HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 02-JUL-24 9IMA TITLE CRYO-EM STRUCTURE FOR THE GPRC5D COMPLEXED WITH TALQUETAMAB FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: TALQUETAMAB FAB (ANTI-GPRC5D) HEAVY CHAIN; COMPND 3 CHAIN: C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TALQUETAMAB FAB (ANTI-GPRC5D) LIGHT CHAIN; COMPND 7 CHAIN: D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: G-PROTEIN COUPLED RECEPTOR FAMILY C GROUP 5 MEMBER D; COMPND 11 CHAIN: B, A; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: GPRC5D; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI- KEYWDS TALQUETAMAB, CLASS C GPCR, MULTIPLE MYELOMA, BISPECIFIC ANTIBODY, KEYWDS 2 MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR J.JEONG,J.SHIN,J.PARK,Y.CHO REVDAT 1 11-SEP-24 9IMA 0 JRNL AUTH J.JEONG,J.PARK,G.YOUNG MO,J.SHIN,Y.CHO JRNL TITL STRUCTURAL BASIS FOR THE RECOGNITION OF GPRC5D BY JRNL TITL 2 TALQUETAMAB, A BISPECIFIC ANTIBODY FOR MULTIPLE MYELOMA. JRNL REF J.MOL.BIOL. V. 436 68748 2024 JRNL REFN ESSN 1089-8638 JRNL PMID 39181182 JRNL DOI 10.1016/J.JMB.2024.168748 REMARK 2 REMARK 2 RESOLUTION. 2.65 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) : 2.650 REMARK 3 NUMBER OF PARTICLES : 628867 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9IMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049068. 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 : GPCR ANTIBODY COMPLEX; REMARK 245 ANTIBODY; GPCR REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 8.30 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.73 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 : 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, B, A 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 LEU C 222 REMARK 465 VAL C 223 REMARK 465 PRO C 224 REMARK 465 ARG C 225 REMARK 465 GLY C 226 REMARK 465 SER C 227 REMARK 465 HIS C 228 REMARK 465 HIS C 229 REMARK 465 HIS C 230 REMARK 465 HIS C 231 REMARK 465 HIS C 232 REMARK 465 HIS C 233 REMARK 465 MET B -2 REMARK 465 VAL B -1 REMARK 465 ASP B 0 REMARK 465 MET B 1 REMARK 465 TYR B 2 REMARK 465 LYS B 3 REMARK 465 ASP B 4 REMARK 465 CYS B 5 REMARK 465 ILE B 6 REMARK 465 GLU B 7 REMARK 465 SER B 8 REMARK 465 THR B 9 REMARK 465 GLY B 10 REMARK 465 ASP B 11 REMARK 465 TYR B 12 REMARK 465 PHE B 13 REMARK 465 LEU B 14 REMARK 465 LEU B 15 REMARK 465 CYS B 16 REMARK 465 ASP B 17 REMARK 465 ALA B 18 REMARK 465 GLU B 19 REMARK 465 CYS B 269 REMARK 465 ARG B 270 REMARK 465 GLN B 271 REMARK 465 GLU B 272 REMARK 465 CYS B 273 REMARK 465 PRO B 274 REMARK 465 LEU B 275 REMARK 465 GLN B 276 REMARK 465 GLY B 277 REMARK 465 ASN B 278 REMARK 465 ALA B 279 REMARK 465 CYS B 280 REMARK 465 PRO B 281 REMARK 465 VAL B 282 REMARK 465 THR B 283 REMARK 465 ALA B 284 REMARK 465 TYR B 285 REMARK 465 GLN B 286 REMARK 465 HIS B 287 REMARK 465 SER B 288 REMARK 465 PHE B 289 REMARK 465 GLN B 290 REMARK 465 VAL B 291 REMARK 465 GLU B 292 REMARK 465 ASN B 293 REMARK 465 GLN B 294 REMARK 465 GLU B 295 REMARK 465 LEU B 296 REMARK 465 SER B 297 REMARK 465 ARG B 298 REMARK 465 ALA B 299 REMARK 465 ARG B 300 REMARK 465 ASP B 301 REMARK 465 SER B 302 REMARK 465 ASP B 303 REMARK 465 GLY B 304 REMARK 465 ALA B 305 REMARK 