HEADER MEMBRANE PROTEIN 10-MAY-24 9FAP TITLE CRYOEM STRUCTURE OF HUMAN FULL-LENGTH ALPHA1BETA3GAMMA2 GABA(A)R IN TITLE 2 COMPLEX WITH GARLH4, THE TMD OF NEUROLIGIN2 AND MEGABODY38 IN A TITLE 3 CLOSED STATE (STATEC1) 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: NEUROLIGIN-2; COMPND 19 CHAIN: H; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: LHFPL TETRASPAN SUBFAMILY MEMBER 4 PROTEIN; COMPND 23 CHAIN: L; COMPND 24 SYNONYM: GABAA RECEPTOR REGULATORY LHFPL4,LIPOMA HMGIC FUSION COMPND 25 PARTNER-LIKE 4 PROTEIN; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 6; COMPND 28 MOLECULE: MEGABODY38; COMPND 29 CHAIN: G; COMPND 30 ENGINEERED: YES; COMPND 31 OTHER_DETAILS: THIS MEGABODY IS A CHIMERIC PROTEIN DESIGNED AND COMPND 32 CONSTRUCTED BASED ON A CIRCULAR PERMUTATION OF A NANOBODY (RAISED COMPND 33 AGAINST GABA(A) RECEPTOR SUBUNITS, IN LLAMA) AND HELICOBACTER PYLORI COMPND 34 PROTEIN, HOPQ (UNIPROT ID: B5Z8H1). 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_CELL_LINE: HEK293S-TETR; SOURCE 23 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 24 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 25 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 26 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PCDNA4-TO-HYGROMYCIN-B; SOURCE 29 MOL_ID: 3; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 GENE: GABRG2; SOURCE 34 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 36 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-TETR; SOURCE 37 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 38 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 39 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 40 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 41 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 42 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 43 MOL_ID: 4; SOURCE 44 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 45 ORGANISM_COMMON: HUMAN; SOURCE 46 ORGANISM_TAXID: 9606; SOURCE 47 GENE: NLGN2, KIAA1366; SOURCE 48 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 49 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 50 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-TETR; SOURCE 51 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 52 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 53 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 54 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 55 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 56 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 57 MOL_ID: 5; SOURCE 58 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 59 ORGANISM_COMMON: HUMAN; SOURCE 60 ORGANISM_TAXID: 9606; SOURCE 61 GENE: LHFPL4, GARLH4; SOURCE 62 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 63 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 64 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-TETR; SOURCE 65 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 66 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 67 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 68 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 69 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 70 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 71 MOL_ID: 6; SOURCE 72 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 73 ORGANISM_TAXID: 9844; SOURCE 74 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 75 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 76 EXPRESSION_SYSTEM_STRAIN: WK6SU-; SOURCE 77 EXPRESSION_SYSTEM_PLASMID: PMESD2 KEYWDS GABA, NEUROTRANSMISSION, TERNARY COMPLEX, INHIBITORY POSTSYNAPSE, KEYWDS 2 MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR V.B.KASARAGOD,A.R.ARICESCU REVDAT 1 02-JUL-25 9FAP 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 AND JRNL TITL 3 MEGABODY38 IN A CLOSED STATE (STATEC1) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.80 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 : 6HUO REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER REMARK 3 REFINEMENT TARGET : FSC AT 0.5 REMARK 3 OVERALL ANISOTROPIC B VALUE : 25.000 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) : 2.800 REMARK 3 NUMBER OF PARTICLES : 41368 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 9FAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1292138307. 