HEADER MEMBRANE PROTEIN 18-SEP-24 9GU3 TITLE HUMAN ADULT MUSCLE NACHR IN DESENSITISED STATE IN NANODISC WITH 1 MM TITLE 2 ACETYLCHOLINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA; COMPND 3 CHAIN: A, L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT BETA; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT DELTA; COMPND 11 CHAIN: D; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT EPSILON,GREEN FLUORESCENT COMPND 15 PROTEIN; COMPND 16 CHAIN: E; COMPND 17 ENGINEERED: YES; COMPND 18 MUTATION: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: FAB35 LIGHT CHAIN; COMPND 21 CHAIN: C, G; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: FAB35 HEAVY CHAIN; COMPND 25 CHAIN: F, H; COMPND 26 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: CHRNA1, ACHRA, CHNRA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: TLCV2; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: CHRNB1, ACHRB, CHRNB; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: TLCV2; SOURCE 21 MOL_ID: 3; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 GENE: CHRND, ACHRD; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 30 EXPRESSION_SYSTEM_PLASMID: TLCV2; SOURCE 31 MOL_ID: 4; SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS, AEQUOREA VICTORIA; SOURCE 33 ORGANISM_COMMON: HUMAN; SOURCE 34 ORGANISM_TAXID: 9606, 6100; SOURCE 35 GENE: CHRNE, ACHRE, GFP; SOURCE 36 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 38 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 40 EXPRESSION_SYSTEM_PLASMID: TLCV2; SOURCE 41 MOL_ID: 5; SOURCE 42 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 43 ORGANISM_TAXID: 10116; SOURCE 44 EXPRESSION_SYSTEM: RATTUS NORVEGICUS; SOURCE 45 EXPRESSION_SYSTEM_TAXID: 10116; SOURCE 46 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA; SOURCE 47 EXPRESSION_SYSTEM_ATCC_NUMBER: TIB-175; SOURCE 48 MOL_ID: 6; SOURCE 49 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 50 ORGANISM_TAXID: 10116; SOURCE 51 EXPRESSION_SYSTEM: RATTUS NORVEGICUS; SOURCE 52 EXPRESSION_SYSTEM_TAXID: 10116; SOURCE 53 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA; SOURCE 54 EXPRESSION_SYSTEM_ATCC_NUMBER: TIB-175 KEYWDS LIGAND-GATED ION CHANNEL, NICOTINIC RECEPTOR, PLGIC, CYS-LOOP KEYWDS 2 RECEPTOR, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR A.LI,A.C.W.PIKE,G.CHI,R.WEBSTER,S.MAXWELL,W.LIU,D.BEESON,D.B.SAUER, AUTHOR 2 Y.Y.DONG REVDAT 1 14-MAY-25 9GU3 0 JRNL AUTH A.LI,A.C.W.PIKE,R.WEBSTER,S.MAXWELL,W.W.LIU,G.CHI,J.PALACE, JRNL AUTH 2 D.BEESON,D.B.SAUER,Y.Y.DONG JRNL TITL STRUCTURES OF THE HUMAN ADULT MUSCLE-TYPE NICOTINIC RECEPTOR JRNL TITL 2 IN RESTING AND DESENSITIZED STATES. JRNL REF CELL REP V. 44 15581 2025 JRNL REFN ESSN 2211-1247 JRNL PMID 40252219 JRNL DOI 10.1016/J.CELREP.2025.115581 