HEADER MEMBRANE PROTEIN 10-MAY-24 9FAT TITLE CRYOEM STRUCTURE OF HUMAN FULL-LENGTH ALPHA1BETA3GAMMA2 GABA(A)R IN TITLE 2 COMPLEX WITH GARLH4, THE TMD OF NEUROLIGIN2, MEGABODY38 AND TITLE 3 PREGNENOLONE SULFATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-1; COMPND 3 CHAIN: A, D; COMPND 4 SYNONYM: GABA(A) RECEPTOR SUBUNIT ALPHA-1,GABAAR SUBUNIT ALPHA-1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-3; COMPND 8 CHAIN: B, E; COMPND 9 SYNONYM: GABA(A) RECEPTOR SUBUNIT BETA-3,GABAAR SUBUNIT BETA-3; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: ISOFORM 2 OF GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT COMPND 13 GAMMA-2; COMPND 14 CHAIN: C; COMPND 15 SYNONYM: GABA(A) RECEPTOR SUBUNIT GAMMA-2,GABAAR SUBUNIT GAMMA-2; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: MEGABODY38; COMPND 19 CHAIN: G; COMPND 20 ENGINEERED: YES; COMPND 21 OTHER_DETAILS: THIS MEGABODY IS A CHIMERIC PROTEIN DESIGNED AND COMPND 22 CONSTRUCTED BASED ON A CIRCULAR PERMUTATION OF A NANOBODY (RAISED COMPND 23 AGAINST GABA(A) RECEPTOR SUBUNITS, IN LLAMA) AND HELICOBACTER PYLORI COMPND 24 PROTEIN, HOPQ (UNIPROT ID: B5Z8H1).; COMPND 25 MOL_ID: 5; COMPND 26 MOLECULE: NEUROLIGIN-2; COMPND 27 CHAIN: H; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 6; COMPND 30 MOLECULE: LHFPL TETRASPAN SUBFAMILY MEMBER 4 PROTEIN; COMPND 31 CHAIN: L; COMPND 32 SYNONYM: GABAA RECEPTOR REGULATORY LHFPL4,LIPOMA HMGIC FUSION COMPND 33 PARTNER-LIKE 4 PROTEIN; COMPND 34 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: GABRA1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-TETR; SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 10 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 11 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 12 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PCDNA4-TO-ZEOCIN; SOURCE 15 MOL_ID: 2; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GABRB3; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_STRAIN: HEK293S; SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-TETR; SOURCE 24 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 25 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 26 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 27 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PCDNA4-TO-HYGROMYCIN-B; SOURCE 30 MOL_ID: 3; SOURCE 31 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 32 ORGANISM_COMMON: HUMAN; SOURCE 33 ORGANISM_TAXID: 9606; SOURCE 34 GENE: GABRG2; SOURCE 35 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 36 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 37 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-TETR; SOURCE 38 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 39 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 40 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 41 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 42 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 43 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 44 MOL_ID: 4; SOURCE 45 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 46 ORGANISM_TAXID: 9844; SOURCE 47 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 48 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 49 EXPRESSION_SYSTEM_STRAIN: WK6SU-; SOURCE 50 EXPRESSION_SYSTEM_PLASMID: PMESD2; SOURCE 51 MOL_ID: 5; SOURCE 52 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 53 ORGANISM_COMMON: HUMAN; SOURCE 54 ORGANISM_TAXID: 9606; SOURCE 55 GENE: NLGN2, KIAA1366; SOURCE 56 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 57 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 58 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-TETR; SOURCE 59 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 60 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 61 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 62 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 63 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 64 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 65 MOL_ID: 6; SOURCE 66 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 67 ORGANISM_COMMON: HUMAN; SOURCE 68 ORGANISM_TAXID: 9606; SOURCE 69 GENE: LHFPL4, GARLH4; SOURCE 70 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 71 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 72 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-TETR; SOURCE 73 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 74 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 75 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 76 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 77 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 78 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2 KEYWDS GABA, NEUROTRANSMISSION, TERNARY COMPLEX, INHIBITORY SYNAPSE, KEYWDS 2 NEUROSTEROID, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR V.B.KASARAGOD,A.R.ARICESCU REVDAT 1 02-JUL-25 9FAT 0 JRNL AUTH V.B.KASARAGOD,A.R.ARICESCU JRNL TITL CRYOEM STRUCTURE OF HUMAN FULL-LENGTH ALPHA1BETA3GAMMA2 JRNL TITL 2 GABA(A)R IN COMPLEX WITH GARLH4, THE TMD OF NEUROLIGIN2, JRNL TITL 3 MEGABODY38 AND PREGNENOLONE SULFATE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : WARP, EPU, CTFFIND, PHENIX, CRYOSPARC, REMARK 3 RELION, RELION, RELION, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6HUK REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER REMARK 3 REFINEMENT TARGET : FSC AT 0.5 REMARK 3 OVERALL ANISOTROPIC B VALUE : 45.000 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) : 3.600 REMARK 3 NUMBER OF PARTICLES : 20534 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 9FAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1292138345. 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 : CRYOEM STRUCTURE OF HUMAN FULL REMARK 245 -LENGTH ALPHA1BETA3GAMMA2 REMARK 245 GABA(A)R IN COMPLEX WITH GARLH4, REMARK 245 THE TMD OF NEUROLIGIN2, REMARK 245 MEGABODY38 AND PREGNENOLONE REMARK 245 SULFATE REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : CURRENT: 30 MA REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 8892 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) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 3113.