HEADER MEMBRANE PROTEIN 01-JUL-23 8JXS TITLE STRUCTURE OF NANOBODY-BOUND DRD1_PF-6142 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: D(1A) DOPAMINE RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: DOPAMINE D1 RECEPTOR; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NBA3; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: MALTOSE/MALTODEXTRIN-BINDING PERIPLASMIC PROTEIN, COMPND 13 IMMUNOGLOBULIN G-BINDING PROTEIN A,IMMUNOGLOBULIN G-BINDING PROTEIN COMPND 14 G; COMPND 15 CHAIN: C; COMPND 16 SYNONYM: IGG-BINDING PROTEIN A,STAPHYLOCOCCAL PROTEIN A,SPA,IGG- COMPND 17 BINDING PROTEIN G; COMPND 18 ENGINEERED: YES; COMPND 19 MUTATION: YES; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: FAB 8D3 HEAVY CHAIN; COMPND 22 CHAIN: H; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 5; COMPND 25 MOLECULE: FAB 8D3 LIGHT CHAIN; COMPND 26 CHAIN: L; COMPND 27 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: DRD1; 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_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12, STAPHYLOCOCCUS AUREUS; SOURCE 15 ORGANISM_TAXID: 83333, 1280; SOURCE 16 GENE: MALE, SPA, SPA, SAV0111, SPG; SOURCE 17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 21 ORGANISM_TAXID: 10090; SOURCE 22 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 24 MOL_ID: 5; SOURCE 25 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 26 ORGANISM_TAXID: 10090; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, DRD1, PF-6142, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.ZHUANG,Y.XU,L.FAN,S.WANG,H.E.XU REVDAT 1 04-SEP-24 8JXS 0 JRNL AUTH L.FAN,Y.ZHUANG,H.WU,H.LI,Y.XU,Y.WANG,L.HE,S.WANG,Z.CHEN, JRNL AUTH 2 J.CHENG,H.E.XU,S.WANG JRNL TITL STRUCTURAL BASIS OF PSYCHEDELIC LSD RECOGNITION AT DOPAMINE JRNL TITL 2 D 1 RECEPTOR. JRNL REF NEURON 2024 JRNL REFN ISSN 0896-6273 JRNL PMID 39094559 JRNL DOI 10.1016/J.NEURON.2024.07.003 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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 : 104462 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 8JXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUL-23. REMARK 100 THE DEPOSITION ID IS D_1300038980. 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 : NANOBODY-BOUND DRD1_PF-6142 REMARK 245 COMPLEX; DRD1; PRAC-PRAD-PRG; REMARK 245 FAB 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) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 5000.00 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) : 5000.00 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: A, B, C, H, L 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 11 REMARK 465 THR A 12 REMARK 465 GLY A 13 REMARK 465 LEU A 14 REMARK 465 VAL A 15 REMARK 465 VAL A 16 REMARK 465 GLU A 17 REMARK 465 ARG A 18 REMARK 465 ASP A 19 REMARK 465 PHE A 20 REMARK 465 SER A 21 REMARK 465 ALA A 166 REMARK 465 LYS A 167 REMARK 465 PRO A 168 REMARK 465 THR A 169 REMARK 465 SER A 170 REMARK 465 PRO A 171 REMARK 465 SER A 172 REMARK 465 ASP A 173 REMARK 465 GLY A 174 REMARK 465 ASN A 175 REMARK 465 ALA A 176 REMARK 465 THR A 177 REMARK 465 SER A 178 REMARK 465 LEU A 179 REMARK 465 ALA A 180 REMARK 465 GLU A 181 REMARK 465 THR A 182 REMARK 465 ILE A 183 REMARK 465 ASP A 184 REMARK 465 HIS A 237 REMARK 465 ALA A 238 REMARK 465 LYS A 239 REMARK 465 ASN A 240 REMARK 465 CYS A 241 REMARK 465 GLN A 242 REMARK 465 THR A 243 REMARK 465 THR A 244 REMARK 465 THR A 245 REMARK 465 GLY A 246 REMARK 465 ASN A 247 REMARK 465 GLY A 248 REMARK 465 LYS A 249 REMARK 465 PRO A 250 