HEADER STRUCTURAL PROTEIN 28-JAN-25 9LQX TITLE CRYO-EM STRUCTURE OF THE JN241-9-BOUND STATE 1C OF APLNR HOMODIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: APELIN RECEPTOR; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: ANGIOTENSIN RECEPTOR-LIKE 1,G-PROTEIN COUPLED RECEPTOR APJ, COMPND 5 G-PROTEIN COUPLED RECEPTOR HG11; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: JN241-9; COMPND 9 CHAIN: D, C; COMPND 10 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: APLNR, AGTRL1, APJ; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630; SOURCE 11 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS JN241-9, APLNR, DIMER, STRUCTURAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.JI,W.WANG,Y.YANG,Q.SHEN,Y.ZHANG REVDAT 1 04-FEB-26 9LQX 0 JRNL AUTH S.JI,W.WANG,Y.YANG,Q.SHEN,Y.ZHANG JRNL TITL CRYO-EM STRUCTURE OF THE JN241-9-BOUND STATE 1C OF APLNR JRNL TITL 2 HOMODIMER JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION, 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) : 2.700 REMARK 3 NUMBER OF PARTICLES : 138605 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 9LQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 31-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1300055686. 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 : CRYO-EM STRUCTURE OF THE JN241 REMARK 245 -9-BOUND STATE 1C OF APLNR REMARK 245 HOMODIMER 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C 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 GLU A 2 REMARK 465 GLU A 3 REMARK 465 GLY A 4 REMARK 465 GLY A 5 REMARK 465 ASP A 6 REMARK 465 PHE A 7 REMARK 465 ASP A 8 REMARK 465 ASN A 9 REMARK 465 TYR A 10 REMARK 465 TYR A 11 REMARK 465 GLY A 12 REMARK 465 ALA A 13 REMARK 465 ASP A 14 REMARK 465 ASN A 15 REMARK 465 GLN A 16 REMARK 465 SER A 17 REMARK 465 GLU A 18 REMARK 465 CYS A 19 REMARK 465 GLU A 20 REMARK 465 TYR A 21 REMARK 465 THR A 22 REMARK 465 ASP A 23 REMARK 465 TRP A 24 REMARK 465 LYS A 25 REMARK 465 SER A 26 REMARK 465 SER A 27 REMARK 465 SER A 57 REMARK 465 ARG A 58 REMARK 465 GLU A 59 REMARK 465 LYS A 60 REMARK 465 VAL A 135 REMARK 465 ALA A 136 REMARK 465 ASN A 137 REMARK 465 ALA A 138 REMARK 465 ARG A 139 REMARK 465 LEU A 140 REMARK 465 ARG A 141 REMARK 465 LEU A 142 REMARK 465 ARG A 143 REMARK 465 VAL A 144 REMARK 465 GLY A 230 REMARK 465 HIS A 231 REMARK 465 PHE A 232 REMARK 465 ARG A 233 REMARK 465 LYS A 234 REMARK 465 GLU A 235 REMARK 465 ARG A 236 REMARK 465 ILE A 237 REMARK 465 GLU A 238 REMARK 465 GLY A 239 REMARK 465 LEU A 240 REMARK 465 ARG A 241 REMARK 465 LEU A 324 REMARK 465 CYS A 325 REMARK 465 CYS A 326 REMARK 465 GLY A 327 REMARK 465 GLN A 328 REMARK 465 SER A 329 REMARK 