HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 25-JUN-24 9IJS TITLE CRYO-EM STRUCTURE OF THE ORPHAN GPR52 BOUND TO BETA-ARRESTIN 1 IN TITLE 2 LIGAND-FREE STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: G-PROTEIN COUPLED RECEPTOR 52; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BETA-ARRESTIN-1; COMPND 7 CHAIN: C; COMPND 8 SYNONYM: ARRESTIN BETA-1,NON-VISUAL ARRESTIN-2; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: SCFV30 ANTIBODY; COMPND 12 CHAIN: H; COMPND 13 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: GPR52; 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: ARRB1, ARR1; 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: SPODOPTERA FRUGIPERDA; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS COMPLEX, MEMBRANE PROTEIN, GPCR, ARRESTIN, MEMBRANE PROTEIN/IMMUNE KEYWDS 2 SYSTEM, MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR X.LIN,F.XU REVDAT 1 03-SEP-25 9IJS 0 JRNL AUTH X.LIN,X.WEI,N.PU,L.WANG,Z.ZHANG,C.LI,Y.YUE,J.LIU,Q.TAN, JRNL AUTH 2 Q.SUN,F.XU JRNL TITL CONSTITUTIVE ARRESTIN RECRUITMENT BY ORPHAN GPR52 VIA AN JRNL TITL 2 ATYPICAL BINDING MODE. JRNL REF CELL RES. 2025 JRNL REFN ISSN 1001-0602 JRNL PMID 40813798 JRNL DOI 10.1038/S41422-025-01165-W REMARK 2 REMARK 2 RESOLUTION. 3.64 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 3.640 REMARK 3 NUMBER OF PARTICLES : 136991 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9IJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 27-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1300048899. 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 : THE COMPLEX OF GPCR WITH REMARK 245 ARRESTIN 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 : 7.50 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 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : OTHER REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, H 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 ASN A 2 REMARK 465 GLU A 3 REMARK 465 SER A 4 REMARK 465 ARG A 5 REMARK 465 TRP A 6 REMARK 465 THR A 7 REMARK 465 GLU A 8 REMARK 465 TRP A 9 REMARK 465 ARG A 10 REMARK 465 ILE A 11 REMARK 465 LEU A 12 REMARK 465 ASN A 13 REMARK 465 MET A 14 REMARK 465 SER A 15 REMARK 465 SER A 16 REMARK 465 GLY A 17 REMARK 465 ILE A 18 REMARK 465 VAL A 19 REMARK 465 ASN A 20 REMARK 465 VAL A 21 REMARK 465 SER A 22 REMARK 465 GLU A 23 REMARK 465 ARG A 24 REMARK 465 HIS A 25 REMARK 465 SER A 26 REMARK 465 CYS A 27 REMARK 465 PRO A 28 REMARK 465 LEU A 29 REMARK 465 GLY A 30 REMARK 465 PHE A 31 REMARK 465 GLY A 32 REMARK 465 HIS A 33 REMARK 465 TYR A 34 REMARK 465 SER A 35 REMARK 465 VAL A 36 REMARK 465 VAL A 37 REMARK 465 ASP A 38 REMARK 465 VAL A 39 REMARK 465 CYS A 40 REMARK 465 ILE A 41 REMARK 465 LYS A 235 REMARK 465 GLU A 236 REMARK 465 ILE A 237 REMARK 465 ASN A 238 REMARK 465 ASP A 239 REMARK 465 ARG A 240 REMARK 465 ARG A 241 REMARK 465 ALA A 242 REMARK 465 ARG A 243 REMARK 465 PHE A 244 REMARK 465 PRO A 245 REMARK 465 SER A 246 REMARK 465 HIS A 247 REMARK 465 GLU A 248 REMARK 465 VAL A 249 REMARK 465 ASP A 250 REMARK 465 SER A 251 REMARK 465 SER A 252 REMARK 465 ARG A 253 REMARK 465 GLU A 254 REMARK 465 THR A 