HEADER MEMBRANE PROTEIN 25-MAR-24 9ERX TITLE STRUCTURAL BASIS OF D9-THC ANALOG ACTIVITY AT THE CANNABINOID 1 TITLE 2 RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 8 BETA-1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 14 GAMMA-2; COMPND 15 CHAIN: C; COMPND 16 SYNONYM: G GAMMA-I; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: CANNABINOID RECEPTOR 1; COMPND 20 CHAIN: R; COMPND 21 SYNONYM: CB-R,CB1,CANN6; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: ANTIBODY SCFV16 FAB FRAGMENT; COMPND 25 CHAIN: F; COMPND 26 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: GNAI1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: GNB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNG2; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: CNR1, CNR; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 31 ORGANISM_COMMON: MOUSE; SOURCE 32 ORGANISM_TAXID: 10090; SOURCE 33 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS GPCR, CANNABINOID RECEPTOR 1, THC ANALOG COMPLEX, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR T.S.THORSEN,Y.KULKARNI,A.BOGGILD,T.DRACE,P.NISSEN,M.GAJHEDE,T.BOESEN, AUTHOR 2 J.S.KASTRUP,D.GLORIAM JRNL AUTH D.GLORIAM,T.THORSEN,Y.KULKARNI,D.SYKES,A.BOGGILD,T.DRACE, JRNL AUTH 2 P.HOMPLUEM,C.ILIOPOULOS-TSOUTSOUVAS,S.NIKAS,H.DAVER, JRNL AUTH 3 A.MAKRIYANNIS,P.NISSEN,M.GAJHEDE,D.VEPRINTSEV,T.BOESEN, JRNL AUTH 4 J.KASTRUP JRNL TITL STRUCTURAL BASIS OF DELTA 9 -THC ANALOG ACTIVITY AT THE JRNL TITL 2 CANNABINOID 1 RECEPTOR. JRNL REF RES SQ 2024 JRNL REFN ISSN 2693-5015 JRNL PMID 38826401 JRNL DOI 10.21203/RS.3.RS-4277209/V1 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EPU 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 : NULL 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) : 2.900 REMARK 3 NUMBER OF PARTICLES : 187493 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 9ERX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292137384. 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 : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : HU210/CB1/GI1 SIGNALING REMARK 245 COMPLEX; CANNABINOID 1 RECEPTOR REMARK 245 COMPLEXED WITH A G PROTEIN; REMARK 245 ANTIBODY SCFV16 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.85 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 60.60 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 130000 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, R, F 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 GLY A 2 REMARK 465 ILE A 55 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 MET B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 LEU B -10 REMARK 465 GLU B -9 REMARK 465 VAL B -8 REMARK 465 LEU B -7 REMARK 465 PHE B -6 REMARK 465 GLN B -5 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 SER C 3 REMARK 465 ASN C 4 REMARK 465 ASN C 5 REMARK 465 THR C 6 REMARK 465 LYS C 64 REMARK 465 LYS C 65 REMARK 465 PHE C 66 REMARK 465 PHE C 67 REMARK 465 CYS C 68 REMARK 465 ALA C 69 REMARK 465 ILE C 70 REMARK 465 LEU C 71 REMARK 465 MET R -24 REMARK 465 LYS R -23 REMARK 465 THR R -22 REMARK 465 ILE R -21 REMARK 465 ILE R -20 REMARK 465 ALA R -19 REMARK 465 LEU R -18 REMARK 465 SER R -17 REMARK 465 TYR