465 GLU B 306 REMARK 465 GLU B 307 REMARK 465 ASP B 308 REMARK 465 SER B 309 REMARK 465 GLY B 310 REMARK 465 SER B 311 REMARK 465 GLY B 312 REMARK 465 SER B 313 REMARK 465 GLY B 314 REMARK 465 ARG B 315 REMARK 465 GLY B 316 REMARK 465 ARG B 317 REMARK 465 GLY B 318 REMARK 465 GLY B 319 REMARK 465 SER B 320 REMARK 465 GLU B 321 REMARK 465 ASN B 322 REMARK 465 LEU B 323 REMARK 465 TYR B 324 REMARK 465 PHE B 325 REMARK 465 GLN B 326 REMARK 465 GLY B 327 REMARK 465 GLY B 328 REMARK 465 SER B 329 REMARK 465 GLY B 330 REMARK 465 SER B 331 REMARK 465 GLY B 332 REMARK 465 GLY B 333 REMARK 465 ASP B 334 REMARK 465 TYR B 335 REMARK 465 LYS B 336 REMARK 465 ASP B 337 REMARK 465 ASP B 338 REMARK 465 ASP B 339 REMARK 465 ASP B 340 REMARK 465 LYS B 341 REMARK 465 ASP B 342 REMARK 465 TYR B 343 REMARK 465 LYS B 344 REMARK 465 ASP B 345 REMARK 465 ASP B 346 REMARK 465 ASP B 347 REMARK 465 ASP B 348 REMARK 465 LYS B 349 REMARK 465 MET A -2 REMARK 465 VAL A -1 REMARK 465 ASP A 0 REMARK 465 MET A 1 REMARK 465 TYR A 2 REMARK 465 LYS A 3 REMARK 465 ASP A 4 REMARK 465 CYS A 5 REMARK 465 ILE A 6 REMARK 465 GLU A 7 REMARK 465 SER A 8 REMARK 465 THR A 9 REMARK 465 GLY A 10 REMARK 465 ASP A 11 REMARK 465 TYR A 12 REMARK 465 PHE A 13 REMARK 465 LEU A 14 REMARK 465 LEU A 15 REMARK 465 CYS A 16 REMARK 465 ASP A 17 REMARK 465 ALA A 18 REMARK 465 GLU A 19 REMARK 465 CYS A 269 REMARK 465 ARG A 270 REMARK 465 GLN A 271 REMARK 465 GLU A 272 REMARK 465 CYS A 273 REMARK 465 PRO A 274 REMARK 465 LEU A 275 REMARK 465 GLN A 276 REMARK 465 GLY A 277 REMARK 465 ASN A 278 REMARK 465 ALA A 279 REMARK 465 CYS A 280 REMARK 465 PRO A 281 REMARK 465 VAL A 282 REMARK 465 THR A 283 REMARK 465 ALA A 284 REMARK 465 TYR A 285 REMARK 465 GLN A 286 REMARK 465 HIS A 287 REMARK 465 SER A 288 REMARK 465 PHE A 289 REMARK 465 GLN A 290 REMARK 465 VAL A 291 REMARK 465 GLU A 292 REMARK 465 ASN A 293 REMARK 465 GLN A 294 REMARK 465 GLU A 295 REMARK 465 LEU A 296 REMARK 465 SER A 297 REMARK 465 ARG A 298 REMARK 465 ALA A 299 REMARK 465 ARG A 300 REMARK 465 ASP A 301 REMARK 465 SER A 302 REMARK 465 ASP A 303 REMARK 465 GLY A 304 REMARK 465 ALA A 305 REMARK 465 GLU A 306 REMARK 465 GLU A 307 REMARK 465 ASP A 308 REMARK 465 SER A 309 REMARK 465 GLY A 310 REMARK 465 SER A 311 REMARK 465 GLY A 312 REMARK 465 SER A 313 REMARK 465 GLY A 314 REMARK 465 ARG A 315 REMARK 465 GLY A 316 REMARK 465 ARG A 317 REMARK 465 GLY A 318 REMARK 465 GLY A 319 REMARK 465 SER A 320 REMARK 465 GLU A 321 REMARK 465 ASN A 322 REMARK 465 LEU A 323 REMARK 465 TYR A 324 REMARK 465 PHE A 325 REMARK 465 GLN A 326 REMARK 465 GLY A 327 REMARK 465 GLY A 328 REMARK 465 SER A 329 REMARK 465 GLY A 330 REMARK 465 SER A 331 REMARK 465 GLY A 332 REMARK 465 GLY A 333 REMARK 465 ASP A 334 REMARK 465 TYR A 335 REMARK 465 LYS A 336 REMARK 465 ASP A 337 REMARK 465 ASP A 338 REMARK 465 ASP A 339 REMARK 465 ASP A 340 REMARK 465 LYS A 341 REMARK 465 ASP A 342 REMARK 465 TYR A 343 REMARK 465 LYS A 344 REMARK 465 ASP A 345 REMARK 465 ASP A 346 REMARK 465 ASP A 347 REMARK 465 ASP A 348 REMARK 465 LYS A 349 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO C 14 41.44 -78.03 REMARK 500 ARG C 102 -2.94 67.08 REMARK 500 ALA C 104 -165.01 -114.96 REMARK 500 LEU