HEADER MEMBRANE PROTEIN 31-JAN-24 8VVF TITLE KAPPA OPIOID RECEPTOR:GALPHAI PROTEIN IN COMPLEX WITH INVERSE AGONIST TITLE 2 JDTIC COMPND MOL_ID: 1; COMPND 2 MOLECULE: KAPPA-TYPE OPIOID RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: K-OR-1,KOR-1; 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: C; 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: D; COMPND 16 SYNONYM: G GAMMA-I; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 20 CHAIN: B; COMPND 21 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: SCFV16; COMPND 25 CHAIN: E; 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: OPRK1, OPRK; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: GNB1; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: GNG2; SOURCE 22 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 23 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 GENE: GNAI1; SOURCE 30 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 31 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 33 MOL_ID: 5; SOURCE 34 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 35 ORGANISM_COMMON: MOUSE; SOURCE 36 ORGANISM_TAXID: 10090; SOURCE 37 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 38 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 39 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS G PROTEIN COUPLED RECEPTOR, OPIOID RECEPTOR, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR C.GATI,Z.MOTIWALA,A.S.TYSON,D.STYRPEJKO,G.W.HAN,S.KHAN,N.RAMOS- AUTHOR 2 GONZALEZ,R.SHENVI,S.MAJUMDAR REVDAT 1 15-JAN-25 8VVF 0 JRNL AUTH A.S.TYSON,S.KHAN,Z.MOTIWALA,G.W.HAN,Z.ZHANG,M.RANJBAR, JRNL AUTH 2 D.STYRPEJKO,N.RAMOS-GONZALEZ,S.WOO,K.VILLERS,D.LANDAKER, JRNL AUTH 3 T.KENAKIN,R.SHENVI,S.MAJUMDA,C.GATI JRNL TITL MOLECULAR MECHANISMS OF INVERSE AGONISM VIA KAPPA-OPIOID JRNL TITL 2 RECEPTOR-G PROTEIN COMPLEXES JRNL REF NAT.CHEM.BIOL. 2025 JRNL REFN ESSN 1552-4469 JRNL DOI 10.1038/S41589-024-01812-0 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EPU, CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 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 : 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 330302 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 8VVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1000279786. 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 : KAPPA OPIOID RECEPTOR IN REMARK 245 COMPLEX WITH HETEROTRIMERIC G REMARK 245 PROTEIN (GAI/B/G) AND INVERSE REMARK 245 AGONIST JDTIC REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 18.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 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) : -15000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : -25000.00 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) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : 105000 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 APPLY THE FOLLOWING TO CHAINS: A, C, D, B, 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 ASP A 2 REMARK 465 SER A 3 REMARK 465 PRO A 4 REMARK 465 ILE A 5 REMARK 465 GLN A 6 REMARK 465 ILE A 7 REMARK 