REMARK 465 VAL A 251 REMARK 465 GLU A 252 REMARK 465 CYS A 253 REMARK 465 SER A 254 REMARK 465 GLN A 255 REMARK 465 PRO A 256 REMARK 465 GLU A 257 REMARK 465 SER A 258 REMARK 465 SER A 259 REMARK 465 PHE A 260 REMARK 465 LYS A 261 REMARK 465 MET A 262 REMARK 465 SER A 263 REMARK 465 GLY A 299 REMARK 465 SER A 300 REMARK 465 GLY A 301 REMARK 465 GLU A 302 REMARK 465 THR A 303 REMARK 465 GLN A 304 REMARK 465 PRO A 305 REMARK 465 PHE A 306 REMARK 465 GLY A 346 REMARK 465 CYS A 347 REMARK 465 TYR A 348 REMARK 465 ARG A 349 REMARK 465 LEU A 350 REMARK 465 CYS A 351 REMARK 465 PRO A 352 REMARK 465 ALA A 353 REMARK 465 THR A 354 REMARK 465 ASN A 355 REMARK 465 ASN A 356 REMARK 465 ALA A 357 REMARK 465 ILE A 358 REMARK 465 GLU A 359 REMARK 465 THR A 360 REMARK 465 VAL A 361 REMARK 465 SER A 362 REMARK 465 HIS B 125 REMARK 465 MET C -19 REMARK 465 GLY C -18 REMARK 465 SER C -17 REMARK 465 SER C -16 REMARK 465 HIS C -15 REMARK 465 HIS C -14 REMARK 465 HIS C -13 REMARK 465 HIS C -12 REMARK 465 HIS C -11 REMARK 465 HIS C -10 REMARK 465 SER C -9 REMARK 465 SER C -8 REMARK 465 GLY C -7 REMARK 465 LEU C -6 REMARK 465 VAL C -5 REMARK 465 PRO C -4 REMARK 465 ARG C -3 REMARK 465 GLY C -2 REMARK 465 SER C -1 REMARK 465 HIS C 0 REMARK 465 MET C 1 REMARK 465 LYS C 2 REMARK 465 ILE C 3 REMARK 465 GLU C 4 REMARK 465 GLU C 5 REMARK 465 GLY C 6 REMARK 465 LYS C 7 REMARK 465 LEU C 8 REMARK 465 VAL C 9 REMARK 465 ILE C 10 REMARK 465 TRP C 11 REMARK 465 ILE C 12 REMARK 465 ASN C 13 REMARK 465 GLY C 14 REMARK 465 ASP C 15 REMARK 465 LYS C 16 REMARK 465 GLY C 17 REMARK 465 TYR C 18 REMARK 465 ASN C 19 REMARK 465 GLY C 20 REMARK 465 LEU C 21 REMARK 465 ALA C 22 REMARK 465 GLU C 23 REMARK 465 VAL C 24 REMARK 465 GLY C 25 REMARK 465 LYS C 26 REMARK 465 LYS C 27 REMARK 465 PHE C 28 REMARK 465 GLU C 29 REMARK 465 LYS C 30 REMARK 465 ASP C 31 REMARK 465 THR C 32 REMARK 465 GLY C 33 REMARK 465 ILE C 34 REMARK 465 LYS C 35 REMARK 465 VAL C 36 REMARK 465 THR C 37 REMARK 465 VAL C 38 REMARK 465 ALA C 53 REMARK 465 THR C 54 REMARK 465 GLY C 55 REMARK 465 ASP C 56 REMARK 465 GLY C 57 REMARK 465 ALA C 142 REMARK 465 LYS C 143 REMARK 465 GLY C 144 REMARK 465 LYS C 145 REMARK 465 SER C 146 REMARK 465 ALA C 147 REMARK 465 ASP C 237 REMARK 465 THR C 238 REMARK 465 SER C 239 REMARK 465 LYS C 240 REMARK 465 VAL C 241 REMARK 465 ASN C 242 REMARK 465 GLY C 266 REMARK 465 ILE C 267 REMARK 465 ASN C 268 REMARK 465 ALA C 269 REMARK 465 ALA C 270 REMARK 465 SER C 271 REMARK 465 PRO C 272 REMARK 465 ASN C 273 REMARK 465 LYS C 274 REMARK 465 GLU C 275 REMARK 465 LEU C 276 REMARK 465 ALA C 277 REMARK 465 LYS C 278 REMARK 465 GLU C 279 REMARK 465 PHE C 280 REMARK 465 LEU C 281 REMARK 465 GLU C 282 REMARK 465 ASN C 283 REMARK 465 TYR C 284 REMARK 465 LEU C 285 REMARK 465 LEU C 286 REMARK 465 THR C 287 REMARK 465 ASP C 288 REMARK 465 GLU C 289 REMARK 465 GLY C 290 REMARK 465 LEU C 291 REMARK 465 GLU C 292 REMARK 465 ALA C 293 REMARK 465 VAL C 294 REMARK 465 ASN C 295 REMARK 465 LYS C 296 REMARK 465 ASP C 297 REMARK 465 LYS C 298 REMARK 465 PRO C 299 REMARK 465 LEU C 300 REMARK 465 GLY C 301 REMARK 465 ALA C 302 REMARK 465 VAL C 303 REMARK 465 ALA C 304 REMARK 465 LEU C 305 REMARK 465 LYS C 306 REMARK 465 SER C 307 REMARK 465 TYR C 308 REMARK 465 GLU C 309 REMARK 465 GLU C 310 REMARK 465 GLU C 311 REMARK 465 LEU C 312 REMARK 465 ALA C 313 REMARK 465 LYS C 314 REMARK 465 LYS C 409 REMARK 465 GLY C 410 REMARK 465 GLY C 411 REMARK 465 SER C 412 REMARK 465 GLY C 413 REMARK 465 GLY C 414 REMARK 465 ALA C 415 REMARK 465 GLY C 416 