C 105 94.93 -65.92 REMARK 500 SER C 137 -153.29 53.98 REMARK 500 ASP C 149 60.33 61.56 REMARK 500 ASN C 160 -3.37 66.29 REMARK 500 SER C 161 -9.45 70.55 REMARK 500 LYS C 219 -144.02 60.94 REMARK 500 TYR C 220 -149.14 61.01 REMARK 500 ALA D 30 -114.74 54.41 REMARK 500 LEU D 47 -55.18 -120.22 REMARK 500 SER D 52 2.07 -152.54 REMARK 500 ALA D 84 -168.50 -160.32 REMARK 500 GLU D 187 54.52 -91.75 REMARK 500 GLN D 199 46.87 -91.16 REMARK 500 ILE B 25 -53.24 -128.54 REMARK 500 ASN B 85 -150.25 55.27 REMARK 500 LEU B 117 -166.35 -79.28 REMARK 500 VAL B 118 -49.54 64.13 REMARK 500 ARG B 154 33.69 -97.18 REMARK 500 ASP B 238 -63.21 -97.43 REMARK 500 CYS A 54 -4.31 69.85 REMARK 500 ASN A 160 41.49 -107.16 REMARK 500 PRO A 235 37.36 -98.76 REMARK 500 ARG A 267 48.81 -88.21 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60686 RELATED DB: EMDB REMARK 900 GPCR ANTIBODY COMPLEX DBREF 9IMA C 1 233 PDB 9IMA 9IMA 1 233 DBREF 9IMA D 1 214 PDB 9IMA 9IMA 1 214 DBREF 9IMA B 1 308 UNP Q9NZD1 GPC5D_HUMAN 1 308 DBREF 9IMA A 1 308 UNP Q9NZD1 GPC5D_HUMAN 1 308 SEQADV 9IMA MET B -2 UNP Q9NZD1 INITIATING METHIONINE SEQADV 9IMA VAL B -1 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 0 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER B 309 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 310 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER B 311 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 312 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER B 313 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 314 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ARG B 315 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 316 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ARG B 317 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 318 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 319 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER B 320 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLU B 321 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASN B 322 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LEU B 323 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA TYR B 324 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA PHE B 325 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLN B 326 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 327 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 328 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER B 329 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 330 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER B 331 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 332 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY B 333 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 334 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA TYR B 335 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LYS B 336 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 337 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 338 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 339 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 340 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LYS B 341 