HEADER MEMBRANE PROTEIN 10-MAY-24 9FAX TITLE CRYOEM STRUCTURE OF HUMAN FULL-LENGTH BETA3GAMMA2 GABA(A) RECEPTOR IN TITLE 2 COMPLEX WITH MEGABODY25, DOUBLY OCCUPIED GARLH4 AND NEUROLIGIN2 TMD, TITLE 3 IN A CLOSED STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ISOFORM 2 OF GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT COMPND 3 GAMMA-2; COMPND 4 CHAIN: E, C; COMPND 5 SYNONYM: GABA(A) RECEPTOR SUBUNIT GAMMA-2,GABAAR SUBUNIT GAMMA-2; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NEUROLIGIN-2; COMPND 9 CHAIN: G, H; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: LHFPL TETRASPAN SUBFAMILY MEMBER 4 PROTEIN; COMPND 13 CHAIN: I, L; COMPND 14 SYNONYM: GABAA RECEPTOR REGULATORY LHFPL4,LIPOMA HMGIC FUSION COMPND 15 PARTNER-LIKE 4 PROTEIN; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-3; COMPND 19 CHAIN: B, A, D; COMPND 20 SYNONYM: GABA(A) RECEPTOR SUBUNIT BETA-3,GABAAR SUBUNIT BETA-3; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: MEGABODY25; COMPND 24 CHAIN: F; COMPND 25 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: GABRG2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-GNTI(-)TETR; SOURCE 9 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 10 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 11 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 14 MOL_ID: 2; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 GENE: NLGN2, KIAA1366; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-GNTI(-)TETR; SOURCE 22 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 23 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 24 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 27 MOL_ID: 3; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: LHFPL4, GARLH4; SOURCE 32 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-GNTI(-)TETR; SOURCE 35 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 36 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 37 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 38 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 39 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 40 MOL_ID: 4; SOURCE 41 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 42 ORGANISM_COMMON: HUMAN; SOURCE 43 ORGANISM_TAXID: 9606; SOURCE 44 GENE: GABRB3; SOURCE 45 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 46 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 47 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-GNTI(-)TETR; SOURCE 48 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 49 EXPRESSION_SYSTEM_TISSUE: KIDNEY; EMBRYO; SOURCE 50 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 51 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 52 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 53 MOL_ID: 5; SOURCE 54 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 55 ORGANISM_TAXID: 9844; SOURCE 56 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 57 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 58 EXPRESSION_SYSTEM_STRAIN: WK6SU-; SOURCE 59 EXPRESSION_SYSTEM_PLASMID: PMESD2 KEYWDS GABA, NEUROTRANSMISSION, TERNARY COMPLEX, INHIBITORY SYNAPSE, KEYWDS 2 MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR V.B.KASARAGOD,A.R.ARICESCU REVDAT 1 02-JUL-25 9FAX 0 JRNL AUTH V.B.KASARAGOD,A.R.ARICESCU JRNL TITL CRYOEM STRUCTURE OF HUMAN FULL-LENGTH BETA3GAMMA2 GABA(A) JRNL TITL 2 RECEPTOR IN COMPLEX WITH MEGABODY25, DOUBLY OCCUPIED GARLH4 JRNL TITL 3 AND NEUROLIGIN2 TMD, IN A CLOSED STATE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : WARP, EPU, CTFFIND, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7QNB REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER REMARK 3 REFINEMENT TARGET : FSC AT 0.5 REMARK 3 OVERALL ANISOTROPIC B VALUE : 20.000 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) : 2.900 REMARK 3 NUMBER OF PARTICLES : 62730 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 9FAX 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_1292138342. 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 BETA3GAMMA2 GABA(A) REMARK 245 RECEPTOR IN COMPLEX WITH REMARK 245 MEGABODY25, DOUBLY OCCUPIED REMARK 245 GARLH4 AND NEUROLIGIN2 TMD, IN REMARK 245 A CLOSED STATE 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 : 22699 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 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) : 4528.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 165000 REMARK 245 CALIBRATED MAGNIFICATION : 165000 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: DECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, G, I, B, A, D, C, H, L, F, REMARK 350 AND CHAINS: J, K, M, N, O, P 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 E 326 REMARK 465 SER E 327 REMARK 465 LYS E 328 REMARK 465 ASP E 329 REMARK 465 LYS E 330 REMARK 465 ASP E 331 REMARK 465 LYS E 332 REMARK 465 LYS E 333 REMARK 465 LYS E 334 REMARK 465 LYS E 335 REMARK 465 ASN E 336 REMARK 465 PRO E 337 REMARK 465 ALA E 338 REMARK 465 PRO E 339 REMARK 465 THR E 340 REMARK 465 ILE E 341 REMARK 465 ASP E 342 REMARK 465 ILE E 343 REMARK 465 ARG E 344 REMARK 465 PRO E 345 REMARK 465 ARG E 346 REMARK 465 SER E 347 REMARK 465 ALA E 348 REMARK 465 THR E 349 REMARK 465 ILE E 350 REMARK 465 GLN E 351 REMARK 465 MET E 352 REMARK 465 ASN E 353 REMARK 465 ASN E 354 REMARK 465 ALA E 355 REMARK 465 THR E 356 REMARK 465 HIS E 357 REMARK 465 LEU E 358 REMARK 465 GLN E 359 REMARK 465 GLU E 360 REMARK 465 ARG E 361 REMARK 465 ASP E 362 REMARK 465 GLU E 363 REMARK 465 GLU E 364 REMARK 465 TYR E 365 REMARK 465 GLY E 366 REMARK 465 TYR E 367 REMARK 465 GLU E 368 REMARK 465 ARG E 386 REMARK 465 THR E 387 REMARK 465 GLY E 388 REMARK 465 ALA E 389 REMARK 465 TRP E 390 REMARK 465 ARG E 391 REMARK 