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN, REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY, REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON, REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL, REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS, REMARK 1 AUTH 6 P.D.ADAMS REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS, REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX REMARK 1 REF ACTA CRYSTALLOGR., SECT. D: V. 75 861 2019 REMARK 1 REF 2 BIOL. CRYSTALLOGR. REMARK 1 REFN ISSN 0907-4449 REMARK 1 PMID 31588918 REMARK 1 DOI 10.1107/S2059798319011471 REMARK 2 REMARK 2 RESOLUTION. 2.64 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, UCSF CHIMERAX, REMARK 3 COOT, ISOLDE, CRYOSPARC, CRYOSPARC, REMARK 3 RELION, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : INITIAL FITTING OF ALPHAFOLD MODELS USING REMARK 3 CHIMERAX FOLLOWED BY MANUAL REBUILDING IN COOT AND FINAL REMARK 3 REFINEMENT IN ISOLDE AND PHENIX 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) : 2.640 REMARK 3 NUMBER OF PARTICLES : 434976 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: NON-UNIFORM REFINENEMENT REMARK 4 REMARK 4 9GU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1292141760. 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 : HUMAN ADULT MUSCLE NACHR IN REMARK 245 DESENSITISED STATE IN NANODISC REMARK 245 WITH 1 MM ACETYLCHOLINE REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : 2.5 UL SAMPLE, BLOT TIME=4 S, REMARK 245 BLOT FORCE=-10 REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NACHR IN COMPLEX WITH REMARK 245 ACETYLCHOLINE AND FAB35 IN MSP2N2-SOY POLAR LIPIDS NANODISCS REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 19925 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) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 130000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: NONAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E, L, C, F, G, H, I, REMARK 350 AND CHAINS: J, K, M, N, O REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 THR A 298 REMARK 465 HIS A 299 REMARK 465 HIS A 300 REMARK 465 ARG A 301 REMARK 465 SER A 302 REMARK 465 PRO A 303 REMARK 465 SER A 304 REMARK 465 THR A 305 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 MET A 308 REMARK 465 PRO A 309 REMARK 465 ASN A 310 REMARK 465 TRP A 311 REMARK 465 VAL A 312 REMARK 465 ARG A 313 REMARK 465 LYS A 314 REMARK 465 VAL A 315 REMARK 465 PHE A 316 REMARK 465 ILE A 317 REMARK 465 ASP A 318 REMARK 465 THR A 319 REMARK 465 ILE A 320 REMARK 465 PRO A 321 REMARK 465 ASN A 322 REMARK 465 ILE A 323 REMARK 465 MET A 324 REMARK 465 PHE A 325 REMARK 465 PHE A 326 REMARK 465 SER A 327 REMARK 465 THR A 328 REMARK 465 MET A 329 REMARK 465 LYS A 330 REMARK 465 ARG A 331 REMARK 465 PRO A 332 REMARK 465 SER A 333 REMARK 465 ARG A 334 REMARK 465 GLU A 335 REMARK 465 LYS A 336 REMARK 465 GLN A 337 REMARK 465 ASP A 338 REMARK 465 LYS A 339 