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 AND REMARK 245 MEGABODY38 IN A CLOSED STATE REMARK 245 (STATEC1) 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 : 9004 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1700.00 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) : 4670.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 130000 REMARK 245 CALIBRATED MAGNIFICATION : 130000 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, H, L, G, F, I, REMARK 350 AND CHAINS: J, K, M, N 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 324 REMARK 465 GLU A 325 REMARK 465 LYS A 326 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 LYS B 315 REMARK 465 LYS B 316 REMARK 465 LEU B 317 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 LYS B 413 REMARK 465 ILE B 414 REMARK 465 PRO B 415 REMARK 465 ASP B 416 REMARK 465 LEU B 417 REMARK 465 THR B 418 REMARK 465 ARG C 324 REMARK 465 LYS C 325 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 PRO D 327 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 GLN E 314 REMARK 465 LYS E 315 REMARK 465 LYS E 316 REMARK 465 LEU E 317 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 ND2 ASN A 111 C2 NAG F 1 1.78 REMARK 500 ND2 ASN A 111 N2 NAG F 1 1.95 REMARK 500 O3 BMA M 3 C2 MAN M 6 2.01 REMARK 500 O4 NAG M 2 C2 BMA M 3 2.03 REMARK 500 O4 NAG M 1 O5 NAG M 2 2.10 REMARK 500 O3 BMA M 3 O2 MAN M 6 2.15 REMARK 500 O6 BMA F 3 O5 MAN F 7 2.16 REMARK 500 OD2 ASP A 318 OG SER A 321 2.16 REMARK 500 ND2 ASN E 149 O5 NAG M 1 2.19 REMARK 500 ND2 ASN B 80 O5 NAG J 1 2.19 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 THR A 113 -57.04 75.91 REMARK 500 ASP A 145 31.02 -98.46 REMARK 500 ARG A 173 -168.01 -116.90 REMARK 500 ARG A 187 51.61 -93.35 REMARK 500 SER A 276 40.38 -103.79 REMARK 500 LYS A 312 -60.35 -93.22 REMARK 500 SER B 46 147.29 -170.70 REMARK 500 LEU B 145 51.77 -91.75 REMARK 500 LYS C 94 -9.05 73.97 REMARK 500 ASP C 110 30.23 -90.94 REMARK 500 THR C 193 -5.72 76.36 REMARK 500 ARG C 197 35.23 -98.33 REMARK 500 ASP C 260 -5.12 77.79 REMARK 500 SER C 291 30.36 -96.42 REMARK 500 CYS C 375 4.37 -67.15 REMARK 500 PHE C 379 -74.30 -71.10 REMARK 500 ASP C 384 -76.60 57.09 REMARK 500 ARG C 398 52.06 -91.76 REMARK 500 LEU D 75 31.37 -97.32 REMARK 500 ASP D 98 52.72 -90.41 REMARK 500 LYS D 106 107.97 -59.04 REMARK 500 ARG D 173 -165.61 -125.81 REMARK 500 LYS E 103 116.07 -160.13 REMARK 500 LEU E 145 52.50 -92.35 REMARK 500 PRO E 276 77.13 -67.99 REMARK 500 GLU L 74 46.70 38.41 REMARK 500 LYS G 449 65.28 61.85 REMARK 500 LEU G 510 -9.68 78.74 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 502 REMARK 610 PGW D 3906 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-50277 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 AND MEGABODY38 IN A REMARK 900 CLOSED STATE (STATEC1) DBREF 9FAP A 12 416 UNP P14867 GBRA1_HUMAN 39 443 DBREF 9FAP B 9 447 UNP P28472 GBRB3_HUMAN 34 472 DBREF 9FAP C 27 428 UNP P18507 GBRG2_HUMAN 66 467 DBREF 9FAP D 12 416 UNP P14867 GBRA1_HUMAN 39 443 DBREF 9FAP E 9 447 UNP P28472 GBRB3_HUMAN 34 472 DBREF 9FAP H 668 700 UNP Q8NFZ4 NLGN2_HUMAN 668 700 DBREF 9FAP L 11 203 UNP Q7Z7J7 LHPL4_HUMAN 11 203 DBREF 9FAP G 1 539 PDB 9FAP 9FAP 1 539 SEQADV 9FAP GLY C 429 UNP P18507 EXPRESSION TAG SEQRES 1 A 405 THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU LEU