465 HIS E 392 REMARK 465 GLY E 393 REMARK 465 ARG E 394 REMARK 465 ILE E 395 REMARK 465 GLN I 201 REMARK 465 THR I 202 REMARK 465 ASP I 203 REMARK 465 GLY B 310 REMARK 465 PRO B 311 REMARK 465 GLN B 312 REMARK 465 ARG B 313 REMARK 465 GLN B 314 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 GLY A 310 REMARK 465 PRO A 311 REMARK 465 GLN A 312 REMARK 465 ARG A 313 REMARK 465 GLN A 314 REMARK 465 LYS A 315 REMARK 465 LYS A 316 REMARK 465 LEU A 317 REMARK 465 ALA A 318 REMARK 465 GLU A 319 REMARK 465 LYS A 320 REMARK 465 THR A 321 REMARK 465 ALA A 322 REMARK 465 LYS A 323 REMARK 465 ALA A 324 REMARK 465 LYS A 325 REMARK 465 ASN A 326 REMARK 465 ASP A 327 REMARK 465 ARG A 328 REMARK 465 SER A 329 REMARK 465 LYS A 330 REMARK 465 SER A 331 REMARK 465 GLU A 332 REMARK 465 SER A 333 REMARK 465 ASN A 334 REMARK 465 ARG A 335 REMARK 465 VAL A 336 REMARK 465 ASP A 337 REMARK 465 ALA A 338 REMARK 465 HIS A 339 REMARK 465 GLY A 340 REMARK 465 ASN A 341 REMARK 465 ILE A 342 REMARK 465 LEU A 343 REMARK 465 LEU A 344 REMARK 465 THR A 345 REMARK 465 SER A 346 REMARK 465 LEU A 347 REMARK 465 GLU A 348 REMARK 465 VAL A 349 REMARK 465 HIS A 350 REMARK 465 ASN A 351 REMARK 465 GLU A 352 REMARK 465 MET A 353 REMARK 465 ASN A 354 REMARK 465 GLU A 355 REMARK 465 VAL A 356 REMARK 465 SER A 357 REMARK 465 GLY A 358 REMARK 465 GLY A 359 REMARK 465 ILE A 360 REMARK 465 GLY A 361 REMARK 465 ASP A 362 REMARK 465 THR A 363 REMARK 465 ARG A 364 REMARK 465 ASN A 365 REMARK 465 SER A 366 REMARK 465 ALA A 367 REMARK 465 ILE A 368 REMARK 465 SER A 369 REMARK 465 PHE A 370 REMARK 465 ASP A 371 REMARK 465 ASN A 372 REMARK 465 SER A 373 REMARK 465 GLY A 374 REMARK 465 ILE A 375 REMARK 465 GLN A 376 REMARK 465 TYR A 377 REMARK 465 ARG A 378 REMARK 465 LYS A 379 REMARK 465 GLN A 380 REMARK 465 SER A 381 REMARK 465 MET A 382 REMARK 465 PRO A 383 REMARK 465 ARG A 384 REMARK 465 GLU A 385 REMARK 465 GLY A 386 REMARK 465 HIS A 387 REMARK 465 GLY A 388 REMARK 465 ARG A 389 REMARK 465 PHE A 390 REMARK 465 LEU A 391 REMARK 465 GLY A 392 REMARK 465 ASP A 393 REMARK 465 ARG A 394 REMARK 465 SER A 395 REMARK 465 LEU A 396 REMARK 465 PRO A 397 REMARK 465 HIS A 398 REMARK 465 LYS A 399 REMARK 465 LYS A 400 REMARK 465 THR A 401 REMARK 465 HIS A 402 REMARK 465 LEU A 403 REMARK 465 ARG A 404 REMARK 465 ARG A 405 REMARK 465 ARG A 406 REMARK 465 SER A 407 REMARK 465 SER A 408 REMARK 465 GLN A 409 REMARK 465 LEU A 410 REMARK 465 LYS A 411 REMARK 465 ILE A 412 REMARK 465 LYS A 413 REMARK 465 ILE A 414 REMARK 465 PRO A 415 REMARK 465 ASP A 416 REMARK 465 LEU A 417 REMARK 465 THR A 418 REMARK 465 GLY D 310 REMARK 465 PRO D 311 REMARK 465 GLN D 312 REMARK 465 ARG D 313 REMARK 465 GLN D 314 REMARK 465 LYS D 315 REMARK 465 LYS D 316 REMARK 465 LEU D 317 REMARK 465 ALA D 318 REMARK 465 GLU D 319 REMARK 465 LYS D 320 REMARK 465 THR D 321 REMARK 465 ALA D 322 REMARK 465 LYS D 323 REMARK 465 ALA D 324 REMARK 465 LYS D 325 REMARK 465 ASN D 326 REMARK 465 ASP D 327 REMARK 465 ARG D 328 REMARK 465 SER D 329 REMARK 465 LYS D 330 REMARK 465 SER D 331 REMARK 465 GLU D 332 REMARK 465 SER D 333 REMARK 465 ASN D 334 REMARK 465 ARG D 335 REMARK 465 VAL D 336 REMARK 465 ASP D 337 REMARK 465 ALA D 338 REMARK 465 HIS D 339 REMARK 465 GLY D 340 REMARK 465 ASN D 341 REMARK 465 ILE D 342 REMARK 465 LEU D 343 REMARK 465 LEU D 344 REMARK 465 THR D 345 REMARK 465 SER D 346 REMARK 465 LEU D 347 REMARK 465 GLU D 348 REMARK 465 VAL D 349 REMARK 465 HIS D 350 REMARK 465 ASN D 351 REMARK 465 GLU D 352 REMARK 465 MET D 353 REMARK 465 ASN D 354 REMARK 465 GLU D 355 REMARK 465 VAL D 356 REMARK 465 SER D 357 REMARK 465 GLY D 358 REMARK 465 GLY D 359 REMARK 465 ILE D 360 REMARK 465 GLY D 361 REMARK 465 ASP D 362 REMARK 465 THR D 363 REMARK 465 ARG D 364 REMARK 465 ASN D 365 REMARK 465 SER D 366 REMARK 465 ALA D 367 REMARK 465 ILE D 368 REMARK 465 SER D 369 REMARK 465 PHE D 370 REMARK 465 ASP D 371 REMARK 465 ASN D 372 REMARK 465 SER D 373 REMARK 465 GLY D 374 REMARK 465 ILE D 375 REMARK 465 GLN D 376 REMARK 465 TYR D 377 REMARK 465 ARG D 378 REMARK 465 LYS D 379 REMARK 465 GLN D 380 REMARK 465 SER D 381 REMARK 465 MET D 382 REMARK 465 PRO D 383 REMARK 465 ARG D 384 REMARK 465 GLU D 385 REMARK 465 GLY D 386 REMARK 465 HIS D 387 REMARK 465 GLY D 388 REMARK 465 ARG D 389 REMARK 465 PHE D 390 REMARK 465 LEU D 391 REMARK 465 GLY D 392 REMARK 465 ASP D 393 REMARK 465 ARG D 394 REMARK 465 SER D 395 REMARK 465 LEU D 396 REMARK 465 PRO D 397 REMARK 465 HIS D 398 REMARK 465 LYS D 399 REMARK 465 LYS D 400 REMARK 465 THR D 401 REMARK 465 HIS D 402 REMARK 465 LEU D 403 REMARK 465 ARG D 404 REMARK 465 ARG D 405 REMARK 465 ARG D 406 REMARK 465 SER D 407 REMARK 465 SER D 408 REMARK 465 GLN D 409 REMARK 465 LEU D 410 REMARK 465 LYS D 411 REMARK 465 ILE D 412 REMARK 465 LYS D 413 REMARK 465 ILE D 414 REMARK 465 PRO D 415 REMARK 465 ASP D 416 REMARK 465 LEU D 417 REMARK 465 THR D 418 REMARK 465 GLY C 25 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 GLY F 10 REMARK 465 LEU F 11 REMARK 465 VAL F 12 REMARK 465 GLN F 13 REMARK 465 THR F 14 REMARK 465 LYS F 15 REMARK 465 THR F 16 REMARK 465 THR F 17 REMARK 465 THR F 18 REMARK 465 SER F 19 REMARK 465 VAL F 20 REMARK 465 ILE F 21 REMARK 465 ASP F 22 REMARK 465 THR F 23 REMARK 465 THR F 24 REMARK 465 ASN F 25 REMARK 465 ASP F 26 REMARK 465 ALA F 27 REMARK 465 GLN F 28 REMARK 465 ASN F 29 REMARK 465 LEU F 30 REMARK 465 LEU F 31 REMARK 465 THR F 32 REMARK 465 GLN F 33 REMARK 465 ALA F 34 REMARK 465 GLN F 35 REMARK 465 THR F 36 REMARK 465 ILE F 37 REMARK 465 VAL F 38 REMARK 465 ASN F 39 REMARK 465 THR F 40 REMARK 465 LEU F 41 REMARK 465 LYS F 42 REMARK 465 ASP F 43 REMARK 465 TYR F 44 REMARK 465 CYS F 45 REMARK 465 PRO F 46 REMARK 465 ILE F 47 REMARK 465 LEU F 48 REMARK 465 ILE