REMARK 465 LYS A 340 REMARK 465 ILE A 341 REMARK 465 PHE A 342 REMARK 465 THR A 343 REMARK 465 GLU A 344 REMARK 465 ASP A 345 REMARK 465 ILE A 346 REMARK 465 ASP A 347 REMARK 465 ILE A 348 REMARK 465 SER A 349 REMARK 465 ASP A 350 REMARK 465 ILE A 351 REMARK 465 SER A 352 REMARK 465 GLY A 353 REMARK 465 LYS A 354 REMARK 465 PRO A 355 REMARK 465 GLY A 356 REMARK 465 PRO A 357 REMARK 465 PRO A 358 REMARK 465 PRO A 359 REMARK 465 MET A 360 REMARK 465 GLY A 361 REMARK 465 PHE A 362 REMARK 465 HIS A 363 REMARK 465 SER A 364 REMARK 465 PRO A 365 REMARK 465 LEU A 366 REMARK 465 ILE A 367 REMARK 465 LYS A 368 REMARK 465 HIS A 369 REMARK 465 PRO A 370 REMARK 465 GLU A 371 REMARK 465 VAL A 372 REMARK 465 LYS A 373 REMARK 465 SER A 374 REMARK 465 ALA A 375 REMARK 465 ILE A 376 REMARK 465 GLU A 377 REMARK 465 GLY A 378 REMARK 465 ILE A 379 REMARK 465 LYS A 380 REMARK 465 TYR A 381 REMARK 465 ILE A 382 REMARK 465 ALA A 383 REMARK 465 GLU A 384 REMARK 465 THR A 385 REMARK 465 MET A 386 REMARK 465 LYS A 387 REMARK 465 SER A 388 REMARK 465 ASP A 389 REMARK 465 GLN A 390 REMARK 465 GLU A 391 REMARK 465 SER A 392 REMARK 465 ASN A 393 REMARK 465 ASN A 394 REMARK 465 ALA A 395 REMARK 465 ALA A 396 REMARK 465 ALA A 397 REMARK 465 GLU A 398 REMARK 465 TRP A 399 REMARK 465 LYS A 400 REMARK 465 TYR A 401 REMARK 465 ALA A 427 REMARK 465 GLY A 428 REMARK 465 ARG A 429 REMARK 465 LEU A 430 REMARK 465 ILE A 431 REMARK 465 GLU A 432 REMARK 465 LEU A 433 REMARK 465 ASN A 434 REMARK 465 GLN A 435 REMARK 465 GLN A 436 REMARK 465 GLY A 437 REMARK 465 GLY B 199 REMARK 465 ASP B 200 REMARK 465 PRO B 201 REMARK 465 ARG B 202 REMARK 465 GLY B 203 REMARK 465 GLY B 204 REMARK 465 ARG B 205 REMARK 465 GLU B 206 REMARK 465 HIS B 310 REMARK 465 HIS B 311 REMARK 465 ARG B 312 REMARK 465 SER B 313 REMARK 465 PRO B 314 REMARK 465 HIS B 315 REMARK 465 THR B 316 REMARK 465 HIS B 317 REMARK 465 GLN B 318 REMARK 465 MET B 319 REMARK 465 PRO B 320 REMARK 465 LEU B 321 REMARK 465 TRP B 322 REMARK 465 VAL B 323 REMARK 465 ARG B 324 REMARK 465 GLN B 325 REMARK 465 ILE B 326 REMARK 465 PHE B 327 REMARK 465 ILE B 328 REMARK 465 HIS B 329 REMARK 465 LYS B 330 REMARK 465 LEU B 331 REMARK 465 PRO B 332 REMARK 465 LEU B 333 REMARK 465 TYR B 334 REMARK 465 LEU B 335 REMARK 465 ARG B 336 REMARK 465 LEU B 337 REMARK 465 LYS B 338 REMARK 465 ARG B 339 REMARK 465 PRO B 340 REMARK 465 LYS B 341 REMARK 465 PRO B 342 REMARK 465 GLU B 343 REMARK 465 ARG B 344 REMARK 465 ASP B 345 REMARK 465 LEU B 346 REMARK 465 MET B 347 REMARK 465 PRO B 348 REMARK 465 GLU B 349 REMARK 465 PRO B 350 REMARK 465 PRO B 351 REMARK 465 HIS B 352 REMARK 465 CYS B 353 REMARK 465 SER B 354 REMARK 465 SER B 355 REMARK 465 PRO B 356 REMARK 465 GLY B 357 REMARK 465 SER B 358 REMARK 465 GLY B 359 REMARK 465 TRP B 360 REMARK 465 GLY B 361 REMARK 465 ARG B 362 REMARK 465 GLY B 363 REMARK 465 THR B 364 REMARK 