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 342 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA TYR B 343 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LYS B 344 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 345 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 346 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 347 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP B 348 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LYS B 349 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA MET A -2 UNP Q9NZD1 INITIATING METHIONINE SEQADV 9IMA VAL A -1 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 0 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER A 309 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 310 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER A 311 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 312 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER A 313 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 314 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ARG A 315 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 316 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ARG A 317 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 318 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 319 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER A 320 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLU A 321 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASN A 322 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LEU A 323 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA TYR A 324 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA PHE A 325 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLN A 326 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 327 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 328 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER A 329 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 330 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA SER A 331 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 332 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA GLY A 333 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 334 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA TYR A 335 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LYS A 336 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 337 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 338 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 339 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 340 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LYS A 341 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 342 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA TYR A 343 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LYS A 344 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 345 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 346 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 347 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA ASP A 348 UNP Q9NZD1 EXPRESSION TAG SEQADV 9IMA LYS A 349 UNP Q9NZD1 EXPRESSION TAG SEQRES 1 C 233 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 233 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 233 TYR SER PHE THR GLY TYR THR MET ASN TRP VAL ARG GLN SEQRES 4 C 233 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY LEU ILE ASN SEQRES 5 C 233 PRO TYR ASN SER ASP THR ASN TYR ALA GLN LYS LEU GLN SEQRES 6 C 233 GLY ARG VAL THR MET THR THR ASP THR SER THR SER THR SEQRES 7 C 233 ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR SEQRES 8 C 233 ALA VAL TYR TYR CYS ALA ARG VAL ALA LEU ARG VAL ALA SEQRES 9 C 233 LEU ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 C 233 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 C 233 PRO CYS SER ARG SER THR SER GLU SER THR ALA ALA LEU SEQRES 12 C 233 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 C 233 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 C 233 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 C 233 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 C 233 THR LYS THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER SEQRES 17 C 233 ASN THR LYS VAL ASP LYS ARG VAL GLU SER LYS TYR GLY SEQRES 18 C 233 LEU VAL PRO ARG GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 D 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 D 214 GLN ASN VAL ALA THR HIS VAL GLY TRP TYR GLN GLN LYS SEQRES 4 D 214 PRO GLY LYS ALA PRO LYS ARG LEU ILE TYR SER ALA SER SEQRES 5 D 214 TYR ARG TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER ASN LEU SEQRES 7 D 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 D 214 ASN ARG TYR PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 352 MET VAL ASP MET TYR LYS ASP CYS ILE GLU SER THR GLY SEQRES 2 B 352 ASP TYR PHE LEU LEU CYS ASP ALA GLU GLY PRO TRP GLY SEQRES 3 B 352 ILE ILE LEU GLU SER LEU ALA ILE LEU GLY ILE VAL VAL SEQRES 4 B 352 THR ILE LEU LEU LEU LEU ALA PHE LEU PHE LEU MET ARG SEQRES 5 B 352 LYS ILE GLN ASP CYS SER GLN TRP ASN VAL LEU PRO THR SEQRES 6 B 352 GLN LEU LEU PHE LEU LEU SER VAL LEU GLY LEU PHE GLY SEQRES 7 B 352 LEU ALA PHE ALA PHE ILE ILE GLU LEU ASN GLN GLN THR SEQRES 8 B 352 ALA PRO VAL ARG TYR PHE LEU PHE GLY VAL LEU PHE ALA SEQRES 9 B 352 LEU CYS PHE SER CYS LEU LEU ALA HIS ALA SER ASN LEU SEQRES 10 B 352 VAL LYS LEU VAL ARG GLY CYS VAL SER PHE SER TRP THR SEQRES 11 B 352 THR ILE LEU CYS ILE ALA ILE GLY CYS SER LEU LEU GLN SEQRES 12 B 352 ILE ILE ILE ALA THR GLU TYR VAL THR LEU ILE MET THR SEQRES 13 B 352 ARG GLY MET MET PHE VAL ASN MET THR PRO CYS GLN LEU SEQRES 14 B 352 ASN VAL ASP PHE VAL VAL LEU LEU VAL TYR VAL LEU PHE SEQRES 15 B 352 LEU MET ALA LEU THR PHE PHE VAL SER LYS ALA THR PHE SEQRES 16 B 352 CYS GLY PRO CYS GLU ASN TRP LYS GLN HIS GLY ARG LEU SEQRES 17 B 352 ILE PHE ILE THR VAL LEU PHE SER ILE ILE ILE TRP VAL SEQRES 18 B 352 VAL TRP ILE SER MET LEU LEU ARG GLY ASN PRO GLN PHE SEQRES 19 B 352 GLN ARG GLN PRO GLN TRP ASP ASP PRO VAL VAL CYS ILE SEQRES 20 B 352 ALA LEU VAL THR ASN ALA TRP VAL PHE LEU LEU LEU TYR SEQRES 21 B 352 ILE VAL PRO GLU LEU CYS ILE LEU TYR ARG SER CYS ARG SEQRES 22 B 352 GLN GLU CYS PRO LEU GLN GLY ASN ALA CYS PRO VAL THR SEQRES 23 B 352 ALA TYR GLN HIS SER PHE GLN VAL GLU ASN GLN GLU LEU SEQRES 24 B 352 SER ARG ALA ARG ASP SER ASP GLY ALA GLU GLU ASP SER SEQRES 25 B 352 GLY SER GLY SER GLY ARG