F 49 REMARK 465 ALA F 50 REMARK 465 LYS F 51 REMARK 465 SER F 52 REMARK 465 SER F 53 REMARK 465 SER F 54 REMARK 465 SER F 55 REMARK 465 ASN F 56 REMARK 465 GLY F 57 REMARK 465 GLY F 58 REMARK 465 THR F 59 REMARK 465 ASN F 60 REMARK 465 ASN F 61 REMARK 465 ALA F 62 REMARK 465 ASN F 63 REMARK 465 THR F 64 REMARK 465 PRO F 65 REMARK 465 SER F 66 REMARK 465 TRP F 67 REMARK 465 GLN F 68 REMARK 465 THR F 69 REMARK 465 ALA F 70 REMARK 465 GLY F 71 REMARK 465 GLY F 72 REMARK 465 GLY F 73 REMARK 465 LYS F 74 REMARK 465 ASN F 75 REMARK 465 SER F 76 REMARK 465 CYS F 77 REMARK 465 ALA F 78 REMARK 465 THR F 79 REMARK 465 PHE F 80 REMARK 465 GLY F 81 REMARK 465 ALA F 82 REMARK 465 GLU F 83 REMARK 465 PHE F 84 REMARK 465 SER F 85 REMARK 465 ALA F 86 REMARK 465 ALA F 87 REMARK 465 SER F 88 REMARK 465 ASP F 89 REMARK 465 MET F 90 REMARK 465 ILE F 91 REMARK 465 ASN F 92 REMARK 465 ASN F 93 REMARK 465 ALA F 94 REMARK 465 GLN F 95 REMARK 465 LYS F 96 REMARK 465 ILE F 97 REMARK 465 VAL F 98 REMARK 465 GLN F 99 REMARK 465 GLU F 100 REMARK 465 THR F 101 REMARK 465 GLN F 102 REMARK 465 GLN F 103 REMARK 465 LEU F 104 REMARK 465 SER F 105 REMARK 465 ALA F 106 REMARK 465 ASN F 107 REMARK 465 GLN F 108 REMARK 465 PRO F 109 REMARK 465 LYS F 110 REMARK 465 ASN F 111 REMARK 465 ILE F 112 REMARK 465 THR F 113 REMARK 465 GLN F 114 REMARK 465 PRO F 115 REMARK 465 HIS F 116 REMARK 465 ASN F 117 REMARK 465 LEU F 118 REMARK 465 ASN F 119 REMARK 465 LEU F 120 REMARK 465 ASN F 121 REMARK 465 SER F 122 REMARK 465 PRO F 123 REMARK 465 SER F 124 REMARK 465 SER F 125 REMARK 465 LEU F 126 REMARK 465 THR F 127 REMARK 465 ALA F 128 REMARK 465 LEU F 129 REMARK 465 ALA F 130 REMARK 465 GLN F 131 REMARK 465 LYS F 132 REMARK 465 MET F 133 REMARK 465 LEU F 134 REMARK 465 LYS F 135 REMARK 465 ASN F 136 REMARK 465 ALA F 137 REMARK 465 GLN F 138 REMARK 465 SER F 139 REMARK 465 GLN F 140 REMARK 465 ALA F 141 REMARK 465 GLU F 142 REMARK 465 ILE F 143 REMARK 465 LEU F 144 REMARK 465 LYS F 145 REMARK 465 LEU F 146 REMARK 465 ALA F 147 REMARK 465 ASN F 148 REMARK 465 GLN F 149 REMARK 465 VAL F 150 REMARK 465 GLU F 151 REMARK 465 SER F 152 REMARK 465 ASP F 153 REMARK 465 PHE F 154 REMARK 465 ASN F 155 REMARK 465 LYS F 156 REMARK 465 LEU F 157 REMARK 465 SER F 158 REMARK 465 SER F 159 REMARK 465 GLY F 160 REMARK 465 HIS F 161 REMARK 465 LEU F 162 REMARK 465 LYS F 163 REMARK 465 ASP F 164 REMARK 465 TYR F 165 REMARK 465 ILE F 166 REMARK 465 GLY F 167 REMARK 465 LYS F 168 REMARK 465 CYS F 169 REMARK 465 ASP F 170 REMARK 465 ALA F 171 REMARK 465 SER F 172 REMARK 465 ALA F 173 REMARK 465 ILE F 174 REMARK 465 SER F 175 REMARK 465 SER F 176 REMARK 465 ALA F 177 REMARK 465 ASN F 178 REMARK 465 MET F 179 REMARK 465 THR F 180 REMARK 465 MET F 181 REMARK 465 GLN F 182 REMARK 465 ASN F 183 REMARK 465 GLN F 184 REMARK 465 LYS F 185 REMARK 465 ASN F 186 REMARK 465 ASN F 187 REMARK 465 TRP F 188 REMARK 465 GLY F 189 REMARK 465 ASN F 190 REMARK 465 GLY F 191 REMARK 465 CYS F 192 REMARK 465 ALA F 193 REMARK 465 GLY F 194 REMARK 465 VAL F 195 REMARK 465 GLU F 196 REMARK 465 GLU F 197 REMARK 465 THR F 198 REMARK 465 GLN F 199 REMARK 465 SER F 200 REMARK 465 LEU F 201 REMARK 465 LEU F 202 REMARK 465 LYS F 203 REMARK 465 THR F 204 REMARK 465 SER F 205 REMARK 465 ALA F 206 REMARK 465 ALA F 207 REMARK 465 ASP F 208 REMARK 465 PHE F 209 REMARK 465 ASN F 210 REMARK 465 ASN F 211 REMARK 465 GLN F 212 REMARK 465 THR F 213 REMARK 465 PRO F 214 REMARK 465 GLN F 215 REMARK 465 ILE F 216 REMARK 465 ASN F 217 REMARK 465 GLN F 218 REMARK 465 ALA F 219 REMARK 465 GLN F 220 REMARK 465 ASN F 221 REMARK 465 LEU F 222 REMARK 465 ALA F 223 REMARK 465 ASN F 224 REMARK 465 THR F 225 REMARK 465 LEU F 226 REMARK 465 ILE F 227 REMARK 465 GLN F 228 REMARK 465 GLU F 229 REMARK 465 LEU F 230 REMARK 465 GLY F 231 REMARK 465 ASN F 232 REMARK 465 ASN F 233 REMARK 465 THR F 234 REMARK 465 TYR F 235 REMARK 465 GLU F 236 REMARK 465 GLN F 237 REMARK 465 LEU F 238 REMARK 465 SER F 239 REMARK 465 ARG F 240 REMARK 465 LEU F 241 REMARK 465 LEU F 242 REMARK 465 THR F 243 REMARK 465 ASN F 244 REMARK 465 ASP F 245 REMARK 465 ASN F 246 REMARK 465 GLY F 247 REMARK 465 THR F 248 REMARK 465 ASN F 249 REMARK 465 SER F 250 REMARK 465 LYS F 251 REMARK 465 THR F 252 REMARK 465 SER F 253 REMARK 465 ALA F 254 REMARK 465 GLN F 255 REMARK 465 ALA F 256 REMARK 465 ILE F 257 REMARK 465 ASN F 258 REMARK 465 GLN F 259 REMARK 465 ALA F 260 REMARK 465 VAL F 261 REMARK 465 ASN F 262 REMARK 465 ASN F 263 REMARK 465 LEU F 264 REMARK 465 ASN F 265 REMARK 465 GLU F 266 REMARK 465 ARG F 267 REMARK 465 ALA F 268 REMARK 465 LYS F 269 REMARK 465 THR F 270 REMARK 465 LEU F 271 REMARK 465 ALA F 272 REMARK 465 GLY F 273 REMARK 465 GLY F 274 REMARK 465 THR F 275 REMARK 465 THR F 276 REMARK 465 ASN F 277 REMARK 465 SER F 278 REMARK 465 PRO F 279 REMARK 465 ALA F 280 REMARK 465 TYR F 281 REMARK 465 GLN F 282 REMARK 465 ALA F 283 REMARK 465 THR F 284 REMARK 465 LEU F 285 REMARK 465 LEU F 286 REMARK 465 ALA F 287 REMARK 465 LEU F 288 REMARK 465 ARG F 289 REMARK 465 SER F 290 REMARK 465 VAL F 291 REMARK 465 LEU F 292 REMARK 465 GLY F 293 REMARK 465 LEU F 294 REMARK 465 TRP F 295 REMARK 465 ASN F 296 REMARK 465 SER F 297 REMARK 465 MET F 298 REMARK 465 GLY F 299 REMARK 465 TYR F 300 REMARK 465 ALA F 301 REMARK 465 VAL F 302 REMARK 465 ILE F 303 REMARK 465 CYS F 304 REMARK 465 GLY F 305 REMARK 465 GLY F 306 REMARK 465 TYR F 307 REMARK 465 THR F 308 REMARK 465 LYS F 309 REMARK 465 SER F 310 REMARK 465 PRO F 311 REMARK 465 GLY F 312 REMARK 465 GLU F 313 REMARK 465 ASN F 314 REMARK 465 ASN F 315 REMARK 465 GLN F 316 REMARK 465 LYS F 317 REMARK 465 ASP F 318 REMARK 465 PHE F 319 REMARK 465 HIS F 320 REMARK 465 TYR F 321 REMARK 465 THR F 322 REMARK 465 ASP F 323 REMARK 465 GLU