465 ASP B 365 REMARK 465 GLU B 366 REMARK 465 TYR B 367 REMARK 465 PHE B 368 REMARK 465 ILE B 369 REMARK 465 ARG B 370 REMARK 465 LYS B 371 REMARK 465 PRO B 372 REMARK 465 PRO B 373 REMARK 465 SER B 374 REMARK 465 ASP B 375 REMARK 465 PHE B 376 REMARK 465 LEU B 377 REMARK 465 PHE B 378 REMARK 465 PRO B 379 REMARK 465 LYS B 380 REMARK 465 PRO B 381 REMARK 465 ASN B 382 REMARK 465 ARG B 383 REMARK 465 PHE B 384 REMARK 465 GLN B 385 REMARK 465 PRO B 386 REMARK 465 GLU B 387 REMARK 465 LEU B 388 REMARK 465 SER B 389 REMARK 465 ALA B 390 REMARK 465 PRO B 391 REMARK 465 ASP B 392 REMARK 465 LEU B 393 REMARK 465 ARG B 394 REMARK 465 ARG B 395 REMARK 465 PHE B 396 REMARK 465 ILE B 397 REMARK 465 ASP B 398 REMARK 465 GLY B 399 REMARK 465 PRO B 400 REMARK 465 ASN B 401 REMARK 465 ARG B 402 REMARK 465 ALA B 403 REMARK 465 VAL B 404 REMARK 465 ALA B 405 REMARK 465 LEU B 406 REMARK 465 LEU B 407 REMARK 465 PRO B 408 REMARK 465 GLU B 409 REMARK 465 LEU B 410 REMARK 465 ARG B 411 REMARK 465 GLU B 412 REMARK 465 VAL B 413 REMARK 465 VAL B 414 REMARK 465 SER B 415 REMARK 465 SER B 416 REMARK 465 ILE B 417 REMARK 465 SER B 418 REMARK 465 TYR B 419 REMARK 465 ILE B 420 REMARK 465 ALA B 421 REMARK 465 ARG B 422 REMARK 465 GLN B 423 REMARK 465 LEU B 424 REMARK 465 GLN B 425 REMARK 465 GLU B 426 REMARK 465 GLN B 427 REMARK 465 GLU B 428 REMARK 465 ASP B 429 REMARK 465 HIS B 430 REMARK 465 ASP B 431 REMARK 465 ALA B 432 REMARK 465 LEU B 433 REMARK 465 LYS B 434 REMARK 465 GLU B 435 REMARK 465 ASP B 436 REMARK 465 HIS D 313 REMARK 465 PHE D 314 REMARK 465 ARG D 315 REMARK 465 THR D 316 REMARK 465 PRO D 317 REMARK 465 SER D 318 REMARK 465 THR D 319 REMARK 465 HIS D 320 REMARK 465 VAL D 321 REMARK 465 LEU D 322 REMARK 465 SER D 323 REMARK 465 GLU D 324 REMARK 465 GLY D 325 REMARK 465 VAL D 326 REMARK 465 LYS D 327 REMARK 465 LYS D 328 REMARK 465 LEU D 329 REMARK 465 PHE D 330 REMARK 465 LEU D 331 REMARK 465 GLU D 332 REMARK 465 THR D 333 REMARK 465 LEU D 334 REMARK 465 PRO D 335 REMARK 465 GLU D 336 REMARK 465 LEU D 337 REMARK 465 LEU D 338 REMARK 465 HIS D 339 REMARK 465 MET D 340 REMARK 465 SER D 341 REMARK 465 ARG D 342 REMARK 465 PRO D 343 REMARK 465 ALA D 344 REMARK 465 GLU D 345 REMARK 465 ASP D 346 REMARK 465 GLY D 347 REMARK 465 PRO D 348 REMARK 465 SER D 349 REMARK 465 PRO D 350 REMARK 465 GLY D 351 REMARK 465 ALA D 352 REMARK 465 LEU D 353 REMARK 465 VAL D 354 REMARK 465 ARG D 355 REMARK 465 ARG D 356 REMARK 465 SER D 357 REMARK 465 SER D 358 REMARK 465 SER D 359 REMARK 465 LEU D 360 REMARK 465 GLY D 361 REMARK 465 TYR D 362 REMARK 465 ILE D 363 REMARK 465 SER D 364 REMARK 465 LYS D 365 REMARK 465 ALA D 366 REMARK 465 GLU D 367 REMARK 465 GLU D 368 REMARK 465 TYR D 369 REMARK 465 PHE D 370 REMARK 465 LEU D 371 REMARK 465 LEU D 372 REMARK 465 LYS D 373 REMARK 465 SER D 374 REMARK 465 ARG D 375 REMARK 465 SER D 376 REMARK 