R -16 REMARK 465 ILE R -15 REMARK 465 PHE R -14 REMARK 465 CYS R -13 REMARK 465 LEU R -12 REMARK 465 VAL R -11 REMARK 465 PHE R -10 REMARK 465 ALA R -9 REMARK 465 ASP R -8 REMARK 465 TYR R -7 REMARK 465 LYS R -6 REMARK 465 ASP R -5 REMARK 465 ASP R -4 REMARK 465 ASP R -3 REMARK 465 ASP R -2 REMARK 465 LYS R -1 REMARK 465 GLY R 0 REMARK 465 SER R 1 REMARK 465 LYS R 2 REMARK 465 SER R 3 REMARK 465 ILE R 4 REMARK 465 LEU R 5 REMARK 465 ASP R 6 REMARK 465 GLY R 7 REMARK 465 LEU R 8 REMARK 465 ALA R 9 REMARK 465 ASP R 10 REMARK 465 THR R 11 REMARK 465 THR R 12 REMARK 465 PHE R 13 REMARK 465 ARG R 14 REMARK 465 THR R 15 REMARK 465 ILE R 16 REMARK 465 THR R 17 REMARK 465 THR R 18 REMARK 465 ASP R 19 REMARK 465 LEU R 20 REMARK 465 LEU R 21 REMARK 465 TYR R 22 REMARK 465 VAL R 23 REMARK 465 GLY R 24 REMARK 465 SER R 25 REMARK 465 ASN R 26 REMARK 465 ASP R 27 REMARK 465 ILE R 28 REMARK 465 GLN R 29 REMARK 465 TYR R 30 REMARK 465 GLU R 31 REMARK 465 ASP R 32 REMARK 465 ILE R 33 REMARK 465 LYS R 34 REMARK 465 GLY R 35 REMARK 465 ASP R 36 REMARK 465 MET R 37 REMARK 465 ALA R 38 REMARK 465 SER R 39 REMARK 465 LYS R 40 REMARK 465 LEU R 41 REMARK 465 GLY R 42 REMARK 465 TYR R 43 REMARK 465 PHE R 44 REMARK 465 PRO R 45 REMARK 465 GLN R 46 REMARK 465 LYS R 47 REMARK 465 PHE R 48 REMARK 465 PRO R 49 REMARK 465 LEU R 50 REMARK 465 THR R 51 REMARK 465 SER R 52 REMARK 465 PHE R 53 REMARK 465 ARG R 54 REMARK 465 GLY R 55 REMARK 465 SER R 56 REMARK 465 PRO R 57 REMARK 465 PHE R 58 REMARK 465 GLN R 59 REMARK 465 GLU R 60 REMARK 465 LYS R 61 REMARK 465 MET R 62 REMARK 465 THR R 63 REMARK 465 ALA R 64 REMARK 465 GLY R 65 REMARK 465 ASP R 66 REMARK 465 ASN R 67 REMARK 465 PRO R 68 REMARK 465 GLN R 69 REMARK 465 LEU R 70 REMARK 465 VAL R 71 REMARK 465 PRO R 72 REMARK 465 ALA R 73 REMARK 465 ASP R 74 REMARK 465 GLN R 75 REMARK 465 VAL R 76 REMARK 465 ASN R 77 REMARK 465 ILE R 78 REMARK 465 THR R 79 REMARK 465 GLU R 80 REMARK 465 PHE R 81 REMARK 465 TYR R 82 REMARK 465 ASN R 83 REMARK 465 LYS R 84 REMARK 465 SER R 85 REMARK 465 LEU R 86 REMARK 465 SER R 87 REMARK 465 SER R 88 REMARK 465 PHE R 89 REMARK 465 LYS R 90 REMARK 465 GLU R 91 REMARK 465 ASN R 92 REMARK 465 GLU R 93 REMARK 465 GLU R 94 REMARK 465 ASN R 95 REMARK 465 ILE R 96 REMARK 465 GLN R 97 REMARK 465 CYS R 98 REMARK 465 GLY R 99 REMARK 465 SER R 316 REMARK 465 ILE R 317 REMARK 465 ILE R 318 REMARK 465 ILE R 319 REMARK 465 HIS R 320 REMARK 465 THR R 321 REMARK 465 SER R 322 REMARK 465 GLU R 323 REMARK 465 ASP R 324 REMARK 465 GLY R 325 REMARK 465 LYS R 326 REMARK 465 VAL R 327 REMARK 465 GLN R 328 REMARK 465 VAL R 329 REMARK 465 THR R 330 REMARK 465 ARG R 331 REMARK 465 PRO R 332 REMARK 465 ASP R 333 REMARK 465 GLN R 334 REMARK 465 PRO R 413 REMARK 465 SER R 414 REMARK 465 CYS R 415 REMARK 465 GLU R 416 REMARK 465 GLY R 417 REMARK 465 THR R 418 REMARK 465 ALA R 419 REMARK 465 GLN R 420 REMARK 465 PRO R 421 REMARK 465 LEU R 422 REMARK 465 ASP R 423 REMARK 465 ASN R 424 REMARK 465 SER R 425 REMARK 465 MET R 426 REMARK 465 GLY R 427 REMARK 465 ASP R 428 REMARK 465 SER R 429 REMARK 465 ASP R 430 REMARK 465 CYS R 431 REMARK 465 LEU R 432 REMARK 465 HIS R 433 REMARK 465 LYS R 434 REMARK 465 HIS R 435 