F 324 REMARK 465 ASN F 325 REMARK 465 GLY F 326 REMARK 465 ASN F 327 REMARK 465 GLY F 328 REMARK 465 THR F 329 REMARK 465 THR F 330 REMARK 465 ILE F 331 REMARK 465 ASN F 332 REMARK 465 CYS F 333 REMARK 465 GLY F 334 REMARK 465 GLY F 335 REMARK 465 SER F 336 REMARK 465 THR F 337 REMARK 465 ASN F 338 REMARK 465 SER F 339 REMARK 465 ASN F 340 REMARK 465 GLY F 341 REMARK 465 THR F 342 REMARK 465 HIS F 343 REMARK 465 SER F 344 REMARK 465 TYR F 345 REMARK 465 ASN F 346 REMARK 465 GLY F 347 REMARK 465 THR F 348 REMARK 465 ASN F 349 REMARK 465 THR F 350 REMARK 465 LEU F 351 REMARK 465 LYS F 352 REMARK 465 ALA F 353 REMARK 465 ASP F 354 REMARK 465 LYS F 355 REMARK 465 ASN F 356 REMARK 465 VAL F 357 REMARK 465 SER F 358 REMARK 465 LEU F 359 REMARK 465 SER F 360 REMARK 465 ILE F 361 REMARK 465 GLU F 362 REMARK 465 GLN F 363 REMARK 465 TYR F 364 REMARK 465 GLU F 365 REMARK 465 LYS F 366 REMARK 465 ILE F 367 REMARK 465 HIS F 368 REMARK 465 GLU F 369 REMARK 465 ALA F 370 REMARK 465 TYR F 371 REMARK 465 GLN F 372 REMARK 465 ILE F 373 REMARK 465 LEU F 374 REMARK 465 SER F 375 REMARK 465 LYS F 376 REMARK 465 ALA F 377 REMARK 465 LEU F 378 REMARK 465 LYS F 379 REMARK 465 GLN F 380 REMARK 465 ALA F 381 REMARK 465 GLY F 382 REMARK 465 LEU F 383 REMARK 465 ALA F 384 REMARK 465 PRO F 385 REMARK 465 LEU F 386 REMARK 465 ASN F 387 REMARK 465 SER F 388 REMARK 465 LYS F 389 REMARK 465 GLY F 390 REMARK 465 GLU F 391 REMARK 465 LYS F 392 REMARK 465 LEU F 393 REMARK 465 GLU F 394 REMARK 465 ALA F 395 REMARK 465 HIS F 396 REMARK 465 VAL F 397 REMARK 465 THR F 398 REMARK 465 THR F 399 REMARK 465 SER F 400 REMARK 465 LYS F 401 REMARK 465 TYR F 402 REMARK 465 SER F 511 REMARK 465 SER F 512 REMARK 465 HIS F 513 REMARK 465 HIS F 514 REMARK 465 HIS F 515 REMARK 465 HIS F 516 REMARK 465 HIS F 517 REMARK 465 HIS F 518 REMARK 465 GLU F 519 REMARK 465 PRO F 520 REMARK 465 GLU F 521 REMARK 465 ALA F 522 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 D 149 C1 NAG P 1 1.63 REMARK 500 ND2 ASN B 149 O5 NAG J 1 2.02 REMARK 500 O4 NAG J 2 C2 BMA J 3 2.03 REMARK 500 O PHE C 382 O P1L C 385 2.11 REMARK 500 O3 BMA P 3 O5 MAN P 4 2.15 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 GLU E 36 -107.28 39.60 REMARK 500 ASP E 45 64.36 60.41 REMARK 500 SER E 61 149.63 -173.44 REMARK 500 ASN E 115 52.35 -91.71 REMARK 500 ASN E 128 39.79 -97.86 REMARK 500 MET E 160 30.67 -96.02 REMARK 500 ARG E 185 172.97 68.34 REMARK 500 SER E 187 -177.04 63.40 REMARK 500 ARG E 197 48.11 -92.53 REMARK 500 VAL E 204 -55.15 -124.79 REMARK 500 THR E 240 -50.77 -120.20 REMARK 500 PRO E 288 -174.56 -67.21 REMARK 500 LYS E 289 30.43 -88.95 REMARK 500 LEU E 370 -129.01 61.81 REMARK 500 LYS E 373 -136.35 -109.62 REMARK 500 PHE E 379 -123.65 -105.02 REMARK 500 PHE E 382 10.29 38.89 REMARK 500 GLU E 383 132.89 -38.95 REMARK 500 ASP E 384 -72.83 57.30 REMARK 500 SER G 669 -95.05 58.08 REMARK 500 ARG I 73 -10.29 73.25 REMARK 500 GLU I 74 -1.18 63.48 REMARK 500 PRO I 88 44.77 -87.20 REMARK 500 ASP I 170 31.12 -92.38 REMARK 500 LEU B 72 54.72 -92.85 REMARK 500 LEU B 145 30.49 -92.02 REMARK 500 ILE B 275 74.57 49.23 REMARK 500 SER A 46 133.07 174.54 REMARK 500 MET A 49 149.74 67.43 REMARK 500 ASN A 80 68.89 68.77 REMARK 500 LEU A 81 107.60 -59.68 REMARK 500 ASN A 85 -147.27 62.34 REMARK 500 ASP A 95 32.83 -93.46 REMARK 500 LYS A 274 -86.71 -62.34 REMARK 500 ILE A 275 91.54 38.18 REMARK 500 PHE A 307 -12.75 73.75 REMARK 500 TYR D 66 116.48 -166.14 REMARK 500 ASP D 95 34.51 -96.73 REMARK 500 PRO D 276 73.31 -68.88 REMARK 500 VAL C 48 -61.33 -104.81 REMARK 500 LYS C 94 21.60 -140.25 REMARK 500 ASN C 99 -168.45 -117.31 REMARK 500 ALA C 121 -168.78 -79.61 REMARK 500 PRO C 127 140.04 -30.42 REMARK 500 LEU C 155 32.64 -97.73 REMARK 500 SER C 187 -104.68 60.95 REMARK 500 ARG C 197 54.43 -91.30 REMARK 500 ARG C 284 59.76 -97.29 REMARK 500 LYS C 289 53.90 -90.02 REMARK 500 LYS C 373 -125.66 -145.64 REMARK 500 REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS. 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 NAG P 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-50285 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF HUMAN FULL-LENGTH BETA3GAMMA2 GABA(A) RECEPTOR REMARK 900 IN COMPLEX WITH MEGABODY25, DOUBLY OCCUPIED GARLH4 AND NEUROLIGIN2 REMARK 900 TMD, IN A CLOSED STATE DBREF 9FAX E 25 428 UNP P18507 GBRG2_HUMAN 64 467 DBREF 9FAX G 668 700 UNP Q8NFZ4 NLGN2_HUMAN 668 700 DBREF 9FAX I 16 203 UNP Q7Z7J7 LHPL4_HUMAN 16 203 DBREF 9FAX B 9 447 UNP P28472 GBRB3_HUMAN 34 472 DBREF 9FAX A 9 447 UNP P28472 GBRB3_HUMAN 34 472 DBREF 9FAX D 9 447 UNP P28472 GBRB3_HUMAN 34 472 DBREF 9FAX C 25 428 UNP P18507 GBRG2_HUMAN 64 467 DBREF 9FAX H 668 700 UNP Q8NFZ4 NLGN2_HUMAN 668 700 DBREF 9FAX L 16 203 UNP Q7Z7J7 LHPL4_HUMAN 16 203 DBREF 9FAX F 1 522 PDB 9FAX 9FAX 1 522 SEQADV 9FAX GLY E 429 UNP P18507 EXPRESSION TAG SEQADV 9FAX GLY C 429 UNP P18507 EXPRESSION TAG SEQRES 1 E 405 GLY ASP VAL THR VAL ILE LEU ASN ASN LEU LEU GLU GLY SEQRES 2 E 405 TYR ASP ASN LYS LEU ARG PRO ASP ILE GLY VAL LYS PRO SEQRES 3 E 405 THR LEU ILE HIS THR ASP MET TYR VAL ASN SER ILE GLY SEQRES 4 E 405 PRO VAL ASN ALA ILE ASN MET GLU TYR THR ILE ASP ILE SEQRES 5 E 405 PHE PHE ALA GLN THR TRP TYR ASP ARG ARG LEU LYS PHE SEQRES 6 E 405 ASN SER THR ILE LYS VAL LEU ARG LEU ASN SER ASN MET SEQRES 7 E 405 VAL GLY LYS ILE TRP ILE PRO ASP THR PHE PHE ARG ASN SEQRES 8 E 405 SER LYS LYS ALA ASP ALA HIS TRP ILE THR THR PRO ASN SEQRES 9 E 405 ARG MET LEU ARG ILE TRP ASN ASP GLY ARG VAL LEU TYR SEQRES 10 E 405 THR LEU ARG LEU THR ILE ASP ALA GLU CYS GLN LEU GLN SEQRES 11 E 405 LEU HIS ASN PHE PRO MET ASP GLU HIS SER CYS PRO LEU SEQRES 12 E 405 GLU PHE SER SER TYR GLY TYR PRO ARG GLU GLU ILE VAL SEQRES 13 E 405 TYR GLN TRP LYS ARG SER SER