HEADER MEMBRANE PROTEIN 15-SEP-25 9WSV TITLE CRYO-EM STRUCTURE OF DAMGO-MUOR-ARRESTIN-1-FAB30 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: MU-TYPE OPIOID RECEPTOR,VASOPRESSIN V2 RECEPTOR; COMPND 3 CHAIN: R; COMPND 4 SYNONYM: M-OR-1,MOR-1,V2R,AVPR V2,ANTIDIURETIC HORMONE RECEPTOR, COMPND 5 RENAL-TYPE ARGININE VASOPRESSIN RECEPTOR; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: BETA-ARRESTIN-1; COMPND 9 CHAIN: C; COMPND 10 SYNONYM: ARRESTIN BETA-1,ARRESTIN-2; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: FAB30 HEAVY CHAIN; COMPND 14 CHAIN: H; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: FAB30 LIGHT CHAIN; COMPND 18 CHAIN: L; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: DAMGO; COMPND 22 CHAIN: P; COMPND 23 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE, HUMAN; SOURCE 4 ORGANISM_TAXID: 10090, 9606; SOURCE 5 GENE: OPRM1, MOR, OPRM, AVPR2, ADHR, DIR, DIR3, V2R; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 10 ORGANISM_COMMON: DOMESTIC CATTLE; SOURCE 11 ORGANISM_TAXID: 9913; SOURCE 12 GENE: ARRB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 17 ORGANISM_TAXID: 32630; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 22 ORGANISM_TAXID: 32630; SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 25 MOL_ID: 5; SOURCE 26 SYNTHETIC: YES; SOURCE 27 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 28 ORGANISM_TAXID: 32630 KEYWDS G-PROTEIN-COUPLED RECEPTORS, MU-OPIOID RECEPTOR, SINGLE PARTICLE, KEYWDS 2 CRYO-EM, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR H.ZHANG,X.WANG,K.XI,Q.SHEN,J.XUE,Y.ZHU,G.YANG,Y.ZHANG REVDAT 1 26-NOV-25 9WSV 0 JRNL AUTH H.ZHANG,X.WANG,K.XI,Q.SHEN,J.XUE,Y.ZHU,S.K.ZANG,T.YU, JRNL AUTH 2 D.D.SHEN,J.GUO,L.N.CHEN,S.Y.JI,J.QIN,Y.DONG,M.ZHAO,M.YANG, JRNL AUTH 3 H.WU,G.YANG,Y.ZHANG JRNL TITL THE MOLECULAR BASIS OF MU-OPIOID RECEPTOR SIGNALING JRNL TITL 2 PLASTICITY. JRNL REF CELL RES. 2025 JRNL REFN ISSN 1001-0602 JRNL PMID 41199005 JRNL DOI 10.1038/S41422-025-01191-8 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, RELION 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) : 2.800 REMARK 3 NUMBER OF PARTICLES : 233269 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9WSV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 17-SEP-25. REMARK 100 THE DEPOSITION ID IS D_1300060358. 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 : COMPLEX OF DAMGO BOUND MOR REMARK 245 -ARRESTIN2 PROTEIN REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 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 : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5200.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, C, H, L, P 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 400 REMARK 400 COMPOUND REMARK 400 REMARK 400 THE DAMGO IS PEPTIDE-LIKE, A MEMBER OF SYNTHETIC OPIOID CLASS. REMARK 400 REMARK 400 GROUP: 1 REMARK 400 NAME: DAMGO REMARK 400 CHAIN: P REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER REMARK 400 DESCRIPTION: NULL 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 R 3 REMARK 465 PRO R 4 REMARK 465 MET R 5 REMARK 465 GLY R 6 REMARK 465 PRO R 7 REMARK 465 GLY R 8 REMARK 465 