465 ARG A 330 REMARK 465 CYS A 331 REMARK 465 ALA A 332 REMARK 465 GLY A 333 REMARK 465 THR A 334 REMARK 465 SER A 335 REMARK 465 HIS A 336 REMARK 465 SER A 337 REMARK 465 SER A 338 REMARK 465 SER A 339 REMARK 465 GLY A 340 REMARK 465 GLU A 341 REMARK 465 LYS A 342 REMARK 465 SER A 343 REMARK 465 ALA A 344 REMARK 465 SER A 345 REMARK 465 TYR A 346 REMARK 465 SER A 347 REMARK 465 SER A 348 REMARK 465 GLY A 349 REMARK 465 HIS A 350 REMARK 465 SER A 351 REMARK 465 GLN A 352 REMARK 465 GLY A 353 REMARK 465 PRO A 354 REMARK 465 GLY A 355 REMARK 465 PRO A 356 REMARK 465 ASN A 357 REMARK 465 MET A 358 REMARK 465 GLY A 359 REMARK 465 LYS A 360 REMARK 465 GLY A 361 REMARK 465 GLY A 362 REMARK 465 GLU A 363 REMARK 465 GLN A 364 REMARK 465 MET A 365 REMARK 465 HIS A 366 REMARK 465 GLU A 367 REMARK 465 LYS A 368 REMARK 465 SER A 369 REMARK 465 ILE A 370 REMARK 465 PRO A 371 REMARK 465 TYR A 372 REMARK 465 SER A 373 REMARK 465 GLN A 374 REMARK 465 GLU A 375 REMARK 465 THR A 376 REMARK 465 LEU A 377 REMARK 465 VAL A 378 REMARK 465 VAL A 379 REMARK 465 ASP A 380 REMARK 465 MET B 1 REMARK 465 GLU B 2 REMARK 465 GLU B 3 REMARK 465 GLY B 4 REMARK 465 GLY B 5 REMARK 465 ASP B 6 REMARK 465 PHE B 7 REMARK 465 ASP B 8 REMARK 465 ASN B 9 REMARK 465 TYR B 10 REMARK 465 TYR B 11 REMARK 465 GLY B 12 REMARK 465 ALA B 13 REMARK 465 ASP B 14 REMARK 465 ASN B 15 REMARK 465 GLN B 16 REMARK 465 SER B 17 REMARK 465 GLU B 18 REMARK 465 CYS B 19 REMARK 465 GLU B 20 REMARK 465 TYR B 21 REMARK 465 THR B 22 REMARK 465 ASP B 23 REMARK 465 TRP B 24 REMARK 465 LYS B 25 REMARK 465 SER B 26 REMARK 465 SER B 27 REMARK 465 ALA B 136 REMARK 465 ASN B 137 REMARK 465 ALA B 138 REMARK 465 ARG B 139 REMARK 465 LEU B 140 REMARK 465 ARG B 141 REMARK 465 LEU B 142 REMARK 465 ARG B 143 REMARK 465 VAL B 144 REMARK 465 GLY B 230 REMARK 465 HIS B 231 REMARK 465 PHE B 232 REMARK 465 ARG B 233 REMARK 465 LYS B 234 REMARK 465 GLU B 235 REMARK 465 ARG B 236 REMARK 465 ILE B 237 REMARK 465 GLU B 238 REMARK 465 GLY B 239 REMARK 465 LEU B 240 REMARK 465 ARG B 241 REMARK 465 CYS B 325 REMARK 465 CYS B 326 REMARK 465 GLY B 327 REMARK 465 GLN B 328 REMARK 465 SER B 329 REMARK 465 ARG B 330 REMARK 465 CYS B 331 REMARK 465 ALA B 332 REMARK 465 GLY B 333 REMARK 465 THR B 334 REMARK 465 SER B 335 REMARK 465 HIS B 336 REMARK 465 SER B 337 REMARK 465 SER B 338 REMARK 465 SER B 339 REMARK 465 GLY B 340 REMARK 465 GLU B 341 REMARK 465 LYS B 342 REMARK 465 SER B 343 REMARK 465 ALA B 344 REMARK 465 SER B 345 REMARK 465 TYR B 346 REMARK 465 SER B 347 REMARK 465 SER B 348 REMARK 465 GLY B 349 REMARK 465 HIS B 350 REMARK 465 SER B 351 REMARK 465 GLN B 352 REMARK 465 GLY B 353 REMARK 465 PRO B 354 REMARK 