VAL GLU VAL GLY ASP THR SEQRES 14 E 405 ARG SER TRP ARG LEU TYR GLN PHE SER PHE VAL GLY LEU SEQRES 15 E 405 ARG ASN THR THR GLU VAL VAL LYS THR THR SER GLY ASP SEQRES 16 E 405 TYR VAL VAL MET SER VAL TYR PHE ASP LEU SER ARG ARG SEQRES 17 E 405 MET GLY TYR PHE THR ILE GLN THR TYR ILE PRO CYS THR SEQRES 18 E 405 LEU ILE VAL VAL LEU SER TRP VAL SER PHE TRP ILE ASN SEQRES 19 E 405 LYS ASP ALA VAL PRO ALA ARG THR SER LEU GLY ILE THR SEQRES 20 E 405 THR VAL LEU THR MET THR THR LEU SER THR ILE ALA ARG SEQRES 21 E 405 LYS SER LEU PRO LYS VAL SER TYR VAL THR ALA MET ASP SEQRES 22 E 405 LEU PHE VAL SER VAL CYS PHE ILE PHE VAL PHE SER ALA SEQRES 23 E 405 LEU VAL GLU TYR GLY THR LEU HIS TYR PHE VAL SER ASN SEQRES 24 E 405 ARG LYS PRO SER LYS ASP LYS ASP LYS LYS LYS LYS ASN SEQRES 25 E 405 PRO ALA PRO THR ILE ASP ILE ARG PRO ARG SER ALA THR SEQRES 26 E 405 ILE GLN MET ASN ASN ALA THR HIS LEU GLN GLU ARG ASP SEQRES 27 E 405 GLU GLU TYR GLY TYR GLU CYS LEU ASP GLY LYS ASP CYS SEQRES 28 E 405 ALA SER PHE PHE P1L P1L PHE GLU ASP P1L ARG THR GLY SEQRES 29 E 405 ALA TRP ARG HIS GLY ARG ILE HIS ILE ARG ILE ALA LYS SEQRES 30 E 405 MET ASP SER TYR ALA ARG ILE PHE PHE PRO THR ALA PHE SEQRES 31 E 405 CYS LEU PHE ASN LEU VAL TYR TRP VAL SER TYR LEU TYR SEQRES 32 E 405 LEU GLY SEQRES 1 G 33 ASP SER ARG ASP TYR SER THR GLU LEU SER VAL THR VAL SEQRES 2 G 33 ALA VAL GLY ALA SER LEU LEU PHE LEU ASN ILE LEU ALA SEQRES 3 G 33 PHE ALA ALA LEU TYR TYR LYS SEQRES 1 I 188 MET ARG ASN SER ARG ALA ILE GLY VAL LEU TRP ALA ILE SEQRES 2 I 188 PHE THR ILE CYS PHE ALA ILE ILE ASN VAL VAL VAL PHE SEQRES 3 I 188 ILE GLN PRO TYR TRP VAL GLY ASP SER VAL SER THR PRO SEQRES 4 I 188 LYS PRO GLY TYR PHE GLY LEU PHE HIS TYR CYS VAL GLY SEQRES 5 I 188 SER GLY LEU ALA GLY ARG GLU LEU THR CYS ARG GLY SER SEQRES 6 I 188 PHE THR ASP PHE SER THR ILE PRO SER SER ALA PHE LYS SEQRES 7 I 188 ALA ALA ALA PHE PHE VAL LEU LEU SER MET VAL LEU ILE SEQRES 8 I 188 LEU GLY CYS ILE THR CYS PHE SER LEU PHE PHE PHE CYS SEQRES 9 I 188 ASN THR ALA THR VAL TYR LYS ILE CYS ALA TRP MET GLN SEQRES 10 I 188 LEU LEU ALA ALA LEU CYS LEU VAL LEU GLY CYS MET ILE SEQRES 11 I 188 PHE PRO ASP GLY TRP ASP ALA GLU THR ILE ARG ASP MET SEQRES 12 I 188 CYS GLY ALA LYS THR GLY LYS TYR SER LEU GLY ASP CYS SEQRES 13 I 188 SER VAL ARG TRP ALA TYR ILE LEU ALA ILE ILE GLY ILE SEQRES 14 I 188 LEU ASN ALA LEU ILE LEU SER PHE LEU ALA PHE VAL LEU SEQRES 15 I 188 GLY ASN ARG GLN THR ASP 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 A 439 MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS SEQRES 2 A 439 GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO SEQRES 3 A 439 PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE SEQRES 4 A 439 ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU THR SEQRES 5 A 439 MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA SEQRES 6 A 439 TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG SEQRES 7 A 439 VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU SEQRES 8 A 439 ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS SEQRES 9 A 439 ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU SEQRES 10 A 439 TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET MET SEQRES 11 A 439 ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR SEQRES 12 A 439 LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE SEQRES 13 A 439 GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY SEQRES 14 A 439 VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU SEQRES 15 A 439 HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY SEQRES 16 A 439 ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG SEQRES 17 A 439 ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER SEQRES 18 A 439 ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE SEQRES 19 A 439 ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE SEQRES 20 A 439 THR THR VAL LEU THR MET THR THR ILE ASN THR HIS LEU SEQRES 21 A 439 ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE SEQRES 22 A 439 ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU SEQRES 23 A 439 ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SEQRES 24 A 439 GLY ARG GLY PRO GLN ARG GLN LYS LYS LEU ALA GLU LYS SEQRES 25 A 439 THR ALA LYS ALA LYS ASN ASP ARG SER LYS SER GLU SER SEQRES 26 A 439 ASN ARG VAL ASP ALA HIS GLY ASN ILE LEU LEU THR SER SEQRES 27 A 439 LEU GLU VAL HIS ASN GLU MET ASN GLU VAL SER GLY GLY SEQRES 28 A 439 ILE GLY ASP THR ARG ASN SER ALA ILE SER PHE ASP ASN SEQRES 29 A 439 SER GLY ILE GLN TYR ARG LYS GLN SER MET PRO ARG GLU SEQRES 30 A 439 GLY HIS GLY ARG PHE LEU GLY ASP ARG SER LEU PRO HIS SEQRES 31 A 439 LYS LYS THR HIS LEU ARG ARG ARG SER SER GLN LEU LYS SEQRES 32 A 439 ILE LYS ILE PRO ASP LEU THR ASP VAL ASN ALA ILE ASP SEQRES 33 A 439 ARG TRP SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU SEQRES 34 A 439 PHE ASN LEU VAL TYR TRP LEU TYR TYR VAL SEQRES 1 D 439 MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS SEQRES 2 D 439 GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO SEQRES 3 D 439 PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE SEQRES 4 D 439 ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU THR SEQRES 5 D 439 MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA SEQRES 6 D 439 TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG SEQRES 7 D 439 VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU SEQRES 8 D 439 ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS SEQRES 9 D 439 ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU SEQRES 10 D 439 TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET MET SEQRES 11 D 439 ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR SEQRES 12 D 439 LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE SEQRES 13 D 439 GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY SEQRES 14 D 439 VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU SEQRES 15 D 439 HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY SEQRES 16 D 439 ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG SEQRES 17 D 439 ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER SEQRES 18 D 439 ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE SEQRES 19 D 439 ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE SEQRES 20 D 439 THR THR VAL LEU THR MET THR THR ILE ASN THR HIS LEU SEQRES 21 D 439 ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE SEQRES 22 D 439 ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU SEQRES 23 D 439 ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SEQRES 24 D 439 GLY ARG GLY PRO GLN ARG GLN LYS LYS LEU ALA GLU LYS SEQRES 25 D 439 THR ALA LYS ALA LYS ASN ASP ARG SER LYS SER GLU SER SEQRES 26 D 439 ASN ARG VAL ASP ALA HIS GLY ASN ILE LEU LEU THR SER SEQRES 27 D 439 LEU GLU VAL HIS ASN GLU MET ASN GLU VAL SER GLY GLY SEQRES 28 D 439 ILE GLY ASP THR ARG ASN SER ALA ILE SER PHE ASP ASN SEQRES 29 D 439 SER GLY ILE GLN TYR ARG LYS GLN SER MET PRO ARG GLU SEQRES 30 D 439 GLY HIS GLY ARG PHE LEU GLY ASP ARG SER LEU PRO HIS SEQRES 31 D 439 LYS LYS THR HIS LEU ARG ARG ARG SER SER GLN LEU LYS SEQRES 32 D 439 ILE LYS ILE PRO ASP LEU THR ASP VAL ASN ALA ILE ASP SEQRES 33 D 439 ARG TRP SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU SEQRES 34 D 439 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 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 188 MET ARG ASN SER ARG ALA ILE GLY VAL LEU TRP ALA ILE SEQRES 2 L 188 PHE THR ILE CYS PHE ALA ILE ILE ASN VAL VAL VAL PHE SEQRES 3 L 188 ILE GLN PRO TYR TRP VAL GLY ASP SER VAL SER THR PRO SEQRES 4 L 188 LYS PRO GLY TYR PHE GLY LEU PHE HIS TYR CYS VAL GLY SEQRES 5 L 188 SER GLY LEU ALA GLY ARG GLU LEU THR CYS ARG GLY SER SEQRES 6 L 188 PHE THR ASP PHE SER THR ILE PRO SER SER ALA PHE LYS SEQRES 7 L 188 ALA ALA ALA PHE PHE VAL LEU LEU SER MET VAL LEU ILE SEQRES 8 L 188 LEU GLY CYS ILE THR CYS PHE SER LEU PHE PHE PHE CYS SEQRES 9 L 188 ASN THR ALA THR VAL TYR LYS ILE CYS ALA TRP MET GLN SEQRES 10 L 188 LEU LEU ALA ALA LEU CYS LEU VAL LEU GLY CYS MET ILE SEQRES 11 L 188 PHE PRO ASP GLY TRP ASP ALA GLU THR ILE ARG ASP MET SEQRES 12 L 188 CYS GLY ALA LYS THR GLY LYS TYR SER LEU GLY ASP CYS SEQRES 13 L 188 SER VAL ARG TRP ALA TYR ILE LEU ALA ILE ILE GLY ILE SEQRES 14 L 188 LEU ASN ALA LEU ILE LEU SER PHE LEU ALA PHE VAL LEU SEQRES 15 L 188 GLY ASN ARG GLN THR ASP SEQRES 1 F 522 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 522 THR LYS THR THR THR SER VAL ILE ASP THR THR ASN ASP SEQRES 3 F 522 ALA GLN ASN LEU LEU THR GLN ALA GLN THR ILE VAL ASN SEQRES 4 F 522 THR LEU LYS ASP TYR CYS PRO ILE LEU ILE ALA LYS SER SEQRES 5 F 522 SER SER SER ASN GLY GLY THR ASN ASN ALA ASN THR PRO SEQRES 6 F 522 SER TRP GLN THR ALA GLY GLY GLY LYS ASN SER CYS ALA SEQRES 7 F 522 THR PHE GLY ALA GLU PHE SER ALA ALA SER ASP MET ILE SEQRES 8 F 522 ASN ASN ALA GLN LYS ILE VAL GLN GLU THR GLN GLN LEU SEQRES 9 F 522 SER ALA ASN GLN PRO LYS ASN ILE THR GLN PRO HIS ASN SEQRES 10 F 522 LEU ASN LEU ASN SER PRO SER SER LEU THR ALA LEU ALA SEQRES 11 F 522 GLN LYS MET LEU LYS ASN ALA GLN SER GLN ALA GLU ILE SEQRES 12 F 522 LEU LYS LEU ALA ASN GLN VAL GLU SER ASP PHE ASN LYS SEQRES 13 F 522 LEU SER SER GLY HIS LEU LYS ASP TYR ILE GLY LYS CYS SEQRES 14 F 522 ASP ALA SER ALA ILE SER SER ALA ASN MET THR MET GLN SEQRES 15 F 522 ASN GLN LYS ASN ASN TRP GLY ASN GLY CYS ALA GLY VAL SEQRES 16 F 522 GLU GLU THR GLN SER LEU LEU LYS THR SER ALA ALA ASP SEQRES 17 F 522 PHE ASN ASN GLN THR PRO GLN ILE ASN GLN ALA GLN ASN SEQRES 18 F 522 LEU ALA ASN THR LEU ILE GLN GLU LEU GLY ASN ASN THR SEQRES 19 F 522 TYR GLU GLN LEU SER ARG LEU LEU THR ASN ASP ASN GLY SEQRES 20 F 522 THR ASN SER LYS THR SER ALA GLN ALA ILE ASN GLN ALA SEQRES 21 F 522 VAL ASN ASN LEU ASN GLU ARG ALA LYS THR LEU ALA GLY SEQRES 22 F 522 GLY THR THR ASN SER PRO ALA TYR GLN ALA THR LEU LEU SEQRES 23 F 522 ALA LEU ARG SER VAL LEU GLY LEU TRP ASN SER MET GLY SEQRES 24 F 522 TYR ALA VAL ILE CYS GLY GLY TYR THR LYS SER PRO GLY SEQRES 25 F 522 GLU ASN ASN GLN LYS ASP PHE HIS TYR THR ASP GLU ASN SEQRES 26 F 522 GLY ASN GLY THR THR ILE ASN CYS GLY GLY SER THR ASN SEQRES 27 F 522 SER ASN GLY THR HIS SER TYR ASN GLY THR ASN THR LEU SEQRES 28 F 522 LYS ALA ASP LYS ASN VAL SER LEU SER ILE GLU GLN TYR SEQRES 29 F 522 GLU LYS ILE HIS GLU ALA TYR GLN ILE LEU SER LYS ALA SEQRES 30 F 522 LEU LYS GLN ALA GLY LEU ALA PRO LEU ASN SER LYS GLY SEQRES 31 F 522 GLU LYS LEU GLU ALA HIS VAL THR THR SER LYS TYR GLY SEQRES 32 F 522 SER LEU ARG LEU SER CYS ALA ALA SER GLY HIS THR PHE SEQRES 33 F 522 ASN TYR PRO ILE MET GLY TRP PHE ARG GLN ALA PRO GLY SEQRES 34 F 522 LYS GLU ARG GLU PHE VAL GLY ALA ILE SER TRP SER GLY SEQRES 35 F 522 GLY SER THR SER TYR ALA ASP SER VAL LYS ASP ARG PHE SEQRES 36 F 522 THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL TYR LEU SEQRES 37 F 522 GLU MET ASN ASN LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 38 F 522 TYR CYS ALA ALA LYS GLY ARG TYR SER GLY GLY LEU TYR SEQRES 39 F 522 TYR PRO THR ASN TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 40 F 522 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS GLU PRO SEQRES 41 F 522 GLU ALA MODRES 9FAX P1L E 380 CYS MODIFIED RESIDUE MODRES 9FAX P1L E 381 CYS MODIFIED RESIDUE MODRES 9FAX P1L E 385 CYS MODIFIED RESIDUE MODRES 9FAX P1L C 380 CYS MODIFIED RESIDUE MODRES 9FAX P1L C 381 CYS MODIFIED RESIDUE MODRES 9FAX P1L C 385 CYS MODIFIED RESIDUE HET P1L E 380 23 HET P1L E 381 23 HET P1L E 385 23 HET P1L C 380 23 HET P1L C 381 23 HET P1L C 385 23 