REMARK 465 ALA R 436 REMARK 465 ASN R 437 REMARK 465 ASN R 438 REMARK 465 ALA R 439 REMARK 465 ALA R 440 REMARK 465 SER R 441 REMARK 465 VAL R 442 REMARK 465 HIS R 443 REMARK 465 ARG R 444 REMARK 465 ALA R 445 REMARK 465 ALA R 446 REMARK 465 GLU R 447 REMARK 465 SER R 448 REMARK 465 CYS R 449 REMARK 465 ILE R 450 REMARK 465 LYS R 451 REMARK 465 SER R 452 REMARK 465 THR R 453 REMARK 465 VAL R 454 REMARK 465 LYS R 455 REMARK 465 ILE R 456 REMARK 465 ALA R 457 REMARK 465 LYS R 458 REMARK 465 VAL R 459 REMARK 465 THR R 460 REMARK 465 MET R 461 REMARK 465 SER R 462 REMARK 465 VAL R 463 REMARK 465 SER R 464 REMARK 465 THR R 465 REMARK 465 ASP R 466 REMARK 465 THR R 467 REMARK 465 SER R 468 REMARK 465 ALA R 469 REMARK 465 GLU R 470 REMARK 465 ALA R 471 REMARK 465 LEU R 472 REMARK 465 HIS R 473 REMARK 465 HIS R 474 REMARK 465 HIS R 475 REMARK 465 HIS R 476 REMARK 465 HIS R 477 REMARK 465 HIS R 478 REMARK 465 HIS R 479 REMARK 465 HIS R 480 REMARK 465 HIS R 481 REMARK 465 HIS R 482 REMARK 465 MET F -37 REMARK 465 LEU F -36 REMARK 465 LEU F -35 REMARK 465 VAL F -34 REMARK 465 ASN F -33 REMARK 465 GLN F -32 REMARK 465 SER F -31 REMARK 465 HIS F -30 REMARK 465 GLN F -29 REMARK 465 GLY F -28 REMARK 465 PHE F -27 REMARK 465 ASN F -26 REMARK 465 LYS F -25 REMARK 465 GLU F -24 REMARK 465 HIS F -23 REMARK 465 THR F -22 REMARK 465 SER F -21 REMARK 465 LYS F -20 REMARK 465 MET F -19 REMARK 465 VAL F -18 REMARK 465 SER F -17 REMARK 465 ALA F -16 REMARK 465 ILE F -15 REMARK 465 VAL F -14 REMARK 465 LEU F -13 REMARK 465 TYR F -12 REMARK 465 VAL F -11 REMARK 465 LEU F -10 REMARK 465 LEU F -9 REMARK 465 ALA F -8 REMARK 465 ALA F -7 REMARK 465 ALA F -6 REMARK 465 ALA F -5 REMARK 465 HIS F -4 REMARK 465 SER F -3 REMARK 465 ALA F -2 REMARK 465 PHE F -1 REMARK 465 ALA F 0 REMARK 465 ASP F 1 REMARK 465 GLY F 123 REMARK 465 GLY F 124 REMARK 465 GLY F 125 REMARK 465 SER F 126 REMARK 465 GLY F 127 REMARK 465 GLY F 128 REMARK 465 GLY F 129 REMARK 465 GLY F 130 REMARK 465 SER F 131 REMARK 465 GLY F 132 REMARK 465 GLY F 133 REMARK 465 GLY F 134 REMARK 465 ALA F 249 REMARK 465 ALA F 250 REMARK 465 ALA F 251 REMARK 465 LEU F 252 REMARK 465 GLU F 253 REMARK 465 VAL F 254 REMARK 465 LEU F 255 REMARK 465 PHE F 256 REMARK 465 GLN F 257 REMARK 465 GLY F 258 REMARK 465 PRO F 259 REMARK 465 GLY F 260 REMARK 465 SER F 261 REMARK 465 HIS F 262 REMARK 465 HIS F 263 REMARK 465 HIS F 264 REMARK 465 HIS F 265 REMARK 465 HIS F 266 REMARK 465 HIS F 267 REMARK 465 HIS F 268 REMARK 465 HIS F 269 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 SER A 6 175.68 64.68 REMARK 500 ASP A 229 30.81 -94.64 REMARK 500 GLU A 238 17.17 -143.24 REMARK 500 GLU A 239 -8.49 72.05 REMARK 500 PHE A 259 57.25 -94.87 REMARK 500 ASP B 163 30.36 -94.95 REMARK 500 THR B 164 18.91 59.19 REMARK 500 THR B 196 18.88 50.89 REMARK 500 ALA B 203 -169.37 -126.53 REMARK 500 CYS B 271 72.77 61.12 REMARK 500 ASP B 291 35.34 -95.39 REMARK 500 PHE B 292 12.76 82.64 REMARK 500 LEU B 308 41.47 -104.09 REMARK 500 ASP R 104 63.78 62.52 REMARK 500 LEU R 111 36.18 -99.48 REMARK 500 PHE R 180 -8.82 71.78 REMARK 500 VAL F 48 -63.51 -104.89 REMARK 500 MET F 192 -12.22 73.11 REMARK 500 SER F 193 -2.37 -140.