465 PHE A 8 REMARK 465 ARG A 9 REMARK 465 GLY A 10 REMARK 465 GLU A 11 REMARK 465 PRO A 12 REMARK 465 GLY A 13 REMARK 465 PRO A 14 REMARK 465 THR A 15 REMARK 465 CYS A 16 REMARK 465 ALA A 17 REMARK 465 PRO A 18 REMARK 465 SER A 19 REMARK 465 ALA A 20 REMARK 465 CYS A 21 REMARK 465 LEU A 22 REMARK 465 PRO A 23 REMARK 465 PRO A 24 REMARK 465 ASN A 25 REMARK 465 SER A 26 REMARK 465 SER A 27 REMARK 465 ALA A 28 REMARK 465 TRP A 29 REMARK 465 PHE A 30 REMARK 465 PRO A 31 REMARK 465 GLY A 32 REMARK 465 TRP A 33 REMARK 465 ALA A 34 REMARK 465 GLU A 35 REMARK 465 PRO A 36 REMARK 465 ASP A 37 REMARK 465 SER A 38 REMARK 465 ASN A 39 REMARK 465 GLY A 40 REMARK 465 SER A 41 REMARK 465 ALA A 42 REMARK 465 GLY A 43 REMARK 465 SER A 44 REMARK 465 GLU A 45 REMARK 465 ASP A 46 REMARK 465 ALA A 47 REMARK 465 GLN A 48 REMARK 465 LEU A 49 REMARK 465 GLU A 50 REMARK 465 PRO A 51 REMARK 465 ALA A 52 REMARK 465 HIS A 53 REMARK 465 ILE A 54 REMARK 465 SER A 55 REMARK 465 PRO A 56 REMARK 465 ASP A 343 REMARK 465 PHE A 344 REMARK 465 CYS A 345 REMARK 465 PHE A 346 REMARK 465 PRO A 347 REMARK 465 LEU A 348 REMARK 465 LYS A 349 REMARK 465 MET A 350 REMARK 465 ARG A 351 REMARK 465 MET A 352 REMARK 465 GLU A 353 REMARK 465 ARG A 354 REMARK 465 GLN A 355 REMARK 465 SER A 356 REMARK 465 THR A 357 REMARK 465 SER A 358 REMARK 465 ARG A 359 REMARK 465 VAL A 360 REMARK 465 ARG A 361 REMARK 465 ASN A 362 REMARK 465 THR A 363 REMARK 465 VAL A 364 REMARK 465 GLN A 365 REMARK 465 ASP A 366 REMARK 465 PRO A 367 REMARK 465 ALA A 368 REMARK 465 TYR A 369 REMARK 465 LEU A 370 REMARK 465 ARG A 371 REMARK 465 ASP A 372 REMARK 465 ILE A 373 REMARK 465 ASP A 374 REMARK 465 GLY A 375 REMARK 465 MET A 376 REMARK 465 ASN A 377 REMARK 465 LYS A 378 REMARK 465 PRO A 379 REMARK 465 VAL A 380 REMARK 465 MET C 1 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 SER D 3 REMARK 465 ASN D 4 REMARK 465 ASN D 5 REMARK 465 THR D 6 REMARK 465 ALA D 7 REMARK 465 GLU D 63 REMARK 465 LYS D 64 REMARK 465 LYS D 65 REMARK 465 PHE D 66 REMARK 465 PHE D 67 REMARK 465 CYS D 68 REMARK 465 ALA D 69 REMARK 465 ILE D 70 REMARK 465 LEU D 71 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 CYS B 3 REMARK 465 THR B 4 REMARK 465 MET B 53 REMARK 465 LYS B 54 REMARK 465 ILE B 55 REMARK 465 ILE B 56 REMARK 465 HIS B 57 REMARK 465 GLU B 58 REMARK 465 ALA B 59 REMARK 465 GLY B 60 REMARK 465 TYR B 61 REMARK 465 SER B 62 REMARK 465 GLU B 63 REMARK 465 GLU B 64 REMARK 465 GLU B 65 REMARK 465 CYS B 66 REMARK 465 LYS B 67 REMARK 465 GLN B 68 REMARK 465 TYR B 69 REMARK 465 LYS B 70 REMARK 465 ALA B 71 REMARK 465 VAL B 72 REMARK 465 VAL B 73 REMARK 465 TYR B 74 REMARK 465 SER B 75 REMARK 465 ASN B 76 REMARK 465 THR B 77 REMARK 465 ILE B 78 REMARK 465 GLN B 79 REMARK 465 SER B 80 REMARK 465 ILE B 81 REMARK 465 ILE B 82 REMARK 465 ALA B 83 REMARK 465 ILE B 84 REMARK 465 ILE B 85 REMARK 465 ARG B 86 REMARK 465 ALA B 87 REMARK 465 MET B 88 REMARK 465 GLY B 89 REMARK 465 ARG B 90 REMARK 465 LEU B 91 REMARK 465 LYS B 92 REMARK 465 ILE B 93 REMARK 465 ASP B 94 REMARK 465 PHE B 95 REMARK 465 GLY B 96 REMARK 465 