ASN R 9 REMARK 465 ILE R 10 REMARK 465 SER R 11 REMARK 465 ASP R 12 REMARK 465 CYS R 13 REMARK 465 SER R 14 REMARK 465 ASP R 15 REMARK 465 PRO R 16 REMARK 465 LEU R 17 REMARK 465 ALA R 18 REMARK 465 PRO R 19 REMARK 465 ALA R 20 REMARK 465 SER R 21 REMARK 465 CYS R 22 REMARK 465 SER R 23 REMARK 465 PRO R 24 REMARK 465 ALA R 25 REMARK 465 PRO R 26 REMARK 465 GLY R 27 REMARK 465 SER R 28 REMARK 465 TRP R 29 REMARK 465 LEU R 30 REMARK 465 ASN R 31 REMARK 465 LEU R 32 REMARK 465 SER R 33 REMARK 465 HIS R 34 REMARK 465 VAL R 35 REMARK 465 ASP R 36 REMARK 465 GLY R 37 REMARK 465 ASN R 38 REMARK 465 GLN R 39 REMARK 465 SER R 40 REMARK 465 ASP R 41 REMARK 465 PRO R 42 REMARK 465 CYS R 43 REMARK 465 GLY R 44 REMARK 465 PRO R 45 REMARK 465 ASN R 46 REMARK 465 ARG R 47 REMARK 465 THR R 48 REMARK 465 GLY R 49 REMARK 465 LEU R 50 REMARK 465 GLY R 51 REMARK 465 GLY R 52 REMARK 465 SER R 53 REMARK 465 HIS R 54 REMARK 465 SER R 55 REMARK 465 LEU R 56 REMARK 465 CYS R 57 REMARK 465 PRO R 58 REMARK 465 GLN R 59 REMARK 465 THR R 60 REMARK 465 GLY R 61 REMARK 465 SER R 62 REMARK 465 ARG R 263 REMARK 465 MET R 264 REMARK 465 LEU R 265 REMARK 465 SER R 266 REMARK 465 GLY R 267 REMARK 465 SER R 268 REMARK 465 LYS R 269 REMARK 465 ILE R 351A REMARK 465 CYS R 351B REMARK 465 ALA R 351C REMARK 465 ARG R 351D REMARK 465 GLY R 351E REMARK 465 ARG R 351F REMARK 465 THR R 351G REMARK 465 PRO R 351H REMARK 465 PRO R 351I REMARK 465 SER R 351J REMARK 465 LEU R 351K REMARK 465 GLY R 351L REMARK 465 PRO R 351M REMARK 465 GLN R 351N REMARK 465 ASP R 351O REMARK 465 ASP R 375 REMARK 465 THR R 376 REMARK 465 SER R 377 REMARK 465 SER R 378 REMARK 465 LEU R 379 REMARK 465 GLU R 380 REMARK 465 VAL R 381 REMARK 465 LEU R 382 REMARK 465 PHE R 383 REMARK 465 GLN R 384 REMARK 465 MET C 1 REMARK 465 GLY C 2 REMARK 465 ASP C 3 REMARK 465 LYS C 4 REMARK 465 GLY C 5 REMARK 465 GLU C 359 REMARK 465 PRO C 360 REMARK 465 PRO C 361 REMARK 465 HIS C 362 REMARK 465 ARG C 363 REMARK 465 GLU C 364 REMARK 465 VAL C 365 REMARK 465 PRO C 366 REMARK 465 GLU C 367 REMARK 465 HIS C 368 REMARK 465 GLU C 369 REMARK 465 THR C 370 REMARK 465 PRO C 371 REMARK 465 VAL C 372 REMARK 465 ASP C 373 REMARK 465 THR C 374 REMARK 465 ASN C 375 REMARK 465 LEU C 376 REMARK 465 ILE C 377 REMARK 465 GLU C 378 REMARK 465 LEU C 379 REMARK 465 ASP C 380 REMARK 465 THR C 381 REMARK 465 ASN C 382 REMARK 465 ASP C 383 REMARK 465 ASP C 384 REMARK 465 ASP C 385 REMARK 465 ALA C 386 REMARK 465 ALA C 387 REMARK 465 ALA C 388 REMARK 465 GLU C 389 REMARK 465 ASP C 390 REMARK 465 PHE C 391 REMARK 465 ALA C 392 REMARK 465 ARG C 393 REMARK 465 MET H 0 REMARK 465 GLU H 1 REMARK 465 ILE H 2 REMARK 465 SER H 3 REMARK 465 GLU H 4 REMARK 465 PRO H 136 REMARK 465 SER H 137 REMARK 465 SER H 138 REMARK 465 LYS H 139 REMARK 465 SER H 140 REMARK 465 THR H 141 REMARK 465 SER H 142 REMARK 465 GLY H 143 REMARK 465 GLY H 144 REMARK 465 THR H 145 REMARK 465 ALA H 146 REMARK 465 ALA H 147 REMARK 465 PRO H 195 REMARK 465 SER H 196 REMARK 465 SER H 197 REMARK 465 SER H 198 REMARK 465 LEU H 199 REMARK 465 GLY H 200 REMARK 465 THR H 201 REMARK 465 GLN H 202 REMARK 465 THR H 203 REMARK 465 GLU H 222 REMARK 