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-19929 RELATED DB: EMDB REMARK 900 STRUCTURAL BASIS OF D9-THC ANALOG ACTIVITY AT THE CANNABINOID 1 REMARK 900 RECEPTOR DBREF 9ERX A 2 354 UNP P63096 GNAI1_HUMAN 2 354 DBREF 9ERX B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9ERX C 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9ERX R 2 472 UNP P21554 CNR1_HUMAN 2 472 DBREF 9ERX F -37 269 PDB 9ERX 9ERX -37 269 SEQADV 9ERX ALA A 203 UNP P63096 GLY 203 CONFLICT SEQADV 9ERX SER A 326 UNP P63096 ALA 326 CONFLICT SEQADV 9ERX MET B -17 UNP P62873 INITIATING METHIONINE SEQADV 9ERX HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 9ERX HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 9ERX HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 9ERX HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 9ERX HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 9ERX HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 9ERX LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 9ERX GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 9ERX VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 9ERX LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 9ERX PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 9ERX GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 9ERX GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 9ERX PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 9ERX GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 9ERX SER B -1 UNP P62873 EXPRESSION TAG SEQADV 9ERX SER B 0 UNP P62873 EXPRESSION TAG SEQADV 9ERX GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 9ERX MET R -24 UNP P21554 INITIATING METHIONINE SEQADV 9ERX LYS R -23 UNP P21554 EXPRESSION TAG SEQADV 9ERX THR R -22 UNP P21554 EXPRESSION TAG SEQADV 9ERX ILE R -21 UNP P21554 EXPRESSION TAG SEQADV 9ERX ILE R -20 UNP P21554 EXPRESSION TAG SEQADV 9ERX ALA R -19 UNP P21554 EXPRESSION TAG SEQADV 9ERX LEU R -18 UNP P21554 EXPRESSION TAG SEQADV 9ERX SER R -17 UNP P21554 EXPRESSION TAG SEQADV 9ERX TYR R -16 UNP P21554 EXPRESSION TAG SEQADV 9ERX ILE R -15 UNP P21554 EXPRESSION TAG SEQADV 9ERX PHE R -14 UNP P21554 EXPRESSION TAG SEQADV 9ERX CYS R -13 UNP P21554 EXPRESSION TAG SEQADV 9ERX LEU R -12 UNP P21554 EXPRESSION TAG SEQADV 9ERX VAL R -11 UNP P21554 EXPRESSION TAG SEQADV 9ERX PHE R -10 UNP P21554 EXPRESSION TAG SEQADV 9ERX ALA R -9 UNP P21554 EXPRESSION TAG SEQADV 9ERX ASP R -8 UNP P21554 EXPRESSION TAG SEQADV 9ERX TYR R -7 UNP P21554 EXPRESSION TAG SEQADV 9ERX LYS R -6 UNP P21554 EXPRESSION TAG SEQADV 9ERX ASP R -5 UNP P21554 EXPRESSION TAG SEQADV 9ERX ASP R -4 UNP P21554 EXPRESSION TAG SEQADV 9ERX ASP R -3 UNP P21554 EXPRESSION TAG SEQADV 9ERX ASP R -2 UNP P21554 EXPRESSION TAG SEQADV 9ERX LYS R -1 UNP P21554 EXPRESSION TAG SEQADV 9ERX GLY R 0 UNP P21554 EXPRESSION TAG SEQADV 9ERX SER R 1 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 473 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 474 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 475 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 476 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 477 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 