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 96000 REMARK 245 CALIBRATED MAGNIFICATION : 96000 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: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, G, H, L, F, I, REMARK 350 AND CHAINS: J, K, M, N, O 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 PRO A 327 REMARK 465 LYS A 328 REMARK 465 LYS A 329 REMARK 465 VAL A 330 REMARK 465 LYS A 331 REMARK 465 ASP A 332 REMARK 465 PRO A 333 REMARK 465 LEU A 334 REMARK 465 ILE A 335 REMARK 465 LYS A 336 REMARK 465 LYS A 337 REMARK 465 ASN A 338 REMARK 465 ASN A 339 REMARK 465 THR A 340 REMARK 465 TYR A 341 REMARK 465 ALA A 342 REMARK 465 PRO A 343 REMARK 465 THR A 344 REMARK 465 ALA A 345 REMARK 465 THR A 346 REMARK 465 SER A 347 REMARK 465 TYR A 348 REMARK 465 THR A 349 REMARK 465 PRO A 350 REMARK 465 ASN A 351 REMARK 465 LEU A 352 REMARK 465 ALA A 353 REMARK 465 ARG A 354 REMARK 465 GLY A 355 REMARK 465 ASP A 356 REMARK 465 PRO A 357 REMARK 465 GLY A 358 REMARK 465 LEU A 359 REMARK 465 ALA A 360 REMARK 465 THR A 361 REMARK 465 ILE A 362 REMARK 465 ALA A 363 REMARK 465 LYS A 364 REMARK 465 SER A 365 REMARK 465 ALA A 366 REMARK 465 THR A 367 REMARK 465 ILE A 368 REMARK 465 GLU A 369 REMARK 465 PRO A 370 REMARK 465 LYS A 371 REMARK 465 GLU A 372 REMARK 465 VAL A 373 REMARK 465 LYS A 374 REMARK 465 PRO A 375 REMARK 465 GLU A 376 REMARK 465 THR A 377 REMARK 465 LYS A 378 REMARK 465 PRO A 379 REMARK 465 PRO A 380 REMARK 465 GLU A 381 REMARK 465 PRO A 382 REMARK 465 LYS A 383 REMARK 465 GLY B 7 REMARK 465 ALA B 318 REMARK 465 GLU B 319 REMARK 465 LYS B 320 REMARK 465 THR B 321 REMARK 465 ALA B 322 REMARK 465 LYS B 323 REMARK 465 ALA B 324 REMARK 465 LYS B 325 REMARK 465 ASN B 326 REMARK 465 ASP B 327 REMARK 465 ARG B 328 REMARK 465 SER B 329 REMARK 465 LYS B 330 REMARK 465 SER B 331 REMARK 465 GLU B 332 REMARK 465 SER B 333 REMARK 465 ASN B 334 REMARK 465 ARG B 335 REMARK 465 VAL B 336 REMARK 465 ASP B 337 REMARK 465 ALA B 338 REMARK 465 HIS B 339 REMARK 465 GLY B 340 REMARK 465 ASN B 341 REMARK 465 ILE B 342 REMARK 465 LEU B 343 REMARK 465 LEU B 344 REMARK 465 THR B 345 REMARK 465 SER B 346 REMARK 465 LEU B 347 REMARK 465 GLU B 348 REMARK 465 VAL B 349 REMARK 465 HIS B 350 REMARK 465 ASN B 351 REMARK 465 GLU B 352 REMARK 465 MET B 353 REMARK 465 ASN B 354 REMARK 465 GLU B 355 REMARK 465 VAL B 356 REMARK 465 SER B 357 REMARK 465 GLY B 358 REMARK 465 GLY B 359 REMARK 465 ILE B 360 REMARK 465 GLY B 361 REMARK 465 ASP B 362 REMARK 465 THR B 363 REMARK 465 ARG B 364 REMARK 465 ASN B 365 REMARK 465 SER B 366 REMARK 465 ALA B 367 REMARK 465 ILE B 368 REMARK 465 SER B 369 REMARK 465 PHE B 370 REMARK 465 ASP B 371 REMARK 465 ASN B 372 REMARK 465 SER B 373 REMARK 465 GLY B 374 REMARK 465 ILE B 375 REMARK 465 GLN B 376 REMARK 465 TYR B 377 REMARK 465 ARG B 378 REMARK 465 LYS B 379 REMARK 465 GLN B 380 REMARK 465 SER B 381 REMARK 465 MET B 382 REMARK 465 PRO B 383 REMARK 465 ARG B 384 REMARK 465 GLU B 385 REMARK 465 GLY B 386 REMARK 465 HIS B 387 REMARK 465 GLY B 388 REMARK 465 ARG B 389 REMARK 465 PHE B 390 REMARK 465 LEU B 391 REMARK 465 GLY B 392 REMARK 465 ASP B 393 REMARK 465 ARG B 394 REMARK 465 SER B 395 REMARK 465 LEU B 396 REMARK 465 PRO B 397 REMARK 465 HIS B 398 REMARK 465 LYS B 399 REMARK 465 LYS B 400 REMARK 465 THR B 401 REMARK 465 HIS B 402 REMARK 465 LEU B 403 REMARK 465 ARG B 404 REMARK 465 ARG B 405 REMARK 465 ARG B 406 REMARK 465 SER B 407 REMARK 465 SER B 408 REMARK 465 GLN B 409 REMARK 465 LEU B 410 REMARK 465 LYS B 411 REMARK 465 ILE B 412 REMARK 465 PRO C 326 REMARK 465 SER C 327 REMARK 465 LYS C 328 REMARK 465 ASP C 329 REMARK 465 LYS C 330 REMARK 465 ASP C 331 REMARK 465 LYS C 332 REMARK 465 LYS C 333 REMARK 465 LYS C 334 REMARK 465 LYS C 335 REMARK 465 ASN C 336 REMARK 465 PRO C 337 REMARK 465 ALA C 338 REMARK 465 PRO C 339 REMARK 465 THR C 340 REMARK 465 ILE C 341 REMARK 465 ASP C 342 REMARK 465 ILE C 343 REMARK 465 ARG C 344 REMARK 465 PRO C 345 REMARK 465 ARG C 346 REMARK 465 SER C 347 REMARK 465 ALA C 348 REMARK 465 THR C 349 REMARK 465 ILE C 350 REMARK 465 GLN C 351 REMARK 465 MET C 352 REMARK 465 ASN C 353 REMARK 465 ASN C 354 REMARK 465 ALA C 355 REMARK 465 THR C 356 REMARK 465 HIS C 357 REMARK 465 LEU C 358 REMARK 465 GLN C 359 REMARK 465 GLU C 360 REMARK 465 ARG C 361 REMARK 465 ASP C 362 REMARK 465 GLU C 363 REMARK 465 GLU C 364 REMARK 465 TYR C 365 REMARK 465 GLY C 366 REMARK 465 TYR C 367 REMARK 465 GLU C 368 REMARK 465 ARG C 386 REMARK 465 THR C 387 REMARK 465 GLY C 388 REMARK 465 ALA C 389 REMARK 465 TRP C 390 REMARK 465 ARG C 391 REMARK 465 HIS C 392 REMARK 465 GLY C 393 REMARK 465 ARG C 394 REMARK 465 ILE C 395 REMARK 465 LYS D 328 REMARK 465 LYS D 329 REMARK 465 VAL D 330 REMARK 465 LYS D 331 REMARK 465 ASP D 332 REMARK 465 PRO D 333 REMARK 465 LEU D 334 REMARK 465 ILE D 335 REMARK 465 LYS D 336 REMARK 465 LYS D 337 REMARK 465 ASN D 338 REMARK 465 ASN D 339 REMARK 465 THR D 340 REMARK 465 TYR D 341 REMARK 465 ALA D 342 REMARK 465 PRO D 343 REMARK 465 THR D 344 REMARK 465 ALA D 345 REMARK 465 THR D 346 REMARK 465 SER D 347 REMARK 465 TYR D 348 REMARK 465 THR D 349 REMARK 465 PRO D 350 REMARK 465 ASN D 351 REMARK 465 LEU D 352 REMARK 465 ALA D 353 REMARK 465 ARG D 354 REMARK 465 GLY D 355 REMARK 465 ASP D 356 REMARK 465 PRO D 357 REMARK 465 GLY D 358 REMARK 465 LEU D 359 REMARK 465 ALA D 360 REMARK 465 THR D 361 REMARK 465 ILE D 362 REMARK 465 ALA D 363 REMARK 465 LYS D 364 REMARK 465 SER D 365 REMARK 465 ALA D 366 REMARK 465 THR D 367 REMARK 465 ILE D 368 REMARK 465 GLU D 369 REMARK 465 PRO D 370 REMARK 465 LYS D 371 REMARK 465 GLU D 372 REMARK 465 VAL D 373 REMARK 465 LYS D 374 REMARK 465 PRO D 375 REMARK 465 GLU D 376 REMARK 465 THR D 377 REMARK 465 LYS D 378 REMARK 465 PRO D 379 REMARK 465 PRO D 380 REMARK 465 GLU D 381 REMARK 465 PRO D 382 REMARK 465 GLU D 419 REMARK 465 PRO D 420 REMARK 465 GLN D 421 REMARK 465 LEU D 422 REMARK 465 ALA E 318 REMARK 465 GLU E 319 REMARK 465 LYS E 320 REMARK 465 THR E 321 REMARK 465 ALA E 322 REMARK 465 LYS E 323 REMARK 465 ALA E 324 REMARK 465 LYS E 325 REMARK 465 ASN E 326 REMARK 465 ASP E 327 REMARK 465 ARG E 328 REMARK 465 SER E 329 REMARK 465 LYS E 330 REMARK 465 SER E 331 REMARK 465 GLU E 332 REMARK 465 SER E 333 REMARK 465 ASN E 334 REMARK 465 ARG E 335 REMARK 465 VAL E 336 REMARK 465 ASP E 337 REMARK 465 ALA E 338 REMARK 465 HIS E 339 REMARK 465 GLY E 340 REMARK 465 ASN E 341 REMARK 465 ILE E 342 REMARK 465 LEU E 343 REMARK 465 LEU E 344 REMARK 465 THR E 345 REMARK 465 SER E 346 REMARK 465 LEU E 347 REMARK 465 GLU E 348 REMARK 465 VAL E 349 REMARK 465 HIS E 350 REMARK 465 ASN E 351 REMARK 465 GLU E 352 REMARK 465 MET E 353 REMARK 465 ASN E 354 REMARK 465 GLU E 355 REMARK 465 VAL E 356 REMARK 465 SER E 357 REMARK 465 GLY E 358 REMARK 465 GLY E 359 REMARK 465 ILE E 360 REMARK 465 GLY E 361 REMARK 465 ASP E 362 REMARK 465 THR E 363 REMARK 465 ARG E 364 REMARK 465 ASN E 365 REMARK 465 SER E 366 REMARK 465 ALA E 367 REMARK 465 ILE E 368 REMARK 465 SER E 369 REMARK 465 PHE E 370 REMARK 465 ASP E 371 REMARK 465 ASN E 372 REMARK 465 SER E 373 REMARK 465 GLY E 374 REMARK 465 ILE E 375 REMARK 465 GLN E 376 REMARK 465 TYR E 377 REMARK 465 ARG E 378 REMARK 465 LYS E 379 REMARK 465 GLN E 380 REMARK 465 SER E 381 REMARK 465 MET E 382 REMARK 465 PRO E 383 REMARK 465 ARG E 384 REMARK 465 GLU E 385 REMARK 465 GLY E 386 REMARK 465 HIS E 387 