465 GLY B 355 REMARK 465 PRO B 356 REMARK 465 ASN B 357 REMARK 465 MET B 358 REMARK 465 GLY B 359 REMARK 465 LYS B 360 REMARK 465 GLY B 361 REMARK 465 GLY B 362 REMARK 465 GLU B 363 REMARK 465 GLN B 364 REMARK 465 MET B 365 REMARK 465 HIS B 366 REMARK 465 GLU B 367 REMARK 465 LYS B 368 REMARK 465 SER B 369 REMARK 465 ILE B 370 REMARK 465 PRO B 371 REMARK 465 TYR B 372 REMARK 465 SER B 373 REMARK 465 GLN B 374 REMARK 465 GLU B 375 REMARK 465 THR B 376 REMARK 465 LEU B 377 REMARK 465 VAL B 378 REMARK 465 VAL B 379 REMARK 465 ASP B 380 REMARK 465 SER D 130 REMARK 465 SER C 130 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 SER A 145 OG REMARK 470 SER B 57 OG REMARK 470 ARG B 58 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 59 CG CD OE1 OE2 REMARK 470 LYS B 60 CG CD CE NZ REMARK 470 GLN D 3 CG CD OE1 NE2 REMARK 470 SER D 11 OG REMARK 470 GLN D 13 CG CD OE1 NE2 REMARK 470 PRO D 41 CG CD REMARK 470 LYS D 43 CG CD CE NZ REMARK 470 GLU D 44 CG CD OE1 OE2 REMARK 470 GLU D 46 CG CD OE1 OE2 REMARK 470 THR D 68 OG1 CG2 REMARK 470 GLN D 71 CG CD OE1 NE2 REMARK 470 ASP D 72 CG OD1 OD2 REMARK 470 LYS D 86 CG CD CE NZ REMARK 470 GLN D 122 CG CD OE1 NE2 REMARK 470 THR D 127 OG1 CG2 REMARK 470 SER D 129 OG REMARK 470 SER C 11 OG REMARK 470 VAL C 12 CG1 CG2 REMARK 470 GLN C 13 CG CD OE1 NE2 REMARK 470 SER C 14 OG REMARK 470 PRO C 41 CG CD REMARK 470 VAL C 63 CG1 CG2 REMARK 470 ARG C 66 CG CD NE CZ NH1 NH2 REMARK 470 LEU C 85 CG CD1 CD2 REMARK 470 SER C 129 OG 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 SER A 63 -19.99 -48.84 REMARK 500 PHE A 210 -35.90 -131.49 REMARK 500 HIS A 278 -68.61 64.38 REMARK 500 TRP A 279 164.71 63.20 REMARK 500 SER B 56 -138.51 47.29 REMARK 500 GLU B 59 -121.56 48.18 REMARK 500 PHE B 210 -35.53 -131.51 REMARK 500 ALA D 40 -93.51 -54.70 REMARK 500 GLN C 39 79.70 -153.20 REMARK 500 PRO C 41 -151.29 -106.50 REMARK 500 ALA C 49 117.68 -164.54 REMARK 500 GLU C 104 -145.17 -71.80 REMARK 500 SER C 106 -26.82 -150.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63308 RELATED DB: EMDB REMARK 900 JN241-9-BOUND APLNR DIMER INTERMEDIATE-STATE 1C DBREF 9LQX A 1 380 UNP P35414 APJ_HUMAN 1 380 DBREF 9LQX B 1 380 UNP P35414 APJ_HUMAN 1 380 DBREF 9LQX D 1 130 PDB 9LQX 9LQX 1 130 DBREF 9LQX C 1 130 PDB 9LQX 9LQX 1 130 SEQRES 1 A 380 MET GLU GLU GLY GLY ASP PHE ASP ASN TYR TYR GLY ALA SEQRES 2 A 380 ASP ASN GLN SER GLU CYS GLU TYR THR ASP TRP LYS SER SEQRES 3 A 380 SER GLY ALA LEU ILE PRO ALA ILE TYR MET LEU VAL PHE SEQRES 4 A 380 LEU LEU GLY THR THR GLY ASN GLY LEU VAL LEU TRP THR SEQRES 5 A 380 VAL PHE ARG SER SER ARG GLU LYS ARG ARG SER ALA ASP SEQRES 6 A 380 ILE PHE ILE ALA SER LEU ALA VAL ALA ASP LEU THR