478 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 479 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 480 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 481 UNP P21554 EXPRESSION TAG SEQADV 9ERX HIS R 482 UNP P21554 EXPRESSION TAG SEQRES 1 A 353 GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL GLU SEQRES 2 A 353 ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP GLY SEQRES 3 A 353 GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU GLY SEQRES 4 A 353 ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN MET SEQRES 5 A 353 LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU CYS SEQRES 6 A 353 LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE GLN SEQRES 7 A 353 SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU LYS SEQRES 8 A 353 ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA ARG SEQRES 9 A 353 GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY PHE SEQRES 10 A 353 MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU TRP SEQRES 11 A 353 LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER ARG SEQRES 12 A 353 GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU ASN SEQRES 13 A 353 ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO THR SEQRES 14 A 353 GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR GLY SEQRES 15 A 353 ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS PHE SEQRES 16 A 353 LYS MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG LYS SEQRES 17 A 353 LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE ILE SEQRES 18 A 353 PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU ALA SEQRES 19 A 353 GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER MET LYS SEQRES 20 A 353 LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR ASP SEQRES 21 A 353 THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU PHE SEQRES 22 A 353 GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS TYR SEQRES 23 A 353 PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA ALA SEQRES 24 A 353 ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS ARG SEQRES 25 A 353 LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SER SEQRES 26 A 353 THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA VAL SEQRES 27 A 353 THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS GLY SEQRES 28 A 353 LEU PHE SEQRES 1 B 358 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 B 358 GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG SEQRES 3 B 358 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 4 B 358 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 5 B 358 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 6 B 358 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 7 B 358 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 8 B 358 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 9 B 358 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 10 B 358 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 11 B 358 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 12 B 358 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 13 B 358 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 14 B 358 