255 REMARK 465 GLY A 256 REMARK 465 HIS A 257 REMARK 465 SER A 258 REMARK 465 PRO A 259 REMARK 465 ASP A 260 REMARK 465 MET A 468 REMARK 465 CYS A 469 REMARK 465 THR A 470 REMARK 465 SER A 471 REMARK 465 CYS A 472 REMARK 465 MET A 473 REMARK 465 ALA A 474 REMARK 465 ARG A 475 REMARK 465 GLY A 476 REMARK 465 ARG A 477 REMARK 465 PRO A 478 REMARK 465 LEU A 479 REMARK 465 PRO A 480 REMARK 465 GLU A 481 REMARK 465 THR A 482 REMARK 465 GLY A 483 REMARK 465 GLY A 484 REMARK 465 GLY A 485 REMARK 465 ASP A 486 REMARK 465 THR A 500 REMARK 465 SER A 501 REMARK 465 SER A 502 REMARK 465 MET C -8 REMARK 465 GLY C -7 REMARK 465 SER C -6 REMARK 465 PRO C -5 REMARK 465 GLU C -4 REMARK 465 PHE C -3 REMARK 465 PRO C -2 REMARK 465 GLY C -1 REMARK 465 ARG C 0 REMARK 465 LEU C 1 REMARK 465 GLY C 2 REMARK 465 ASP C 3 REMARK 465 LYS C 4 REMARK 465 GLY C 5 REMARK 465 LYS C 357 REMARK 465 GLU C 358 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 SER 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 ILE C 386 REMARK 465 VAL C 387 REMARK 465 PHE 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 -16 REMARK 465 VAL H -15 REMARK 465 SER H -14 REMARK 465 ALA H -13 REMARK 465 ILE H -12 REMARK 465 VAL H -11 REMARK 465 LEU H -10 REMARK 465 TYR H -9 REMARK 465 VAL H -8 REMARK 465 LEU H -7 REMARK 465 LEU H -6 REMARK 465 ALA H -5 REMARK 465 ALA H -4 REMARK 465 ALA H -3 REMARK 465 ALA H -2 REMARK 465 HIS H -1 REMARK 465 SER H 0 REMARK 465 ALA H 1 REMARK 465 PHE H 2 REMARK 465 ALA H 3 REMARK 465 ASP H 4 REMARK 465 SER H 123 REMARK 465 SER H 124 REMARK 465 GLY H 125 REMARK 465 GLY H 126 REMARK 465 GLY H 127 REMARK 465 GLY H 128 REMARK 465 SER H 129 REMARK 465 GLY H 130 REMARK 465 GLY H 131 REMARK 465 GLY H 132 REMARK 465 GLY H 133 REMARK 465 SER H 134 REMARK 465 GLY H 135 REMARK 465 GLY H 136 REMARK 465 GLY H 137 REMARK 465 GLY H 138 REMARK 465 LYS H 246 REMARK 465 ALA H 247 REMARK 465 ALA H 248 REMARK 465 ALA H 249 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 VAL A 45 CG1 CG2 REMARK 470 LEU A 49 CG CD1 CD2 REMARK 470 LEU A 50 CG CD1 CD2 REMARK 470 PHE A 52 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 53 CG CD1 CD2 REMARK 470 ILE A 54 CG1 CG2 CD1 REMARK 470 TYR A 74 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 95 CG CD1 CD2 REMARK 470 LEU A 99 CG CD1 CD2 REMARK 470 HIS A 103 CG ND1 CD2 CE1 NE2 REMARK 470 HIS A 109 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 112 CG CD1 CD2 REMARK 470 GLN A 115 CG CD OE1 NE2 REMARK 470 ASN A 150 CG OD1 ND2 REMARK 470 GLN A 151 CG CD OE1 NE2 REMARK 470 PRO A 155 CG CD REMARK 470 ILE A 160 CG1 CG2 CD1 REMARK 470 LEU A 164 CG CD1 CD2 REMARK 470 CYS A 170 SG REMARK 470 PHE A 177 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 191 CG CD OE1 OE2 REMARK 470 LEU A 198 CG CD1 CD2 REMARK 470 CYS A 209 SG REMARK 470 PHE A 224 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE A 227 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 228 CG CD CE NZ REMARK 470 GLN A 232 CG CD OE1 NE2 REMARK 470 HIS A 233 CG ND1 CD2 CE1 NE2 REMARK 470 ARG A 261 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 262 CG CD NE CZ NH1 NH2 REMARK 470 MET A 265 CG SD CE REMARK 