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET MAN J 4 11 HET MAN J 5 11 HET MAN J 6 11 HET MAN J 7 11 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 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 NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET MAN P 4 11 HET MAN P 5 11 HET NAG E 501 14 HET R16 E 502 16 HET R16 E 503 16 HET PX2 E 504 36 HET CLR E 505 28 HET R16 E 506 16 HET PGW I 301 51 HET PGW I 302 51 HET PX2 B 501 36 HET HEX B 502 6 HET HEX B 503 6 HET D10 B 504 10 HET HEX B 505 6 HET D10 B 506 10 HET PLM A 501 18 HET HEX A 502 6 HET HEX A 503 6 HET HEX A 504 6 HET HEX A 505 6 HET HEX A 506 6 HET D10 D 501 10 HET PLM D 502 18 HET D10 D 503 10 HET D10 D 504 10 HET HEX D 505 6 HET HEX D 506 6 HET PLM D 507 18 HET HEX D 508 6 HET HEX D 509 6 HET NAG C 501 14 HET R16 C 502 16 HET R16 C 503 16 HET PLM C 504 18 HET PLM C 505 18 HET HEX C 506 6 HET CLR C 507 28 HET PGW C 508 51 HET PGW L 301 51 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 R16 HEXADECANE HETNAM PX2 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE HETNAM CLR CHOLESTEROL 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 HEX HEXANE HETNAM D10 DECANE HETNAM PLM PALMITIC ACID 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 PGW 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-(1- HETSYN 2 PGW GLYCEROL)]; PHOSPHATIDYLGLYCEROL FORMUL 1 P1L 6(C19 H37 N O3 S) FORMUL 11 NAG 14(C8 H15 N O6) FORMUL 11 BMA 5(C6 H12 O6) FORMUL 11 MAN 9(C6 H12 O6) FORMUL 18 R16 5(C16 H34) FORMUL 20 PX2 2(C27 H52 O8 P 1-) FORMUL 21 CLR 2(C27 H46 O) FORMUL 23 PGW 4(C40 H77 O10 P) FORMUL 26 HEX 13(C6 H14) FORMUL 28 D10 5(C10 H22) FORMUL 31 PLM 5(C16 H32 O2) HELIX 1 AA1 GLY E 25 GLU E 36 1 12 HELIX 2 AA2 ASN E 101 LYS E 105 5 5 HELIX 3 AA3 GLN E 154 PHE E 158 5 5 HELIX 4 AA4 ASP E 192 TRP E 196 5 5 HELIX 5 AA5 MET E 233 THR E 240 1 8 HELIX 6 AA6 THR E 240 VAL E 253 1 14 HELIX 7 AA7 SER E 254 ILE E 257 5 4 HELIX 8 AA8 ALA E 261 ARG E 284 1 24 HELIX 9 AA9 THR E 294 SER E 322 1 29 HELIX 10 AB1 ASP E 374 PHE E 379 1 6 HELIX 11 AB2 HIS E 396 ALA E 400 5 5 HELIX 12 AB3 LYS E 401 TYR E 427 1 27 HELIX 13 AB4 TYR G 672 TYR G 699 1 28 HELIX 14 AB5 ARG I 17 GLN I 43 1 27 HELIX 15 AB6 ASP I 83 ILE I 87 5 5 HELIX 16 AB7 SER I 89 PHE I 113 1 25 HELIX 17 AB8 SER I 114 PHE I 118 5 5 HELIX 18 AB9 ASN I 120 PHE I 146 1 27 HELIX 19 AC1 PRO I 147 ASP I 151 5 5 HELIX 20 AC2 ALA I 152 CYS I 159 1 8 HELIX 21 AC3 ARG I 174 ARG I 200 1 27 HELIX 22 AC4 SER B 10 LYS B 21 1 12 HELIX 23 AC5 ASP B 84 GLN B 90 5 7 HELIX 24 AC6 GLY B 170 LYS B 173 5 4 HELIX 25 AC7 ILE B 218 THR B 225 1 8 HELIX 26 AC8 THR B 225 TRP B 237 1 13 HELIX 27 AC9 VAL B 238 ILE B 242 5 5 HELIX 28 AD1 ALA B 246 LEU B 272 1 27 HELIX 29 AD2 LYS B 279 GLY B 308 1 30 HELIX 30 AD3 ASN B 421 TYR B 446 1 26 HELIX 31 AD4 SER A 10 LYS A 21 1 12 HELIX 32 AD5 LYS A 70 ALA A 73 5 4 HELIX 33 AD6 ASP A 84 LEU A 91 1 8 HELIX 34 AD7 ASP A 139 TYR A 143 5 5 HELIX 35 AD8 GLY A 170 LYS A 173 5 4 HELIX 36 AD9 GLY A 219 THR A 225 1 7 HELIX 37 AE1 THR A 225 VAL A 238 1 14 HELIX 38 AE2 SER A 239 TRP A 241 5 3 HELIX 39 AE3 ALA A 246 GLU A 270 1 25 HELIX 40 AE4 LYS A 279 PHE A 306 1 28 HELIX 41 AE5 ASN A 421 VAL A 447 1 27 HELIX 42 AE6 SER D 10 LYS D 21 1 12 HELIX 43 AE7 LYS D 70 ALA D 73 5 4 HELIX 44 AE8 ASP D 84 LEU D 91 5 8 HELIX 45 AE9 ASP D 139 TYR D 143 5 5 HELIX 46 AF1 GLY D 170 LYS D 173 5 4 HELIX 47 AF2 ILE D 218 THR D 225 1 8 HELIX 48 AF3 THR D 225 VAL D 238 1 14 HELIX 49 AF4 SER D 239 ILE D 242 5 4 HELIX 50 AF5 ALA D 246 GLU D 270 1 25 HELIX 51 AF6 LYS D 279 PHE D 306 1 28 HELIX 52 AF7 ASN D 421 VAL D 447 1 27 HELIX 53 AF8 VAL C 27 LEU C 34 1 8 HELIX 54 AF9 ARG C 85 LYS C 88 5 4 HELIX 55 AG1 ASN C 99 ILE C 106 1 8 HELIX 56 AG2 ASP C 192 TRP C 196 5 5 HELIX 57 AG3 MET C 233 ILE C 257 1 25 HELIX 58 AG4 ALA C 261 ILE C 282 1 22 HELIX 59 AG5 ALA C 283 SER C 286 5 4 HELIX 60 AG6 THR C 294 ARG C 324 1 31 HELIX 61 AG7 ASP C 374 P1L C 380 1 7 HELIX 62 AG8 ARG C 398 ALA C 400 5 3 HELIX 63 AG9 LYS C 401 TYR C 427 1 27 HELIX 64 AH1 TYR H 672 TYR H 699 1 28 HELIX 65 AH2 ARG L 17 GLN L 43 1 27 HELIX 66 AH3 SER L 89 PHE L 116 1 28 HELIX 67 AH4 ASN L 120 PHE L 146 1 27 HELIX 68 AH5 PRO L 147 ASP L 151 5 5 HELIX 69 AH6 ALA L 152 GLY L 160 1 9 HELIX 70 AH7 ARG L 174 ARG L 200 1 27 HELIX 71 AH8 LYS F 474 THR F 478 5 5 SHEET 1 AA1 5 VAL E 95 LEU E 98 0 SHEET 2 AA1 5 MET E 130 TRP E 134 -1 O LEU E 131 N LEU E 98 SHEET 3 AA1 5 ARG E 138 THR E 142 -1 O THR E 142 N MET E 130 SHEET 4 AA1 5 ILE E 74 TYR E 83 -1 N TRP E 82 O VAL E 139 SHEET 5 AA1 5 LEU E 145 ILE E 147 -1 O LEU E 145 N ILE E 76 SHEET 1 AA2 6 VAL E 95 LEU E 98 0 SHEET 2 AA2 6 MET E 130 TRP E 134 -1 O LEU E 131 N LEU E 98 SHEET 3 AA2 6 ARG E 138 THR E 142 -1 O THR E 142 N MET E 130 SHEET 4 AA2 6 ILE E 74 TYR E 83 -1 N TRP E 82 O VAL E 139 SHEET 5 AA2 6 THR E 51 ILE E 62 -1 N TYR E 58 O PHE E 77 SHEET 6 AA2 6 ILE E 179 TRP E 183 1 O GLN E 182 N THR E 55 SHEET 1 AA3 4 THR E 111 PHE E 113 0 SHEET 2 AA3 4 GLU E 162 SER E 171 -1 O SER E 170 N PHE E 112 SHEET 3 AA3 4 VAL E 221 ARG E 231 -1 O LEU E 229 N HIS E 163 SHEET 4 AA3 4 PHE E 201 VAL E 212 -1 N GLY E 205 O ASP E 228 SHEET 1 AA4 4 VAL I 47 GLY I 48 0 SHEET 2 AA4 4 GLY I 57 PHE I 59 -1 O PHE I 59 N VAL I 47 SHEET 3 AA4 4 TYR I 64 VAL I 66 -1 O CYS I 65 N TYR I 58 SHEET 4 AA4 4 THR I 76 ARG I 78 -1 O THR I 76 N VAL I 66 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 LEU B 125 N ARG B 117 SHEET 4 AA5 6 ASP B 56 ARG B 68 -1 N LEU B 59 O THR B 132 SHEET 5 AA5 6 VAL B 36 SER B 51 -1 N SER B 51 O ASP B 56 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 102 SHEET 3 AA6 5 ASP B 56 ARG B 68 -1 N LEU B 59 O THR B 132 SHEET 4 AA6 5 VAL B 36 SER B 51 -1 N SER B 51 O ASP B 56 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 GLU B 190 