REMARK 465 SER C 417 REMARK 465 GLY C 418 REMARK 465 ASP C 419 REMARK 465 GLN C 420 REMARK 465 GLN C 421 REMARK 465 SER C 422 REMARK 465 ALA C 423 REMARK 465 PHE C 424 REMARK 465 TYR C 425 REMARK 465 GLU C 426 REMARK 465 ILE C 427 REMARK 465 LEU C 428 REMARK 465 ASN C 429 REMARK 465 MET C 430 REMARK 465 PRO C 431 REMARK 465 ASN C 432 REMARK 465 LEU C 433 REMARK 465 ASN C 434 REMARK 465 GLU C 435 REMARK 465 ALA C 436 REMARK 465 GLN C 437 REMARK 465 ARG C 438 REMARK 465 ASN C 439 REMARK 465 GLY C 440 REMARK 465 PHE C 441 REMARK 465 ILE C 442 REMARK 465 GLN C 443 REMARK 465 SER C 444 REMARK 465 LEU C 445 REMARK 465 LYS C 446 REMARK 465 ASP C 447 REMARK 465 ASP C 448 REMARK 465 PRO C 449 REMARK 465 SER C 450 REMARK 465 GLN C 451 REMARK 465 SER C 452 REMARK 465 THR C 453 REMARK 465 ASN C 454 REMARK 465 VAL C 455 REMARK 465 LEU C 456 REMARK 465 GLY C 457 REMARK 465 GLU C 458 REMARK 465 ALA C 459 REMARK 465 LYS C 460 REMARK 465 LYS C 461 REMARK 465 LEU C 462 REMARK 465 ASN C 463 REMARK 465 GLU C 464 REMARK 465 SER C 465 REMARK 465 GLN C 466 REMARK 465 ALA C 467 REMARK 465 GLY C 468 REMARK 465 GLY C 469 REMARK 465 GLY C 470 REMARK 465 SER C 471 REMARK 465 GLY C 472 REMARK 465 GLY C 473 REMARK 465 GLY C 474 REMARK 465 SER C 475 REMARK 465 GLY C 476 REMARK 465 GLY C 477 REMARK 465 SER C 478 REMARK 465 ALA C 479 REMARK 465 VAL C 480 REMARK 465 THR C 481 REMARK 465 THR C 482 REMARK 465 THR C 498 REMARK 465 LYS C 499 REMARK 465 ALA C 500 REMARK 465 VAL C 501 REMARK 465 ASP C 502 REMARK 465 VAL C 519 REMARK 465 ASP C 520 REMARK 465 GLY C 521 REMARK 465 VAL C 522 REMARK 465 TRP C 523 REMARK 465 THR C 524 REMARK 465 TYR C 525 REMARK 465 ASP C 526 REMARK 465 ASP C 527 REMARK 465 ALA C 528 REMARK 465 THR C 529 REMARK 465 LYS C 530 REMARK 465 GLY C 537 REMARK 465 SER C 538 REMARK 465 GLY C 539 REMARK 465 MET H -18 REMARK 465 ASP H -17 REMARK 465 TRP H -16 REMARK 465 THR H -15 REMARK 465 TRP H -14 REMARK 465 ARG H -13 REMARK 465 VAL H -12 REMARK 465 PHE H -11 REMARK 465 CYS H -10 REMARK 465 LEU H -9 REMARK 465 LEU H -8 REMARK 465 ALA H -7 REMARK 465 VAL H -6 REMARK 465 ALA H -5 REMARK 465 PRO H -4 REMARK 465 GLY H -3 REMARK 465 ALA H -2 REMARK 465 HIS H -1 REMARK 465 SER H 0 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 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 TYR H 204 REMARK 465 VAL H 221 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 GLY H 227 REMARK 465 SER H 228 REMARK 465 HIS H 229 REMARK 465 HIS H 230 REMARK 465 HIS H 231 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 MET L -19 REMARK 465 VAL L -18 REMARK 465 LEU L -17 REMARK 465 GLN L -16 REMARK 465 THR L -15 REMARK 465 GLN L -14 REMARK 465 VAL L -13 REMARK 465 PHE L -12 REMARK 465 ILE L -11 REMARK 465 SER L -10 REMARK 465 LEU L -9 REMARK 465 LEU L -8 REMARK 465 LEU L -7 REMARK 465 TRP L -6 REMARK 465 ILE L -5 REMARK 465 SER L -4 REMARK 465 GLY L -3 REMARK 465 ALA L -2 REMARK 465 TYR L -1 REMARK 465 GLY L 0 REMARK 465 LYS L 150 REMARK 465 VAL L 151 REMARK 465 GLN L 152 REMARK 465 TRP L 153 REMARK 465 LYS L 154 REMARK 465 VAL L 155 REMARK 465 ASP L 156 REMARK 465 ASN L 157 REMARK 465 ALA L 158 REMARK 465 LEU L 159 REMARK 465 GLN L 160 REMARK 465 SER L 161 REMARK 465 GLY L 162 REMARK 465 THR L 185 REMARK 465 LEU L 186 REMARK 465 SER L 187 REMARK 465 LYS L 188 REMARK 465 ALA L 189 REMARK 465 ASP L 190 REMARK 465 TYR L 191 REMARK 465 GLU L 192 REMARK 465 LYS L 193 REMARK 465 HIS L 194 REMARK 465 LYS L 195 REMARK 465 VAL L 196 REMARK 465 TYR L 197 REMARK 465 ALA L 198 REMARK 465 CYS L 199 