PHE SEQRES 7 A 380 VAL VAL THR LEU PRO LEU TRP ALA THR TYR THR TYR ARG SEQRES 8 A 380 ASP TYR ASP TRP PRO PHE GLY THR PHE PHE CYS LYS LEU SEQRES 9 A 380 SER SER TYR LEU ILE PHE VAL ASN MET TYR ALA SER VAL SEQRES 10 A 380 PHE CYS LEU THR GLY LEU SER PHE ASP ARG TYR LEU ALA SEQRES 11 A 380 ILE VAL ARG PRO VAL ALA ASN ALA ARG LEU ARG LEU ARG SEQRES 12 A 380 VAL SER GLY ALA VAL ALA THR ALA VAL LEU TRP VAL LEU SEQRES 13 A 380 ALA ALA LEU LEU ALA MET PRO VAL MET VAL LEU ARG THR SEQRES 14 A 380 THR GLY ASP LEU GLU ASN THR THR LYS VAL GLN CYS TYR SEQRES 15 A 380 MET ASP TYR SER MET VAL ALA THR VAL SER SER GLU TRP SEQRES 16 A 380 ALA TRP GLU VAL GLY LEU GLY VAL SER SER THR THR VAL SEQRES 17 A 380 GLY PHE VAL VAL PRO PHE THR ILE MET LEU THR CYS TYR SEQRES 18 A 380 PHE PHE ILE ALA GLN THR ILE ALA GLY HIS PHE ARG LYS SEQRES 19 A 380 GLU ARG ILE GLU GLY LEU ARG LYS ARG ARG ARG LEU LEU SEQRES 20 A 380 SER ILE ILE VAL VAL LEU VAL VAL THR PHE ALA LEU CYS SEQRES 21 A 380 TRP MET PRO TYR HIS LEU VAL LYS THR LEU TYR MET LEU SEQRES 22 A 380 GLY SER LEU LEU HIS TRP PRO CYS ASP PHE ASP LEU PHE SEQRES 23 A 380 LEU MET ASN ILE PHE PRO TYR CYS THR CYS ILE SER TYR SEQRES 24 A 380 VAL ASN SER CYS LEU ASN PRO PHE LEU TYR ALA PHE PHE SEQRES 25 A 380 ASP PRO ARG PHE ARG GLN ALA CYS THR SER MET LEU CYS SEQRES 26 A 380 CYS GLY GLN SER ARG CYS ALA GLY THR SER HIS SER SER SEQRES 27 A 380 SER GLY GLU LYS SER ALA SER TYR SER SER GLY HIS SER SEQRES 28 A 380 GLN GLY PRO GLY PRO ASN MET GLY LYS GLY GLY GLU GLN SEQRES 29 A 380 MET HIS GLU LYS SER ILE PRO TYR SER GLN GLU THR LEU SEQRES 30 A 380 VAL VAL ASP SEQRES 1 B 380 MET GLU GLU GLY GLY ASP PHE ASP ASN TYR TYR GLY ALA SEQRES 2 B 380 ASP ASN GLN SER GLU CYS GLU TYR THR ASP TRP LYS SER SEQRES 3 B 380 SER GLY ALA LEU ILE PRO ALA ILE TYR MET LEU VAL PHE SEQRES 4 B 380 LEU LEU GLY THR THR GLY ASN GLY LEU VAL LEU TRP THR SEQRES 5 B 380 VAL PHE ARG SER SER ARG GLU LYS ARG ARG SER ALA ASP SEQRES 6 B 380 ILE PHE ILE ALA SER LEU ALA VAL ALA ASP LEU THR PHE SEQRES 7 B 380 VAL VAL THR LEU PRO LEU TRP ALA THR TYR THR TYR ARG SEQRES 8 B 380 ASP TYR ASP TRP PRO PHE GLY THR PHE PHE CYS LYS LEU SEQRES 9 B 380 SER SER TYR LEU ILE PHE VAL ASN MET TYR ALA SER VAL SEQRES 10 B 380 PHE CYS LEU THR GLY LEU SER PHE ASP ARG TYR LEU ALA SEQRES 11 B 380 ILE VAL ARG PRO VAL ALA ASN ALA ARG LEU ARG LEU ARG SEQRES 12 B 380 VAL SER GLY ALA VAL ALA THR ALA VAL LEU TRP VAL LEU SEQRES 13 B 380 ALA ALA LEU LEU ALA MET PRO VAL MET VAL LEU ARG THR SEQRES 14 B 380 THR GLY ASP LEU GLU ASN THR THR LYS VAL GLN CYS TYR SEQRES 15 B 380 MET ASP TYR SER MET VAL ALA THR VAL SER SER GLU TRP SEQRES 16 B 380 ALA TRP GLU VAL GLY LEU GLY VAL SER SER THR THR VAL