ASP B 97 REMARK 465 SER B 98 REMARK 465 ALA B 99 REMARK 465 ARG B 100 REMARK 465 ALA B 101 REMARK 465 ASP B 102 REMARK 465 ASP B 103 REMARK 465 ALA B 104 REMARK 465 ARG B 105 REMARK 465 GLN B 106 REMARK 465 LEU B 107 REMARK 465 PHE B 108 REMARK 465 VAL B 109 REMARK 465 LEU B 110 REMARK 465 ALA B 111 REMARK 465 GLY B 112 REMARK 465 ALA B 113 REMARK 465 ALA B 114 REMARK 465 GLU B 115 REMARK 465 GLU B 116 REMARK 465 GLY B 117 REMARK 465 PHE B 118 REMARK 465 MET B 119 REMARK 465 THR B 120 REMARK 465 ALA B 121 REMARK 465 GLU B 122 REMARK 465 LEU B 123 REMARK 465 ALA B 124 REMARK 465 GLY B 125 REMARK 465 VAL B 126 REMARK 465 ILE B 127 REMARK 465 LYS B 128 REMARK 465 ARG B 129 REMARK 465 LEU B 130 REMARK 465 TRP B 131 REMARK 465 LYS B 132 REMARK 465 ASP B 133 REMARK 465 SER B 134 REMARK 465 GLY B 135 REMARK 465 VAL B 136 REMARK 465 GLN B 137 REMARK 465 ALA B 138 REMARK 465 CYS B 139 REMARK 465 PHE B 140 REMARK 465 ASN B 141 REMARK 465 ARG B 142 REMARK 465 SER B 143 REMARK 465 ARG B 144 REMARK 465 GLU B 145 REMARK 465 TYR B 146 REMARK 465 GLN B 147 REMARK 465 LEU B 148 REMARK 465 ASN B 149 REMARK 465 ASP B 150 REMARK 465 SER B 151 REMARK 465 ALA B 152 REMARK 465 ALA B 153 REMARK 465 TYR B 154 REMARK 465 TYR B 155 REMARK 465 LEU B 156 REMARK 465 ASN B 157 REMARK 465 ASP B 158 REMARK 465 LEU B 159 REMARK 465 ASP B 160 REMARK 465 ARG B 161 REMARK 465 ILE B 162 REMARK 465 ALA B 163 REMARK 465 GLN B 164 REMARK 465 PRO B 165 REMARK 465 ASN B 166 REMARK 465 TYR B 167 REMARK 465 ILE B 168 REMARK 465 PRO B 169 REMARK 465 THR B 170 REMARK 465 GLN B 171 REMARK 465 GLN B 172 REMARK 465 ASP B 173 REMARK 465 VAL B 174 REMARK 465 LEU B 175 REMARK 465 ARG B 176 REMARK 465 THR B 177 REMARK 465 ARG B 178 REMARK 465 VAL B 179 REMARK 465 ASP E 1 REMARK 465 GLY E 121A REMARK 465 GLY E 121B REMARK 465 GLY E 121C REMARK 465 GLY E 121D REMARK 465 SER E 121E REMARK 465 GLY E 121F REMARK 465 GLY E 121G REMARK 465 GLY E 121H REMARK 465 GLY E 121I REMARK 465 SER E 121J REMARK 465 GLY E 121K REMARK 465 GLY E 121L REMARK 465 GLY E 121M REMARK 465 GLY E 121N REMARK 465 LYS E 236 REMARK 465 ALA E 237 REMARK 465 ALA E 238 REMARK 465 ALA E 239 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 PHE A 82 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE A 85 CG1 CG2 CD1 REMARK 470 ARG A 86 CG CD NE CZ NH1 NH2 REMARK 470 TYR A 87 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 89 CG CD CE NZ REMARK 470 LYS A 91 CG CD CE NZ REMARK 470 MET A 112 CG SD CE REMARK 470 GLU A 203 CG CD OE1 OE2 REMARK 470 GLN A 213 CG CD OE1 NE2 REMARK 470 PHE A 214 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 216 CG OD1 OD2 REMARK 470 ASP A 217 CG OD1 OD2 REMARK 470 ASP A 218 CG OD1 OD2 REMARK 470 TYR A 219 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 220 OG REMARK 470 TRP A 221 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 221 CZ3 CH2 REMARK 470 TRP A 222 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 222 CZ3 CH2 REMARK 470 ARG A 263 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 296 CG1 CG2 REMARK 470 GLU A 297 CG CD OE1 OE2 REMARK 470 