REMARK 465 GLU L 200 REMARK 465 VAL L 201 REMARK 465 THR L 202 REMARK 465 HIS L 203 REMARK 465 GLN L 204 REMARK 465 GLY L 205 REMARK 465 LEU L 206 REMARK 465 SER L 207 REMARK 465 SER L 208 REMARK 465 PRO L 209 REMARK 465 VAL L 210 REMARK 465 THR L 211 REMARK 465 LYS L 212 REMARK 465 SER L 213 REMARK 465 PHE L 214 REMARK 465 ASN L 215 REMARK 465 ARG L 216 REMARK 465 GLY L 217 REMARK 465 GLU L 218 REMARK 465 CYS L 219 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 ARG A 23 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 138 CG CD CE NZ REMARK 470 GLN B 1 CG CD OE1 NE2 REMARK 470 GLN B 5 CG CD OE1 NE2 REMARK 470 SER B 25 OG REMARK 470 LYS C 220 CG CD CE NZ REMARK 470 TYR C 483 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS C 484 CG CD CE NZ REMARK 470 ASN C 488 CG OD1 ND2 REMARK 470 LYS C 490 CG CD CE NZ REMARK 470 LEU C 492 CG CD1 CD2 REMARK 470 GLU C 495 CG CD OE1 OE2 REMARK 470 THR C 496 OG1 CG2 REMARK 470 LYS H 219 CG CD CE NZ REMARK 470 ASP L 127 CG OD1 OD2 REMARK 470 LEU L 130 CG CD1 CD2 REMARK 470 THR L 134 OG1 CG2 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 VAL A 77 -59.58 -122.96 REMARK 500 GLN B 112 -2.86 71.06 REMARK 500 MET C 149 116.74 -160.10 REMARK 500 ASP C 388 84.70 -157.63 REMARK 500 PRO H 159 80.52 -69.67 REMARK 500 ALA L 57 -0.91 67.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36711 RELATED DB: EMDB REMARK 900 STRUCTURE OF NANOBODY-BOUND DRD1_PF-6142 COMPLEX DBREF 8JXS A 11 362 UNP P21728 DRD1_HUMAN 11 362 DBREF 8JXS B 1 125 PDB 8JXS 8JXS 1 125 DBREF 8JXS C 2 369 UNP P0AEX9 MALE_ECOLI 27 394 DBREF 8JXS C 371 409 UNP P38507 SPA_STAAU 289 327 DBREF 8JXS C 419 467 UNP P0A015 SPA_STAAM 103 151 DBREF 8JXS C 479 536 UNP P06654 SPG1_STRSG 295 352 DBREF 8JXS H -18 234 PDB 8JXS 8JXS -18 234 DBREF 8JXS L -19 219 PDB 8JXS 8JXS -19 219 SEQADV 8JXS TRP A 112 UNP P21728 LEU 112 ENGINEERED MUTATION SEQADV 8JXS ALA A 325 UNP P21728 SER 325 ENGINEERED MUTATION SEQADV 8JXS MET C -19 UNP P0AEX9 INITIATING METHIONINE SEQADV 8JXS GLY C -18 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS SER C -17 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS SER C -16 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS HIS C -15 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS HIS C -14 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS HIS C -13 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS HIS C -12 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS HIS C -11 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS HIS C -10 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS SER C -9 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS SER C -8 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS GLY C -7 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS LEU C -6 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS VAL C -5 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS PRO C -4 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS ARG C -3 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS GLY C -2 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS SER C -1 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS HIS C 0 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS MET C 1 UNP P0AEX9 CLONING ARTIFACT SEQADV 8JXS GLN C 360 UNP P0AEX9 GLU 385 ENGINEERED MUTATION SEQADV 8JXS ALA C 363 UNP P0AEX9 LYS 388 ENGINEERED MUTATION SEQADV 8JXS PHE C 364 UNP P0AEX9 ASP 389 ENGINEERED MUTATION SEQADV 8JXS ILE C 367 UNP P0AEX9 THR 392 ENGINEERED MUTATION SEQADV 8JXS LEU C 368 