 CYS B 481 CYS B 573 1555 1555 2.03 SSBOND 15 CYS C 23 CYS C 99 1555 1555 2.04 SSBOND 16 CYS E 23 CYS E 99 1555 1555 2.04 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000