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 15 B 358 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 16 B 358 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 17 B 358 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 18 B 358 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 19 B 358 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 20 B 358 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 21 B 358 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 22 B 358 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 23 B 358 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 24 B 358 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 25 B 358 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 26 B 358 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 27 B 358 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 28 B 358 SER PHE LEU LYS ILE TRP ASN SEQRES 1 C 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 C 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 C 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 C 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 C 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 C 71 PHE PHE CYS ALA ILE LEU SEQRES 1 R 507 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 507 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS GLY SER SEQRES 3 R 507 LYS SER ILE LEU ASP GLY LEU ALA ASP THR THR PHE ARG SEQRES 4 R 507 THR ILE THR THR ASP LEU LEU TYR VAL GLY SER ASN ASP SEQRES 5 R 507 ILE GLN TYR GLU ASP ILE LYS GLY ASP MET ALA SER LYS SEQRES 6 R 507 LEU GLY TYR PHE PRO GLN LYS PHE PRO LEU THR SER PHE SEQRES 7 R 507 ARG GLY SER PRO PHE GLN GLU LYS MET THR ALA GLY ASP SEQRES 8 R 507 ASN PRO GLN LEU VAL PRO ALA ASP GLN VAL ASN ILE THR SEQRES 9 R 507 GLU PHE TYR ASN LYS SER LEU SER SER PHE LYS GLU ASN SEQRES 10 R 507 GLU GLU ASN ILE GLN CYS GLY GLU ASN PHE MET ASP ILE SEQRES 11 R 507 GLU CYS PHE MET VAL LEU ASN PRO SER GLN GLN LEU ALA SEQRES 12 R 507 ILE ALA VAL LEU SER LEU THR LEU GLY THR PHE THR VAL SEQRES 13 R 507 LEU GLU ASN LEU LEU VAL LEU CYS VAL ILE LEU HIS SER SEQRES 14 R 507 ARG SER LEU ARG CYS ARG PRO SER TYR HIS PHE ILE GLY SEQRES 15 R 507 SER LEU ALA VAL ALA ASP LEU LEU GLY SER VAL ILE PHE SEQRES 16 R 507 VAL TYR SER PHE ILE ASP PHE HIS VAL PHE HIS ARG LYS SEQRES 17 R 507 ASP SER ARG ASN VAL PHE LEU PHE LYS LEU GLY GLY VAL SEQRES 18 R 507 THR ALA SER PHE THR ALA SER VAL GLY SER LEU PHE LEU SEQRES 19 R 507 THR ALA ILE ASP ARG TYR ILE SER ILE HIS ARG PRO LEU SEQRES 20 R 507 ALA TYR LYS ARG ILE VAL THR ARG PRO LYS ALA VAL VAL SEQRES 21 R 507 ALA PHE CYS LEU MET TRP THR ILE ALA ILE VAL ILE ALA SEQRES 22 R 507 VAL LEU PRO LEU LEU GLY TRP ASN CYS GLU LYS LEU GLN SEQRES 23 R 507 SER VAL CYS SER ASP ILE PHE PRO HIS ILE ASP GLU THR SEQRES 24 R 507 TYR LEU MET PHE TRP ILE GLY VAL THR SER VAL LEU LEU SEQRES 25 R 507 LEU PHE ILE VAL TYR ALA TYR MET TYR ILE LEU TRP LYS SEQRES 26 R 507 ALA HIS SER HIS ALA VAL ARG MET ILE GLN ARG GLY THR SEQRES 27 R 507 GLN LYS SER ILE ILE ILE HIS THR SER GLU ASP GLY LYS SEQRES 28 R 507 VAL GLN VAL THR ARG PRO ASP GLN ALA ARG MET ASP ILE SEQRES 29 R 507 ARG LEU ALA LYS THR LEU VAL LEU ILE LEU VAL VAL LEU SEQRES 30 R 507 