O ARG B 213 SHEET 1 AA8 6 THR A 82 LEU A 83 0 SHEET 2 AA8 6 ARG A 114 LEU A 118 -1 O ILE A 116 N LEU A 83 SHEET 3 AA8 6 THR A 123 ALA A 135 -1 O LEU A 125 N ARG A 117 SHEET 4 AA8 6 ASP A 56 ARG A 68 -1 N TRP A 67 O VAL A 124 SHEET 5 AA8 6 VAL A 36 SER A 51 -1 N ASP A 48 O THR A 58 SHEET 6 AA8 6 ILE A 164 TRP A 168 1 O GLU A 165 N VAL A 38 SHEET 1 AA9 5 SER A 104 VAL A 106 0 SHEET 2 AA9 5 THR A 123 ALA A 135 -1 O THR A 131 N PHE A 105 SHEET 3 AA9 5 ASP A 56 ARG A 68 -1 N TRP A 67 O VAL A 124 SHEET 4 AA9 5 VAL A 36 SER A 51 -1 N ASP A 48 O THR A 58 SHEET 5 AA9 5 VAL A 175 THR A 176 1 O THR A 176 N ILE A 42 SHEET 1 AB1 4 THR A 96 PHE A 98 0 SHEET 2 AB1 4 GLU A 147 SER A 156 -1 O GLU A 155 N TYR A 97 SHEET 3 AB1 4 ALA A 204 ARG A 216 -1 O LEU A 208 N ILE A 154 SHEET 4 AB1 4 PHE A 186 VAL A 199 -1 N GLU A 190 O ARG A 213 SHEET 1 AB2 5 ASP D 101 VAL D 106 0 SHEET 2 AB2 5 THR D 123 ALA D 135 -1 O THR D 133 N LYS D 103 SHEET 3 AB2 5 ASP D 56 ARG D 68 -1 N PHE D 63 O LEU D 128 SHEET 4 AB2 5 VAL D 36 SER D 51 -1 N GLY D 39 O TYR D 66 SHEET 5 AB2 5 ILE D 164 TRP D 168 1 O GLU D 165 N VAL D 38 SHEET 1 AB3 5 ARG D 114 LEU D 118 0 SHEET 2 AB3 5 THR D 123 ALA D 135 -1 O GLY D 127 N MET D 115 SHEET 3 AB3 5 ASP D 56 ARG D 68 -1 N PHE D 63 O LEU D 128 SHEET 4 AB3 5 VAL D 36 SER D 51 -1 N GLY D 39 O TYR D 66 SHEET 5 AB3 5 VAL D 175 THR D 176 1 O THR D 176 N ILE D 44 SHEET 1 AB4 4 THR D 96 PHE D 98 0 SHEET 2 AB4 4 GLU D 147 SER D 156 -1 O GLU D 155 N TYR D 97 SHEET 3 AB4 4 ALA D 204 ARG D 216 -1 O LEU D 208 N ILE D 154 SHEET 4 AB4 4 PHE D 186 VAL D 199 -1 N GLU D 190 O ARG D 213 SHEET 1 AB5 6 LEU C 96 ARG C 97 0 SHEET 2 AB5 6 ARG C 129 ILE C 133 -1 O ILE C 133 N LEU C 96 SHEET 3 AB5 6 ARG C 138 GLU C 150 -1 O LEU C 140 N ARG C 132 SHEET 4 AB5 6 GLU C 71 TYR C 83 -1 N TRP C 82 O VAL C 139 SHEET 5 AB5 6 THR C 51 ASN C 66 -1 N ASP C 56 O ALA C 79 SHEET 6 AB5 6 ILE C 179 TRP C 183 1 O VAL C 180 N ILE C 53 SHEET 1 AB6 5 SER C 116 ASP C 120 0 SHEET 2 AB6 5 ARG C 138 GLU C 150 -1 O ASP C 148 N LYS C 117 SHEET 3 AB6 5 GLU C 71 TYR C 83 -1 N TRP C 82 O VAL C 139 SHEET 4 AB6 5 THR C 51 ASN C 66 -1 N ASP C 56 O ALA C 79 SHEET 5 AB6 5 GLU C 189 VAL C 190 1 O GLU C 189 N VAL C 59 SHEET 1 AB7 4 PHE C 112 PHE C 113 0 SHEET 2 AB7 4 GLU C 162 SER C 170 -1 O SER C 170 N PHE C 112 SHEET 3 AB7 4 ASP C 219 ARG C 231 -1 O MET C 223 N PHE C 169 SHEET 4 AB7 4 PHE C 201 LYS C 214 -1 N VAL C 213 O TYR C 220 SHEET 1 AB8 2 VAL L 47 GLY L 48 0 SHEET 2 AB8 2 SER L 172 VAL L 173 -1 O SER L 172 N GLY L 48 SHEET 1 AB9 3 GLY L 57 PHE L 59 0 SHEET 2 AB9 3 TYR L 64 VAL L 66 -1 O CYS L 65 N TYR L 58 SHEET 3 AB9 3 THR L 76 ARG L 78 -1 O ARG L 78 N TYR L 64 SHEET 1 AC1 4 VAL F 2 SER F 7 0 SHEET 2 AC1 4 LEU F 405 GLY F 413 -1 O SER F 408 N SER F 7 SHEET 3 AC1 4 THR F 465 MET F 470 -1 O LEU F 468 N LEU F 407 SHEET 4 AC1 4 PHE F 455 ASP F 460 -1 N SER F 458 O TYR F 467 SHEET 1 AC2 5 SER F 446 TYR F 447 0 SHEET 2 AC2 5 ARG F 432 ILE F 438 -1 N ALA F 437 O SER F 446 SHEET 3 AC2 5 ILE F 420 GLN F 426 -1 N ARG F 425 O GLU F 433 SHEET 4 AC2 5 ALA F 479 LYS F 486 -1 O VAL F 480 N GLN F 426 SHEET 5 AC2 5 TYR F 501 TRP F 502 -1 O TYR F 501 N ALA F 485 SHEET 1 AC3 5 SER F 446 TYR F 447 0 SHEET 2 AC3 5 ARG F 432 ILE F 438 -1 N ALA F 437 O SER F 446 SHEET 3 AC3 5 ILE F 420 GLN F 426 -1 N ARG F 425 O GLU F 433 SHEET 4 AC3 5 ALA F 479 LYS F 486 -1 O VAL F 480 N GLN F 426 SHEET 5 AC3 5 THR F 506 VAL F 508 -1 O VAL F 508 N ALA F 479 SSBOND 1 CYS E 151 CYS E 165 1555 1555 2.04 SSBOND 2 CYS I 65 CYS I 77 1555 1555 2.03 SSBOND 3 CYS I 109 CYS I 128 1555 1555 2.04 SSBOND 4 CYS I 159 CYS I 171 1555 1555 2.04 SSBOND 5 CYS B 136 CYS B 150 1555 1555 2.08 SSBOND 6 CYS A 136 CYS A 150 1555 1555 2.03 SSBOND 7 CYS D 136 CYS D 150 1555 1555 2.04 SSBOND 8 CYS C 151 CYS C 165 1555 1555 2.04 SSBOND 9 CYS L 65 CYS L 77 1555 1555 2.03 SSBOND 10 CYS L 109 CYS L 128 1555 1555 2.04 SSBOND 11 CYS L 159 CYS L 171 1555 1555 2.03 SSBOND 12 CYS F 409 CYS F 483 1555 1555 2.03 LINK ND2 ASN E 208 C1 NAG E 501 1555 1555 1.50 LINK C PHE E 379 N P1L E 380 1555 1555 1.34 LINK C P1L E 380 N P1L E 381 1555 1555 1.34 LINK C P1L E 381 N PHE E 382 1555 1555 1.34 LINK C ASP E 384 N P1L E 385 1555 1555 1.33 LINK ND2 ASN B 80 C1 NAG K 1 1555 1555 1.43 LINK ND2 ASN B 149 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 80 C1 NAG N 1 1555 1555 1.46 LINK ND2 ASN A 149 C1 NAG M 1 1555 1555 1.50 LINK ND2 ASN D 80 C1 NAG O 1 1555 1555 1.43 LINK ND2 ASN C 208 C1 NAG C 501 1555 1555 1.44 LINK C PHE C 379 N P1L C 380 1555 1555 1.34 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 O4 NAG J 1 C1 NAG J 2 1555 1555 1.42 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.43 LINK O6 BMA J 3 C1 MAN J 4 1555 1555 1.44 LINK O3 BMA J 3 C1 MAN J 7 1555 1555 1.43 LINK O3 MAN J 4 C1 MAN J 5 1555 1555 1.45 LINK O6 MAN J 4 C1 MAN J 6 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.39 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.39 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.43 LINK O6 BMA M 3 C1 MAN M 4 1555 1555 1.44 LINK O3 BMA M 3 C1 MAN M 6 1555 1555 1.44 LINK O3 MAN M 4 C1 MAN M 5 1555 1555 1.45 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 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.43 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.43 LINK O6 BMA P 3 C1 MAN P 5 1555 1555 1.44 CISPEP 1 ILE E 124 THR E 125 0 -7.38 CISPEP 2 PHE E 158 PRO E 159 0 0.90 CISPEP 3 VAL B 109 THR B 110 0 -2.88 CISPEP 4 TYR B 143 PRO B 144 0 3.36 CISPEP 5 VAL A 109 THR A 110 0 -5.01 CISPEP 6 TYR A 143 PRO A 144 0 1.18 CISPEP 7 VAL D 109 THR D 110 0 -8.52 CISPEP 8 TYR D 143 PRO D 144 0 -2.09 CISPEP 9 ILE C 124 THR C 125 0 -14.27 CISPEP 10 PHE C 158 PRO C 159 0 3.53 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