REMARK 465 GLY E 388 REMARK 465 ARG E 389 REMARK 465 PHE E 390 REMARK 465 LEU E 391 REMARK 465 GLY E 392 REMARK 465 ASP E 393 REMARK 465 ARG E 394 REMARK 465 SER E 395 REMARK 465 LEU E 396 REMARK 465 PRO E 397 REMARK 465 HIS E 398 REMARK 465 LYS E 399 REMARK 465 LYS E 400 REMARK 465 THR E 401 REMARK 465 HIS E 402 REMARK 465 LEU E 403 REMARK 465 ARG E 404 REMARK 465 ARG E 405 REMARK 465 ARG E 406 REMARK 465 SER E 407 REMARK 465 SER E 408 REMARK 465 GLN E 409 REMARK 465 LEU E 410 REMARK 465 LYS E 411 REMARK 465 THR G 14 REMARK 465 LYS G 15 REMARK 465 THR G 16 REMARK 465 THR G 17 REMARK 465 THR G 18 REMARK 465 SER G 19 REMARK 465 VAL G 20 REMARK 465 ILE G 21 REMARK 465 ASP G 22 REMARK 465 THR G 23 REMARK 465 THR G 24 REMARK 465 ASN G 25 REMARK 465 ASP G 26 REMARK 465 ALA G 27 REMARK 465 GLN G 28 REMARK 465 ASN G 29 REMARK 465 LEU G 30 REMARK 465 LEU G 31 REMARK 465 THR G 32 REMARK 465 GLN G 33 REMARK 465 ALA G 34 REMARK 465 GLN G 35 REMARK 465 THR G 36 REMARK 465 ILE G 37 REMARK 465 VAL G 38 REMARK 465 ASN G 39 REMARK 465 THR G 40 REMARK 465 LEU G 41 REMARK 465 LYS G 42 REMARK 465 ASP G 43 REMARK 465 TYR G 44 REMARK 465 CYS G 45 REMARK 465 PRO G 46 REMARK 465 ILE G 47 REMARK 465 LEU G 48 REMARK 465 ILE G 49 REMARK 465 ALA G 50 REMARK 465 LYS G 51 REMARK 465 SER G 52 REMARK 465 SER G 53 REMARK 465 SER G 54 REMARK 465 SER G 55 REMARK 465 ASN G 56 REMARK 465 GLY G 57 REMARK 465 GLY G 58 REMARK 465 THR G 59 REMARK 465 ASN G 60 REMARK 465 ASN G 61 REMARK 465 ALA G 62 REMARK 465 ASN G 63 REMARK 465 THR G 64 REMARK 465 PRO G 65 REMARK 465 SER G 66 REMARK 465 TRP G 67 REMARK 465 GLN G 68 REMARK 465 THR G 69 REMARK 465 ALA G 70 REMARK 465 GLY G 71 REMARK 465 GLY G 72 REMARK 465 GLY G 73 REMARK 465 LYS G 74 REMARK 465 ASN G 75 REMARK 465 SER G 76 REMARK 465 CYS G 77 REMARK 465 ALA G 78 REMARK 465 THR G 79 REMARK 465 PHE G 80 REMARK 465 GLY G 81 REMARK 465 ALA G 82 REMARK 465 GLU G 83 REMARK 465 PHE G 84 REMARK 465 SER G 85 REMARK 465 ALA G 86 REMARK 465 ALA G 87 REMARK 465 SER G 88 REMARK 465 ASP G 89 REMARK 465 MET G 90 REMARK 465 ILE G 91 REMARK 465 ASN G 92 REMARK 465 ASN G 93 REMARK 465 ALA G 94 REMARK 465 GLN G 95 REMARK 465 LYS G 96 REMARK 465 ILE G 97 REMARK 465 VAL G 98 REMARK 465 GLN G 99 REMARK 465 GLU G 100 REMARK 465 THR G 101 REMARK 465 GLN G 102 REMARK 465 GLN G 103 REMARK 465 LEU G 104 REMARK 465 SER G 105 REMARK 465 ALA G 106 REMARK 465 ASN G 107 REMARK 465 GLN G 108 REMARK 465 PRO G 109 REMARK 465 LYS G 110 REMARK 465 ASN G 111 REMARK 465 ILE G 112 REMARK 465 THR G 113 REMARK 465 GLN G 114 REMARK 465 PRO G 115 REMARK 465 HIS G 116 REMARK 465 ASN G 117 REMARK 465 LEU G 118 REMARK 465 ASN G 119 REMARK 465 LEU G 120 REMARK 465 ASN G 121 REMARK 465 SER G 122 REMARK 465 PRO G 123 REMARK 465 SER G 124 REMARK 465 SER G 125 REMARK 465 LEU G 126 REMARK 465 THR G 127 REMARK 465 ALA G 128 REMARK 465 LEU G 129 REMARK 465 ALA G 130 REMARK 465 GLN G 131 REMARK 465 LYS G 132 REMARK 465 MET G 133 REMARK 465 LEU G 134 REMARK 465 LYS G 135 REMARK 465 ASN G 136 REMARK 465 ALA G 137 REMARK 465 GLN G 138 REMARK 465 SER G 139 REMARK 465 GLN G 140 REMARK 465 ALA G 141 REMARK 465 GLU G 142 REMARK 465 ILE G 143 REMARK 465 LEU G 144 REMARK 465 LYS G 145 REMARK 465 LEU G 146 REMARK 465 ALA G 147 REMARK 465 ASN G 148 REMARK 465 GLN G 149 REMARK 465 VAL G 150 REMARK 465 GLU G 151 REMARK 465 SER G 152 REMARK 465 ASP G 153 REMARK 465 PHE G 154 REMARK 465 ASN G 155 REMARK 465 LYS G 156 REMARK 465 LEU G 157 REMARK 465 SER G 158 REMARK 465 SER G 159 REMARK 465 GLY G 160 REMARK 465 HIS G 161 REMARK 465 LEU G 162 REMARK 465 LYS G 163 REMARK 465 ASP G 164 REMARK 465 TYR G 165 REMARK 465 ILE G 166 REMARK 465 GLY G 167 REMARK 465 LYS G 168 REMARK 465 CYS G 169 REMARK 465 ASP G 170 REMARK 465 ALA G 171 REMARK 465 SER G 172 REMARK 465 ALA G 173 REMARK 465 ILE G 174 REMARK 465 SER G 175 REMARK 465 SER G 176 REMARK 465 ALA G 177 REMARK 465 ASN G 178 REMARK 465 MET G 179 REMARK 465 THR G 180 REMARK 465 MET G 181 REMARK 465 GLN G 182 REMARK 465 ASN G 183 REMARK 465 GLN G 184 REMARK 465 LYS G 185 REMARK 465 ASN G 186 REMARK 465 ASN G 187 REMARK 465 TRP G 188 REMARK 465 GLY G 189 REMARK 465 ASN G 190 REMARK 465 GLY G 191 REMARK 465 CYS G 192 REMARK 465 ALA G 193 REMARK 465 GLY G 194 REMARK 465 VAL G 195 REMARK 465 GLU G 196 REMARK 465 GLU G 197 REMARK 465 THR G 198 REMARK 465 GLN G 199 REMARK 465 SER G 200 REMARK 465 LEU G 201 REMARK 465 LEU G 202 REMARK 465 LYS G 203 REMARK 465 THR G 204 REMARK 465 SER G 205 REMARK 465 ALA G 206 REMARK 465 ALA G 207 REMARK 465 ASP G 208 REMARK 465 PHE G 209 REMARK 465 ASN G 210 REMARK 465 ASN G 211 REMARK 465 GLN G 212 REMARK 465 THR G 213 REMARK 465 PRO G 214 REMARK 465 GLN G 215 REMARK 465 ILE G 216 REMARK 465 ASN G 217 REMARK 465 GLN G 218 REMARK 465 ALA G 219 REMARK 465 GLN G 220 REMARK 465 ASN G 221 REMARK 465 LEU G 222 REMARK 465 ALA G 223 REMARK 465 ASN G 224 REMARK 465 THR G 225 REMARK 465 LEU G 226 REMARK 465 ILE G 227 REMARK 465 GLN G 228 REMARK 465 GLU G 229 REMARK 465 LEU G 230 REMARK 465 GLY G 231 REMARK 465 ASN G 232 REMARK 465 ASN G 233 REMARK 465 PRO G 234 REMARK 465 PHE G 235 REMARK 465 ARG G 236 REMARK 465 ALA G 237 REMARK 465 SER G 238 REMARK 465 GLY G 239 REMARK 465 GLY G 240 REMARK 465 GLY G 241 REMARK 465 SER G 242 REMARK 465 GLY G 243 REMARK 465 GLY G 244 REMARK 465 GLY G 245 REMARK 465 GLY G 246 REMARK 465 SER G 247 REMARK 465 GLY G 248 REMARK 465 LYS G 249 REMARK 465 LEU G 250 REMARK 465 SER G 251 REMARK 465 ASP G 252 REMARK 465 THR G 253 REMARK 465 TYR G 254 REMARK 465 GLU G 255 REMARK 465 GLN G 256 REMARK 465 LEU G 257 REMARK 465 SER G 258 REMARK 465 ARG G 259 REMARK 465 LEU G 260 REMARK 465 LEU G 261 REMARK 465 THR G 262 REMARK 465 ASN G 263 REMARK 465 ASP G 264 REMARK 465 ASN G 265 REMARK 465 GLY G 266 REMARK 465 THR G 267 REMARK 465 ASN G 268 REMARK 465 SER G 269 REMARK 465 LYS G 270 REMARK 465 THR G 271 REMARK 465 SER G 272 REMARK 465 ALA G 273 REMARK 465 GLN G 274 REMARK 465 ALA G 275 REMARK 465 ILE G 276 REMARK 465 ASN G 277 REMARK 465 GLN G 278 REMARK 465 ALA G 279 REMARK 465 VAL G 280 REMARK 465 ASN G 281 REMARK 465 ASN G 282 REMARK 465 LEU G 283 REMARK 465 ASN G 284 REMARK 465 GLU G 285 REMARK 465 ARG G 286 REMARK 465 ALA G 287 REMARK 465 LYS G 288 REMARK 465 THR G 289 REMARK 465 LEU G 290 REMARK 465 ALA G 291 REMARK 465 GLY G 292 REMARK 465 GLY G 293 REMARK 465 THR G 294 REMARK 465 THR G 295 REMARK 465 ASN G 296 REMARK 465 SER G 297 REMARK 465 PRO G 298 REMARK 465 ALA G 299 REMARK 465 TYR G 300 REMARK 465 GLN G 301 REMARK 465 ALA G 302 REMARK 465 THR G 303 REMARK 465 LEU G 304 REMARK 465 LEU G 305 REMARK 465 ALA G 306 REMARK 465 LEU G 307 REMARK 465 ARG G 308 REMARK 465 SER G 309 REMARK 465 VAL G 310 REMARK 465 LEU G 311 REMARK 465 GLY G 312 REMARK 465 LEU G 313 REMARK 465 TRP G 314 REMARK 465 ASN G 315 REMARK 465 