ILE ILE CYS TRP GLY PRO LEU LEU ALA ILE MET VAL TYR SEQRES 31 R 507 ASP VAL PHE GLY LYS MET ASN LYS LEU ILE LYS THR VAL SEQRES 32 R 507 PHE ALA PHE CYS SER MET LEU CYS LEU LEU ASN SER THR SEQRES 33 R 507 VAL ASN PRO ILE ILE TYR ALA LEU ARG SER LYS ASP LEU SEQRES 34 R 507 ARG HIS ALA PHE ARG SER MET PHE PRO SER CYS GLU GLY SEQRES 35 R 507 THR ALA GLN PRO LEU ASP ASN SER MET GLY ASP SER ASP SEQRES 36 R 507 CYS LEU HIS LYS HIS ALA ASN ASN ALA ALA SER VAL HIS SEQRES 37 R 507 ARG ALA ALA GLU SER CYS ILE LYS SER THR VAL LYS ILE SEQRES 38 R 507 ALA LYS VAL THR MET SER VAL SER THR ASP THR SER ALA SEQRES 39 R 507 GLU ALA LEU HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 F 307 MET LEU LEU VAL ASN GLN SER HIS GLN GLY PHE ASN LYS SEQRES 2 F 307 GLU HIS THR SER LYS MET VAL SER ALA ILE VAL LEU TYR SEQRES 3 F 307 VAL LEU LEU ALA ALA ALA ALA HIS SER ALA PHE ALA ASP SEQRES 4 F 307 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 5 F 307 GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE SEQRES 6 F 307 ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA SEQRES 7 F 307 PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER SEQRES 8 F 307 GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY SEQRES 9 F 307 ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU SEQRES 10 F 307 PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA SEQRES 11 F 307 MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SEQRES 12 F 307 SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR SEQRES 13 F 307 VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 14 F 307 GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA THR SEQRES 15 F 307 SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER ILE SEQRES 16 F 307 SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN GLY SEQRES 17 F 307 ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY GLN SEQRES 18 F 307 SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU ALA SEQRES 19 F 307 SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY SEQRES 20 F 307 THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA GLU SEQRES 21 F 307 ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU TYR SEQRES 22 F 307 PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU LYS SEQRES 23 F 307 ALA ALA ALA LEU GLU VAL LEU PHE GLN GLY PRO GLY SER SEQRES 24 F 307 HIS HIS HIS HIS HIS HIS HIS HIS HET H66 R 501 28 FORMUL 6 H66 FORMUL 7 HOH *(H2 O) HELIX 1 AA1 LEU A 5 ALA A 31 1 27 HELIX 2 AA2 GLY A 45 LYS A 54 1 10 HELIX 3 AA3 GLU A 207 GLU A 216 5 10 HELIX 4 AA4 SER A 228 ASP A 231 5 4 HELIX 5 AA5 ASN A 241 ASN A 255 1 15 HELIX 6 AA6 LYS A 270 LYS A 279 1 10 HELIX 7 AA7 PRO A 282 CYS A 286 5 5 HELIX 8 AA8 THR A 295 ASP A 309 1 15 HELIX 9 AA9 LYS A 330 CYS A 351 1 22 HELIX 10 AB1 GLU B 3 ALA B 24 1 22 HELIX 11 AB2 THR B 29 THR B 34 1 6 HELIX 12 AB3 LYS B 280 GLY B 282 5 3 HELIX 13 AB4 SER C 8 ASN C 24 1 17 HELIX 14 AB5 LYS C 29 HIS C 44 1 16 HELIX 15 AB6 SER R 114 SER R 144 1 31 HELIX 16 AB7 SER R 144 CYS R 149 1 6 HELIX 17 AB8 ARG R 150 VAL R 179 1 30 HELIX 18 AB9 SER R 185 ARG R 220 1 36 HELIX 19 AC1 ALA R 223 ILE R 227 5 5 HELIX 20 AC2 THR R 229 GLY R 254 1 26 HELIX 21 AC3 ASP R 272 ARG R 311 1 40 