470 ARG A 269 CG CD NE CZ NH1 NH2 REMARK 470 MET A 276 CG SD CE REMARK 470 LEU A 279 CG CD1 CD2 REMARK 470 LEU A 286 CG CD1 CD2 REMARK 470 LEU A 287 CG CD1 CD2 REMARK 470 LEU A 293 CG CD1 CD2 REMARK 470 ASP A 294 CG OD1 OD2 REMARK 470 THR A 297 OG1 CG2 REMARK 470 LEU A 305 CG CD1 CD2 REMARK 470 PHE A 311 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL A 315 CG1 CG2 REMARK 470 LEU A 319 CG CD1 CD2 REMARK 470 SER A 322 OG REMARK 470 VAL A 323 CG1 CG2 REMARK 470 PHE A 324 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 326 CG CD1 CD2 REMARK 470 ARG A 329 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 330 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 331 CG CD1 CD2 REMARK 470 GLU A 333 CG CD OE1 OE2 REMARK 470 GLU A 487 CG CD OE1 OE2 REMARK 470 LYS A 498 CG CD CE NZ REMARK 470 ARG C 7 CG CD NE CZ NH1 NH2 REMARK 470 SER C 13 OG REMARK 470 ASN C 15 CG OD1 ND2 REMARK 470 LYS C 24 CG CD CE NZ REMARK 470 ILE C 31 CG1 CG2 CD1 REMARK 470 ASP C 32 CG OD1 OD2 REMARK 470 ASP C 35 CG OD1 OD2 REMARK 470 LEU C 42 CG CD1 CD2 REMARK 470 ASP C 44 CG OD1 OD2 REMARK 470 PRO C 45 CG CD REMARK 470 GLU C 46 CG CD OE1 OE2 REMARK 470 LEU C 48 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 51 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 52 CG CD NE CZ NH1 NH2 REMARK 470 VAL C 53 CG1 CG2 REMARK 470 ARG C 65 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 66 CG CD OE1 OE2 REMARK 470 ASP C 67 CG OD1 OD2 REMARK 470 LEU C 68 CG CD1 CD2 REMARK 470 ASP C 69 CG OD1 OD2 REMARK 470 VAL C 70 CG1 CG2 REMARK 470 LEU C 71 CG CD1 CD2 REMARK 470 LEU C 73 CG CD1 CD2 REMARK 470 THR C 74 OG1 CG2 REMARK 470 GLN C 85 CG CD OE1 NE2 REMARK 470 PHE C 87 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO C 88 CG CD REMARK 470 PRO C 89 CG CD REMARK 470 PRO C 91 CG CD REMARK 470 GLU C 92 CG CD OE1 OE2 REMARK 470 ASP C 93 CG OD1 OD2 REMARK 470 LYS C 94 CG CD CE NZ REMARK 470 LYS C 95 CG CD CE NZ REMARK 470 GLN C 101 CG CD OE1 NE2 REMARK 470 GLU C 102 CG CD OE1 OE2 REMARK 470 ARG C 103 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 106 CG CD CE NZ REMARK 470 GLU C 110 CG CD OE1 OE2 REMARK 470 TYR C 113 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU C 118 CG CD OE1 OE2 REMARK 470 GLU C 134 CG CD OE1 OE2 REMARK 470 ASP C 135 CG OD1 OD2 REMARK 470 THR C 136 OG1 CG2 REMARK 470 LYS C 138 CG CD CE NZ REMARK 470 GLU C 145 CG CD OE1 OE2 REMARK 470 LYS C 147 CG CD CE NZ REMARK 470 GLU C 152 CG CD OE1 OE2 REMARK 470 ASN C 153 CG OD1 ND2 REMARK 470 GLU C 155 CG CD OE1 OE2 REMARK 470 GLU C 156 CG CD OE1 OE2 REMARK 470 LYS C 157 CG CD CE NZ REMARK 470 ILE C 158 CG1 CG2 CD1 REMARK 470 HIS C 159 CG ND1 CD2 CE1 NE2 REMARK 470 ARG C 161 CG CD NE CZ NH1 NH2 REMARK 470 PRO C 175 CG CD REMARK 470 GLU C 176 CG CD OE1 OE2 REMARK 470 ARG C 177 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 185 CG CD OE1 OE2 REMARK 470 ARG C 188 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 189 CG CD OE1 NE2 REMARK 470 LEU C 191 CG CD1 CD2 REMARK 470 MET C 192 CG SD CE REMARK 470 SER C 193 OG REMARK 470 ASP C 194 CG OD1 OD2 REMARK 470 LYS C 195 CG CD CE NZ REMARK 470 GLU C 200 CG CD OE1 OE2 REMARK 470 ASP