465 PRO H 223 REMARK 465 LYS H 224 REMARK 465 SER H 225 REMARK 465 CYS H 226 REMARK 465 ASP H 227 REMARK 465 LYS H 228 REMARK 465 THR H 229 REMARK 465 GLU H 230 REMARK 465 ASN H 231 REMARK 465 LEU H 232 REMARK 465 TYR H 233 REMARK 465 PHE H 234 REMARK 465 GLN H 235 REMARK 465 MET L 0 REMARK 465 SER L 1 REMARK 465 SER L 128 REMARK 465 GLY L 129 REMARK 465 THR L 130 REMARK 465 ASP L 152 REMARK 465 ASN L 153 REMARK 465 ALA L 154 REMARK 465 LEU L 155 REMARK 465 GLN L 156 REMARK 465 SER L 157 REMARK 465 LYS L 189 REMARK 465 HIS L 190 REMARK 465 LYS L 191 REMARK 465 VAL L 192 REMARK 465 TYR L 193 REMARK 465 ALA L 194 REMARK 465 CYS L 195 REMARK 465 GLU L 196 REMARK 465 VAL L 197 REMARK 465 THR L 198 REMARK 465 HIS L 199 REMARK 465 GLN L 200 REMARK 465 GLY L 201 REMARK 465 LEU L 202 REMARK 465 SER L 203 REMARK 465 SER L 204 REMARK 465 PRO L 205 REMARK 465 VAL L 206 REMARK 465 THR L 207 REMARK 465 LYS L 208 REMARK 465 SER L 209 REMARK 465 PHE L 210 REMARK 465 ASN L 211 REMARK 465 ARG L 212 REMARK 465 GLY L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 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 R 98 CG CD CE NZ REMARK 470 ASN R 137 CG OD1 ND2 REMARK 470 LEU R 139 CG CD1 CD2 REMARK 470 PHE R 178 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE R 221 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TRP R 226 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 226 CZ3 CH2 REMARK 470 LYS R 260 CG CD CE NZ REMARK 470 LYS R 271 CG CD CE NZ REMARK 470 ARG R 273 CG CD NE CZ NH1 NH2 REMARK 470 GLU R 310 CG CD OE1 OE2 REMARK 470 LEU R 331 CG CD1 CD2 REMARK 470 LYS C 49 CG CD CE NZ REMARK 470 GLU C 50 CG CD OE1 OE2 REMARK 470 ARG C 65 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 66 CG CD OE1 OE2 REMARK 470 LEU C 68 CG CD1 CD2 REMARK 470 ASP C 69 CG OD1 OD2 REMARK 470 LYS C 94 CG CD CE NZ REMARK 470 LYS C 138 CG CD CE NZ REMARK 470 HIS C 159 CG ND1 CD2 CE1 NE2 REMARK 470 LYS C 195 CG CD CE NZ REMARK 470 ARG C 307 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 308 CG CD OE1 OE2 REMARK 470 ARG C 312 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 313 CG CD OE1 OE2 REMARK 470 LEU H 14 CG CD1 CD2 REMARK 470 GLN H 16 CG CD OE1 NE2 REMARK 470 LYS H 46 CG CD CE NZ REMARK 470 GLU H 49 CG CD OE1 OE2 REMARK 470 TYR H 57 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP H 65 CG OD1 OD2 REMARK 470 ASP H 76 CG OD1 OD2 REMARK 470 LYS H 79 CG CD CE NZ REMARK 470 ARG H 90 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 92 CG CD OE1 OE2 REMARK 470 TRP H 113 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 113 CZ3 CH2 REMARK 470 LYS H 127 CG CD CE NZ REMARK 470 PHE H 132 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU H 148 CG CD1 CD2 REMARK 470 LEU H 151 CG CD1 CD2 REMARK 470 LYS H 153 CG CD CE NZ REMARK 470 ASP H 154 CG OD1 OD2 REMARK 470 TYR H 155 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE H 156 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU H 158 CG CD OE1 OE2 REMARK 470 TRP H 164 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 164 CZ3 CH2 REMARK 470 THR H 170 OG1 CG2 REMARK 470 SER H 171 OG REMARK 470 LEU H 180 CG CD1 CD2 REMARK 