SEQRES 17 B 380 GLY PHE VAL VAL PRO PHE THR ILE MET LEU THR CYS TYR SEQRES 18 B 380 PHE PHE ILE ALA GLN THR ILE ALA GLY HIS PHE ARG LYS SEQRES 19 B 380 GLU ARG ILE GLU GLY LEU ARG LYS ARG ARG ARG LEU LEU SEQRES 20 B 380 SER ILE ILE VAL VAL LEU VAL VAL THR PHE ALA LEU CYS SEQRES 21 B 380 TRP MET PRO TYR HIS LEU VAL LYS THR LEU TYR MET LEU SEQRES 22 B 380 GLY SER LEU LEU HIS TRP PRO CYS ASP PHE ASP LEU PHE SEQRES 23 B 380 LEU MET ASN ILE PHE PRO TYR CYS THR CYS ILE SER TYR SEQRES 24 B 380 VAL ASN SER CYS LEU ASN PRO PHE LEU TYR ALA PHE PHE SEQRES 25 B 380 ASP PRO ARG PHE ARG GLN ALA CYS THR SER MET LEU CYS SEQRES 26 B 380 CYS GLY GLN SER ARG CYS ALA GLY THR SER HIS SER SER SEQRES 27 B 380 SER GLY GLU LYS SER ALA SER TYR SER SER GLY HIS SER SEQRES 28 B 380 GLN GLY PRO GLY PRO ASN MET GLY LYS GLY GLY GLU GLN SEQRES 29 B 380 MET HIS GLU LYS SER ILE PRO TYR SER GLN GLU THR LEU SEQRES 30 B 380 VAL VAL ASP SEQRES 1 D 130 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 D 130 SER GLY GLY SER LEU THR LEU SER CYS ALA ALA SER GLY SEQRES 3 D 130 SER THR TYR SER SER HIS CYS MET GLY TRP PHE ARG GLN SEQRES 4 D 130 ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA LEU MET THR SEQRES 5 D 130 ARG SER ARG GLY THR SER TYR ALA ASP SER VAL LYS GLY SEQRES 6 D 130 ARG PHE THR ILE SER GLN ASP ASN THR LYS ASN ILE LEU SEQRES 7 D 130 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 D 130 MET TYR TYR CYS ALA ALA VAL PRO ARG ALA GLY ILE GLU SEQRES 9 D 130 TYR SER GLY ALA TYR CYS LYS TRP ASN MET LYS ASP SER SEQRES 10 D 130 GLY SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 C 130 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 C 130 SER GLY GLY SER LEU THR LEU SER CYS ALA ALA SER GLY SEQRES 3 C 130 SER THR TYR SER SER HIS CYS MET GLY TRP PHE ARG GLN SEQRES 4 C 130 ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA LEU MET THR SEQRES 5 C 130 ARG SER ARG GLY THR SER TYR ALA ASP SER VAL LYS GLY SEQRES 6 C 130 ARG PHE THR ILE SER GLN ASP ASN THR LYS ASN ILE LEU SEQRES 7 C 130 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 C 130 MET TYR TYR CYS ALA ALA VAL PRO ARG ALA GLY ILE GLU SEQRES 9 C 130 TYR SER GLY ALA TYR CYS LYS TRP ASN MET LYS ASP SER SEQRES 10 C 130 GLY SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HET CLR A 401 28 HET CLR A 402 28 HET CLR A 403 28 HET CLR A 404 28 HET CLR A 405 28 HET CLR A 406 28 HET CLR A 407 28 HET CLR A 408 28 HET CLR A 409 28 HET PCF B 401 50 HET PCF B 402 50 HET PCF B 403 50 HET CLR B 404 28 HET CLR B 405 28 HET CLR B 406 28 HET CLR B 407 28 HET CLR B 408 28 HET CLR B 409 28 HET CLR B 410 28 HETNAM CLR CHOLESTEROL HETNAM PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE FORMUL 5 