SER A 301 OG REMARK 470 THR A 302 OG1 CG2 REMARK 470 SER A 303 OG REMARK 470 HIS A 304 CG ND1 CD2 CE1 NE2 REMARK 470 SER A 305 OG REMARK 470 SER A 311 OG REMARK 470 ILE A 328 CG1 CG2 CD1 REMARK 470 PHE A 332 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 339 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 341 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 342 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 5 CG OD1 OD2 REMARK 470 ARG C 8 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 15 CG CD CE NZ REMARK 470 ARG C 42 CG CD NE CZ NH1 NH2 REMARK 470 ILE C 43 CG1 CG2 CD1 REMARK 470 GLN C 44 CG CD OE1 NE2 REMARK 470 ARG C 129 CG CD NE CZ NH1 NH2 REMARK 470 ASN C 268 CG OD1 ND2 REMARK 470 ASN C 295 CG OD1 ND2 REMARK 470 GLN D 11 CG CD OE1 NE2 REMARK 470 LYS D 14 CG CD CE NZ REMARK 470 LYS D 20 CG CD CE NZ REMARK 470 GLU D 47 CG CD OE1 OE2 REMARK 470 VAL D 54 CG1 CG2 REMARK 470 SER D 57 OG REMARK 470 GLU D 58 CG CD OE1 OE2 REMARK 470 ARG D 62 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 180 CG CD CE NZ REMARK 470 ARG B 205 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 236 CG CD OE1 OE2 REMARK 470 MET B 240 CG SD CE REMARK 470 GLU B 245 CG CD OE1 OE2 REMARK 470 ASP B 272 CG OD1 OD2 REMARK 470 GLU B 298 CG CD OE1 OE2 REMARK 470 LYS B 312 CG CD CE NZ REMARK 470 ARG B 313 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 315 CG OD1 OD2 REMARK 470 LYS B 330 CG CD CE NZ REMARK 470 LEU E 11 CG CD1 CD2 REMARK 470 GLN E 13 CG CD OE1 NE2 REMARK 470 ARG E 18 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 19 CG CD CE NZ REMARK 470 GLU E 42 CG CD OE1 OE2 REMARK 470 TRP E 47 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 47 CZ3 CH2 REMARK 470 THR E 69 OG1 CG2 REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 GLN E 82 CG CD OE1 NE2 REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 GLU E 141 CG CD OE1 OE2 REMARK 470 LYS E 151 CG CD CE NZ REMARK 470 LEU E 154 CG CD1 CD2 REMARK 470 ARG E 168 CG CD NE CZ NH1 NH2 REMARK 470 GLN E 171 CG CD OE1 NE2 REMARK 470 GLN E 174 CG CD OE1 NE2 REMARK 470 MET E 180 CG SD CE REMARK 470 ASP E 189 CG OD1 OD2 REMARK 470 ARG E 206 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 208 CG CD OE1 OE2 REMARK 470 GLU E 210 CG CD OE1 OE2 REMARK 470 LYS E 232 CG CD CE NZ REMARK 470 GLU E 234 CG CD OE1 OE2 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 PRO A 125 53.88 -90.07 REMARK 500 GLU A 203 46.61 -91.01 REMARK 500 ASP A 204 -37.49 -130.79 REMARK 500 VAL A 236 -61.45 -124.22 REMARK 500 ARG A 263 -63.36 -94.09 REMARK 500 GLU A 297 45.58 -91.92 REMARK 500 ALA A 298 -50.50 -126.33 REMARK 500 GLU A 335 -12.20 71.16 REMARK 500 ASN C 35 4.39 -67.25 REMARK 500 ARG C 68 -9.70 74.40 REMARK 500 ASN C 132 -178.97 -175.83 REMARK 500 MET C 188 31.52 -141.20 REMARK 500 ASP C 246 56.52 -92.03 REMARK 500 LEU C 308 54.68 -91.78 REMARK 500 GLU D 47 53.35 -92.31 REMARK 500 ASN D 59 73.56 58.45 REMARK 500 SER B 44 31.40 -95.76 REMARK 500 HIS B 195 66.46 60.20 REMARK 500 LYS B 270 59.72 38.71 REMARK 500 PRO B 288 37.51 -84.46 REMARK 500 VAL E 48 -61.72 -108.