ASP SEQRES 2 A 405 GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY GLU ARG SEQRES 3 A 405 VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SER PHE SEQRES 4 A 405 GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR ILE ASP SEQRES 5 A 405 VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG LEU LYS SEQRES 6 A 405 PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN ASN LEU SEQRES 7 A 405 MET ALA SER LYS ILE TRP THR PRO ASP THR PHE PHE HIS SEQRES 8 A 405 ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR MET PRO SEQRES 9 A 405 ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR LEU LEU SEQRES 10 A 405 TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS PRO MET SEQRES 11 A 405 HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA CYS PRO SEQRES 12 A 405 LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA GLU VAL SEQRES 13 A 405 VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER VAL VAL SEQRES 14 A 405 VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR ASP LEU SEQRES 15 A 405 LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SER SER SEQRES 16 A 405 THR GLY GLU TYR VAL VAL MET THR THR HIS PHE HIS LEU SEQRES 17 A 405 LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR TYR LEU SEQRES 18 A 405 PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SER PHE SEQRES 19 A 405 TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR VAL PHE SEQRES 20 A 405 GLY VAL THR THR VAL LEU THR MET THR THR LEU SER ILE SEQRES 21 A 405 SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR ALA THR SEQRES 22 A 405 ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA PHE VAL SEQRES 23 A 405 PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN TYR PHE SEQRES 24 A 405 THR LYS ARG GLY TYR ALA TRP ASP GLY LYS SER VAL VAL SEQRES 25 A 405 PRO GLU LYS PRO LYS LYS VAL LYS ASP PRO LEU ILE LYS SEQRES 26 A 405 LYS ASN ASN THR TYR ALA PRO THR ALA THR SER TYR THR SEQRES 27 A 405 PRO ASN LEU ALA ARG GLY ASP PRO GLY LEU ALA THR ILE SEQRES 28 A 405 ALA LYS SER ALA THR ILE GLU PRO LYS GLU VAL LYS PRO SEQRES 29 A 405 GLU THR LYS PRO PRO GLU PRO LYS LYS THR PHE ASN SER SEQRES 30 A 405 VAL SER LYS ILE ASP ARG LEU SER ARG ILE ALA PHE PRO SEQRES 31 A 405 LEU LEU PHE GLY ILE PHE ASN LEU VAL TYR TRP ALA THR SEQRES 32 A 405 TYR LEU SEQRES 1 B 439 MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS SEQRES 2 B 439 GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO SEQRES 3 B 439 PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE SEQRES 4 B 439 ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU THR SEQRES 5 B 439 MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA SEQRES 6 B 439 TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG SEQRES 7 B 439 VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU SEQRES 8 B 439 ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS SEQRES 9 B 439 ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU SEQRES 10 B 439 TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET MET SEQRES 11 B 439 ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR SEQRES 12 B 439 LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE SEQRES 13 B 439 GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY SEQRES 14 B 439 VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU SEQRES 15 B 439 HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY SEQRES 16 B 439 ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG SEQRES 17 B 439 ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER SEQRES 18 B 439 ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE SEQRES 19 B 439 ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE SEQRES 20 B 439 THR THR VAL LEU THR MET THR THR ILE ASN THR HIS LEU SEQRES 21 B 439 ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE SEQRES 22 B 439 ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU SEQRES 23 B 439 ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SEQRES 24 B 439 GLY ARG GLY PRO GLN ARG GLN LYS LYS LEU ALA GLU LYS SEQRES 25 B 439 THR ALA LYS ALA LYS ASN ASP ARG SER LYS SER GLU SER SEQRES 26 B 439 ASN ARG VAL ASP ALA HIS GLY ASN ILE LEU LEU THR SER SEQRES 27 B 439 LEU GLU VAL HIS ASN GLU MET ASN GLU VAL SER GLY GLY SEQRES 28 B 439 ILE GLY ASP THR ARG ASN SER ALA ILE SER PHE ASP ASN SEQRES 29 B 439 SER GLY ILE GLN TYR ARG LYS GLN SER MET PRO ARG GLU SEQRES 30 B 439 GLY HIS GLY ARG PHE LEU GLY ASP ARG SER LEU PRO HIS SEQRES 31 B 439 LYS LYS THR HIS LEU ARG ARG ARG SER SER GLN LEU LYS SEQRES 32 B 439 ILE LYS ILE PRO ASP LEU THR ASP VAL ASN ALA ILE ASP SEQRES 33 B 439 ARG TRP SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU SEQRES 34 B 439 PHE ASN LEU VAL TYR TRP LEU TYR TYR VAL SEQRES 1 C 403 VAL THR VAL ILE LEU ASN ASN LEU LEU GLU GLY TYR ASP SEQRES 2 C 403 ASN LYS LEU ARG PRO ASP ILE GLY VAL LYS PRO THR LEU SEQRES 3 C 403 ILE HIS THR ASP MET TYR VAL ASN SER ILE GLY PRO VAL SEQRES 4 C 403 ASN ALA ILE ASN MET GLU TYR THR ILE ASP ILE PHE PHE SEQRES 5 C 403 ALA GLN THR TRP TYR ASP ARG ARG LEU LYS PHE ASN SER SEQRES 6 C 403 THR ILE LYS VAL LEU ARG LEU ASN SER ASN MET VAL GLY SEQRES 7 C 403 LYS ILE TRP ILE PRO ASP THR PHE PHE ARG ASN SER LYS SEQRES 8 C 403 LYS ALA ASP ALA HIS TRP ILE THR THR PRO ASN ARG MET SEQRES 9 C 403 LEU ARG ILE TRP ASN ASP GLY ARG VAL LEU TYR THR LEU SEQRES 10 C 403 ARG LEU THR ILE ASP ALA GLU CYS GLN LEU GLN LEU HIS SEQRES 11 C 403 ASN PHE PRO MET ASP GLU HIS SER CYS PRO LEU GLU PHE SEQRES 12 C 403 SER SER TYR GLY TYR PRO ARG GLU GLU ILE VAL TYR GLN SEQRES 13 C 403 TRP LYS ARG SER SER VAL GLU VAL GLY ASP THR ARG SER SEQRES 14 C 403 TRP ARG LEU TYR GLN PHE SER PHE VAL GLY LEU ARG ASN SEQRES 15 C 403 THR THR GLU VAL VAL LYS THR THR SER GLY ASP TYR VAL SEQRES 16 C 403 VAL MET SER VAL TYR PHE ASP LEU SER ARG ARG MET GLY SEQRES 17 C 403 TYR PHE THR ILE GLN THR TYR ILE PRO CYS THR LEU ILE SEQRES 18 C 403 VAL VAL LEU SER TRP VAL SER PHE TRP ILE ASN LYS ASP SEQRES 19 C 403 ALA VAL PRO ALA ARG THR SER LEU GLY ILE THR THR VAL SEQRES 20 C 403 LEU THR MET THR THR LEU SER THR ILE ALA ARG LYS SER SEQRES 21 C 403 LEU PRO LYS VAL SER TYR VAL THR ALA MET ASP LEU PHE SEQRES 22 C 403 VAL SER VAL CYS PHE ILE PHE VAL PHE SER ALA LEU VAL SEQRES 23 C 403 GLU TYR GLY THR LEU HIS TYR PHE VAL SER ASN ARG LYS SEQRES 24 C 403 PRO SER LYS ASP LYS ASP LYS LYS LYS LYS ASN PRO ALA SEQRES 25 C 403 PRO THR ILE ASP ILE ARG PRO ARG SER ALA THR ILE GLN SEQRES 26 C 403 MET ASN ASN ALA THR HIS LEU GLN GLU ARG ASP GLU GLU SEQRES 27 C 403 TYR GLY TYR GLU CYS LEU ASP GLY LYS ASP CYS ALA SER SEQRES 28 C 403 PHE PHE P1L P1L PHE GLU ASP P1L ARG THR GLY ALA TRP SEQRES 29 C 403 ARG HIS GLY ARG ILE HIS ILE ARG ILE ALA LYS MET ASP SEQRES 30 C 403 SER TYR ALA ARG ILE PHE PHE PRO THR ALA PHE CYS LEU SEQRES 31 C 403 PHE ASN LEU VAL TYR TRP VAL SER TYR LEU TYR LEU GLY SEQRES 1 D 405 THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU LEU ASP SEQRES 2 D 405 GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY GLU ARG SEQRES 3 D 405 VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SER PHE SEQRES 4 D 405 GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR ILE ASP SEQRES 5 D 405 VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG LEU LYS SEQRES 6 D 405 PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN ASN LEU SEQRES 7 D 405 MET ALA SER LYS ILE TRP THR PRO ASP THR PHE PHE HIS SEQRES 8 D 405 ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR MET PRO SEQRES 9 D 405 ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR LEU LEU SEQRES 10 D 405 TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS PRO MET SEQRES 11 D 405 HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA CYS PRO SEQRES 12 D 405 LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA GLU VAL SEQRES 13 D 405 VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER VAL VAL SEQRES 14 D 405 VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR ASP LEU SEQRES 15 D 405 LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SER SER SEQRES 16 D 405 THR GLY GLU TYR VAL VAL MET THR THR HIS PHE HIS LEU SEQRES 17 D 405 LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR TYR LEU SEQRES 18 D 405 PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SER PHE SEQRES 19 D 405 TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR VAL PHE SEQRES 20 D 405 GLY VAL THR THR VAL LEU THR MET THR THR LEU SER ILE SEQRES 21 D 405 SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR ALA THR SEQRES 22 D 405 ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA PHE VAL SEQRES 23 D 405 PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN TYR PHE SEQRES 24 D 405 THR LYS ARG GLY TYR ALA TRP ASP GLY LYS SER VAL VAL SEQRES 25 D 405 PRO GLU LYS PRO LYS LYS VAL LYS ASP PRO LEU ILE LYS SEQRES 26 D 405 LYS ASN ASN THR TYR ALA PRO THR ALA THR SER TYR THR SEQRES 27 D 405 PRO ASN LEU ALA ARG GLY ASP PRO GLY LEU ALA THR ILE SEQRES 28 D 405 ALA LYS SER ALA THR ILE GLU PRO LYS GLU VAL LYS PRO SEQRES 29 D 405 GLU THR LYS PRO PRO GLU PRO LYS LYS THR PHE ASN SER SEQRES 30 D 405 VAL SER LYS ILE ASP ARG LEU SER ARG ILE ALA PHE PRO SEQRES 31 D 405 LEU LEU PHE GLY ILE PHE ASN LEU VAL TYR TRP ALA THR SEQRES 32 D 405 TYR LEU SEQRES 1 E 439 MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS SEQRES 2 E 439 GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO SEQRES 3 E 439 PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE SEQRES 4 E 439 ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU THR SEQRES 5 E 439 MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA SEQRES 6 E 439 TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG SEQRES 7 E 439 VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU SEQRES 8 E 439 ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS SEQRES 9 E 439 ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU SEQRES 10 E 439 TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET MET SEQRES 11 E 439 ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR SEQRES 12 E 439 LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE SEQRES 13 E 439 GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY SEQRES 14 E 439 VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU SEQRES 15 E 439 HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY SEQRES 16 E 439 ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG SEQRES 17 E 439 ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER SEQRES 18 E 439 ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE SEQRES 19 E 439 ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE SEQRES 20 E 439 THR THR VAL LEU THR MET THR THR ILE ASN THR HIS LEU SEQRES 21 E 439 ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE SEQRES 22 E 439 ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU SEQRES 23 E 439 ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SEQRES 24 E 439 GLY ARG GLY PRO GLN ARG GLN LYS LYS LEU ALA GLU LYS SEQRES 25 E 439 THR ALA LYS ALA LYS ASN ASP ARG SER LYS SER GLU SER SEQRES 26 E 439 ASN ARG VAL ASP ALA HIS GLY ASN ILE LEU LEU THR SER SEQRES 27 E 439 LEU GLU VAL HIS ASN GLU MET ASN GLU VAL SER GLY GLY SEQRES 28 E 439 ILE GLY ASP THR ARG ASN SER ALA ILE SER PHE ASP ASN SEQRES 29 E 439 SER GLY ILE GLN TYR ARG LYS GLN SER MET PRO ARG GLU SEQRES 30 E 439 GLY HIS GLY ARG PHE LEU GLY ASP ARG SER LEU PRO HIS SEQRES 31 E 439 LYS LYS THR HIS LEU ARG ARG ARG SER SER GLN LEU LYS SEQRES 32 E 439 ILE LYS ILE PRO ASP LEU THR ASP VAL ASN ALA ILE ASP SEQRES 33 E 439 ARG TRP SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU SEQRES 34 E 439 