470 GLN H 181 CG CD OE1 NE2 REMARK 470 LEU H 185 CG CD1 CD2 REMARK 470 VAL H 192 CG1 CG2 REMARK 470 TYR H 204 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE H 205 CG1 CG2 CD1 REMARK 470 ASN H 207 CG OD1 ND2 REMARK 470 ASN H 209 CG OD1 ND2 REMARK 470 LYS H 211 CG CD CE NZ REMARK 470 ASN H 214 CG OD1 ND2 REMARK 470 LYS H 216 CG CD CE NZ REMARK 470 ASP H 218 CG OD1 OD2 REMARK 470 LYS H 219 CG CD CE NZ REMARK 470 LYS H 220 CG CD CE NZ REMARK 470 ARG L 25 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 28 CG CD OE1 NE2 REMARK 470 TYR L 37 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN L 39 CG CD OE1 NE2 REMARK 470 LYS L 43 CG CD CE NZ REMARK 470 LYS L 46 CG CD CE NZ REMARK 470 LEU L 48 CG CD1 CD2 REMARK 470 ILE L 49 CG1 CG2 CD1 REMARK 470 LEU L 74 CG CD1 CD2 REMARK 470 ILE L 76 CG1 CG2 CD1 REMARK 470 GLU L 82 CG CD OE1 OE2 REMARK 470 ASP L 83 CG OD1 OD2 REMARK 470 PHE L 84 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR L 87 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN L 90 CG CD OE1 NE2 REMARK 470 GLN L 91 CG CD OE1 NE2 REMARK 470 GLU L 106 CG CD OE1 OE2 REMARK 470 ILE L 107 CG1 CG2 CD1 REMARK 470 LYS L 108 CG CD CE NZ REMARK 470 ARG L 109 CG CD NE CZ NH1 NH2 REMARK 470 ILE L 118 CG1 CG2 CD1 REMARK 470 ASP L 123 CG OD1 OD2 REMARK 470 GLN L 125 CG CD OE1 NE2 REMARK 470 LEU L 126 CG CD1 CD2 REMARK 470 LYS L 127 CG CD CE NZ REMARK 470 GLU L 144 CG CD OE1 OE2 REMARK 470 LYS L 146 CG CD CE NZ REMARK 470 GLN L 148 CG CD OE1 NE2 REMARK 470 ASN L 159 CG OD1 ND2 REMARK 470 GLN L 161 CG CD OE1 NE2 REMARK 470 GLU L 162 CG CD OE1 OE2 REMARK 470 GLU L 166 CG CD OE1 OE2 REMARK 470 ASP L 168 CG OD1 OD2 REMARK 470 LYS L 170 CG CD CE NZ REMARK 470 ASP L 171 CG OD1 OD2 REMARK 470 LEU L 180 CG CD1 CD2 REMARK 470 LEU L 182 CG CD1 CD2 REMARK 470 LYS L 184 CG CD CE NZ REMARK 470 ASP L 186 CG OD1 OD2 REMARK 470 TYR L 187 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU L 188 CG CD OE1 OE2 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 OD1 ASP C 204 OH TYR C 208 2.13 REMARK 500 O GLN C 130 N GLY C 286 2.19 REMARK 500 O PRO C 124 OH TYR C 144 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 TYR P 1 CB TYR P 1 CG 0.092 REMARK 500 GLY P 3 C GLY P 3 O -0.110 REMARK 500 GLY P 3 C MEA P 4 N 0.191 REMARK 500 MEA P 4 C ETA P 5 N 0.159 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 ALA R 206 50.18 -109.64 REMARK 500 PHE R 241 -56.53 -122.44 REMARK 500 ALA R 337 -60.61 -95.30 REMARK 500 LEU C 68 -78.61 -70.32 REMARK 500 ASP C 69 3.18 57.90 REMARK 500 ASN C 245 67.35 60.00 REMARK 500 ALA C 247 -169.16 -128.54 REMARK 500 LYS C 292 -179.24 -69.14 REMARK 500 LYS C 294 -167.17 -127.02 REMARK 500 GLU C 313 57.49 -92.11 REMARK 500 TYR H 107 127.31 -37.36 REMARK 500 SER L 51 17.93 59.39 REMARK 500 ALA L 52 -9.59 71.58 REMARK 500 PRO L 142 -165.66 -79.36 REMARK 500 MEA P 4 -85.08 67.