HELIX 22 AC4 MET R 337 ASP R 366 1 30 HELIX 23 AC5 LEU R 374 MET R 384 1 11 HELIX 24 AC6 MET R 384 ALA R 398 1 15 HELIX 25 AC7 SER R 401 PHE R 412 1 12 HELIX 26 AC8 SER F 53 GLY F 56 5 4 HELIX 27 AC9 ARG F 87 THR F 91 5 5 HELIX 28 AD1 GLU F 220 VAL F 224 5 5 SHEET 1 AA1 6 VAL A 185 THR A 190 0 SHEET 2 AA1 6 HIS A 195 ASP A 200 -1 O MET A 198 N THR A 187 SHEET 3 AA1 6 GLU A 33 GLY A 40 1 N VAL A 34 O LYS A 197 SHEET 4 AA1 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37 SHEET 5 AA1 6 SER A 263 ASN A 269 1 O ILE A 265 N ILE A 221 SHEET 6 AA1 6 ILE A 319 PHE A 323 1 O TYR A 320 N ILE A 264 SHEET 1 AA2 4 ARG B 46 ARG B 52 0 SHEET 2 AA2 4 PHE B 335 ASN B 340 -1 O ILE B 338 N ARG B 48 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O ALA B 113 N ALA B 104 SHEET 3 AA4 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 ALA B 140 -1 O ARG B 137 N ILE B 123 SHEET 1 AA5 4 LEU B 146 PHE B 151 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O VAL B 158 N ARG B 150 SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O ALA B 167 N THR B 159 SHEET 4 AA5 4 GLN B 176 THR B 181 -1 O PHE B 180 N CYS B 166 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -1 O GLY B 202 N SER B 189 SHEET 3 AA6 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 CYS B 218 THR B 223 -1 O ARG B 219 N LEU B 210 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLN B 259 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AA8 4 ILE B 273 PHE B 278 0 SHEET 2 AA8 4 LEU B 284 TYR B 289 -1 O GLY B 288 N SER B 275 SHEET 3 AA8 4 ASN B 293 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 VAL B 307 -1 O GLY B 306 N VAL B 296 SHEET 1 AA9 4 GLN F 3 SER F 7 0 SHEET 2 AA9 4 SER F 17 SER F 25 -1 O SER F 23 N VAL F 5 SHEET 3 AA9 4 THR F 78 THR F 84 -1 O LEU F 79 N CYS F 22 SHEET 4 AA9 4 PHE F 68 ASP F 73 -1 N THR F 69 O GLN F 82 SHEET 1 AB1 6 GLY F 10 VAL F 12 0 SHEET 2 AB1 6 THR F 115 VAL F 119 1 O THR F 118 N VAL F 12 SHEET 3 AB1 6 ALA F 92 SER F 99 -1 N TYR F 94 O THR F 115 SHEET 4 AB1 6 GLY F 33 GLN F 39 -1 N VAL F 37 O TYR F 95 SHEET 5 AB1 6 LEU F 45 ILE F 51 -1 O VAL F 48 N TRP F 36 SHEET 6 AB1 6 ILE F 58 TYR F 60 -1 O TYR F 59 N TYR F 50 SHEET 1 AB2 4 GLY F 10 VAL F 12 0 SHEET 2 AB2 4 THR F 115 VAL F 119 1 O THR F 118 N VAL F 12 SHEET 3 AB2 4 ALA F 92 SER F 99 -1 N TYR F 94 O THR F 115 SHEET 4 AB2 4 PHE F 110 TRP F 111 -1 O PHE F 110 N ARG F 98 SHEET 1 AB3 2 MET F 140 GLN F 142 0 SHEET 2 AB3 2 CYS F 159 SER F 161 -1 O ARG F 160 N THR F 141 SHEET 1 AB4 6 SER F 146 VAL F 149 0 SHEET 2 AB4 6 THR F 243 LEU F 247 1 O GLU F 246 N VAL F 149 SHEET 3 AB4 6 GLY F 225 GLN F 231 -1 N TYR F 227 O THR F 243 SHEET 4 AB4 6 LEU F 174 GLN F 179 -1 N GLN F 179 O VAL F 226 SHEET 5 AB4 6 PRO F 185 TYR F 190 -1 O LEU F 188 N TRP F 176 SHEET 6 AB4 6 ASN F 194 LEU F 195 -1 O ASN F 194 N TYR F 190 SHEET 1 AB5 3 SER F 154 ILE F 157 0 SHEET 2 AB5 3 ALA F 211 SER F 217 -1 O ILE F 216 N VAL F 155 SHEET 3 AB5 3 PHE F 203 SER F 208 -1 N SER F 208 O ALA F 211 SSBOND 1 CYS R 257 CYS R 264 1555 1555 2.03 SSBOND 2 CYS F 22 CYS F 96 1555 1555 2.03 SSBOND 3 CYS F 159 CYS F 229 1555 1555 2.03 CISPEP 1 TYR F 235 PRO F 236 0 2.39 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