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43557 RELATED DB: EMDB REMARK 900 KAPPA OPIOID RECEPTOR:GALPHAI PROTEIN IN COMPLEX WITH INVERSE REMARK 900 AGONIST JDTIC COMPOSITE MAP REMARK 900 RELATED ID: EMD-43648 RELATED DB: EMDB REMARK 900 FOCUSED MAP RECEPTOR REMARK 900 RELATED ID: EMD-43649 RELATED DB: EMDB REMARK 900 FOCUSED MAP G PROTEIN REMARK 900 RELATED ID: EMD-46609 RELATED DB: EMDB REMARK 900 CONSENSUS MAP DBREF 8VVF A 1 380 UNP P41145 OPRK_HUMAN 1 380 DBREF 8VVF C 1 340 UNP P62873 GBB1_HUMAN 1 340 DBREF 8VVF D 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8VVF B 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 8VVF E 1 239 PDB 8VVF 8VVF 1 239 SEQRES 1 A 380 MET ASP SER PRO ILE GLN ILE PHE ARG GLY GLU PRO GLY SEQRES 2 A 380 PRO THR CYS ALA PRO SER ALA CYS LEU PRO PRO ASN SER SEQRES 3 A 380 SER ALA TRP PHE PRO GLY TRP ALA GLU PRO ASP SER ASN SEQRES 4 A 380 GLY SER ALA GLY SER GLU ASP ALA GLN LEU GLU PRO ALA SEQRES 5 A 380 HIS ILE SER PRO ALA ILE PRO VAL ILE ILE THR ALA VAL SEQRES 6 A 380 TYR SER VAL VAL PHE VAL VAL GLY LEU VAL GLY ASN SER SEQRES 7 A 380 LEU VAL MET PHE VAL ILE ILE ARG TYR THR LYS MET LYS SEQRES 8 A 380 THR ALA THR ASN ILE TYR ILE PHE ASN LEU ALA LEU ALA SEQRES 9 A 380 ASP ALA LEU VAL THR THR THR MET PRO PHE GLN SER THR SEQRES 10 A 380 VAL TYR LEU MET ASN SER TRP PRO PHE GLY ASP VAL LEU SEQRES 11 A 380 CYS LYS ILE VAL ILE SER ILE ASP TYR TYR ASN MET PHE SEQRES 12 A 380 THR SER ILE PHE THR LEU THR MET MET SER VAL ASP ARG SEQRES 13 A 380 TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA LEU ASP PHE SEQRES 14 A 380 ARG THR PRO LEU LYS ALA LYS ILE ILE ASN ILE CYS ILE SEQRES 15 A 380 TRP LEU LEU SER SER SER VAL GLY ILE SER ALA ILE VAL SEQRES 16 A 380 LEU GLY GLY THR LYS VAL ARG GLU ASP VAL ASP VAL ILE SEQRES 17 A 380 GLU CYS SER LEU GLN PHE PRO ASP ASP ASP TYR SER TRP SEQRES 18 A 380 TRP ASP LEU PHE MET LYS ILE CYS VAL PHE ILE PHE ALA SEQRES 19 A 380 PHE VAL ILE PRO VAL LEU ILE ILE ILE VAL CYS TYR THR SEQRES 20 A 380 LEU MET ILE LEU ARG LEU LYS SER VAL ARG LEU LEU SER SEQRES 21 A 380 GLY SER ARG GLU LYS ASP ARG ASN LEU ARG ARG ILE THR SEQRES 22 A 380 ARG LEU VAL LEU VAL VAL VAL ALA VAL PHE VAL VAL CYS SEQRES 23 A 380 TRP THR PRO ILE HIS ILE PHE ILE LEU VAL GLU ALA LEU SEQRES 24 A 380 GLY SER THR SER HIS SER THR ALA ALA LEU SER SER TYR SEQRES 25 A 380 TYR PHE CYS ILE ALA LEU GLY TYR THR ASN SER SER LEU SEQRES 26 A 380 ASN PRO ILE LEU TYR ALA PHE LEU ASP GLU ASN PHE LYS SEQRES 27 A 380 ARG CYS PHE ARG ASP PHE CYS PHE PRO LEU LYS MET ARG SEQRES 28 A 380 MET GLU ARG GLN SER THR SER ARG VAL ARG ASN THR VAL SEQRES 29 A 380 GLN ASP PRO ALA TYR LEU ARG ASP ILE ASP GLY MET ASN SEQRES 30 A 380 LYS PRO VAL SEQRES 1 C 340 MET SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN SEQRES 2 C 340 LEU LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA SEQRES 3 C 340 ASP ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO SEQRES 4 C 340 VAL GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG SEQRES 5 C 340 GLY HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR SEQRES 6 C 340 