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-66207 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DAMGO-MUOR-GZ-SCFV16 COMPLEX DBREF 9WSV R 6 351A UNP P42866 OPRM_MOUSE 6 352 DBREF 9WSV R 351B 378 UNP P30518 V2R_HUMAN 342 371 DBREF 9WSV C 1 393 UNP P17870 ARRB1_BOVIN 1 393 DBREF 9WSV H 0 235 PDB 9WSV 9WSV 0 235 DBREF 9WSV L 0 215 PDB 9WSV 9WSV 0 215 DBREF 9WSV P 1 5 PDB 9WSV 9WSV 1 5 SEQADV 9WSV GLY R 3 UNP P42866 EXPRESSION TAG SEQADV 9WSV PRO R 4 UNP P42866 EXPRESSION TAG SEQADV 9WSV MET R 5 UNP P42866 EXPRESSION TAG SEQADV 9WSV LEU R 379 UNP P30518 EXPRESSION TAG SEQADV 9WSV GLU R 380 UNP P30518 EXPRESSION TAG SEQADV 9WSV VAL R 381 UNP P30518 EXPRESSION TAG SEQADV 9WSV LEU R 382 UNP P30518 EXPRESSION TAG SEQADV 9WSV PHE R 383 UNP P30518 EXPRESSION TAG SEQADV 9WSV GLN R 384 UNP P30518 EXPRESSION TAG SEQADV 9WSV GLU C 169 UNP P17870 ARG 169 CONFLICT SEQADV 9WSV ALA C 386 UNP P17870 ILE 386 CONFLICT SEQADV 9WSV ALA C 387 UNP P17870 VAL 387 CONFLICT SEQADV 9WSV ALA C 388 UNP P17870 PHE 388 CONFLICT SEQRES 1 R 386 GLY PRO MET GLY PRO GLY ASN ILE SER ASP CYS SER ASP SEQRES 2 R 386 PRO LEU ALA PRO ALA SER CYS SER PRO ALA PRO GLY SER SEQRES 3 R 386 TRP LEU ASN LEU SER HIS VAL ASP GLY ASN GLN SER ASP SEQRES 4 R 386 PRO CYS GLY PRO ASN ARG THR GLY LEU GLY GLY SER HIS SEQRES 5 R 386 SER LEU CYS PRO GLN THR GLY SER PRO SER MET VAL THR SEQRES 6 R 386 ALA ILE THR ILE MET ALA LEU TYR SER ILE VAL CYS VAL SEQRES 7 R 386 VAL GLY LEU PHE GLY ASN PHE LEU VAL MET TYR VAL ILE SEQRES 8 R 386 VAL ARG TYR THR LYS MET LYS THR ALA THR ASN ILE TYR SEQRES 9 R 386 ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU ALA THR SER SEQRES 10 R 386 THR LEU PRO PHE GLN SER VAL ASN TYR LEU MET GLY THR SEQRES 11 R 386 TRP PRO PHE GLY ASN ILE LEU CYS LYS ILE VAL ILE SER SEQRES 12 R 386 ILE ASP TYR TYR ASN MET PHE THR SER ILE PHE THR LEU SEQRES 13 R 386 CYS THR MET SER VAL ASP ARG TYR ILE ALA VAL CYS HIS SEQRES 14 R 386 PRO VAL LYS ALA LEU ASP PHE ARG THR PRO ARG ASN ALA SEQRES 15 R 386 LYS ILE VAL ASN VAL CYS ASN TRP ILE LEU SER SER ALA SEQRES 16 R 386 ILE GLY LEU PRO VAL MET PHE MET ALA THR THR LYS TYR SEQRES 17 R 386 ARG GLN GLY SER ILE ASP CYS THR LEU THR PHE SER HIS SEQRES 18 R 386 PRO THR TRP TYR TRP GLU ASN LEU LEU LYS ILE CYS VAL SEQRES 19 R 386 PHE ILE PHE ALA PHE ILE MET PRO VAL LEU ILE ILE THR SEQRES 20 R 386 VAL CYS TYR GLY LEU MET ILE LEU ARG LEU LYS SER VAL SEQRES 21 R 386 ARG MET LEU SER GLY SER LYS GLU LYS ASP ARG ASN LEU SEQRES 22 R 386 ARG ARG ILE THR ARG MET VAL LEU VAL VAL VAL ALA VAL SEQRES 23 R 386 PHE ILE VAL CYS TRP THR PRO ILE HIS ILE TYR VAL ILE SEQRES 24 R 386 ILE LYS ALA LEU ILE THR ILE PRO GLU THR THR PHE GLN SEQRES 25 R 386 THR VAL SER TRP HIS PHE CYS ILE ALA LEU GLY TYR THR SEQRES 26 R 386 ASN SER CYS LEU ASN PRO VAL LEU TYR ALA PHE LEU ASP SEQRES 27 R 386 GLU ASN PHE LYS ARG CYS PHE ARG GLU PHE CYS ILE CYS SEQRES 28 R 386 ALA ARG GLY ARG THR PRO PRO SER LEU GLY PRO GLN ASP SEQRES 29 R 386 GLU SEP CYS TPO TPO ALA SEP SEP SEP LEU ALA LYS ASP SEQRES 30 R 386 THR SER SER LEU GLU VAL LEU PHE GLN SEQRES 1 C 393 MET GLY ASP LYS GLY THR ARG VAL PHE LYS LYS ALA SER SEQRES 2 C 393 PRO ASN GLY LYS LEU THR VAL TYR LEU GLY LYS ARG ASP SEQRES 3 C 393 PHE VAL ASP HIS ILE ASP LEU VAL GLU PRO VAL ASP GLY SEQRES 4 C 393 VAL VAL LEU VAL ASP PRO GLU TYR LEU LYS GLU ARG ARG SEQRES 5 C 393 VAL TYR VAL THR LEU THR CYS ALA PHE ARG TYR GLY ARG SEQRES 6 C 393 GLU ASP LEU ASP VAL LEU GLY LEU THR PHE ARG