SER G 316 REMARK 465 MET G 317 REMARK 465 GLY G 318 REMARK 465 TYR G 319 REMARK 465 ALA G 320 REMARK 465 VAL G 321 REMARK 465 ILE G 322 REMARK 465 CYS G 323 REMARK 465 GLY G 324 REMARK 465 GLY G 325 REMARK 465 TYR G 326 REMARK 465 THR G 327 REMARK 465 LYS G 328 REMARK 465 SER G 329 REMARK 465 PRO G 330 REMARK 465 GLY G 331 REMARK 465 GLU G 332 REMARK 465 ASN G 333 REMARK 465 ASN G 334 REMARK 465 GLN G 335 REMARK 465 LYS G 336 REMARK 465 ASP G 337 REMARK 465 PHE G 338 REMARK 465 HIS G 339 REMARK 465 TYR G 340 REMARK 465 THR G 341 REMARK 465 ASP G 342 REMARK 465 GLU G 343 REMARK 465 ASN G 344 REMARK 465 GLY G 345 REMARK 465 ASN G 346 REMARK 465 GLY G 347 REMARK 465 THR G 348 REMARK 465 THR G 349 REMARK 465 ILE G 350 REMARK 465 ASN G 351 REMARK 465 CYS G 352 REMARK 465 GLY G 353 REMARK 465 GLY G 354 REMARK 465 SER G 355 REMARK 465 THR G 356 REMARK 465 ASN G 357 REMARK 465 SER G 358 REMARK 465 ASN G 359 REMARK 465 GLY G 360 REMARK 465 THR G 361 REMARK 465 HIS G 362 REMARK 465 SER G 363 REMARK 465 TYR G 364 REMARK 465 ASN G 365 REMARK 465 GLY G 366 REMARK 465 THR G 367 REMARK 465 ASN G 368 REMARK 465 THR G 369 REMARK 465 LEU G 370 REMARK 465 LYS G 371 REMARK 465 ALA G 372 REMARK 465 ASP G 373 REMARK 465 LYS G 374 REMARK 465 ASN G 375 REMARK 465 VAL G 376 REMARK 465 SER G 377 REMARK 465 LEU G 378 REMARK 465 SER G 379 REMARK 465 ILE G 380 REMARK 465 GLU G 381 REMARK 465 GLN G 382 REMARK 465 TYR G 383 REMARK 465 GLU G 384 REMARK 465 LYS G 385 REMARK 465 ILE G 386 REMARK 465 HIS G 387 REMARK 465 GLU G 388 REMARK 465 ALA G 389 REMARK 465 TYR G 390 REMARK 465 GLN G 391 REMARK 465 ILE G 392 REMARK 465 LEU G 393 REMARK 465 SER G 394 REMARK 465 LYS G 395 REMARK 465 ALA G 396 REMARK 465 LEU G 397 REMARK 465 LYS G 398 REMARK 465 GLN G 399 REMARK 465 ALA G 400 REMARK 465 GLY G 401 REMARK 465 LEU G 402 REMARK 465 ALA G 403 REMARK 465 PRO G 404 REMARK 465 LEU G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 LYS G 408 REMARK 465 GLY G 409 REMARK 465 GLU G 410 REMARK 465 LYS G 411 REMARK 465 LEU G 412 REMARK 465 GLU G 413 REMARK 465 ALA G 414 REMARK 465 HIS G 415 REMARK 465 VAL G 416 REMARK 465 THR G 417 REMARK 465 THR G 418 REMARK 465 SER G 419 REMARK 465 LYS G 420 REMARK 465 TYR G 421 REMARK 465 HIS G 530 REMARK 465 HIS G 531 REMARK 465 HIS G 532 REMARK 465 HIS G 533 REMARK 465 HIS G 534 REMARK 465 HIS G 535 REMARK 465 GLU G 536 REMARK 465 PRO G 537 REMARK 465 GLU G 538 REMARK 465 ALA G 539 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O4 NAG J 2 O5 BMA J 3 1.87 REMARK 500 O4 NAG J 1 O5 NAG J 2 2.03 REMARK 500 O ALA C 376 O P1L C 380 2.11 REMARK 500 OH TYR C 38 OD2 ASP C 84 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 98 40.54 -104.10 REMARK 500 LEU A 143 49.72 -91.84 REMARK 500 ASN A 189 -61.16 -93.77 REMARK 500 ARG A 274 33.36 -97.20 REMARK 500 ARG A 274 33.23 -97.07 REMARK 500 ARG A 418 -32.72 -132.24 REMARK 500 TYR B 62 50.86 -116.63 REMARK 500 ASP B 95 39.78 -99.02 REMARK 500 ASN B 100 32.21 -96.40 REMARK 500 ASN B 243 175.27 179.90 REMARK 500 MET C 70 60.86 61.00 REMARK 500 LEU C 87 35.70 -99.36 REMARK 500 ASN C 99 -166.97 -125.54 REMARK 500 ASP C 110 38.95 -98.84 REMARK 500 LEU C 155 34.02 -99.74 REMARK 500 MET C 160 36.84 -99.52 REMARK 500 VAL C 204 -61.55 -97.06 REMARK 500 SER C 291 57.34 -95.53 REMARK 500 VAL C 321 -60.71 -95.07 REMARK 500 SER C 322 -60.24 -92.82 REMARK 500 PHE C 379 -72.09 -86.65 REMARK 500 LEU D 23 54.61 -93.44 REMARK 500 TYR D 26 94.88 -67.51 REMARK 500 PHE D 65 51.79 -117.26 REMARK 500 ASP D 98 40.44 -102.89 REMARK 500 PRO D 147 34.16 -94.94 REMARK 500 ASN D 189 -62.08 -94.19 REMARK 500 LYS D 279 38.45 -96.78 REMARK 500 ALA D 281 37.80 -98.80 REMARK 500 ASN E 100 30.16 -97.46 REMARK 500 LEU E 145 35.34 -99.85 REMARK 500 THR E 271 50.00 -91.17 REMARK 500 PHE G 435 33.08 -96.38 REMARK 500 ASN G 482 61.33 61.17 REMARK 500 TRP G 508 18.69 58.90 REMARK 500 LEU G 510 -7.09 78.12 REMARK 500 GLU L 74 47.57 37.95 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PLM C 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-50281 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF HUMAN FULL-LENGTH ALPHA1BETA3GAMMA2 GABA(A)R IN REMARK 900 COMPLEX WITH GARLH4, THE TMD OF NEUROLIGIN2, MEGABODY38 AND REMARK 900 PREGNENOLONE SULFATE DBREF 9FAT A 10 422 UNP P14867 GBRA1_HUMAN 37 449 DBREF 9FAT B 7 447 UNP P28472 GBRB3_HUMAN 32 472 DBREF 9FAT C 25 428 UNP P18507 GBRG2_HUMAN 64 467 DBREF 9FAT D 10 422 UNP P14867 GBRA1_HUMAN 37 449 DBREF 9FAT E 7 447 UNP P28472 GBRB3_HUMAN 32 472 DBREF 9FAT G 1 539 PDB 9FAT 9FAT 1 539 DBREF 9FAT H 668 700 UNP Q8NFZ4 NLGN2_HUMAN 668 700 DBREF 9FAT L 14 203 UNP Q7Z7J7 LHPL4_HUMAN 14 203 SEQADV 9FAT GLY C 429 UNP P18507 EXPRESSION TAG SEQRES 1 A 413 ASP ASN THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU SEQRES 2 A 413 LEU ASP GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY SEQRES 3 A 413 GLU ARG VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SEQRES 4 A 413 SER PHE GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR SEQRES 5 A 413 ILE ASP VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG SEQRES 6 A 413 LEU LYS PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN SEQRES 7 A 413 ASN LEU MET ALA SER LYS ILE TRP THR PRO ASP THR PHE SEQRES 8 A 413 PHE HIS ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR SEQRES 9 A 413 MET PRO ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR SEQRES 10 A 413 LEU LEU TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS SEQRES 11 A 413 PRO MET HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA SEQRES 12 A 413 CYS PRO LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA SEQRES 13 A 413 GLU VAL VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER SEQRES 14 A 413 VAL VAL VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR SEQRES 15 A 413 ASP LEU LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SEQRES 16 A 413 SER SER THR GLY GLU TYR VAL VAL MET THR THR HIS PHE SEQRES 17 A 413 HIS LEU LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR SEQRES 18 A 413 TYR LEU PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SEQRES 19 A 413 SER PHE TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR SEQRES 20 A 413 VAL PHE GLY VAL THR THR VAL LEU THR MET THR THR LEU SEQRES 21 A 413 SER ILE SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR SEQRES 22 A 413 ALA THR ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA SEQRES 23 A 413 PHE VAL PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN SEQRES 24 A 413 TYR PHE THR LYS ARG GLY TYR ALA TRP ASP GLY LYS SER SEQRES 25 A 413 VAL VAL PRO GLU LYS PRO LYS LYS VAL LYS ASP PRO LEU SEQRES 26 A 413 ILE LYS LYS ASN ASN THR TYR ALA PRO THR ALA THR SER SEQRES 27 A 413 TYR THR PRO ASN LEU ALA ARG GLY ASP PRO GLY LEU ALA SEQRES 28 A 413 THR ILE ALA LYS SER