ASP SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS SEQRES 7 C 340 LEU ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS SEQRES 8 C 340 ALA ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA SEQRES 9 C 340 TYR ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU SEQRES 10 C 340 ASP ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU SEQRES 11 C 340 GLY ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR SEQRES 12 C 340 GLY TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN SEQRES 13 C 340 ILE VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP SEQRES 14 C 340 ASP ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY SEQRES 15 C 340 HIS THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP SEQRES 16 C 340 THR ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA SEQRES 17 C 340 LYS LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR SEQRES 18 C 340 PHE THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE SEQRES 19 C 340 PHE PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP SEQRES 20 C 340 ALA THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU SEQRES 21 C 340 LEU MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE SEQRES 22 C 340 THR SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU SEQRES 23 C 340 ALA GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA SEQRES 24 C 340 LEU LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP SEQRES 25 C 340 ASN ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET SEQRES 26 C 340 ALA VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE SEQRES 27 C 340 TRP ASN SEQRES 1 D 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 D 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 D 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 D 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 D 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 D 71 PHE PHE CYS ALA ILE LEU SEQRES 1 B 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 B 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 B 354 GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU SEQRES 4 B 354 GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 B 354 MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU SEQRES 6 B 354 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 B 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 B 354 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 B 354 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 B 354 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 B 354 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 B 354 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 B 354 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 B 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 B 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS SEQRES 16 B 354 PHE LYS MET PHE ASP VAL GLY GLY GLN ARG SER GLU ARG SEQRES 17 B 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 B 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 B 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER MET