PHE ASN LEU VAL TYR TRP LEU TYR TYR VAL 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 193 TYR HIS GLU HIS TYR MET ARG ASN SER ARG ALA ILE GLY SEQRES 2 L 193 VAL LEU TRP ALA ILE PHE THR ILE CYS PHE ALA ILE ILE SEQRES 3 L 193 ASN VAL VAL VAL PHE ILE GLN PRO TYR TRP VAL GLY ASP SEQRES 4 L 193 SER VAL SER THR PRO LYS PRO GLY TYR PHE GLY LEU PHE SEQRES 5 L 193 HIS TYR CYS VAL GLY SER GLY LEU ALA GLY ARG GLU LEU SEQRES 6 L 193 THR CYS ARG GLY SER PHE THR ASP PHE SER THR ILE PRO SEQRES 7 L 193 SER SER ALA PHE LYS ALA ALA ALA PHE PHE VAL LEU LEU SEQRES 8 L 193 SER MET VAL LEU ILE LEU GLY CYS ILE THR CYS PHE SER SEQRES 9 L 193 LEU PHE PHE PHE CYS ASN THR ALA THR VAL TYR LYS ILE SEQRES 10 L 193 CYS ALA TRP MET GLN LEU LEU ALA ALA LEU CYS LEU VAL SEQRES 11 L 193 LEU GLY CYS MET ILE PHE PRO ASP GLY TRP ASP ALA GLU SEQRES 12 L 193 THR ILE ARG ASP MET CYS GLY ALA LYS THR GLY LYS TYR SEQRES 13 L 193 SER LEU GLY ASP CYS SER VAL ARG TRP ALA TYR ILE LEU SEQRES 14 L 193 ALA ILE ILE GLY ILE LEU ASN ALA LEU ILE LEU SER PHE SEQRES 15 L 193 LEU ALA PHE VAL LEU GLY ASN ARG GLN THR ASP 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 MODRES 9FAP P1L C 380 CYS MODIFIED RESIDUE MODRES 9FAP P1L C 381 CYS MODIFIED RESIDUE MODRES 9FAP 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 MAN I 6 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 BMA K 3 11 HET MAN K 4 11 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 NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET PIO A3901 47 HET PGW A3902 51 HET PX2 B 501 36 HET PLM B 502 18 HET NAG C 501 14 HET PLM C 502 14 HET CLR C 503 28 HET D10 C 504 10 HET PLM C 505 18 HET PIO D3901 47 HET HEX D3902 6 HET PGW D3903 51 HET PLM D3904 18 HET HEX D3905 6 HET PGW D3906 32 HET PLM E4401 18 HET PGW L 301 51 HET PGW L 302 51 HET CL L 303 1 HET PX2 L 304 36 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 PX2 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE HETNAM PLM PALMITIC ACID HETNAM CLR CHOLESTEROL HETNAM D10 DECANE HETNAM HEX HEXANE HETNAM CL CHLORIDE ION 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 FORMUL 3 P1L 3(C19 H37 N O3 S) FORMUL 9 NAG 13(C8 H15 N O6) FORMUL 9 BMA 6(C6 H12 O6) FORMUL 9 MAN 14(C6 H12 O6) FORMUL 15 PIO 2(C25 H49 O19 P3) FORMUL 16 PGW 5(C40 H77 O10 P) FORMUL 17 PX2 2(C27 H52 O8 P 1-) FORMUL 18 PLM 5(C16 H32 O2) FORMUL 21 CLR C27 H46 O FORMUL 22 D10 C10 H22 FORMUL 25 HEX 2(C6 H14) FORMUL 33 CL CL 1- FORMUL 35 HOH *64(H2 O) HELIX 1 AA1 THR A 12 LEU A 23 1 12 HELIX 2 AA2 GLU A 73 LYS A 76 5 4 HELIX 3 AA3 ASN A 87 SER A 92 1 6 HELIX 4 AA4 HIS A 142 PHE A 146 5 5 HELIX 5 AA5 ILE A 223 THR A 230 1 8 HELIX 6 AA6 THR A 230 SER A 244 1 15 HELIX 7 AA7 PHE A 245 LEU A 247 5 3 HELIX 8 AA8 SER A 251 SER A 276 1 26 HELIX 9 AA9 THR A 284 PHE A 310 1 27 HELIX 10 AB1 SER A 390 TYR A 415 1 26 HELIX 11 AB2 SER B 10 LYS B 21 1 12 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 GLY B 170 LYS B 173 5 4 HELIX 15 AB6 ILE B 218 THR B 225 1 8 HELIX 16 AB7 THR B 225 TRP B 237 1 13 HELIX 17 AB8 VAL B 238 ILE B 242 5 5 HELIX 18 AB9 ALA B 246 LEU B 272 1 27 HELIX 19 AC1 LYS B 279 GLY B 308 1 30 HELIX 20 AC2 ARG B 309 GLN B 314 1 6 HELIX 21 AC3 VAL B 420 TYR B 446 1 27 HELIX 22 AC4 THR C 28 GLU C 36 1 9 HELIX 23 AC5 ARG C 85 LYS C 88 5 4 HELIX 24 AC6 ASN C 99 ILE C 106 5 8 HELIX 25 AC7 MET C 233 THR C 240 1 8 HELIX 26 AC8 THR C 240 ILE C 257 1 18 HELIX 27 AC9 ALA C 261 ILE C 282 1 22 HELIX 28 AD1 ALA C 283 LYS C 285 5 3 HELIX 29 AD2 THR C 294 ASN C 323 1 30 HELIX 30 AD3 LYS C 401 TYR C 427 1 27 HELIX 31 AD4 THR D 13 LEU D 22 1 10 HELIX 32 AD5 GLU D 73 LYS D 76 5 4 HELIX 33 AD6 ASN D 87 SER D 92 1 6 HELIX 34 AD7 HIS D 142 PHE D 146 5 5 HELIX 35 AD8 ILE D 223 THR D 230 1 8 HELIX 36 AD9 THR D 230 SER D 244 1 15 HELIX 37 AE1 PHE D 245 LEU D 247 5 3 HELIX 38 AE2 SER D 251 SER D 276 1 26 HELIX 39 AE3 THR