ALA THR ILE GLU PRO LYS GLU VAL SEQRES 29 A 413 LYS PRO GLU THR LYS PRO PRO GLU PRO LYS LYS THR PHE SEQRES 30 A 413 ASN SER VAL SER LYS ILE ASP ARG LEU SER ARG ILE ALA SEQRES 31 A 413 PHE PRO LEU LEU PHE GLY ILE PHE ASN LEU VAL TYR TRP SEQRES 32 A 413 ALA THR TYR LEU ASN ARG GLU PRO GLN LEU SEQRES 1 B 441 GLY ASN MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU SEQRES 2 B 441 LEU LYS GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY SEQRES 3 B 441 GLY PRO PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SEQRES 4 B 441 SER ILE ASP MET VAL SER GLU VAL ASN MET ASP TYR THR SEQRES 5 B 441 LEU THR MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG SEQRES 6 B 441 LEU ALA TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP SEQRES 7 B 441 ASN ARG VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR SEQRES 8 B 441 PHE LEU ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR SEQRES 9 B 441 VAL LYS ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR SEQRES 10 B 441 VAL LEU TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS SEQRES 11 B 441 MET MET ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN SEQRES 12 B 441 CYS THR LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP SEQRES 13 B 441 ASP ILE GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL SEQRES 14 B 441 THR GLY VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE SEQRES 15 B 441 VAL GLU HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA SEQRES 16 B 441 THR GLY ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU SEQRES 17 B 441 LYS ARG ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET SEQRES 18 B 441 PRO SER ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE SEQRES 19 B 441 TRP ILE ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU SEQRES 20 B 441 GLY ILE THR THR VAL LEU THR MET THR THR ILE ASN THR SEQRES 21 B 441 HIS LEU ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS SEQRES 22 B 441 ALA ILE ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL SEQRES 23 B 441 PHE LEU ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE SEQRES 24 B 441 PHE PHE GLY ARG GLY PRO GLN ARG GLN LYS LYS LEU ALA SEQRES 25 B 441 GLU LYS THR ALA LYS ALA LYS ASN ASP ARG SER LYS SER SEQRES 26 B 441 GLU SER ASN ARG VAL ASP ALA HIS GLY ASN ILE LEU LEU SEQRES 27 B 441 THR SER LEU GLU VAL HIS ASN GLU MET ASN GLU VAL SER SEQRES 28 B 441 GLY GLY ILE GLY ASP THR ARG ASN SER ALA ILE SER PHE SEQRES 29 B 441 ASP ASN SER GLY ILE GLN TYR ARG LYS GLN SER MET PRO SEQRES 30 B 441 ARG GLU GLY HIS GLY ARG PHE LEU GLY ASP ARG SER LEU SEQRES 31 B 441 PRO HIS LYS LYS THR HIS LEU ARG ARG ARG SER SER GLN SEQRES 32 B 441 LEU LYS ILE LYS ILE PRO ASP LEU THR ASP VAL ASN ALA SEQRES 33 B 441 ILE ASP ARG TRP SER ARG ILE VAL PHE PRO PHE THR PHE SEQRES 34 B 441 SER LEU PHE ASN LEU VAL TYR TRP LEU TYR TYR VAL SEQRES 1 C 405 GLY ASP VAL THR VAL ILE LEU ASN ASN LEU LEU GLU GLY SEQRES 2 C 405 TYR ASP ASN LYS LEU ARG PRO ASP ILE GLY VAL LYS PRO SEQRES 3 C 405 THR LEU ILE HIS THR ASP MET TYR VAL ASN SER ILE GLY SEQRES 4 C 405 PRO VAL ASN ALA ILE ASN MET GLU TYR THR ILE ASP ILE SEQRES 5 C 405 PHE PHE ALA GLN THR TRP TYR ASP ARG ARG LEU LYS PHE SEQRES 6 C 405 ASN SER THR ILE LYS VAL LEU ARG LEU ASN SER ASN MET SEQRES 7 C 405 VAL GLY LYS ILE TRP ILE PRO ASP THR PHE PHE ARG ASN SEQRES 8 C 405 SER LYS LYS ALA ASP ALA HIS TRP ILE THR THR PRO ASN SEQRES 9 C 405 ARG MET LEU ARG ILE TRP ASN ASP GLY ARG VAL LEU TYR SEQRES 10 C 405 THR LEU ARG LEU THR ILE ASP ALA GLU CYS GLN LEU GLN SEQRES 11 C 405 LEU HIS ASN PHE PRO MET ASP GLU HIS SER CYS PRO LEU SEQRES 12 C 405 GLU PHE SER SER TYR GLY TYR PRO ARG GLU GLU ILE VAL SEQRES 13 C 405 TYR GLN TRP LYS ARG SER SER VAL GLU VAL GLY ASP THR SEQRES 14 C 405 ARG SER TRP ARG LEU TYR GLN PHE SER PHE VAL GLY LEU SEQRES 15 C 405 ARG ASN THR THR GLU VAL VAL LYS THR THR SER GLY ASP SEQRES 16 C 405 TYR VAL VAL MET SER VAL TYR PHE ASP LEU SER ARG ARG SEQRES 17 C 405 MET GLY TYR PHE THR ILE GLN THR TYR ILE PRO CYS THR SEQRES 18 C 405 LEU ILE VAL VAL LEU SER TRP VAL SER PHE TRP ILE ASN SEQRES 19 C 405 LYS ASP ALA VAL PRO ALA ARG THR SER LEU GLY ILE THR SEQRES 20 C 405 THR VAL LEU THR MET THR THR LEU SER THR ILE ALA ARG SEQRES 21 C 405 LYS SER LEU PRO LYS VAL SER TYR VAL THR ALA MET ASP SEQRES 22 C 405 LEU PHE VAL SER VAL CYS PHE ILE PHE VAL PHE SER ALA SEQRES 23 C 405 LEU VAL GLU TYR GLY THR LEU HIS TYR PHE VAL SER ASN SEQRES 24 C 405 ARG LYS PRO SER LYS ASP LYS ASP LYS LYS LYS LYS ASN SEQRES 25 C 405 PRO ALA PRO THR ILE ASP ILE ARG PRO ARG SER ALA THR SEQRES 26 C 405 ILE GLN MET ASN ASN ALA THR HIS LEU GLN GLU ARG ASP SEQRES 27 C 405 GLU GLU TYR GLY TYR GLU CYS LEU ASP GLY LYS ASP CYS SEQRES 28 C 405 ALA SER PHE PHE P1L P1L PHE GLU ASP P1L ARG THR GLY SEQRES 29 C 405 ALA TRP ARG HIS GLY ARG ILE HIS ILE ARG ILE ALA LYS SEQRES 30 C 405 MET ASP SER TYR ALA ARG ILE PHE PHE PRO THR ALA PHE SEQRES 31 C 405 CYS LEU PHE ASN LEU VAL TYR TRP VAL SER TYR LEU TYR SEQRES 32 C 405 LEU GLY SEQRES 1 D 413 ASP ASN THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU SEQRES 2 D 413 LEU ASP GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY SEQRES 3 D 413 GLU ARG VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SEQRES 4 D 413 SER PHE GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR SEQRES 5 D 413 ILE ASP VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG SEQRES 6 D 413 LEU LYS PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN SEQRES 7 D 413 ASN LEU MET ALA SER LYS ILE TRP THR PRO ASP THR PHE SEQRES 8 D 413 PHE HIS ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR SEQRES 9 D 413 MET PRO ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR SEQRES 10 D 413 LEU LEU TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS SEQRES 11 D 413 PRO MET HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA SEQRES 12 D 413 CYS PRO LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA SEQRES 13 D 413 GLU VAL VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER SEQRES 14 D 413 VAL VAL VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR SEQRES 15 D 413 ASP LEU LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SEQRES 16 D 413 SER SER THR GLY GLU TYR VAL VAL MET THR THR HIS PHE SEQRES 17 D 413 HIS LEU LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR SEQRES 18 D 413 TYR LEU PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SEQRES 19 D 413 SER PHE TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR SEQRES 20 D 413 VAL PHE GLY VAL THR THR VAL LEU THR MET THR THR LEU SEQRES 21 D 413 SER ILE SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR SEQRES 22 D 413 ALA THR ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA SEQRES 23 D 413 PHE VAL PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN SEQRES 24 D 413 TYR PHE THR