SEQRES 20 B 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 B 354 ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 B 354 PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS SEQRES 23 B 354 TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 B 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS SEQRES 25 B 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 B 354 ALA THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 B 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS SEQRES 28 B 354 GLY LEU PHE SEQRES 1 E 251 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 251 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 E 251 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 E 251 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 E 251 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 E 251 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 E 251 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 E 251 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 E 251 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 E 251 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 E 251 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 E 251 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 E 251 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 E 251 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 E 251 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 E 251 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 E 251 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 E 251 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 E 251 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 E 251 LYS ALA ALA ALA HET JDC A 401 34 HETNAM JDC (3R)-7-HYDROXY-N-{(2S)-1-[(3R,4R)-4-(3-HYDROXYPHENYL)- HETNAM 2 JDC 3,4-DIMETHYLPIPERIDIN-1-YL]-3-METHYLBUTAN-2-YL}-1,2,3, HETNAM 3 JDC 4-TETRAHYDROISOQUINOLINE-3-CARBOXAMIDE FORMUL 6 JDC C28 H39 N3 O3 HELIX 1 AA1 ALA A 57 TYR A 87 1 31 HELIX 2 AA2 THR A 92 THR A 110 1 19 HELIX 3 AA3 THR A 110 ASN A 122 1 13 HELIX 4 AA4 LEU A 130 CYS A 161 1 32 HELIX 5 AA5 HIS A 162 ARG A 170 1 9 HELIX 6 AA6 THR A 171 LEU A 196 1 26 HELIX 7 AA7 TYR A 219 VAL A 236 1 18 HELIX 8 AA8 VAL A 236 VAL A 256 1 21 HELIX 9 AA9 GLU A 264 GLY A 300 1 37 HELIX 10 AB1 SER A 305 LEU A 333 1 29 HELIX 11 AB2 GLU A 335 ARG A 342 1 8 HELIX 12 AB3 GLU C 3 ALA C 26 1 24 HELIX 13 AB4 LEU C 30 ASN C 35 1 6 HELIX 14 AB5 ILE D 9 ASN D 24 1 16 HELIX 15 AB6 LYS D 29 HIS D 44 1 16 HELIX 16 AB7 SER B 6 GLU B 28 1 23 HELIX 17 AB8 GLU B 28 GLU B 33 1 6 HELIX 18 AB9 GLU B 207 PHE B 215 5 9 HELIX 19 AC1 ASN B 241 ASN B 255 1 15 HELIX 20 AC2 LYS B 270 LYS B 277 1 8 HELIX 21 AC3 THR B 295 ASP B 309 1 15 HELIX 22 AC4 ASN B 331 CYS B 351 1 21 HELIX 23 AC5 ALA E 28 PHE E 32 5 5 HELIX 24 AC6 SER E 53 GLY E 56 5 4 HELIX 25 AC7 ARG E 87 THR E 91 5 5 HELIX 26 AC8 GLU E 208 VAL E 212 5 5 SHEET 1 AA1 2 GLY A 197 VAL A 201 0 SHEET 2 AA1 2 ILE A 208 LEU A 212 -1 O SER A 211 N GLY A 198 SHEET 1 AA2 4 THR C 47 THR C 50 0 SHEET 2 AA2 4 LEU C 336 TRP C 339 -1 O ILE C 338 N ARG C 48 SHEET 3 AA2 