C 204 CG OD1 OD2 REMARK 470 GLU C 212 CG CD OE1 OE2 REMARK 470 ASN C 217 CG OD1 ND2 REMARK 470 HIS C 219 CG ND1 CD2 CE1 NE2 REMARK 470 ASN C 225 CG OD1 ND2 REMARK 470 LYS C 226 CG CD CE NZ REMARK 470 ASP C 240 CG OD1 OD2 REMARK 470 LYS C 250 CG CD CE NZ REMARK 470 MET C 255 CG SD CE REMARK 470 ASP C 259 CG OD1 OD2 REMARK 470 ASP C 260 CG OD1 OD2 REMARK 470 GLU C 296 CG CD OE1 OE2 REMARK 470 GLU C 308 CG CD OE1 OE2 REMARK 470 ASN C 311 CG OD1 ND2 REMARK 470 ARG C 312 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 313 CG CD OE1 OE2 REMARK 470 ARG C 331 CG CD NE CZ NH1 NH2 REMARK 470 LEU C 334 CG CD1 CD2 REMARK 470 LEU C 335 CG CD1 CD2 REMARK 470 ASP C 337 CG OD1 OD2 REMARK 470 LEU C 338 CG CD1 CD2 REMARK 470 SER C 340 OG REMARK 470 SER C 341 OG REMARK 470 LYS C 355 CG CD CE NZ REMARK 470 GLU H 9 CG CD OE1 OE2 REMARK 470 GLN H 16 CG CD OE1 NE2 REMARK 470 PRO H 17 CG CD REMARK 470 ARG H 22 CG CD NE CZ NH1 NH2 REMARK 470 LEU H 23 CG CD1 CD2 REMARK 470 ARG H 41 CG CD NE CZ NH1 NH2 REMARK 470 PRO H 44 CG CD REMARK 470 LYS H 46 CG CD CE NZ REMARK 470 GLU H 49 CG CD OE1 OE2 REMARK 470 ASP H 65 CG OD1 OD2 REMARK 470 LYS H 68 CG CD CE NZ REMARK 470 ARG H 70 CG CD NE CZ NH1 NH2 REMARK 470 THR H 72 OG1 CG2 REMARK 470 THR H 77 OG1 CG2 REMARK 470 LYS H 79 CG CD CE NZ REMARK 470 ASN H 80 CG OD1 ND2 REMARK 470 TYR H 83 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN H 85 CG CD OE1 NE2 REMARK 470 MET H 86 CG SD CE REMARK 470 ASN H 87 CG OD1 ND2 REMARK 470 LEU H 89 CG CD1 CD2 REMARK 470 ARG H 90 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 92 CG CD OE1 OE2 REMARK 470 ASP H 93 CG OD1 OD2 REMARK 470 THR H 94 OG1 CG2 REMARK 470 GLN H 104 CG CD OE1 NE2 REMARK 470 ASP H 111 CG OD1 OD2 REMARK 470 LEU H 118 CG CD1 CD2 REMARK 470 THR H 120 OG1 CG2 REMARK 470 SER H 122 OG REMARK 470 GLN H 142 CG CD OE1 NE2 REMARK 470 MET H 143 CG SD CE REMARK 470 GLN H 145 CG CD OE1 NE2 REMARK 470 SER H 151 OG REMARK 470 ASP H 156 CG OD1 OD2 REMARK 470 THR H 159 OG1 CG2 REMARK 470 ARG H 163 CG CD NE CZ NH1 NH2 REMARK 470 PRO H 179 CG CD REMARK 470 LYS H 181 CG CD CE NZ REMARK 470 SER H 191 OG REMARK 470 SER H 192 OG REMARK 470 LEU H 193 CG CD1 CD2 REMARK 470 THR H 208 OG1 CG2 REMARK 470 ASP H 209 CG OD1 OD2 REMARK 470 LEU H 217 CG CD1 CD2 REMARK 470 PRO H 219 CG CD REMARK 470 GLU H 220 CG CD OE1 OE2 REMARK 470 PHE H 222 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR H 225 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN H 239 CG CD OE1 NE2 REMARK 470 LYS H 242 CG CD CE NZ REMARK 470 GLU H 244 CG CD OE1 OE2 REMARK 470 ILE H 245 CG1 CG2 CD1 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 HIS A 72 108.66 -58.16 REMARK 500 THR A 76 48.28 -93.10 REMARK 500 LEU A 152 -30.97 -130.07 REMARK 500 SEP A 494 -132.36 -153.56 REMARK 500 ASP C 44 109.51 -58.69 REMARK 500 ARG C 65 -151.25 57.98 REMARK 500 THR C 74 -0.49 64.78 REMARK 500 PHE C 75 46.92 37.46 REMARK 500 PRO C 89 48.41 -78.73 REMARK 500 ALA C 90 71.39 52.73 REMARK 500 LEU C 140 -169.48 -79.87 REMARK 500 ASP C 259 51.84 -92.38 REMARK 500 SER H 74 117.62 -160.82 REMARK 500 TYR H 107 127.68 -39.89 REMARK 500 SER H 169 43.39 -108.57 REMARK 500 SER H 189 19.56 58.