UNP P0AEX9 ARG 393 ENGINEERED MUTATION SEQADV 8JXS MET C 370 UNP P0AEX9 LINKER SEQADV 8JXS GLU C 404 UNP P38507 ASP 322 ENGINEERED MUTATION SEQADV 8JXS HIS C 405 UNP P38507 ALA 323 ENGINEERED MUTATION SEQADV 8JXS GLY C 410 UNP P38507 LINKER SEQADV 8JXS GLY C 411 UNP P38507 LINKER SEQADV 8JXS SER C 412 UNP P38507 LINKER SEQADV 8JXS GLY C 413 UNP P38507 LINKER SEQADV 8JXS GLY C 414 UNP P38507 LINKER SEQADV 8JXS ALA C 415 UNP P38507 LINKER SEQADV 8JXS GLY C 416 UNP P38507 LINKER SEQADV 8JXS SER C 417 UNP P38507 LINKER SEQADV 8JXS GLY C 418 UNP P38507 LINKER SEQADV 8JXS GLY C 468 UNP P0A015 LINKER SEQADV 8JXS GLY C 469 UNP P0A015 LINKER SEQADV 8JXS GLY C 470 UNP P0A015 LINKER SEQADV 8JXS SER C 471 UNP P0A015 LINKER SEQADV 8JXS GLY C 472 UNP P0A015 LINKER SEQADV 8JXS GLY C 473 UNP P0A015 LINKER SEQADV 8JXS GLY C 474 UNP P0A015 LINKER SEQADV 8JXS SER C 475 UNP P0A015 LINKER SEQADV 8JXS GLY C 476 UNP P0A015 LINKER SEQADV 8JXS GLY C 477 UNP P0A015 LINKER SEQADV 8JXS SER C 478 UNP P0A015 LINKER SEQADV 8JXS GLY C 537 UNP P06654 CLONING ARTIFACT SEQADV 8JXS SER C 538 UNP P06654 CLONING ARTIFACT SEQADV 8JXS GLY C 539 UNP P06654 CLONING ARTIFACT SEQRES 1 A 352 GLY THR GLY LEU VAL VAL GLU ARG ASP PHE SER VAL ARG SEQRES 2 A 352 ILE LEU THR ALA CYS PHE LEU SER LEU LEU ILE LEU SER SEQRES 3 A 352 THR LEU LEU GLY ASN THR LEU VAL CYS ALA ALA VAL ILE SEQRES 4 A 352 ARG PHE ARG HIS LEU ARG SER LYS VAL THR ASN PHE PHE SEQRES 5 A 352 VAL ILE SER LEU ALA VAL SER ASP LEU LEU VAL ALA VAL SEQRES 6 A 352 LEU VAL MET PRO TRP LYS ALA VAL ALA GLU ILE ALA GLY SEQRES 7 A 352 PHE TRP PRO PHE GLY SER PHE CYS ASN ILE TRP VAL ALA SEQRES 8 A 352 PHE ASP ILE MET CYS SER THR ALA SER ILE TRP ASN LEU SEQRES 9 A 352 CYS VAL ILE SER VAL ASP ARG TYR TRP ALA ILE SER SER SEQRES 10 A 352 PRO PHE ARG TYR GLU ARG LYS MET THR PRO LYS ALA ALA SEQRES 11 A 352 PHE ILE LEU ILE SER VAL ALA TRP THR LEU SER VAL LEU SEQRES 12 A 352 ILE SER PHE ILE PRO VAL GLN LEU SER TRP HIS LYS ALA SEQRES 13 A 352 LYS PRO THR SER PRO SER ASP GLY ASN ALA THR SER LEU SEQRES 14 A 352 ALA GLU THR ILE ASP ASN CYS ASP SER SER LEU SER ARG SEQRES 15 A 352 THR TYR ALA ILE SER SER SER VAL ILE SER PHE TYR ILE SEQRES 16 A 352 PRO VAL ALA ILE MET ILE VAL THR TYR THR ARG ILE TYR SEQRES 17 A 352 ARG ILE ALA GLN LYS GLN ILE ARG ARG ILE ALA ALA LEU SEQRES 18 A 352 GLU ARG ALA ALA VAL HIS ALA LYS ASN CYS GLN THR THR SEQRES 19 A 352 THR GLY ASN GLY LYS PRO VAL GLU CYS SER GLN PRO GLU SEQRES 20 A 352 SER SER PHE LYS MET SER PHE LYS ARG GLU THR LYS VAL SEQRES 21 A 352 LEU LYS THR LEU SER VAL ILE MET GLY VAL PHE VAL CYS SEQRES 22 A 352 CYS TRP LEU PRO PHE PHE ILE LEU ASN CYS ILE LEU PRO SEQRES 23 A 352 PHE CYS GLY SER GLY GLU THR GLN PRO PHE CYS ILE ASP SEQRES 24 A 352 SER ASN THR PHE ASP VAL PHE VAL TRP PHE GLY TRP ALA SEQRES 25 A 352 ASN SER ALA LEU ASN PRO ILE ILE TYR ALA PHE ASN ALA SEQRES 26 A 352 ASP PHE ARG LYS ALA PHE SER THR LEU LEU GLY CYS TYR SEQRES 27 A 352 ARG LEU CYS PRO ALA THR ASN ASN ALA ILE GLU THR VAL SEQRES 28 A 352 SER SEQRES 1 B 125 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 125 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 125 SER ILE PHE ALA LEU ASN ILE MET GLY TRP TYR ARG GLN SEQRES 4 B 125 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE HIS SEQRES 5 B 125 SER GLY GLY THR THR ASN TYR ALA ASN SER VAL LYS GLY SEQRES 6 B 125 ARG PHE THR ILE SER ARG ASP ASN ALA ALA ASN THR VAL SEQRES 7 B 125 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 B 125 VAL TYR TYR CYS ASN VAL LYS ASP PHE GLY ALA ILE VAL SEQRES 