LYS ARG GLY TYR ALA TRP ASP GLY LYS SER SEQRES 25 D 413 VAL VAL PRO GLU LYS PRO LYS LYS VAL LYS ASP PRO LEU SEQRES 26 D 413 ILE LYS LYS ASN ASN THR TYR ALA PRO THR ALA THR SER SEQRES 27 D 413 TYR THR PRO ASN LEU ALA ARG GLY ASP PRO GLY LEU ALA SEQRES 28 D 413 THR ILE ALA LYS SER ALA THR ILE GLU PRO LYS GLU VAL SEQRES 29 D 413 LYS PRO GLU THR LYS PRO PRO GLU PRO LYS LYS THR PHE SEQRES 30 D 413 ASN SER VAL SER LYS ILE ASP ARG LEU SER ARG ILE ALA SEQRES 31 D 413 PHE PRO LEU LEU PHE GLY ILE PHE ASN LEU VAL TYR TRP SEQRES 32 D 413 ALA THR TYR LEU ASN ARG GLU PRO GLN LEU SEQRES 1 E 441 GLY ASN MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU SEQRES 2 E 441 LEU LYS GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY SEQRES 3 E 441 GLY PRO PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SEQRES 4 E 441 SER ILE ASP MET VAL SER GLU VAL ASN MET ASP TYR THR SEQRES 5 E 441 LEU THR MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG SEQRES 6 E 441 LEU ALA TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP SEQRES 7 E 441 ASN ARG VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR SEQRES 8 E 441 PHE LEU ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR SEQRES 9 E 441 VAL LYS ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR SEQRES 10 E 441 VAL LEU TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS SEQRES 11 E 441 MET MET ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN SEQRES 12 E 441 CYS THR LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP SEQRES 13 E 441 ASP ILE GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL SEQRES 14 E 441 THR GLY VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE SEQRES 15 E 441 VAL GLU HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA SEQRES 16 E 441 THR GLY ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU SEQRES 17 E 441 LYS ARG ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET SEQRES 18 E 441 PRO SER ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE SEQRES 19 E 441 TRP ILE ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU SEQRES 20 E 441 GLY ILE THR THR VAL LEU THR MET THR THR ILE ASN THR SEQRES 21 E 441 HIS LEU ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS SEQRES 22 E 441 ALA ILE ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL SEQRES 23 E 441 PHE LEU ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE SEQRES 24 E 441 PHE PHE GLY ARG GLY PRO GLN ARG GLN LYS LYS LEU ALA SEQRES 25 E 441 GLU LYS THR ALA LYS ALA LYS ASN ASP ARG SER LYS SER SEQRES 26 E 441 GLU SER ASN ARG VAL ASP ALA HIS GLY ASN ILE LEU LEU SEQRES 27 E 441 THR SER LEU GLU VAL HIS ASN GLU MET ASN GLU VAL SER SEQRES 28 E 441 GLY GLY ILE GLY ASP THR ARG ASN SER ALA ILE SER PHE SEQRES 29 E 441 ASP ASN SER GLY ILE GLN TYR ARG LYS GLN SER MET PRO SEQRES 30 E 441 ARG GLU GLY HIS GLY ARG PHE LEU GLY ASP ARG SER LEU SEQRES 31 E 441 PRO HIS LYS LYS THR HIS LEU ARG ARG ARG SER SER GLN SEQRES 32 E 441 LEU LYS ILE LYS ILE PRO ASP LEU THR ASP VAL ASN ALA SEQRES 33 E 441 ILE ASP ARG TRP SER ARG ILE VAL PHE PRO PHE THR PHE SEQRES 34 E 441 SER LEU PHE ASN LEU VAL TYR TRP LEU TYR TYR VAL SEQRES 1 G 539 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 539 THR LYS THR THR THR SER VAL ILE ASP THR THR ASN ASP SEQRES 3 G 539 ALA GLN ASN LEU LEU THR GLN ALA GLN THR ILE VAL ASN SEQRES 4 G 539 THR LEU LYS ASP TYR CYS PRO ILE LEU ILE ALA LYS SER SEQRES 5 G 539 SER SER SER ASN GLY GLY THR ASN ASN ALA ASN THR PRO SEQRES 6 G 539 SER TRP GLN THR ALA GLY GLY GLY LYS ASN SER CYS ALA SEQRES 7 G 539 THR PHE GLY ALA GLU PHE SER ALA ALA SER ASP MET ILE SEQRES 8 G 539 ASN ASN ALA GLN LYS ILE VAL GLN GLU THR GLN GLN LEU SEQRES 9 G 539 SER ALA ASN GLN PRO LYS ASN ILE THR GLN PRO HIS ASN SEQRES 10 G 539 LEU ASN LEU ASN SER PRO SER SER LEU THR ALA LEU ALA SEQRES 11 G 539 GLN LYS MET LEU LYS ASN ALA GLN SER GLN ALA GLU ILE SEQRES 12 G 539 LEU LYS LEU ALA ASN GLN VAL GLU SER ASP PHE ASN LYS SEQRES 13 G 539 LEU SER SER GLY HIS LEU LYS ASP TYR ILE GLY LYS CYS SEQRES 14 G 539 ASP ALA SER ALA ILE SER SER ALA ASN MET THR MET GLN SEQRES 15 G 539 ASN GLN LYS ASN ASN TRP GLY ASN GLY CYS ALA GLY VAL SEQRES 16 G 539 GLU GLU THR GLN SER LEU LEU LYS THR SER ALA ALA ASP SEQRES 17 G 539 PHE ASN ASN GLN THR PRO GLN ILE ASN GLN ALA GLN ASN SEQRES 18 G 539 LEU ALA ASN THR LEU ILE GLN GLU LEU GLY ASN ASN PRO SEQRES 19 G 539 PHE ARG ALA SER GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 20 G 539 GLY LYS LEU SER ASP THR TYR GLU GLN LEU SER ARG LEU SEQRES 21 G 539 LEU THR ASN ASP ASN GLY THR ASN SER LYS THR SER ALA SEQRES 22 G 539 GLN ALA ILE ASN GLN ALA VAL ASN ASN LEU ASN GLU ARG SEQRES 23 G 539 ALA LYS THR LEU ALA GLY GLY THR THR ASN SER PRO ALA SEQRES 24 G 539 TYR GLN ALA THR LEU LEU ALA LEU ARG SER VAL LEU GLY SEQRES 25 G 539 LEU TRP ASN SER MET GLY TYR ALA VAL ILE CYS GLY GLY SEQRES 26 G 539 TYR THR LYS SER PRO GLY GLU ASN ASN GLN LYS ASP PHE SEQRES 27 G 539 HIS TYR THR ASP GLU ASN GLY ASN GLY THR THR ILE ASN SEQRES 28 G 539 CYS GLY GLY SER THR ASN SER ASN GLY THR HIS SER TYR SEQRES 29 G 539 ASN GLY THR ASN THR LEU LYS ALA ASP LYS ASN VAL SER SEQRES 30 G 539 LEU SER ILE GLU GLN TYR GLU LYS ILE HIS GLU ALA TYR SEQRES 31 G 539 GLN ILE LEU SER LYS ALA LEU LYS GLN ALA GLY LEU ALA SEQRES 32 G 539 PRO LEU ASN SER LYS GLY GLU LYS LEU GLU ALA HIS VAL SEQRES 33 G 539 THR THR SER LYS TYR GLY SER LEU ARG VAL SER CYS ALA SEQRES 34 G 539 ALA SER GLY ARG THR PHE THR THR TYR ILE MET ALA TRP SEQRES 35 G 539 PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE LEU ALA SEQRES 36 G 539 ALA MET ASP GLN GLY ARG ILE GLN TYR TYR GLY ASP SER SEQRES 37 G 539 VAL ARG GLY ARG PHE THR ILE SER ARG ASP TYR ALA LYS SEQRES 38 G 539 ASN SER VAL ASP LEU GLN LEU ASP GLY LEU ARG PRO GLU SEQRES 39 G 539 ASP THR ALA VAL TYR TYR CYS ALA ALA GLY ALA GLY PHE SEQRES 40 G 539 TRP GLY LEU ARG THR ALA SER SER TYR HIS TYR TRP GLY SEQRES 41 G 539 GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS SEQRES 42 G 539 HIS HIS GLU PRO GLU ALA SEQRES 1 H 33 ASP SER ARG ASP TYR SER THR GLU LEU SER VAL THR VAL SEQRES 2 H 33 ALA VAL GLY ALA SER LEU LEU PHE LEU ASN ILE LEU ALA SEQRES 3 H 33 PHE ALA ALA LEU TYR TYR LYS SEQRES 1 L 190 HIS TYR MET ARG ASN SER ARG ALA ILE GLY VAL LEU TRP SEQRES 2 L 190 ALA ILE PHE THR ILE CYS PHE ALA ILE ILE ASN VAL VAL SEQRES 3 L 190 VAL PHE ILE GLN PRO TYR TRP VAL GLY ASP SER VAL SER SEQRES 4 L 190 THR PRO LYS PRO GLY TYR PHE GLY LEU PHE HIS TYR CYS SEQRES 5 L 190 VAL GLY SER GLY LEU ALA GLY ARG GLU LEU THR CYS ARG SEQRES 6 L 190 GLY SER PHE THR ASP PHE SER THR ILE PRO SER SER ALA SEQRES 7 L 190 PHE LYS ALA ALA ALA PHE PHE VAL LEU LEU SER MET VAL SEQRES 8 L 190 LEU ILE LEU GLY CYS ILE THR CYS PHE SER LEU PHE PHE SEQRES 9 L 190 PHE CYS ASN THR ALA THR VAL TYR LYS ILE CYS ALA TRP SEQRES 10 L 190 MET GLN LEU LEU ALA ALA LEU