LYS ASP SEQRES 7 C 393 LEU PHE VAL ALA ASN VAL GLN SER PHE PRO PRO ALA PRO SEQRES 8 C 393 GLU ASP LYS LYS PRO LEU THR ARG LEU GLN GLU ARG LEU SEQRES 9 C 393 ILE LYS LYS LEU GLY GLU HIS ALA TYR PRO PHE THR PHE SEQRES 10 C 393 GLU ILE PRO PRO ASN LEU PRO CYS SER VAL THR LEU GLN SEQRES 11 C 393 PRO GLY PRO GLU ASP THR GLY LYS ALA CYS GLY VAL ASP SEQRES 12 C 393 TYR GLU VAL LYS ALA PHE CYS ALA GLU ASN LEU GLU GLU SEQRES 13 C 393 LYS ILE HIS LYS ARG ASN SER VAL ARG LEU VAL ILE GLU SEQRES 14 C 393 LYS VAL GLN TYR ALA PRO GLU ARG PRO GLY PRO GLN PRO SEQRES 15 C 393 THR ALA GLU THR THR ARG GLN PHE LEU MET SER ASP LYS SEQRES 16 C 393 PRO LEU HIS LEU GLU ALA SER LEU ASP LYS GLU ILE TYR SEQRES 17 C 393 TYR HIS GLY GLU PRO ILE SER VAL ASN VAL HIS VAL THR SEQRES 18 C 393 ASN ASN THR ASN LYS THR VAL LYS LYS ILE LYS ILE SER SEQRES 19 C 393 VAL ARG GLN TYR ALA ASP ILE CYS LEU PHE ASN THR ALA SEQRES 20 C 393 GLN TYR LYS CYS PRO VAL ALA MET GLU GLU ALA ASP ASP SEQRES 21 C 393 THR VAL ALA PRO SER SER THR PHE CYS LYS VAL TYR THR SEQRES 22 C 393 LEU THR PRO PHE LEU ALA ASN ASN ARG GLU LYS ARG GLY SEQRES 23 C 393 LEU ALA LEU ASP GLY LYS LEU LYS HIS GLU ASP THR ASN SEQRES 24 C 393 LEU ALA SER SER THR LEU LEU ARG GLU GLY ALA ASN ARG SEQRES 25 C 393 GLU ILE LEU GLY ILE ILE VAL SER TYR LYS VAL LYS VAL SEQRES 26 C 393 LYS LEU VAL VAL SER ARG GLY GLY LEU LEU GLY ASP LEU SEQRES 27 C 393 ALA SER SER ASP VAL ALA VAL GLU LEU PRO PHE THR LEU SEQRES 28 C 393 MET HIS PRO LYS PRO LYS GLU GLU PRO PRO HIS ARG GLU SEQRES 29 C 393 VAL PRO GLU HIS GLU THR PRO VAL ASP THR ASN LEU ILE SEQRES 30 C 393 GLU LEU ASP THR ASN ASP ASP ASP ALA ALA ALA GLU ASP SEQRES 31 C 393 PHE ALA ARG SEQRES 1 H 236 MET GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY SEQRES 2 H 236 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3 H 236 ALA ALA SER GLY PHE ASN VAL TYR SER SER SER ILE HIS SEQRES 4 H 236 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5 H 236 ALA SER ILE SER SER TYR TYR GLY TYR THR TYR TYR ALA SEQRES 6 H 236 ASP SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SEQRES 7 H 236 SER LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG SEQRES 8 H 236 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER ARG SEQRES 9 H 236 GLN PHE TRP TYR SER GLY LEU ASP TYR TRP GLY GLN GLY SEQRES 10 H 236 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 236 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 236 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 236 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 236 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 236 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 236 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 236 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 236 VAL GLU PRO LYS SER CYS ASP LYS THR GLU ASN LEU TYR SEQRES 19 H 236 PHE GLN SEQRES 1 L 216 MET SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SEQRES 2 L 216 SER ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG SEQRES 3 L 216 ALA SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN SEQRES 4 L 216 GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER SEQRES 5 L 216 