4 VAL C 327 SER C 331 -1 N VAL C 327 O TRP C 339 SHEET 4 AA2 4 VAL C 315 VAL C 320 -1 N CYS C 317 O GLY C 330 SHEET 1 AA3 4 ILE C 58 TRP C 63 0 SHEET 2 AA3 4 LEU C 69 SER C 74 -1 O VAL C 71 N HIS C 62 SHEET 3 AA3 4 LYS C 78 ASP C 83 -1 O TRP C 82 N LEU C 70 SHEET 4 AA3 4 LYS C 89 PRO C 94 -1 O ILE C 93 N LEU C 79 SHEET 1 AA4 4 VAL C 100 TYR C 105 0 SHEET 2 AA4 4 TYR C 111 GLY C 116 -1 O ALA C 113 N ALA C 104 SHEET 3 AA4 4 ILE C 120 ASN C 125 -1 O SER C 122 N CYS C 114 SHEET 4 AA4 4 ARG C 134 ALA C 140 -1 O ARG C 134 N ASN C 125 SHEET 1 AA5 4 LEU C 146 CYS C 148 0 SHEET 2 AA5 4 GLN C 156 SER C 161 -1 O SER C 160 N SER C 147 SHEET 3 AA5 4 THR C 165 ASP C 170 -1 O TRP C 169 N ILE C 157 SHEET 4 AA5 4 GLN C 176 THR C 181 -1 O PHE C 180 N CYS C 166 SHEET 1 AA6 4 SER C 191 LEU C 192 0 SHEET 2 AA6 4 LEU C 198 GLY C 202 -1 O VAL C 200 N SER C 191 SHEET 3 AA6 4 SER C 207 ASP C 212 -1 O TRP C 211 N PHE C 199 SHEET 4 AA6 4 CYS C 218 THR C 223 -1 O GLN C 220 N LEU C 210 SHEET 1 AA7 4 ILE C 229 PHE C 234 0 SHEET 2 AA7 4 ALA C 240 SER C 245 -1 O GLY C 244 N ALA C 231 SHEET 3 AA7 4 CYS C 250 ASP C 254 -1 O PHE C 253 N PHE C 241 SHEET 4 AA7 4 MET C 262 TYR C 264 -1 O TYR C 264 N CYS C 250 SHEET 1 AA8 4 VAL C 276 PHE C 278 0 SHEET 2 AA8 4 LEU C 284 GLY C 288 -1 O LEU C 286 N SER C 277 SHEET 3 AA8 4 CYS C 294 ASP C 298 -1 O TRP C 297 N LEU C 285 SHEET 4 AA8 4 ARG C 304 VAL C 307 -1 O GLY C 306 N VAL C 296 SHEET 1 AA9 4 LEU B 37 LEU B 39 0 SHEET 2 AA9 4 ALA B 220 ALA B 226 1 O ILE B 222 N LEU B 39 SHEET 3 AA9 4 SER B 263 ASN B 269 1 O ILE B 265 N ILE B 221 SHEET 4 AA9 4 ILE B 319 PHE B 323 1 O TYR B 320 N LEU B 266 SHEET 1 AB1 2 VAL B 185 PHE B 189 0 SHEET 2 AB1 2 PHE B 196 ASP B 200 -1 O ASP B 200 N VAL B 185 SHEET 1 AB2 4 LEU E 4 SER E 7 0 SHEET 2 AB2 4 SER E 17 ALA E 24 -1 O SER E 23 N VAL E 5 SHEET 3 AB2 4 THR E 78 THR E 84 -1 O LEU E 79 N CYS E 22 SHEET 4 AB2 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AB3 6 GLY E 10 VAL E 12 0 SHEET 2 AB3 6 THR E 115 VAL E 119 1 O THR E 118 N GLY E 10 SHEET 3 AB3 6 ALA E 92 ARG E 98 -1 N TYR E 94 O THR E 115 SHEET 4 AB3 6 MET E 34 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AB3 6 LEU E 45 ILE E 51 -1 O VAL E 48 N TRP E 36 SHEET 6 AB3 6 ILE E 58 TYR E 60 -1 O TYR E 59 N TYR E 50 SHEET 1 AB4 4 GLY E 10 VAL E 12 0 SHEET 2 AB4 4 THR E 115 VAL E 119 1 O THR E 118 N GLY E 10 SHEET 3 AB4 4 ALA E 92 ARG E 98 -1 N TYR E 94 O THR E 115 SHEET 4 AB4 4 PHE E 110 TRP E 111 -1 O PHE E 110 N ARG E 98 SHEET 1 AB5 3 MET E 128 THR E 129 0 SHEET 2 AB5 3 SER E 144 SER E 149 -1 O ARG E 148 N THR E 129 SHEET 3 AB5 3 ALA E 199 THR E 203 -1 O LEU E 202 N ILE E 145 SHEET 1 AB6 5 VAL E 135 PRO E 136 0 SHEET 2 AB6 5 THR E 231 GLU E 234 1 O GLU E 234 N VAL E 135 SHEET 3 AB6 5 VAL E 214 GLN E 219 -1 N TYR E 215 O THR E 231 SHEET 4 AB6 5 LEU E 162 GLN E 167 -1 N TYR E 163 O MET E 218 SHEET 5 AB6 5 PRO E 173 ILE E 177 -1 O GLN E 174 N LEU E 166 SSBOND 1 CYS A 131 CYS A 210 1555 1555 2.03 SSBOND 2 CYS E 147 CYS E 217 1555 1555 2.03 CISPEP 1 TYR E 223 PRO E 224 0 2.64 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