CYS LEU VAL LEU GLY CYS SEQRES 11 L 190 MET ILE PHE PRO ASP GLY TRP ASP ALA GLU THR ILE ARG SEQRES 12 L 190 ASP MET CYS GLY ALA LYS THR GLY LYS TYR SER LEU GLY SEQRES 13 L 190 ASP CYS SER VAL ARG TRP ALA TYR ILE LEU ALA ILE ILE SEQRES 14 L 190 GLY ILE LEU ASN ALA LEU ILE LEU SER PHE LEU ALA PHE SEQRES 15 L 190 VAL LEU GLY ASN ARG GLN THR ASP MODRES 9FAT P1L C 380 CYS MODIFIED RESIDUE MODRES 9FAT P1L C 381 CYS MODIFIED RESIDUE MODRES 9FAT P1L C 385 CYS MODIFIED RESIDUE HET P1L C 380 23 HET P1L C 381 23 HET P1L C 385 23 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET MAN F 4 11 HET MAN F 5 11 HET MAN F 6 11 HET MAN F 7 11 HET MAN F 8 11 HET MAN F 9 11 HET MAN F 10 11 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 11 HET MAN I 5 11 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET NAG K 1 14 HET NAG K 2 14 HET NAG M 1 14 HET NAG M 2 14 HET BMA M 3 11 HET MAN M 4 11 HET MAN M 5 11 HET MAN M 6 11 HET MAN M 7 11 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET MAN N 4 11 HET MAN N 5 11 HET MAN N 6 11 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET PIO A3901 47 HET PGW A3902 51 HET D10 A3903 10 HET CL A3904 1 HET R16 B3501 16 HET D10 B3502 10 HET HEX B3503 6 HET PGW B3504 51 HET PLM C 501 14 HET CLR C 502 28 HET D10 C 503 10 HET PX2 D 501 36 HET A8W D 502 27 HET PIO D 503 47 HET HEX D 504 6 HET HEX E4301 6 HET PGW L 301 51 HET CL L 302 1 HETNAM P1L S-PALMITOYL-L-CYSTEINE HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM PIO [(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2, HETNAM 2 PIO 3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY- HETNAM 3 PIO PHOSPHORYL]OXY-PROPYL] OCTANOATE HETNAM PGW (1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY) HETNAM 2 PGW PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL (9Z)- HETNAM 3 PGW OCTADEC-9-ENOATE HETNAM D10 DECANE HETNAM CL CHLORIDE ION HETNAM R16 HEXADECANE HETNAM HEX HEXANE HETNAM PLM PALMITIC ACID HETNAM CLR CHOLESTEROL HETNAM PX2 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE HETNAM A8W PREGNENOLONE SULFATE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN PIO DIOCTANOYL L-ALPHA-PHOSPHATIDYL-D-MYO-INOSITOL 4,5- HETSYN 2 PIO DIPHOSPHATE HETSYN PGW 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-(1- HETSYN 2 PGW GLYCEROL)]; PHOSPHATIDYLGLYCEROL HETSYN A8W PREGN-5-EN-3BETA-OL-20-ONE-3BETA-SULFATE FORMUL 3 P1L 3(C19 H37 N O3 S) FORMUL 9 NAG 14(C8 H15 N O6) FORMUL 9 BMA 6(C6 H12 O6) FORMUL 9 MAN 16(C6 H12 O6) FORMUL 16 PIO 2(C25 H49 O19 P3) FORMUL 17 PGW 3(C40 H77 O10 P) FORMUL 18 D10 3(C10 H22) FORMUL 19 CL 2(CL 1-) FORMUL 20 R16 C16 H34 FORMUL 22 HEX 3(C6 H14) FORMUL 24 PLM C16 H32 O2 FORMUL 25 CLR C27 H46 O FORMUL 27 PX2 C27 H52 O8 P 1- FORMUL 28 A8W C21 H32 O5 S HELIX 1 AA1 THR A 12 LEU A 23 1 12 HELIX 2 AA2 ASP A 72 LYS A 76 5 5 HELIX 3 AA3 ASN A 87 ILE A 94 1 8 HELIX 4 AA4 GLU A 174 VAL A 179 1 6 HELIX 5 AA5 ILE A 223 THR A 230 1 8 HELIX 6 AA6 THR A 230 VAL A 243 1 14 HELIX 7 AA7 SER A 244 TRP A 246 5 3 HELIX 8 AA8 SER A 251 ALA A 273 1 23 HELIX 9 AA9 THR A 284 THR A 311 1 28 HELIX 10 AB1 SER A 390 ASN A 417 1 28 HELIX 11 AB2 MET B 9 LYS B 21 1 13 HELIX 12 AB3 LYS B 70 ALA B 73 5 4 HELIX 13 AB4 ASP B 84 LEU B 91 5 8 HELIX 14 AB5 ASP B 139 TYR B 143 5 5 HELIX 15 AB6 ILE B 218 THR B 225 1 8 HELIX 16 AB7 THR B 225 VAL B 238 1 14 HELIX 17 AB8 SER B 239 ILE B 242 5 4 HELIX 18 AB9 ALA B 246 GLU B 270 1 25 HELIX 19 AC1 LYS B 279 GLY B 308 1 30 HELIX 20 AC2 ARG B 309 LEU B 317 1 9 HELIX 21 AC3 ASP B 419 VAL B 447 1 29 HELIX 22 AC4 ASP C 26 GLU C 36 1 11 HELIX 23 AC5 ARG C 85 LYS C 88 5 4 HELIX 24 AC6 ASN C 99 VAL C 103 5 5 HELIX 25 AC7 ASP C 192 TRP C 196 5 5 HELIX 26 AC8 MET C 233 THR C 240 1 8 HELIX 27 AC9 THR C 240 SER C 254 1 15 HELIX 28 AD1 PHE C 255 ILE C 257 5 3 HELIX 29 AD2 ALA C 261 ARG C 284 1 24 HELIX 30 AD3 LYS C 285 LEU C 287 5 3 HELIX 31 AD4 THR C 294 SER C 322 1 29 HELIX 32 AD5 ASP C 374 PHE C 379 1 6 HELIX 33 AD6 LYS C 401 TYR C 427 1 27 HELIX 34 AD7 ASN D 11 LEU D 23 1 13 HELIX 35 AD8 GLU D 73 LYS D 76 5 4 HELIX 36 AD9 ASN D 88 ILE D 94 5 7 HELIX 37 AE1 GLU D 174 SER D 178 1 5 HELIX 38 AE2 ILE D 223 THR D 230 1 8 HELIX 39 AE3 THR D 230 VAL D 243 1 14 HELIX 40 AE4 SER D 244 LEU D 247 5 4 HELIX 41 AE5 SER D 251 SER D 272 1 22 HELIX 42 AE6 ALA D 273 LEU D 277 5 5 HELIX 43 AE7 THR D 284 THR D 311 1 28 HELIX 44 AE8 SER D 390 ARG D 418 1 29 HELIX 45 AE9 ASN E 8 LYS E 21 1 14 HELIX 46 AF1 ASP E 84 LEU E 91 5 8 HELIX 47 AF2 GLY E 170 ALA E 174 5 5 HELIX 48 AF3 ILE E 218 THR E 225 1 8 HELIX 49 AF4 THR E 225 VAL E 238 1 14 HELIX 50 AF5 SER E 239 ILE E 242 5 4 HELIX 51 AF6 ALA E 246 GLU E 270 1 25 HELIX 52 AF7 LYS E 279 GLY E 308 1 30 HELIX 53 AF8 ARG E 309 LEU E 317 1 9 HELIX 54 AF9 ASP E 419 VAL E 447 1 29 HELIX 55 AG1 ASP G 467 ARG G 470 5 4 HELIX 56 AG2 ARG G 492 THR G 496 5 5 HELIX 57 AG3 THR G 512 TYR G 516 5 5 HELIX 58 AG4 SER H 673 TYR H 699 1 27 HELIX 59 AG5 TYR L 15 GLN L 43 1 29 HELIX 60 AG6 ASP L 83 ILE L 87 5 5 HELIX 61 AG7 SER L 89 PHE L 113 1 25 HELIX 62 AG8 SER L 114 PHE L 118 5 5 HELIX 63 AG9 ASN L 120 PHE L 146 1 27 HELIX 64 AH1 PRO L 147 ASP L 151 5 5 HELIX 65 AH2 ALA L 152 GLY L 160 1 9 HELIX 66 AH3 ARG L 174 ASP L 203 1 30 SHEET 1 AA1 6 VAL A 83 LEU A 86 0 SHEET 2 AA1 6 LEU A 118 THR A 122 -1 O ILE A 121 N LEU A 84 SHEET 3 AA1 6 TYR A 129 THR A 130 -1 O THR A 130 N LEU A 118 SHEET 4 AA1 6 ARG A 67 TRP A 70 -1 N GLN A 68 O TYR A 129 SHEET 5 AA1 6 THR A 39 ASP A 44 -1 N ASP A 44 O ARG A 67 SHEET 6 AA1 6 VAL A 167 TRP A 171 1 O GLU A 170 N THR A 43 SHEET 1 AA2 5 VAL A 108 ALA A 109 0 SHEET 2 AA2 5 LEU A 133 GLU A 138 -1 O THR A 134 N VAL A 108 SHEET 3 AA2 5 GLU A 59 VAL A 64 -1 N TYR A 60 O ALA A 137 SHEET 4 AA2 5 PHE A 46 SER A 54 -1 N SER A 49 O ASP A 63 SHEET 5 AA2 5 VAL A 180 VAL A 181 1 O VAL A 180 N VAL A 47 SHEET 1 AA310 PHE A 100 PHE A 101 0 SHEET 2 AA310 ALA A 150 GLY A 158 -1 O GLY A 158 N PHE A 100 SHEET 3 AA310 GLU A 209 ARG A 221 -1 O MET A 213 N PHE A 157 SHEET 4 AA310 TYR A 191 GLN A 204 -1 N ASP A 199 O THR A 214 SHEET 5 AA310 ILE G 462 TYR G 465 -1 O GLN G 463 N ILE A 202 SHEET 6 AA310 GLU G 450 MET G 457 -1 N ALA G 456 O TYR G 464 SHEET 7 AA310 MET G 440 ALA G 446 -1 N ARG G 444 O GLU G 452 SHEET 8 AA310 ALA G 497 ALA G 503 -1 O ALA G 502 N ALA G 441 SHEET 9 AA310 THR G 523 VAL G 527 -1 O THR G 523 N TYR G 499 SHEET 10 AA310 LEU G 11 VAL G 12 1 N VAL G 12 O THR G 526 SHEET 1 AA4 9 PHE A 100 PHE A 101 0 SHEET 2 AA4 9 ALA A 150 GLY A 158 -1 O GLY A 158 N PHE A 100 SHEET 3 AA4 9 GLU A 209 ARG A 221 -1 O MET A 213 N PHE A 157 SHEET 4 AA4 9 TYR A 191 GLN A 204 -1 N ASP A 199 O THR A 214 SHEET 5 AA4 9 ILE G 462 TYR G 465 -1 O GLN G 463 N ILE A 202 SHEET 6 AA4 9 GLU G 450 MET G 457 -1 N ALA G 456 O TYR G 464 SHEET 7 AA4 9 MET G 440 ALA G 446 -1 N ARG G 444 O GLU G 452 SHEET 8 AA4 9 ALA G 