GLY ARG GLY GLY SER GLU ASN SEQRES 26 B 352 LEU TYR PHE GLN GLY GLY SER GLY SER GLY GLY ASP TYR SEQRES 27 B 352 LYS ASP ASP ASP ASP LYS ASP TYR LYS ASP ASP ASP ASP SEQRES 28 B 352 LYS SEQRES 1 A 352 MET VAL ASP MET TYR LYS ASP CYS ILE GLU SER THR GLY SEQRES 2 A 352 ASP TYR PHE LEU LEU CYS ASP ALA GLU GLY PRO TRP GLY SEQRES 3 A 352 ILE ILE LEU GLU SER LEU ALA ILE LEU GLY ILE VAL VAL SEQRES 4 A 352 THR ILE LEU LEU LEU LEU ALA PHE LEU PHE LEU MET ARG SEQRES 5 A 352 LYS ILE GLN ASP CYS SER GLN TRP ASN VAL LEU PRO THR SEQRES 6 A 352 GLN LEU LEU PHE LEU LEU SER VAL LEU GLY LEU PHE GLY SEQRES 7 A 352 LEU ALA PHE ALA PHE ILE ILE GLU LEU ASN GLN GLN THR SEQRES 8 A 352 ALA PRO VAL ARG TYR PHE LEU PHE GLY VAL LEU PHE ALA SEQRES 9 A 352 LEU CYS PHE SER CYS LEU LEU ALA HIS ALA SER ASN LEU SEQRES 10 A 352 VAL LYS LEU VAL ARG GLY CYS VAL SER PHE SER TRP THR SEQRES 11 A 352 THR ILE LEU CYS ILE ALA ILE GLY CYS SER LEU LEU GLN SEQRES 12 A 352 ILE ILE ILE ALA THR GLU TYR VAL THR LEU ILE MET THR SEQRES 13 A 352 ARG GLY MET MET PHE VAL ASN MET THR PRO CYS GLN LEU SEQRES 14 A 352 ASN VAL ASP PHE VAL VAL LEU LEU VAL TYR VAL LEU PHE SEQRES 15 A 352 LEU MET ALA LEU THR PHE PHE VAL SER LYS ALA THR PHE SEQRES 16 A 352 CYS GLY PRO CYS GLU ASN TRP LYS GLN HIS GLY ARG LEU SEQRES 17 A 352 ILE PHE ILE THR VAL LEU PHE SER ILE ILE ILE TRP VAL SEQRES 18 A 352 VAL TRP ILE SER MET LEU LEU ARG GLY ASN PRO GLN PHE SEQRES 19 A 352 GLN ARG GLN PRO GLN TRP ASP ASP PRO VAL VAL CYS ILE SEQRES 20 A 352 ALA LEU VAL THR ASN ALA TRP VAL PHE LEU LEU LEU TYR SEQRES 21 A 352 ILE VAL PRO GLU LEU CYS ILE LEU TYR ARG SER CYS ARG SEQRES 22 A 352 GLN GLU CYS PRO LEU GLN GLY ASN ALA CYS PRO VAL THR SEQRES 23 A 352 ALA TYR GLN HIS SER PHE GLN VAL GLU ASN GLN GLU LEU SEQRES 24 A 352 SER ARG ALA ARG ASP SER ASP GLY ALA GLU GLU ASP SER SEQRES 25 A 352 GLY SER GLY SER GLY ARG GLY ARG GLY GLY SER GLU ASN SEQRES 26 A 352 LEU TYR PHE GLN GLY GLY SER GLY SER GLY GLY ASP TYR SEQRES 27 A 352 LYS ASP ASP ASP ASP LYS ASP TYR LYS ASP ASP ASP ASP SEQRES 28 A 352 LYS HET CLR B 401 28 HET CLR B 402 28 HET CLR B 403 28 HET CLR A 401 28 HET CLR A 402 28 HET CLR A 403 28 HETNAM CLR CHOLESTEROL FORMUL 5 CLR 6(C27 H46 O) HELIX 1 AA1 SER C 28 TYR C 32 5 5 HELIX 2 AA2 GLN C 62 GLN C 65 5 4 HELIX 3 AA3 ARG C 87 THR C 91 5 5 HELIX 4 AA4 GLN D 79 PHE D 83 5 5 HELIX 5 AA5 SER D 121 GLY D 128 1 8 HELIX 6 AA6 LYS D 183 GLU D 187 1 5 HELIX 7 AA7 ILE B 25 ARG B 49 1 25 HELIX 8 AA8 GLN B 56 ASN B 58 5 3 HELIX 9 AA9 VAL B 59 ILE B 82 1 24 HELIX 10 AB1 THR B 88 LEU B 117 1 30 HELIX 11 AB2 SER B 125 THR B 153 1 29 HELIX 12 AB3 MET B 157 MET B 161 5 5 HELIX 13 AB4 THR B 162 LEU B 173 1 12 HELIX 14 AB5 LEU B 174 THR B 191 1 18 HELIX 15 AB6 TRP B 199 ARG B 226 1 28 HELIX 16 AB7 ARG B 226 PHE B 231 1 6 HELIX 17 AB8 ASP B 238 TYR B 257 1 20 HELIX 18 AB9 TYR B 257 SER B 268 1 12 HELIX 19 AC1 PRO A 21 PHE A 46 1 26 HELIX 20 AC2 LEU A 47 LYS A 50 5 4 HELIX 21 AC3 GLN A 56 ASN A 58 5 3 HELIX 22 AC4 VAL A 59 ILE A 82 1 24 HELIX 23 AC5 GLN A 87 ARG A 119 1 33 HELIX 24 AC6 SER A 125 CYS A 136 1 12 HELIX 25 AC7 SER A 137 ARG A 154 1 18 HELIX 26 AC8 THR A 162 LEU A 173 1 12 HELIX 27 AC9 LEU A 174 ALA A 190 1 17 HELIX 28 AD1 THR A 191 CYS A 193 5 3 HELIX 