CLR 16(C27 H46 O) FORMUL 14 PCF 3(C40 H80 N O8 P) HELIX 1 AA1 ALA A 29 ARG A 55 1 27 HELIX 2 AA2 ALA A 64 VAL A 80 1 17 HELIX 3 AA3 THR A 81 ARG A 91 1 11 HELIX 4 AA4 GLY A 98 VAL A 132 1 35 HELIX 5 AA5 GLY A 146 ALA A 161 1 16 HELIX 6 AA6 ALA A 161 LEU A 167 1 7 HELIX 7 AA7 ASP A 172 THR A 176 5 5 HELIX 8 AA8 SER A 193 ALA A 229 1 37 HELIX 9 AA9 ARG A 244 LEU A 273 1 30 HELIX 10 AB1 PRO A 280 ASN A 301 1 22 HELIX 11 AB2 LEU A 304 ASP A 313 1 10 HELIX 12 AB3 ASP A 313 MET A 323 1 11 HELIX 13 AB4 ALA B 29 PHE B 54 1 26 HELIX 14 AB5 ARG B 62 VAL B 80 1 19 HELIX 15 AB6 THR B 81 ARG B 91 1 11 HELIX 16 AB7 GLY B 98 VAL B 132 1 35 HELIX 17 AB8 GLY B 146 ALA B 161 1 16 HELIX 18 AB9 ALA B 161 LEU B 167 1 7 HELIX 19 AC1 ASP B 172 THR B 176 5 5 HELIX 20 AC2 SER B 193 ALA B 229 1 37 HELIX 21 AC3 ARG B 244 LEU B 273 1 30 HELIX 22 AC4 PRO B 280 ASN B 301 1 22 HELIX 23 AC5 LEU B 304 ASP B 313 1 10 HELIX 24 AC6 ASP B 313 LEU B 324 1 12 HELIX 25 AC7 LYS D 86 THR D 90 5 5 HELIX 26 AC8 LYS C 86 THR C 90 5 5 SHEET 1 AA1 2 ARG A 168 GLY A 171 0 SHEET 2 AA1 2 GLN A 180 MET A 183 -1 O GLN A 180 N GLY A 171 SHEET 1 AA2 2 ARG B 168 GLY B 171 0 SHEET 2 AA2 2 GLN B 180 MET B 183 -1 O GLN B 180 N GLY B 171 SHEET 1 AA3 4 GLN D 3 SER D 7 0 SHEET 2 AA3 4 LEU D 18 SER D 25 -1 O SER D 21 N SER D 7 SHEET 3 AA3 4 ILE D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AA3 4 PHE D 67 ASP D 72 -1 N SER D 70 O TYR D 79 SHEET 1 AA4 6 SER D 11 GLN D 13 0 SHEET 2 AA4 6 THR D 124 SER D 129 1 O THR D 127 N VAL D 12 SHEET 3 AA4 6 ALA D 91 PRO D 99 -1 N TYR D 93 O THR D 124 SHEET 4 AA4 6 HIS D 32 GLN D 39 -1 N CYS D 33 O VAL D 98 SHEET 5 AA4 6 GLU D 46 MET D 51 -1 O VAL D 48 N TRP D 36 SHEET 6 AA4 6 THR D 57 TYR D 59 -1 O SER D 58 N LEU D 50 SHEET 1 AA5 4 SER D 11 GLN D 13 0 SHEET 2 AA5 4 THR D 124 SER D 129 1 O THR D 127 N VAL D 12 SHEET 3 AA5 4 ALA D 91 PRO D 99 -1 N TYR D 93 O THR D 124 SHEET 4 AA5 4 SER D 119 TRP D 120 -1 O SER D 119 N ALA D 97 SHEET 1 AA6 4 GLN C 3 SER C 7 0 SHEET 2 AA6 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AA6 4 ILE C 77 MET C 82 -1 O LEU C 78 N CYS C 22 SHEET 4 AA6 4 PHE C 67 SER C 70 -1 N SER C 70 O TYR C 79 SHEET 1 AA7 4 THR C 57 TYR C 59 0 SHEET 2 AA7 4 GLU C 46 MET C 51 -1 N LEU C 50 O SER C 58 SHEET 3 AA7 4 HIS C 32 ARG C 38 -1 N TRP C 36 O ALA C 49 SHEET 4 AA7 4 TYR C 93 PRO C 99 -1 O VAL C 98 N CYS C 33 SSBOND 1 CYS A 102 CYS A 181 1555 1555 2.03 SSBOND 2 CYS B 102 CYS B 181 1555 1555 2.03 SSBOND 3 CYS D 22 CYS D 95 1555 1555 2.03 SSBOND 4 CYS D 33 CYS D 110 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 95 1555 1555 2.03 SSBOND 6 CYS C 33 CYS C 110 1555 1555 2.03 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