D 284 PHE D 310 1 27 HELIX 40 AE4 SER D 390 TYR D 415 1 26 HELIX 41 AE5 SER E 10 LYS E 21 1 12 HELIX 42 AE6 LYS E 70 ALA E 73 5 4 HELIX 43 AE7 ASP E 84 GLN E 90 5 7 HELIX 44 AE8 ASP E 139 TYR E 143 5 5 HELIX 45 AE9 GLY E 170 LYS E 173 5 4 HELIX 46 AF1 ILE E 218 THR E 225 1 8 HELIX 47 AF2 THR E 225 TRP E 237 1 13 HELIX 48 AF3 VAL E 238 ILE E 242 5 5 HELIX 49 AF4 ALA E 246 LEU E 272 1 27 HELIX 50 AF5 LYS E 279 GLY E 308 1 30 HELIX 51 AF6 ASP E 419 VAL E 447 1 29 HELIX 52 AF7 SER H 673 TYR H 699 1 27 HELIX 53 AF8 HIS L 12 GLN L 43 1 32 HELIX 54 AF9 ASP L 83 ILE L 87 5 5 HELIX 55 AG1 SER L 89 PHE L 113 1 25 HELIX 56 AG2 SER L 114 PHE L 117 5 4 HELIX 57 AG3 ASN L 120 PHE L 146 1 27 HELIX 58 AG4 PRO L 147 ASP L 151 5 5 HELIX 59 AG5 ALA L 152 GLY L 160 1 9 HELIX 60 AG6 ARG L 174 GLN L 201 1 28 HELIX 61 AG7 ASP G 467 ARG G 470 5 4 HELIX 62 AG8 ARG G 492 THR G 496 5 5 HELIX 63 AG9 THR G 512 TYR G 516 5 5 SHEET 1 AA1 6 VAL A 83 LEU A 86 0 SHEET 2 AA1 6 LYS A 117 THR A 122 -1 O LEU A 119 N LEU A 86 SHEET 3 AA1 6 THR A 126 GLU A 138 -1 O LEU A 128 N ARG A 120 SHEET 4 AA1 6 GLU A 59 LYS A 71 -1 N ILE A 62 O VAL A 135 SHEET 5 AA1 6 THR A 39 SER A 54 -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 VAL A 41 SHEET 1 AA2 5 GLY A 104 ALA A 109 0 SHEET 2 AA2 5 THR A 126 GLU A 138 -1 O THR A 134 N VAL A 108 SHEET 3 AA2 5 GLU A 59 LYS A 71 -1 N ILE A 62 O VAL A 135 SHEET 4 AA2 5 THR A 39 SER A 54 -1 N ASP A 44 O ARG A 67 SHEET 5 AA2 5 VAL A 179 VAL A 181 1 O VAL A 180 N ILE A 45 SHEET 1 AA310 THR A 99 PHE A 101 0 SHEET 2 AA310 ALA A 150 SER A 159 -1 O GLY A 158 N PHE A 100 SHEET 3 AA310 GLU A 209 ARG A 221 -1 O PHE A 217 N CYS A 153 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 ILE G 439 ALA G 446 -1 N ARG G 444 O GLU G 452 SHEET 8 AA310 ALA G 497 GLY G 504 -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 THR A 99 PHE A 101 0 SHEET 2 AA4 9 ALA A 150 SER A 159 -1 O GLY A 158 N PHE A 100 SHEET 3 AA4 9 GLU A 209 ARG A 221 -1 O PHE A 217 N CYS A 153 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 ILE G 439 ALA G 446 -1 N ARG G 444 O GLU G 452 SHEET 8 AA4 9 ALA G 497 GLY G 504 -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 ALA B 135 -1 O GLY B 127 N MET B 115 SHEET 4 AA5 6 ASP B 56 ARG B 68 -1 N PHE B 63 O LEU B 128 SHEET 5 AA5 6 VAL B 36 SER B 51 -1 N SER B 46 O THR B 60 SHEET 6 AA5 6 ILE B 164 TRP B 168 1 O GLU B 165 N VAL B 38 SHEET 1 AA6 5 ASP B 101 VAL B 106 0 SHEET 2 AA6 5 THR B 123 ALA B 135 -1 O THR B 133 N LYS B 103 SHEET 3 AA6 5 ASP B 56 ARG B 68 -1 N PHE B 63 O LEU B 128 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 ALA B 204 ARG B 216 -1 O LEU B 208 N ILE B 154 SHEET 4 AA7 4 PHE B 186 VAL B 199 -1 N ARG B 196 O ARG B 207 SHEET 1 AA8 4 VAL C 95 LEU C 98 0 SHEET 2 AA8 4 ARG C 129 TRP C 134 -1 O ILE C 133 N LEU C 96 SHEET 3 AA8 4 ARG C 138 GLU C 150 -1 O ARG C 138 N TRP C 134 SHEET 4 AA8 4 SER C 116 ALA C 121 -1 N LYS C 118 O ASP C 148 SHEET 1 AA9 6 VAL C 95 LEU C 98 0 SHEET 2 AA9 6 ARG C 129 TRP C 134 -1 O ILE C 133 N LEU C 96 SHEET 3 AA9 6 ARG C 138 GLU C 150 -1 O ARG C 138 N TRP C 134 SHEET 4 AA9 6 GLU C 71 TYR C 83 -1 N PHE C 78 O LEU C 143 SHEET 5 AA9 6 THR C 51 ASN C 66 -1 N ASN C 66 O GLU C 71 SHEET 6 AA9 6 ILE C 179 VAL C 190 1 O GLU C 189 N VAL C 59 SHEET 1 AB1 4 THR C 111 PHE C 112 0 SHEET 2 AB1 4 GLU C 162 SER C 171 -1 O SER C 170 N PHE C 112 SHEET 3 AB1 4 ASP C 219 ARG C 231 -1 O LEU C 229 N HIS C 163 SHEET 4 AB1 4 PHE C 201 LYS C 214 -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 LEU D 119 N LEU D 86 SHEET 3 AB2 6 THR D 126 GLU D 138 -1 O LEU D 128 N ARG D 120 SHEET 4 AB2 6 GLU D 59 LYS D 71 -1 N TYR D 60 O ALA D 137 SHEET 5 AB2 6 THR D 39 SER D 54 -1 N SER D 54 O GLU D 59 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 THR D 126 GLU D 138 -1 O THR D 134 N VAL D 108 SHEET 3 AB3 5 GLU D 59 LYS D 71 -1 N