497 ALA G 503 -1 O ALA G 502 N ALA G 441 SHEET 9 AA4 9 TYR G 518 TRP G 519 -1 O TYR G 518 N ALA G 503 SHEET 1 AA5 6 LEU B 81 LEU B 83 0 SHEET 2 AA5 6 ARG B 114 LEU B 118 -1 O LEU B 118 N LEU B 81 SHEET 3 AA5 6 THR B 123 LEU B 128 -1 O GLY B 127 N MET B 115 SHEET 4 AA5 6 GLN B 64 ARG B 68 -1 N GLN B 65 O TYR B 126 SHEET 5 AA5 6 VAL B 36 SER B 51 -1 N GLY B 39 O TYR B 66 SHEET 6 AA5 6 ILE B 164 TRP B 168 1 O GLU B 165 N VAL B 36 SHEET 1 AA6 5 ASP B 101 VAL B 106 0 SHEET 2 AA6 5 ILE B 130 ALA B 135 -1 O THR B 131 N PHE B 105 SHEET 3 AA6 5 ASP B 56 MET B 61 -1 N MET B 61 O ILE B 130 SHEET 4 AA6 5 VAL B 36 SER B 51 -1 N SER B 46 O THR B 60 SHEET 5 AA6 5 VAL B 175 THR B 176 1 O THR B 176 N ILE B 44 SHEET 1 AA7 4 THR B 96 PHE B 98 0 SHEET 2 AA7 4 GLU B 147 SER B 156 -1 O GLU B 155 N TYR B 97 SHEET 3 AA7 4 GLY B 203 ARG B 216 -1 O PHE B 212 N CYS B 150 SHEET 4 AA7 4 PHE B 186 PHE B 200 -1 N PHE B 200 O GLY B 203 SHEET 1 AA8 6 VAL C 95 LEU C 98 0 SHEET 2 AA8 6 ARG C 129 TRP C 134 -1 O ILE C 133 N LEU C 96 SHEET 3 AA8 6 ARG C 138 GLU C 150 -1 O LEU C 140 N ARG C 132 SHEET 4 AA8 6 GLU C 71 TYR C 83 -1 N TYR C 72 O ALA C 149 SHEET 5 AA8 6 THR C 51 ASN C 66 -1 N GLY C 63 O THR C 73 SHEET 6 AA8 6 ILE C 179 GLN C 182 1 O VAL C 180 N THR C 51 SHEET 1 AA9 5 SER C 116 ALA C 121 0 SHEET 2 AA9 5 ARG C 138 GLU C 150 -1 O ASP C 148 N LYS C 118 SHEET 3 AA9 5 GLU C 71 TYR C 83 -1 N TYR C 72 O ALA C 149 SHEET 4 AA9 5 THR C 51 ASN C 66 -1 N GLY C 63 O THR C 73 SHEET 5 AA9 5 VAL C 188 VAL C 190 1 O GLU C 189 N VAL C 59 SHEET 1 AB1 4 THR C 111 PHE C 113 0 SHEET 2 AB1 4 GLU C 162 SER C 171 -1 O SER C 170 N PHE C 112 SHEET 3 AB1 4 GLY C 218 ARG C 231 -1 O MET C 223 N PHE C 169 SHEET 4 AB1 4 PHE C 201 THR C 215 -1 N VAL C 204 O ASP C 228 SHEET 1 AB2 6 VAL D 83 LEU D 86 0 SHEET 2 AB2 6 LYS D 117 THR D 122 -1 O ILE D 121 N LEU D 84 SHEET 3 AB2 6 THR D 126 MET D 131 -1 O LEU D 128 N ARG D 120 SHEET 4 AB2 6 ARG D 67 LYS D 71 -1 N TRP D 70 O LEU D 127 SHEET 5 AB2 6 THR D 39 SER D 54 -1 N ASP D 44 O ARG D 67 SHEET 6 AB2 6 VAL D 167 TRP D 171 1 O GLU D 170 N THR D 43 SHEET 1 AB3 5 VAL D 108 ALA D 109 0 SHEET 2 AB3 5 LEU D 133 GLU D 138 -1 O THR D 134 N VAL D 108 SHEET 3 AB3 5 GLU D 59 VAL D 64 -1 N ILE D 62 O VAL D 135 SHEET 4 AB3 5 THR D 39 SER D 54 -1 N SER D 54 O GLU D 59 SHEET 5 AB3 5 VAL D 179 VAL D 181 1 O VAL D 180 N VAL D 47 SHEET 1 AB4 4 PHE D 100 PHE D 101 0 SHEET 2 AB4 4 ALA D 150 GLY D 158 -1 O GLY D 158 N PHE D 100 SHEET 3 AB4 4 TYR D 210 ARG D 221 -1 O MET D 213 N PHE D 157 SHEET 4 AB4 4 TYR D 191 ASP D 199 -1 N GLY D 195 O HIS D 218 SHEET 1 AB5 4 PHE D 100 PHE D 101 0 SHEET 2 AB5 4 ALA D 150 GLY D 158 -1 O GLY D 158 N PHE D 100 SHEET 3 AB5 4 TYR D 210 ARG D 221 -1 O MET D 213 N PHE D 157 SHEET 4 AB5 4 ILE D 202 VAL D 203 -1 N VAL D 203 O TYR D 210 SHEET 1 AB6 4 ASP E 43 ILE E 47 0 SHEET 2 AB6 4 ASP E 56 ARG E 68 -1 O THR E 60 N SER E 46 SHEET 3 AB6 4 THR E 123 ALA E 135 -1 O ALA E 134 N TYR E 57 SHEET 4 AB6 4 ASP E 101 VAL E 106 -1 N LYS E 103 O THR E 133 SHEET 1 AB7 6 LEU E 81 LEU E 83 0 SHEET 2 AB7 6 ARG E 114 LEU E 118 -1 O LEU E 118 N LEU E 81 SHEET 3 AB7 6 THR E 123 ALA E 135 -1 O LEU E 125 N ARG E 117 SHEET 4 AB7 6 ASP E 56 ARG E 68 -1 N TYR E 57 O ALA E 134 SHEET 5 AB7 6 VAL E 36 MET E 40 -1 N GLY E 39 O TYR E 66 SHEET 6 AB7 6 ILE E 164 TRP E 168 1 O GLU E 165 N VAL E 38 SHEET 1 AB8 4 THR E 96 TYR E 97 0 SHEET 2 AB8 4 GLU E 147 SER E 156 -1 O GLU E 155 N TYR E 97 SHEET 3 AB8 4 ALA E 204 ARG E 216 -1 O LEU E 214 N GLN E 148 SHEET 4 AB8 4 PHE E 186 VAL E 199 -1 N ARG E 192 O SER E 211 SHEET 1 AB9 4 GLN G 3 SER G 7 0 SHEET 2 AB9 4 LEU G 424 SER G 431 -1 O SER G 431 N GLN G 3 SHEET 3 AB9 4 SER G 483 LEU G 488 -1 O LEU G 486 N VAL G 426 SHEET 4 AB9 4 PHE G 473 ASP G 478 -1 N THR G 474 O GLN G 487 SHEET 1 AC1 5 LEU L 75 ARG L 78 0 SHEET 2 AC1 5 TYR L 64 GLY L 67 -1 N VAL L 66 O THR L 76 SHEET 3 AC1 5 GLY L 57 PHE L 59 -1 N TYR L 58 O CYS L 65 SHEET 4 AC1 5 VAL L 47 GLY L 48 -1 N VAL L 47 O PHE L 59 SHEET 5 AC1 5 SER L 172 VAL L 173 -1 O SER L 172 N GLY L 48 SSBOND 1 CYS A 139 CYS A 153 1555 1555 2.03 SSBOND 2 CYS B 136 CYS B 150 1555 1555 2.04 SSBOND 3 CYS C 151 CYS C 165 1555 1555 2.03 SSBOND 4 CYS D 139 CYS D 153 1555 1555 2.03 SSBOND 5 CYS E 136 CYS E 150 1555 1555 2.04 SSBOND 6 CYS G 428 CYS G 501 1555 1555 2.03 SSBOND 7 CYS L 65 CYS L 77 1555 1555 2.03 SSBOND 8 CYS L 109 CYS L 128 1555 1555 2.03 SSBOND 9 CYS L 159 CYS L 171 1555 1555 2.03 LINK ND2 ASN A 111 C1 NAG F 1 1555 1555 1.43 LINK ND2 ASN B 80 C1 NAG J 1 1555 1555 1.54 LINK ND2 ASN B 149 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN C 208 C1 NAG K 1 1555 1555 1.44 LINK C PHE C 379 N P1L C 380 1555 1555 1.33 LINK C P1L C 380 N P1L C 381 1555 1555 1.33 LINK C P1L C 381 N PHE C 382 1555 1555 1.33 LINK C ASP C 384 N P1L C 385 1555 1555 1.33 LINK ND2 ASN D 111 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN E 80 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN E 149 C1 NAG N 1 1555 1555 1.42 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.39 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.39 LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.39 LINK O6 BMA F 3 C1 MAN F 7 1555 1555 1.41 LINK O2 MAN F 4 C1 MAN F 5 1555 1555 1.39 LINK O2 MAN F 5 C1 MAN F 6 1555 1555 1.39 LINK O6 MAN F 7 C1 MAN F 8 1555 1555 1.42 LINK O3 MAN F 7 C1 MAN F 10 1555 1555 1.40 LINK O2 MAN F 8 C1 MAN F 9 1555 1555 1.40 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.40 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.39 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.39 LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.40 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.43 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.39 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.40 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.40 LINK O3 BMA M 3 C1 MAN M 4 1555 1555 1.40 LINK O6 BMA M 3 C1 MAN M 6 1555 1555 1.41 LINK O2 MAN M 4 C1 MAN M 5 1555 1555 1.39 LINK O6 MAN M 6 C1 MAN M 7 1555 1555 1.40 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.39 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.40 LINK O6 BMA N 3 C1 MAN N 4 1555 1555 1.40 LINK O3 BMA N 3 C1 MAN N 6 1555 1555 1.39 LINK O3 MAN N 4 C1 MAN N 5 1555 1555 1.39 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.39 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.39 CISPEP 1 MET A 112 THR A 113 0 -3.13 CISPEP 2 PHE A 146 PRO A 147 0 -3.76 CISPEP 3 VAL B 109 THR B 110 0 -4.86 CISPEP 4 TYR B 143 PRO B 144 0 0.94 CISPEP 5 ILE C 124 THR C 125 0 -7.82 CISPEP 6 PHE C 158 PRO C 159 0 -2.06 CISPEP 7 MET D 112 THR D 113 0 -25.98 CISPEP 8 PHE D 146 PRO D 147 0 -0.76 CISPEP 9 VAL E 109 THR E 110 0 -14.56 CISPEP 10 TYR E 143 PRO E 144 0 -0.56 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