9 B 125 ALA ASP ARG ASP TYR TRP GLY GLN GLY THR GLN VAL THR SEQRES 10 B 125 VAL SER SER LEU GLU HIS HIS HIS SEQRES 1 C 559 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 C 559 LEU VAL PRO ARG GLY SER HIS MET LYS ILE GLU GLU GLY SEQRES 3 C 559 LYS LEU VAL ILE TRP ILE ASN GLY ASP LYS GLY TYR ASN SEQRES 4 C 559 GLY LEU ALA GLU VAL GLY LYS LYS PHE GLU LYS ASP THR SEQRES 5 C 559 GLY ILE LYS VAL THR VAL GLU HIS PRO ASP LYS LEU GLU SEQRES 6 C 559 GLU LYS PHE PRO GLN VAL ALA ALA THR GLY ASP GLY PRO SEQRES 7 C 559 ASP ILE ILE PHE TRP ALA HIS ASP ARG PHE GLY GLY TYR SEQRES 8 C 559 ALA GLN SER GLY LEU LEU ALA GLU ILE THR PRO ASP LYS SEQRES 9 C 559 ALA PHE GLN ASP LYS LEU TYR PRO PHE THR TRP ASP ALA SEQRES 10 C 559 VAL ARG TYR ASN GLY LYS LEU ILE ALA TYR PRO ILE ALA SEQRES 11 C 559 VAL GLU ALA LEU SER LEU ILE TYR ASN LYS ASP LEU LEU SEQRES 12 C 559 PRO ASN PRO PRO LYS THR TRP GLU GLU ILE PRO ALA LEU SEQRES 13 C 559 ASP LYS GLU LEU LYS ALA LYS GLY LYS SER ALA LEU MET SEQRES 14 C 559 PHE ASN LEU GLN GLU PRO TYR PHE THR TRP PRO LEU ILE SEQRES 15 C 559 ALA ALA ASP GLY GLY TYR ALA PHE LYS TYR GLU ASN GLY SEQRES 16 C 559 LYS TYR ASP ILE LYS ASP VAL GLY VAL ASP ASN ALA GLY SEQRES 17 C 559 ALA LYS ALA GLY LEU THR PHE LEU VAL ASP LEU ILE LYS SEQRES 18 C 559 ASN LYS HIS MET ASN ALA ASP THR ASP TYR SER ILE ALA SEQRES 19 C 559 GLU ALA ALA PHE ASN LYS GLY GLU THR ALA MET THR ILE SEQRES 20 C 559 ASN GLY PRO TRP ALA TRP SER ASN ILE ASP THR SER LYS SEQRES 21 C 559 VAL ASN TYR GLY VAL THR VAL LEU PRO THR PHE LYS GLY SEQRES 22 C 559 GLN PRO SER LYS PRO PHE VAL GLY VAL LEU SER ALA GLY SEQRES 23 C 559 ILE ASN ALA ALA SER PRO ASN LYS GLU LEU ALA LYS GLU SEQRES 24 C 559 PHE LEU GLU ASN TYR LEU LEU THR ASP GLU GLY LEU GLU SEQRES 25 C 559 ALA VAL ASN LYS ASP LYS PRO LEU GLY ALA VAL ALA LEU SEQRES 26 C 559 LYS SER TYR GLU GLU GLU LEU ALA LYS ASP PRO ARG ILE SEQRES 27 C 559 ALA ALA THR MET GLU ASN ALA GLN LYS GLY GLU ILE MET SEQRES 28 C 559 PRO ASN ILE PRO GLN MET SER ALA PHE TRP TYR ALA VAL SEQRES 29 C 559 ARG THR ALA VAL ILE ASN ALA ALA SER GLY ARG GLN THR SEQRES 30 C 559 VAL ASP GLN ALA LEU ALA PHE ALA GLN ILE LEU ILE MET SEQRES 31 C 559 PRO ASN LEU THR GLU GLU GLN ARG ASN GLY PHE ILE GLN SEQRES 32 C 559 SER LEU LYS ASP ASP PRO SER VAL SER LYS GLU ILE LEU SEQRES 33 C 559 ALA GLU ALA LYS LYS LEU ASN GLU HIS GLN ALA PRO LYS SEQRES 34 C 559 GLY GLY SER GLY GLY ALA GLY SER GLY ASP GLN GLN SER SEQRES 35 C 559 ALA PHE TYR GLU ILE LEU ASN MET PRO ASN LEU ASN GLU SEQRES 36 C 559 ALA GLN ARG ASN GLY PHE ILE GLN SER LEU LYS ASP ASP SEQRES 37 C 559 PRO SER GLN SER THR ASN VAL LEU GLY GLU ALA LYS LYS SEQRES 38 C 559 LEU ASN GLU SER GLN ALA GLY GLY GLY SER GLY GLY GLY SEQRES 39 C 559 SER GLY GLY SER ALA VAL THR THR TYR LYS LEU VAL ILE SEQRES 40 C 559 ASN GLY LYS THR LEU LYS GLY GLU THR THR THR LYS ALA SEQRES 41 C 559 VAL ASP ALA GLU THR ALA GLU LYS ALA PHE LYS GLN TYR SEQRES 42 C 559 ALA ASN ASP ASN GLY VAL ASP GLY VAL TRP THR TYR ASP SEQRES 43 C 559 ASP ALA THR LYS THR PHE THR VAL THR GLU GLY SER GLY SEQRES 1 H 253 MET ASP TRP THR TRP ARG VAL PHE CYS LEU LEU ALA VAL SEQRES 2 H 253 ALA PRO GLY ALA HIS SER ASP VAL GLN LEU VAL GLU SER SEQRES 3 H 253 GLY GLY GLY LEU VAL GLN PRO GLY LYS SER LEU ARG LEU SEQRES 4 H 253 SER CYS ALA ALA SER GLY PHE THR PHE SER ASN PHE GLY SEQRES 5 H 253 MET HIS TRP VAL ARG GLN ALA PRO GLU MET GLY LEU GLU SEQRES 6 H 253 TRP VAL ALA TYR ILE SER SER GLY SER THR THR LYS TYR SEQRES 7 H 253 TYR GLY ASP THR VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 8 H 253 ASP ASN PRO