TYR D 60 O ALA D 137 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 ILE D 45 SHEET 1 AB4 4 THR D 99 PHE D 101 0 SHEET 2 AB4 4 ALA D 150 SER D 159 -1 O GLY D 158 N PHE D 100 SHEET 3 AB4 4 GLU D 209 ARG D 221 -1 O LEU D 219 N HIS D 151 SHEET 4 AB4 4 TYR D 191 GLN D 204 -1 N ASP D 199 O THR D 214 SHEET 1 AB5 6 LEU E 81 LEU E 83 0 SHEET 2 AB5 6 ARG E 114 LEU E 118 -1 O LEU E 118 N LEU E 81 SHEET 3 AB5 6 THR E 123 ALA E 135 -1 O LEU E 125 N ARG E 117 SHEET 4 AB5 6 ASP E 56 ARG E 68 -1 N PHE E 63 O LEU E 128 SHEET 5 AB5 6 VAL E 36 ILE E 47 -1 N SER E 46 O THR E 60 SHEET 6 AB5 6 ILE E 164 TRP E 168 1 O GLU E 165 N VAL E 38 SHEET 1 AB6 5 ASP E 101 VAL E 106 0 SHEET 2 AB6 5 THR E 123 ALA E 135 -1 O THR E 133 N LYS E 102 SHEET 3 AB6 5 ASP E 56 ARG E 68 -1 N PHE E 63 O LEU E 128 SHEET 4 AB6 5 VAL E 36 ILE E 47 -1 N SER E 46 O THR E 60 SHEET 5 AB6 5 VAL E 175 THR E 176 1 O THR E 176 N ILE E 44 SHEET 1 AB7 4 THR E 96 PHE E 98 0 SHEET 2 AB7 4 GLU E 147 SER E 156 -1 O GLU E 155 N TYR E 97 SHEET 3 AB7 4 ALA E 204 ARG E 216 -1 O LEU E 208 N ILE E 154 SHEET 4 AB7 4 PHE E 186 VAL E 199 -1 N GLU E 190 O ARG E 213 SHEET 1 AB8 5 THR L 76 ARG L 78 0 SHEET 2 AB8 5 TYR L 64 VAL L 66 -1 N TYR L 64 O ARG L 78 SHEET 3 AB8 5 GLY L 57 PHE L 59 -1 N TYR L 58 O CYS L 65 SHEET 4 AB8 5 VAL L 47 GLY L 48 -1 N VAL L 47 O PHE L 59 SHEET 5 AB8 5 SER L 172 VAL L 173 -1 O SER L 172 N GLY L 48 SHEET 1 AB9 4 GLN G 3 SER G 7 0 SHEET 2 AB9 4 SER G 423 SER G 431 -1 O SER G 431 N GLN G 3 SHEET 3 AB9 4 SER G 483 ASP G 489 -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 SSBOND 1 CYS A 139 CYS A 153 1555 1555 2.04 SSBOND 2 CYS B 136 CYS B 150 1555 1555 2.04 SSBOND 3 CYS C 151 CYS C 165 1555 1555 2.04 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 L 65 CYS L 77 1555 1555 2.03 SSBOND 7 CYS L 109 CYS L 128 1555 1555 2.04 SSBOND 8 CYS L 159 CYS L 171 1555 1555 2.03 SSBOND 9 CYS G 428 CYS G 501 1555 1555 2.03 LINK ND2 ASN A 111 C1 NAG F 1 1555 1555 1.54 LINK ND2 ASN B 80 C1 NAG J 1 1555 1555 1.43 LINK ND2 ASN B 149 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN C 208 C1 NAG C 501 1555 1555 1.45 LINK C PHE C 379 N P1L C 380 1555 1555 1.33 LINK C P1L C 380 N P1L C 381 1555 1555 1.34 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 K 1 1555 1555 1.44 LINK ND2 ASN E 80 C1 NAG N 1 1555 1555 1.42 LINK ND2 ASN E 149 C1 NAG M 1 1555 1555 1.47 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 1.40 LINK O6 BMA F 3 C1 MAN F 7 1555 1555 1.40 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 O3 MAN F 7 C1 MAN F 8 1555 1555 1.39 LINK O6 MAN F 7 C1 MAN F 10 1555 1555 1.40 LINK O2 MAN F 8 C1 MAN F 9 1555 1555 1.39 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.39 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.39 LINK O6 BMA I 3 C1 MAN I 4 1555 1555 1.41 LINK O3 BMA I 3 C1 MAN I 6 1555 1555 1.41 LINK O3 MAN I 4 C1 MAN I 5 1555 1555 1.40 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.39 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.40 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.40 LINK O6 BMA K 3 C1 MAN K 4 1555 1555 1.40 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.41 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.42 LINK O6 BMA M 3 C1 MAN M 4 1555 1555 1.45 LINK O3 BMA M 3 C1 MAN M 6 1555 1555 1.42 LINK O3 MAN M 4 C1 MAN M 5 1555 1555 1.46 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.39 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.39 CISPEP 1 PHE A 146 PRO A 147 0 -4.23 CISPEP 2 VAL B 109 THR B 110 0 -3.95 CISPEP 3 TYR B 143 PRO B 144 0 2.03 CISPEP 4 ILE C 124 THR C 125 0 -3.37 CISPEP 5 PHE C 158 PRO C 159 0 2.63 CISPEP 6 MET D 112 THR D 113 0 -8.33 CISPEP 7 PHE D 146 PRO D 147 0 -1.72 CISPEP 8 VAL E 109 THR E 110 0 -2.33 CISPEP 9 TYR E 143 PRO E 144 0 0.34 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