ALA SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER SEQRES 6 L 216 GLY SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SEQRES 7 L 216 SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN SEQRES 8 L 216 GLN TYR LYS TYR VAL PRO VAL THR PHE GLY GLN GLY THR SEQRES 9 L 216 LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 L 216 PHE ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY SEQRES 11 L 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 L 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 L 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 L 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 L 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 L 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 L 216 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 P 5 TYR DAL GLY MEA ETA MODRES 9WSV SEP R 364 SER MODIFIED RESIDUE MODRES 9WSV TPO R 366 THR MODIFIED RESIDUE MODRES 9WSV TPO R 367 THR MODIFIED RESIDUE MODRES 9WSV SEP R 369 SER MODIFIED RESIDUE MODRES 9WSV SEP R 370 SER MODIFIED RESIDUE MODRES 9WSV SEP R 371 SER MODIFIED RESIDUE HET SEP R 364 10 HET TPO R 366 11 HET TPO R 367 11 HET SEP R 369 10 HET SEP R 370 10 HET SEP R 371 10 HET DAL P 2 5 HET MEA P 4 12 HET ETA P 5 4 HETNAM SEP PHOSPHOSERINE HETNAM TPO PHOSPHOTHREONINE HETNAM DAL D-ALANINE HETNAM MEA N-METHYLPHENYLALANINE HETNAM ETA ETHANOLAMINE HETSYN SEP PHOSPHONOSERINE HETSYN TPO PHOSPHONOTHREONINE FORMUL 1 SEP 4(C3 H8 N O6 P) FORMUL 1 TPO 2(C4 H10 N O6 P) FORMUL 5 DAL C3 H7 N O2 FORMUL 5 MEA C10 H13 N O2 FORMUL 5 ETA C2 H7 N O FORMUL 6 HOH *4(H2 O) HELIX 1 AA1 MET R 65 TYR R 96 1 32 HELIX 2 AA2 THR R 101 SER R 119 1 19 HELIX 3 AA3 THR R 120 MET R 130 1 11 HELIX 4 AA4 GLY R 136 HIS R 171 1 36 HELIX 5 AA5 HIS R 171 ARG R 179 1 9 HELIX 6 AA6 THR R 180 MET R 205 1 26 HELIX 7 AA7 PRO R 224 ALA R 240 1 17 HELIX 8 AA8 PHE R 241 SER R 261 1 21 HELIX 9 AA9 LYS R 271 ILE R 306 1 36 HELIX 10 AB1 THR R 311 ALA R 337 1 27 HELIX 11 AB2 ASP R 340 CYS R 351 1 12 HELIX 12 AB3 THR C 98 LEU C 108 1 11 HELIX 13 AB4 ARG H 90 THR H 94 5 5 HELIX 14 AB5 SER H 166 ALA H 168 5 3 HELIX 15 AB6 GLN L 80 PHE L 84 5 5 HELIX 16 AB7 SER L 122 LYS L 127 1 6 SHEET 1 AA1 5 ALA R 368 SEP R 371 0 SHEET 2 AA1 5 ARG C 7 ALA C 12 -1 O LYS C 10 N ALA R 368 SHEET 3 AA1 5 THR C 19 LEU C 22 -1 O LEU C 22 N PHE C 9 SHEET 4 AA1 5 VAL C 37 LEU C 42 -1 O VAL C 40 N TYR C 21 SHEET 5 AA1 5 ALA C 112 PHE C 117 -1 O TYR C 113 N VAL C 41 SHEET 1 AA2 5 ASP C 26 VAL C 28 0 SHEET 2 AA2 5 SER C 163 VAL C 171 1 O GLU C 169 N PHE C 27 SHEET 3 AA2 5 CYS C 140 ALA C 151 -1 N VAL C 146 O LEU C 166 SHEET 4 AA2 5 ARG C 52 ARG C 62 -1 N ARG C 52 O ALA C 151 SHEET 5 AA2 5 ARG C 76 PHE C 87 -1 O ALA C 82 N LEU C 57 SHEET 1 AA3 5 ASP C 26 VAL C 28 0 SHEET 2 AA3 5 SER C 163 VAL C 171 1 O GLU C 169 N PHE C 27 SHEET 3 AA3 5 CYS C 140 ALA C 151 -1 N VAL C 146 O LEU C 166 SHEET 4 AA3 5 THR C 128 PRO C 131 -1 N LEU C 129 O CYS C 140 SHEET 5 AA3 5 ARG C 285 LEU C 289 -1 O LEU C 289 N THR C 128 SHEET 1 AA4 4 THR C 183 ARG C 188 0 SHEET 2 AA4 4 LEU C 197 LEU C 203 -1 O ALA C 201 N ALA C 184 SHEET 3 AA4 4 ILE C 214 ASN C 222 -1 O THR C 221 N HIS C 198 SHEET 4 AA4 