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60643 RELATED DB: EMDB REMARK 900 CLASSA GPCR IN COMPLEX WITH ARRESTIN DBREF 9IJS A 1 473 UNP Q9Y2T5 GPR52_HUMAN 1 340 DBREF 9IJS C 2 393 UNP P49407 ARRB1_HUMAN 2 393 DBREF 9IJS H -16 249 PDB 9IJS 9IJS -16 249 SEQADV 9IJS TRP A 130 UNP Q9Y2T5 ALA 130 CONFLICT SEQADV 9IJS PRO A 314 UNP Q9Y2T5 CYS 314 CONFLICT SEQADV 9IJS ALA A 474 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS ARG A 475 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS GLY A 476 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS ARG A 477 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS PRO A 478 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS LEU A 479 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS PRO A 480 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS GLU A 481 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS THR A 482 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS GLY A 483 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS GLY A 484 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS GLY A 485 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS ASP A 486 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS GLU A 487 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS SEP A 488 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS ALA A 489 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS TPO A 490 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS TPO A 491 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS ALA A 492 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS SEP A 493 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS SEP A 494 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS SEP A 495 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS LEU A 496 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS ALA A 497 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS LYS A 498 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS ASP A 499 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS THR A 500 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS SER A 501 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS SER A 502 UNP Q9Y2T5 EXPRESSION TAG SEQADV 9IJS MET C -8 UNP P49407 INITIATING METHIONINE SEQADV 9IJS GLY C -7 UNP P49407 EXPRESSION TAG SEQADV 9IJS SER C -6 UNP P49407 EXPRESSION TAG SEQADV 9IJS PRO C -5 UNP P49407 EXPRESSION TAG SEQADV 9IJS GLU C -4 UNP P49407 EXPRESSION TAG SEQADV 9IJS PHE C -3 UNP P49407 EXPRESSION TAG SEQADV 9IJS PRO C -2 UNP P49407 EXPRESSION TAG SEQADV 9IJS GLY C -1 UNP P49407 EXPRESSION TAG SEQADV 9IJS ARG C 0 UNP P49407 EXPRESSION TAG SEQADV 9IJS LEU C 1 UNP P49407 EXPRESSION TAG SEQADV 9IJS VAL C 59 UNP P49407 CYS 59 CONFLICT SEQADV 9IJS SER C 125 UNP P49407 CYS 125 CONFLICT SEQADV 9IJS LEU C 140 UNP P49407 CYS 140 CONFLICT SEQADV 9IJS VAL C 150 UNP P49407 CYS 150 CONFLICT SEQADV 9IJS VAL C 242 UNP P49407 CYS 242 CONFLICT SEQADV 9IJS VAL C 251 UNP P49407 CYS 251 CONFLICT SEQADV 9IJS SER C 269 UNP P49407 CYS 269 CONFLICT SEQADV 9IJS SER C 368 UNP P49407 ASN 368 CONFLICT SEQRES 1 A 369 MET ASN GLU SER ARG