LYS ASN THR LEU TYR LEU GLN MET ASN SER SEQRES 9 H 253 LEU ARG SER GLU ASP THR ALA MET TYR TYR CYS ALA ARG SEQRES 10 H 253 ARG PRO LEU TYR ASP GLY ASP TYR GLY TYR PRO MET ASP SEQRES 11 H 253 TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA SEQRES 12 H 253 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 13 H 253 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 14 H 253 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 15 H 253 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 16 H 253 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 17 H 253 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 18 H 253 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 19 H 253 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY SER SEQRES 20 H 253 HIS HIS HIS HIS HIS HIS SEQRES 1 L 239 MET VAL LEU GLN THR GLN VAL PHE ILE SER LEU LEU LEU SEQRES 2 L 239 TRP ILE SER GLY ALA TYR GLY ASN ILE MET LEU THR GLN SEQRES 3 L 239 SER PRO SER SER LEU ALA VAL SER ALA GLY GLU ARG VAL SEQRES 4 L 239 THR MET SER CYS LYS SER THR GLN SER ILE LEU TYR ASN SEQRES 5 L 239 SER ASN GLN LYS THR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 6 L 239 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 7 L 239 THR ARG ALA SER GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 8 L 239 GLY SER GLY THR ASP PHE THR LEU THR ILE ASN SER VAL SEQRES 9 L 239 GLN PRO GLU ASP LEU ALA VAL TYR TYR CYS HIS GLN TYR SEQRES 10 L 239 LEU SER ALA TRP THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 11 L 239 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 12 L 239 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 13 L 239 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 14 L 239 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 15 L 239 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 16 L 239 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 17 L 239 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 18 L 239 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 19 L 239 ASN ARG GLY GLU CYS HET V6X A 401 27 HETNAM V6X 4-[3-METHYL-4-(6-METHYLIMIDAZO[1,2-A]PYRAZIN-5-YL) HETNAM 2 V6X PHENOXY]FURO[3,2-C]PYRIDINE HETSYN V6X PF-6142 FORMUL 6 V6X C21 H16 N4 O2 HELIX 1 AA1 VAL A 22 PHE A 51 1 30 HELIX 2 AA2 THR A 59 VAL A 77 1 19 HELIX 3 AA3 VAL A 77 GLY A 88 1 12 HELIX 4 AA4 PHE A 95 SER A 127 1 33 HELIX 5 AA5 SER A 127 MET A 135 1 9 HELIX 6 AA6 THR A 136 LEU A 161 1 26 HELIX 7 AA7 SER A 191 PHE A 203 1 13 HELIX 8 AA8 PHE A 203 VAL A 236 1 34 HELIX 9 AA9 LYS A 265 CYS A 298 1 34 HELIX 10 AB1 ASP A 309 ALA A 332 1 24 HELIX 11 AB2 ASN A 334 LEU A 345 1 12 HELIX 12 AB3 LYS B 86 THR B 90 5 5 HELIX 13 AB4 LYS C 43 ALA C 52 1 10 HELIX 14 AB5 HIS C 65 GLY C 75 1 11 HELIX 15 AB6 ASP C 83 LEU C 90 1 8 HELIX 16 AB7 TYR C 91 VAL C 98 1 8 HELIX 17 AB8 THR C 129 GLU C 131 5 3 HELIX 18 AB9 GLU C 132 LYS C 141 1 10 HELIX 19 AC1 GLU C 154 ASP C 165 1 12 HELIX 20 AC2 ASN C 186 ASN C 202 1 17 HELIX 21 AC3 ASP C 210 LYS C 220 1 11 HELIX 22 AC4 GLY C 229 TRP C 233 5 5 HELIX 23 AC5 PRO C 316 LYS C 327 1 12 HELIX 24 AC6 GLN C 336 ALA C 352 1 17 HELIX 25 AC7 THR C 357 MET C 370 1 14 HELIX 26 AC8 THR C 374 ASP C 387 1 14 HELIX 27 AC9 VAL C 391 GLN C 406 1 16 HELIX 28 AD1 GLU C 504 GLY C 518 1 15 HELIX 29 AD2 ASN H 74 LYS H 76 5 3 HELIX 30 AD3 ARG H 87 THR H 91 5 5 HELIX 31 AD4 TYR H 102 GLY H 107 1 6 HELIX 32 AD5 GLN L 85 LEU L 89 5 5 HELIX 33 AD6 SER L 126 GLY L 133 1 8 SHEET 1 AA1 4 GLN B 3 SER B 7 0 SHEET 2 AA1 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 