4 SER C 266 LEU C 274 -1 O PHE C 268 N VAL C 220 SHEET 1 AA5 5 ILE C 207 TYR C 209 0 SHEET 2 AA5 5 SER C 340 MET C 352 1 O THR C 350 N TYR C 208 SHEET 3 AA5 5 GLY C 316 SER C 330 -1 N LEU C 327 O VAL C 343 SHEET 4 AA5 5 VAL C 228 CYS C 242 -1 N ARG C 236 O LYS C 322 SHEET 5 AA5 5 TYR C 249 ALA C 258 -1 O CYS C 251 N GLN C 237 SHEET 1 AA6 4 GLN H 6 SER H 10 0 SHEET 2 AA6 4 LEU H 21 SER H 28 -1 O SER H 28 N GLN H 6 SHEET 3 AA6 4 THR H 81 MET H 86 -1 O LEU H 84 N LEU H 23 SHEET 4 AA6 4 PHE H 71 ASP H 76 -1 N THR H 72 O GLN H 85 SHEET 1 AA7 5 TYR H 60 TYR H 63 0 SHEET 2 AA7 5 LEU H 48 SER H 55 -1 N SER H 53 O TYR H 62 SHEET 3 AA7 5 SER H 35 GLN H 42 -1 N ARG H 41 O GLU H 49 SHEET 4 AA7 5 ALA H 95 ARG H 103 -1 O TYR H 98 N VAL H 40 SHEET 5 AA7 5 TYR H 112 TRP H 113 -1 O TYR H 112 N ARG H 101 SHEET 1 AA8 5 TYR H 60 TYR H 63 0 SHEET 2 AA8 5 LEU H 48 SER H 55 -1 N SER H 53 O TYR H 62 SHEET 3 AA8 5 SER H 35 GLN H 42 -1 N ARG H 41 O GLU H 49 SHEET 4 AA8 5 ALA H 95 ARG H 103 -1 O TYR H 98 N VAL H 40 SHEET 5 AA8 5 THR H 117 VAL H 119 -1 O VAL H 119 N ALA H 95 SHEET 1 AA9 4 SER H 130 PRO H 133 0 SHEET 2 AA9 4 GLY H 149 LYS H 153 -1 O LYS H 153 N SER H 130 SHEET 3 AA9 4 TYR H 186 VAL H 192 -1 O LEU H 188 N VAL H 152 SHEET 4 AA9 4 VAL H 173 LEU H 180 -1 N VAL H 179 O SER H 187 SHEET 1 AB1 3 VAL H 160 TRP H 164 0 SHEET 2 AB1 3 CYS H 206 HIS H 210 -1 O ASN H 207 N SER H 163 SHEET 3 AB1 3 THR H 215 LYS H 219 -1 O LYS H 219 N CYS H 206 SHEET 1 AB2 4 MET L 5 SER L 8 0 SHEET 2 AB2 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AB2 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AB2 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AB3 6 SER L 11 ALA L 14 0 SHEET 2 AB3 6 THR L 103 ILE L 107 1 O GLU L 106 N ALA L 14 SHEET 3 AB3 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AB3 6 VAL L 34 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AB3 6 LYS L 46 TYR L 50 -1 O LYS L 46 N GLN L 38 SHEET 6 AB3 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AB4 4 SER L 115 PHE L 119 0 SHEET 2 AB4 4 VAL L 133 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AB4 4 TYR L 174 LEU L 180 -1 O TYR L 174 N PHE L 140 SHEET 4 AB4 4 GLN L 161 VAL L 164 -1 N GLN L 161 O THR L 179 SSBOND 1 CYS R 140 CYS R 217 1555 1555 2.03 SSBOND 2 CYS H 25 CYS H 99 1555 1555 2.03 SSBOND 3 CYS L 24 CYS L 89 1555 1555 2.04 LINK C GLU R 363 N SEP R 364 1555 1555 1.33 LINK C SEP R 364 N CYS R 365 1555 1555 1.33 LINK C CYS R 365 N TPO R 366 1555 1555 1.33 LINK C TPO R 366 N TPO R 367 1555 1555 1.33 LINK C TPO R 367 N ALA R 368 1555 1555 1.33 LINK C ALA R 368 N SEP R 369 1555 1555 1.33 LINK C SEP R 369 N SEP R 370 1555 1555 1.33 LINK C SEP R 370 N SEP R 371 1555 1555 1.33 LINK C SEP R 371 N LEU R 372 1555 1555 1.33 LINK C TYR P 1 N DAL P 2 1555 1555 1.47 LINK C DAL P 2 N GLY P 3 1555 1555 1.38 LINK C GLY P 3 N MEA P 4 1555 1555 1.53 LINK C MEA P 4 N ETA P 5 1555 1555 1.50 CISPEP 1 PHE C 87 PRO C 88 0 0.97 CISPEP 2 PHE H 156 PRO H 157 0 -0.99 CISPEP 3 GLU H 158 PRO H 159 0 -3.60 CISPEP 4 SER L 8 PRO L 9 0 -6.28 CISPEP 5 VAL L 95 PRO L 96 0 1.17 CISPEP 6 TYR L 141 PRO L 142 0 0.02 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