TRP THR GLU TRP ARG ILE LEU ASN SEQRES 2 A 369 MET SER SER GLY ILE VAL ASN VAL SER GLU ARG HIS SER SEQRES 3 A 369 CYS PRO LEU GLY PHE GLY HIS TYR SER VAL VAL ASP VAL SEQRES 4 A 369 CYS ILE PHE GLU THR VAL VAL ILE VAL LEU LEU THR PHE SEQRES 5 A 369 LEU ILE ILE ALA GLY ASN LEU THR VAL ILE PHE VAL PHE SEQRES 6 A 369 HIS CYS ALA PRO LEU LEU HIS HIS TYR THR THR SER TYR SEQRES 7 A 369 PHE ILE GLN THR MET ALA TYR ALA ASP LEU PHE VAL GLY SEQRES 8 A 369 VAL SER CYS LEU VAL PRO THR LEU SER LEU LEU HIS TYR SEQRES 9 A 369 SER THR GLY VAL HIS GLU SER LEU THR CYS GLN VAL PHE SEQRES 10 A 369 GLY TYR ILE ILE SER VAL LEU LYS SER VAL SER MET TRP SEQRES 11 A 369 CYS LEU ALA CYS ILE SER VAL ASP ARG TYR LEU ALA ILE SEQRES 12 A 369 THR LYS PRO LEU SER TYR ASN GLN LEU VAL THR PRO CYS SEQRES 13 A 369 ARG LEU ARG ILE CYS ILE ILE LEU ILE TRP ILE TYR SER SEQRES 14 A 369 CYS LEU ILE PHE LEU PRO SER PHE PHE GLY TRP GLY LYS SEQRES 15 A 369 PRO GLY TYR HIS GLY ASP ILE PHE GLU TRP CYS ALA THR SEQRES 16 A 369 SER TRP LEU THR SER ALA TYR PHE THR GLY PHE ILE VAL SEQRES 17 A 369 CYS LEU LEU TYR ALA PRO ALA ALA PHE VAL VAL CYS PHE SEQRES 18 A 369 THR TYR PHE HIS ILE PHE LYS ILE CYS ARG GLN HIS THR SEQRES 19 A 369 LYS GLU ILE ASN ASP ARG ARG ALA ARG PHE PRO SER HIS SEQRES 20 A 369 GLU VAL ASP SER SER ARG GLU THR GLY HIS SER PRO ASP SEQRES 21 A 369 ARG ARG TYR ALA MET VAL LEU PHE ARG ILE THR SER VAL SEQRES 22 A 369 PHE TYR MET LEU TRP LEU PRO TYR ILE ILE TYR PHE LEU SEQRES 23 A 369 LEU GLU SER SER ARG VAL LEU ASP ASN PRO THR LEU SER SEQRES 24 A 369 PHE LEU THR THR TRP LEU ALA ILE SER ASN SER PHE CYS SEQRES 25 A 369 ASN PRO VAL ILE TYR SER LEU SER ASN SER VAL PHE ARG SEQRES 26 A 369 LEU GLY LEU ARG ARG LEU SER GLU THR MET CYS THR SER SEQRES 27 A 369 CYS MET ALA ARG GLY ARG PRO LEU PRO GLU THR GLY GLY SEQRES 28 A 369 GLY ASP GLU SEP ALA TPO TPO ALA SEP SEP SEP LEU ALA SEQRES 29 A 369 LYS ASP THR SER SER SEQRES 1 C 402 MET GLY SER PRO GLU PHE PRO GLY ARG LEU GLY ASP LYS SEQRES 2 C 402 GLY THR ARG VAL PHE LYS LYS ALA SER PRO ASN GLY LYS SEQRES 3 C 402 LEU THR VAL TYR LEU GLY LYS ARG ASP PHE VAL ASP HIS SEQRES 4 C 402 ILE ASP LEU VAL ASP PRO VAL ASP GLY VAL VAL LEU VAL SEQRES 5 C 402 ASP PRO GLU TYR LEU LYS GLU ARG ARG VAL TYR VAL THR SEQRES 6 C 402 LEU THR VAL ALA PHE ARG TYR GLY ARG GLU ASP LEU ASP SEQRES 7 C 402 VAL LEU GLY LEU THR PHE ARG LYS ASP LEU PHE VAL ALA SEQRES 8 C 402 ASN VAL GLN SER PHE PRO PRO ALA PRO GLU ASP LYS LYS SEQRES 9 C 402 PRO LEU THR ARG LEU GLN GLU ARG LEU ILE LYS LYS LEU SEQRES 10 C 402 GLY GLU HIS ALA TYR PRO PHE THR PHE GLU ILE PRO PRO SEQRES 11 C 402 ASN LEU PRO SER SER VAL THR LEU GLN PRO GLY PRO GLU SEQRES 12 C 402 ASP THR GLY LYS ALA LEU GLY VAL ASP TYR GLU VAL LYS SEQRES 13 C 402 ALA PHE VAL ALA GLU ASN LEU GLU GLU LYS ILE HIS LYS SEQRES 14 C 402 ARG ASN SER VAL ARG LEU VAL ILE ARG LYS VAL GLN TYR SEQRES 15 C 402 ALA PRO GLU ARG PRO GLY PRO GLN PRO THR ALA GLU THR SEQRES 16 C 402 THR ARG GLN PHE LEU MET SER ASP LYS PRO LEU HIS LEU SEQRES 17 C 402 GLU ALA SER LEU ASP LYS GLU ILE TYR TYR HIS GLY GLU SEQRES 18 C 402 PRO ILE SER VAL ASN VAL HIS VAL THR ASN ASN THR ASN SEQRES 19 C 402 LYS THR VAL LYS LYS ILE