29 AD2 TRP A 199 ARG A 226 1 28 HELIX 30 AD3 ARG A 226 PHE A 231 1 6 HELIX 31 AD4 TRP A 237 TYR A 257 1 21 HELIX 32 AD5 TYR A 257 ARG A 267 1 11 SHEET 1 AA1 4 GLN C 3 GLN C 6 0 SHEET 2 AA1 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AA1 4 THR C 78 LEU C 83 -1 O MET C 81 N VAL C 20 SHEET 4 AA1 4 VAL C 68 ASP C 73 -1 N THR C 69 O GLU C 82 SHEET 1 AA2 6 GLU C 10 LYS C 12 0 SHEET 2 AA2 6 THR C 112 VAL C 116 1 O THR C 115 N LYS C 12 SHEET 3 AA2 6 ALA C 92 VAL C 99 -1 N ALA C 92 O VAL C 114 SHEET 4 AA2 6 THR C 33 GLN C 39 -1 N ASN C 35 O ALA C 97 SHEET 5 AA2 6 LEU C 45 ASN C 52 -1 O GLU C 46 N ARG C 38 SHEET 6 AA2 6 ASP C 57 TYR C 60 -1 O ASP C 57 N ASN C 52 SHEET 1 AA3 4 GLU C 10 LYS C 12 0 SHEET 2 AA3 4 THR C 112 VAL C 116 1 O THR C 115 N LYS C 12 SHEET 3 AA3 4 ALA C 92 VAL C 99 -1 N ALA C 92 O VAL C 114 SHEET 4 AA3 4 LEU C 105 TRP C 108 -1 O TYR C 107 N ARG C 98 SHEET 1 AA4 4 SER C 125 LEU C 129 0 SHEET 2 AA4 4 ALA C 141 TYR C 150 -1 O LEU C 146 N PHE C 127 SHEET 3 AA4 4 TYR C 181 VAL C 189 -1 O TYR C 181 N TYR C 150 SHEET 4 AA4 4 VAL C 168 THR C 170 -1 N HIS C 169 O VAL C 186 SHEET 1 AA5 4 SER C 125 LEU C 129 0 SHEET 2 AA5 4 ALA C 141 TYR C 150 -1 O LEU C 146 N PHE C 127 SHEET 3 AA5 4 TYR C 181 VAL C 189 -1 O TYR C 181 N TYR C 150 SHEET 4 AA5 4 VAL C 174 LEU C 175 -1 N VAL C 174 O SER C 182 SHEET 1 AA6 3 VAL C 157 TRP C 159 0 SHEET 2 AA6 3 THR C 200 VAL C 203 -1 O ASN C 202 N SER C 158 SHEET 3 AA6 3 LYS C 214 ARG C 215 -1 O LYS C 214 N CYS C 201 SHEET 1 AA7 4 MET D 4 SER D 7 0 SHEET 2 AA7 4 VAL D 19 ALA D 25 -1 O THR D 22 N SER D 7 SHEET 3 AA7 4 GLU D 70 ILE D 75 -1 O PHE D 71 N CYS D 23 SHEET 4 AA7 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AA8 6 SER D 10 ALA D 13 0 SHEET 2 AA8 6 THR D 102 ILE D 106 1 O GLU D 105 N ALA D 13 SHEET 3 AA8 6 THR D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AA8 6 VAL D 33 GLN D 38 -1 N GLN D 38 O THR D 85 SHEET 5 AA8 6 LYS D 45 TYR D 49 -1 O LYS D 45 N GLN D 37 SHEET 6 AA8 6 TYR D 53 ARG D 54 -1 O TYR D 53 N TYR D 49 SHEET 1 AA9 4 SER D 10 ALA D 13 0 SHEET 2 AA9 4 THR D 102 ILE D 106 1 O GLU D 105 N ALA D 13 SHEET 3 AA9 4 THR D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AA9 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AB1 4 VAL D 115 PHE D 118 0 SHEET 2 AB1 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AB1 4 TYR D 173 SER D 182 -1 O LEU D 175 N LEU D 136 SHEET 4 AB1 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AB2 4 ALA D 153 LEU D 154 0 SHEET 2 AB2 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AB2 4 TYR D 192 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AB2 4 VAL D 205 PHE D 209 -1 O VAL D 205 N VAL D 196 SSBOND 1 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 2 CYS C 132 CYS D 214 1555 1555 2.03 SSBOND 3 CYS C 145 CYS C 201 1555 1555 2.03 SSBOND 4 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 5 CYS D 134 CYS D 194 1555 1555 2.03 CISPEP 1 PHE C 151 PRO C 152 0 -3.77 CISPEP 2 GLU C 153 PRO C 154 0 -3.62 CISPEP 3 SER D 7 PRO D 8 0 -4.68 CISPEP 4 TYR D 94 PRO D 95 0 -0.58 CISPEP 5 TYR D 140 PRO D 141 0 2.93 CISPEP 6 GLN B 234 PRO B 235 0 1.75 CISPEP 7 GLN A 234 PRO A 235 0 -0.25 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