VAL B 78 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA1 4 PHE B 67 ARG B 71 -1 N SER B 70 O TYR B 79 SHEET 1 AA2 6 LEU B 11 GLN B 13 0 SHEET 2 AA2 6 THR B 114 SER B 119 1 O SER B 119 N VAL B 12 SHEET 3 AA2 6 ALA B 91 ASP B 99 -1 N TYR B 93 O THR B 114 SHEET 4 AA2 6 ASN B 32 GLN B 39 -1 N GLN B 39 O VAL B 92 SHEET 5 AA2 6 GLU B 46 HIS B 52 -1 O GLU B 46 N ARG B 38 SHEET 6 AA2 6 THR B 57 TYR B 59 -1 O ASN B 58 N ALA B 50 SHEET 1 AA3 4 LEU B 11 GLN B 13 0 SHEET 2 AA3 4 THR B 114 SER B 119 1 O SER B 119 N VAL B 12 SHEET 3 AA3 4 ALA B 91 ASP B 99 -1 N TYR B 93 O THR B 114 SHEET 4 AA3 4 ARG B 107 TRP B 110 -1 O ARG B 107 N ASP B 99 SHEET 1 AA4 3 TRP C 63 ALA C 64 0 SHEET 2 AA4 3 PHE C 259 SER C 264 -1 O SER C 264 N TRP C 63 SHEET 3 AA4 3 PRO C 108 GLU C 112 -1 N ILE C 109 O LEU C 263 SHEET 1 AA5 3 TRP C 63 ALA C 64 0 SHEET 2 AA5 3 PHE C 259 SER C 264 -1 O SER C 264 N TRP C 63 SHEET 3 AA5 3 GLU C 329 ILE C 330 1 O GLU C 329 N VAL C 260 SHEET 1 AA6 2 ARG C 99 TYR C 100 0 SHEET 2 AA6 2 LYS C 103 LEU C 104 -1 O LYS C 103 N TYR C 100 SHEET 1 AA7 3 MET C 225 ASN C 228 0 SHEET 2 AA7 3 SER C 115 TYR C 118 -1 N SER C 115 O ASN C 228 SHEET 3 AA7 3 GLY C 244 THR C 246 -1 O GLY C 244 N TYR C 118 SHEET 1 AA8 2 TYR C 172 GLU C 173 0 SHEET 2 AA8 2 LYS C 176 TYR C 177 -1 O LYS C 176 N GLU C 173 SHEET 1 AA9 6 PHE C 532 THR C 535 0 SHEET 2 AA9 6 LEU C 485 ASN C 488 1 N VAL C 486 O VAL C 534 SHEET 3 AA9 6 LYS C 493 THR C 496 -1 O THR C 496 N LEU C 485 SHEET 4 AA9 6 THR H 215 ASP H 218 -1 O ASP H 218 N LYS C 493 SHEET 5 AA9 6 CYS H 206 HIS H 210 -1 N VAL H 208 O VAL H 217 SHEET 6 AA9 6 VAL H 160 TRP H 164 -1 N SER H 163 O ASN H 207 SHEET 1 AB1 4 GLN H 3 SER H 7 0 SHEET 2 AB1 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AB1 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AB2 6 LEU H 11 VAL H 12 0 SHEET 2 AB2 6 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AB2 6 ALA H 92 ARG H 99 -1 N TYR H 94 O THR H 117 SHEET 4 AB2 6 GLY H 33 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB2 6 GLU H 46 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AB2 6 LYS H 58 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AB3 4 SER H 130 LEU H 134 0 SHEET 2 AB3 4 LEU H 148 TYR H 155 -1 O GLY H 149 N LEU H 134 SHEET 3 AB3 4 TYR H 186 VAL H 192 -1 O VAL H 192 N LEU H 148 SHEET 4 AB3 4 VAL H 173 LEU H 180 -1 N PHE H 176 O SER H 189 SHEET 1 AB4 4 LEU L 4 THR L 5 0 SHEET 2 AB4 4 VAL L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB4 4 ASP L 76 ILE L 81 -1 O ILE L 81 N VAL L 19 SHEET 4 AB4 4 PHE L 68 SER L 73 -1 N THR L 69 O THR L 80 SHEET 1 AB5 6 SER L 10 SER L 14 0 SHEET 2 AB5 6 THR L 107 LYS L 112 1 O GLU L 110 N VAL L 13 SHEET 3 AB5 6 VAL L 91 GLN L 96 -1 N TYR L 92 O THR L 107 SHEET 4 AB5 6 LEU L 39 GLN L 44 -1 N GLN L 44 O VAL L 91 SHEET 5 AB5 6 PRO L 50 TYR L 55 -1 O LYS L 51 N GLN L 43 SHEET 6 AB5 6 THR L 59 ARG L 60 -1 O THR L 59 N TYR L 55 SHEET 1 AB6 4 SER L 10 SER L 14 0 SHEET 2 AB6 4 THR L 107 LYS L 112 1 O GLU L 110 N VAL L 13 SHEET 3 AB6 4 VAL L 91 GLN L 96 -1 N TYR L 92 O THR L 107 SHEET 4 AB6 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 96 SHEET 1 AB7 4 SER L 119 PHE L 123 0 SHEET 2 AB7 4 VAL L 138 PHE L 144 -1 O LEU L 140 N PHE L 121 SHEET 3 AB7 4 TYR L 178 THR L 183 -1 O LEU L 180 N LEU L 141 SHEET 4 AB7 4 GLN L 165 VAL L 168 -1 N GLN L 165 O THR L 183 SSBOND 1 CYS A 96 CYS A 186 1555 1555 2.03 SSBOND 2 CYS A 298 CYS A 307 1555 1555 2.03 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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