LYS ILE SER VAL ARG GLN TYR SEQRES 20 C 402 ALA ASP ILE VAL LEU PHE ASN THR ALA GLN TYR LYS VAL SEQRES 21 C 402 PRO VAL ALA MET GLU GLU ALA ASP ASP THR VAL ALA PRO SEQRES 22 C 402 SER SER THR PHE SER LYS VAL TYR THR LEU THR PRO PHE SEQRES 23 C 402 LEU ALA ASN ASN ARG GLU LYS ARG GLY LEU ALA LEU ASP SEQRES 24 C 402 GLY LYS LEU LYS HIS GLU ASP THR ASN LEU ALA SER SER SEQRES 25 C 402 THR LEU LEU ARG GLU GLY ALA ASN ARG GLU ILE LEU GLY SEQRES 26 C 402 ILE ILE VAL SER TYR LYS VAL LYS VAL LYS LEU VAL VAL SEQRES 27 C 402 SER ARG GLY GLY LEU LEU GLY ASP LEU ALA SER SER ASP SEQRES 28 C 402 VAL ALA VAL GLU LEU PRO PHE THR LEU MET HIS PRO LYS SEQRES 29 C 402 PRO LYS GLU GLU PRO PRO HIS ARG GLU VAL PRO GLU SER SEQRES 30 C 402 GLU THR PRO VAL ASP THR ASN LEU ILE GLU LEU ASP THR SEQRES 31 C 402 ASN ASP ASP ASP ILE VAL PHE GLU ASP PHE ALA ARG SEQRES 1 H 266 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA SEQRES 2 H 266 ALA ALA HIS SER ALA PHE ALA ASP VAL GLN LEU VAL GLU SEQRES 3 H 266 SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU ARG SEQRES 4 H 266 LEU SER CYS ALA ALA SER GLY PHE ASN VAL TYR SER SER SEQRES 5 H 266 SER ILE HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU SEQRES 6 H 266 GLU TRP VAL ALA SER ILE SER SER TYR TYR GLY TYR THR SEQRES 7 H 266 TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER SEQRES 8 H 266 ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN MET ASN SEQRES 9 H 266 SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS ALA SEQRES 10 H 266 ARG SER ARG GLN PHE TRP TYR SER GLY LEU ASP TYR TRP SEQRES 11 H 266 GLY GLN GLY THR LEU VAL THR VAL SER SER SER GLY GLY SEQRES 12 H 266 GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 13 H 266 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 14 H 266 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 15 H 266 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 16 H 266 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 17 H 266 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 18 H 266 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 19 H 266 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 20 H 266 LYS TYR VAL PRO VAL THR PHE GLY GLN GLY THR LYS VAL SEQRES 21 H 266 GLU ILE LYS ALA ALA ALA HET SEP A 488 10 HET TPO A 490 11 HET TPO A 491 11 HET SEP A 493 10 HET SEP A 494 10 HET SEP A 495 10 HETNAM SEP PHOSPHOSERINE HETNAM TPO PHOSPHOTHREONINE HETSYN SEP PHOSPHONOSERINE HETSYN TPO PHOSPHONOTHREONINE FORMUL 1 SEP 4(C3 H8 N O6 P) FORMUL 1 TPO 2(C4 H10 N O6 P) HELIX 1 AA1 PHE A 42 ALA A 68 1 27 HELIX 2 AA2 TYR A 74 TYR A 104 1 31 HELIX 3 AA3 GLU A 110 THR A 144 1 35 HELIX 4 AA4 THR A 154 GLY A 179 1 26 HELIX 5 AA5 GLY A 184 ASP A 188 5 5 HELIX 6 AA6 GLU A 191 SER A 196 1 6 HELIX 7 AA7 SER A 200 LEU A 211 1 12 HELIX 8 AA8 LEU A 211 ILE A 229 1 19 HELIX 9 AA9 ARG A 262 SER A 290 1 29 HELIX 10 AB1 ASN A 295 ASN A 321 1 27 HELIX 11 AB2 ASN A 321 THR A 334 1 14 HELIX 12 AB3 THR C 98 LEU C 108 1 11 HELIX 13 AB4 HIS C 159 ARG C 161 5 3 HELIX 14 AB5 ASN H 31 TYR H 33 5 3 HELIX 15 AB6 ARG H 90 THR H 94 5 5 SHEET 1 AA1 5 ALA A 492 SEP A 493 0 SHEET 2 AA1 5 PHE C 9 LYS C 10 -1 O LYS C 10 N ALA A 492 SHEET 3 AA1 5 LEU C 18 LEU C 22 -1 O LEU C 22 N PHE C 9 SHEET 4 AA1 5 ASP C 38 VAL C 43 -1 O VAL C 40 N TYR C 21 SHEET 5 AA1 5 TYR C 113 THR C 116 -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 VAL C 171 N PHE C 27 SHEET 3 AA2 5 GLY C 141 VAL C 150 -1 N VAL C 146 O LEU C 166 SHEET 4 AA2 5 VAL C 53 ARG C 62 -1 N TYR C 54 O PHE C 149 SHEET 5 AA2 5 ASP C 78 PHE C 87 -1 O LEU C 79 N VAL C 59 SHEET 1 AA3 2 VAL C 127 LEU C 129 0 SHEET 2 AA3 2 ALA C 288 ASP C 290 -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 SER C 202 -1 O ALA C 201 N ALA C 184 SHEET 3 AA4 4 ILE C 214 ASN C 222 -1 O ASN C 217 N SER C 202 SHEET 4 AA4 4 SER C 266 LEU C 274 -1 O LEU C 274 N ILE C 214 SHEET 1 AA5 5 ILE C 207 TYR C 208 0 SHEET 2 AA5 5 ASP C 342 LEU C 351 1 O THR C 350 N TYR C 208 SHEET 3 AA5 5 ILE C 317 VAL C 329 -1 N TYR C 321 O PHE C 349 SHEET 4 AA5 5 VAL C 228 ILE C 241 -1 N LYS C 232 O LYS C 326 SHEET 5 AA5 5 ALA C 247 GLN C 248 -1 N ALA C 247 O ILE C 241 SHEET 1 AA6 5 ILE C 207 TYR C 208 0 SHEET 2 AA6 5 ASP C 342 LEU C 351 1 O THR C 350 N TYR C 208 SHEET 3 AA6 5 ILE C 317 VAL C 329 -1 N TYR C 321 O PHE C 349 SHEET 4 AA6 5 VAL C 228 ILE C 241 -1 N LYS C 232 O LYS C 326 SHEET 5 AA6 5 VAL C 251 ALA C 258 -1 O GLU C 256 N ILE C 233 SHEET 1 AA7 4 LEU H 7 GLU H 9 0 SHEET 2 AA7 4 ARG H 22 ALA H 27 -1 O ALA H 26 N VAL H 8 SHEET 3 AA7 4 THR H 81 GLN H 85 -1 O LEU H 84 N LEU H 23 SHEET 4 AA7 4 THR H 72 ASP H 76 -1 N SER H 74 O TYR H 83 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 VAL H 96 ARG H 103 -1 O ALA H 100 N HIS H 38 SHEET 5 AA8 5 LEU H 110 TRP H 113 -1 O TYR H 112 N ARG H 101 SHEET 1 AA9 5 TYR H 60 TYR H 63 0 SHEET 2 AA9 5 LEU H 48 SER H 55 -1 N SER H 53 O TYR H 62 SHEET 3 AA9 5 SER H 35 GLN H 42 -1 N ARG H 41 O GLU H 49 SHEET 4 AA9 5 VAL H 96 ARG H 103 -1 O ALA H 100 N HIS H 38 SHEET 5 AA9 5 THR H 117 LEU H 118 -1 O THR H 117 N TYR H 97 SHEET 1 AB1 4 THR H 144 SER H 146 0 SHEET 2 AB1 4 VAL H 158 ARG H 163 -1 O ARG H 163 N THR H 144 SHEET 3 AB1 4 ASP H 209 ILE H 214 -1 O PHE H 210 N CYS H 162 SHEET 4 AB1 4 SER H 204 SER H 206 -1 N SER H 204 O THR H 211 SHEET 1 AB2 2 SER H 149 SER H 151 0 SHEET 2 AB2 2 LYS H 242 GLU H 244 1 O GLU H 244 N LEU H 150 SHEET 1 AB3 5 SER H 192 LEU H 193 0 SHEET 2 AB3 5 LYS H 184 TYR H 188 -1 N TYR H 188 O SER H 192 SHEET 3 AB3 5 VAL H 172 GLN H 177 -1 N GLN H 176 O LYS H 184 SHEET 4 AB3 5 THR H 224 GLN H 229 -1 O THR H 224 N GLN H 177 SHEET 5 AB3 5 THR H 236 PHE H 237 -1 O THR H 236 N GLN H 229 SSBOND 1 CYS A 114 CYS A 193 1555 1555 2.03 SSBOND 2 CYS H 25 CYS H 99 1555 1555 2.03 SSBOND 3 CYS H 162 CYS H 227 1555 1555 2.03 LINK C GLU A 487 N SEP A 488 1555 1555 1.33 LINK C SEP A 488 N ALA A 489 1555 1555 1.33 LINK C ALA A 489 N TPO A 490 1555 1555 1.33 LINK C TPO A 490 N TPO A 491 1555 1555 1.33 LINK C TPO A 491 N ALA A 492 1555 1555 1.33 LINK C ALA A 492 N SEP A 493 1555 1555 1.33 LINK C SEP A 493 N SEP A 494 1555 1555 1.33 LINK C SEP A 494 N SEP A 495 1555 1555 1.33 LINK C SEP A 495 N LEU A 496 1555 1555 1.33 CISPEP 1 PHE C 87 PRO C 88 0 0.93 CISPEP 2 SER H 146 PRO H 147 0 1.29 CISPEP 3 VAL H 233 PRO H 234 0 0.21 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