465 ASP D 377 REMARK 465 LEU D 378 REMARK 465 MET D 379 REMARK 465 PHE D 380 REMARK 465 GLU D 381 REMARK 465 LYS D 382 REMARK 465 GLN D 383 REMARK 465 SER D 384 REMARK 465 GLU D 385 REMARK 465 ARG D 386 REMARK 465 HIS D 387 REMARK 465 GLY D 388 REMARK 465 LEU D 389 REMARK 465 ALA D 390 REMARK 465 ARG D 391 REMARK 465 ARG D 392 REMARK 465 LEU D 393 REMARK 465 THR D 394 REMARK 465 THR D 395 REMARK 465 ALA D 396 REMARK 465 ARG D 397 REMARK 465 ARG D 398 REMARK 465 PRO D 399 REMARK 465 PRO D 400 REMARK 465 ALA D 401 REMARK 465 SER D 402 REMARK 465 SER D 403 REMARK 465 GLU D 404 REMARK 465 GLN D 405 REMARK 465 ALA D 406 REMARK 465 GLN D 407 REMARK 465 GLN D 408 REMARK 465 GLU D 409 REMARK 465 LEU D 410 REMARK 465 PHE D 411 REMARK 465 ASN D 412 REMARK 465 GLU D 413 REMARK 465 LEU D 414 REMARK 465 LYS D 415 REMARK 465 PRO D 416 REMARK 465 ALA D 417 REMARK 465 VAL D 418 REMARK 465 ASP D 419 REMARK 465 GLY D 420 REMARK 465 ALA D 421 REMARK 465 ASN D 422 REMARK 465 PHE D 423 REMARK 465 ILE D 424 REMARK 465 VAL D 425 REMARK 465 ASN D 426 REMARK 465 HIS D 427 REMARK 465 MET D 428 REMARK 465 ARG D 429 REMARK 465 ASP D 430 REMARK 465 GLN D 431 REMARK 465 ASN D 432 REMARK 465 ASN D 433 REMARK 465 TYR D 434 REMARK 465 ASN D 435 REMARK 465 GLU D 436 REMARK 465 GLU D 437 REMARK 465 LYS D 438 REMARK 465 ASP D 439 REMARK 465 SER D 440 REMARK 465 TRP D 441 REMARK 465 ASN D 442 REMARK 465 ARG D 443 REMARK 465 VAL D 444 REMARK 465 VAL E 307A REMARK 465 SER E 307B REMARK 465 GLN E 307C REMARK 465 ARG E 307D REMARK 465 THR E 307E REMARK 465 PRO E 307F REMARK 465 THR E 307G REMARK 465 THR E 307H REMARK 465 HIS E 307I REMARK 465 ALA E 307J REMARK 465 MET E 307K REMARK 465 SER E 307L REMARK 465 PRO E 307M REMARK 465 ARG E 307N REMARK 465 LEU E 307O REMARK 465 ARG E 307P REMARK 465 HIS E 307Q REMARK 465 VAL E 307R REMARK 465 LEU E 307S REMARK 465 LEU E 307T REMARK 465 GLU E 307U REMARK 465 LEU E 307V REMARK 465 LEU E 307W REMARK 465 PRO E 307X REMARK 465 ARG E 307Y REMARK 465 LEU E 307Z REMARK 465 LEU E 308A REMARK 465 GLY E 308B REMARK 465 SER E 308C REMARK 465 PRO E 308D REMARK 465 PRO E 308E REMARK 465 PRO E 308F REMARK 465 PRO E 308G REMARK 465 GLU E 308H REMARK 465 ALA E 308I REMARK 465 PRO E 308J REMARK 465 ARG E 308K REMARK 465 ALA E 308L REMARK 465 PRO E 308M REMARK 465 PRO E 308N REMARK 465 VAL E 308O REMARK 465 ALA E 308P REMARK 465 THR E 308Q REMARK 465 MET E 308R REMARK 465 VAL E 308S REMARK 465 SER E 308T REMARK 465 LYS E 308U REMARK 465 GLY E 308V REMARK 465 GLU E 308W REMARK 465 GLU E 308X REMARK 465 LEU E 308Y REMARK 465 PHE E 308Z REMARK 465 THR E 309A REMARK 465 GLY E 309B REMARK 465 VAL E 309C REMARK 465 VAL E 309D REMARK 465 PRO E 309E REMARK 465 ILE E 309F REMARK 465 LEU E 309G REMARK 465 VAL E 309H REMARK 465 GLU E 309I REMARK 465 LEU E 309J REMARK 465 ASP E 309K REMARK 465 GLY E 309L REMARK 465 ASP E 309M REMARK 465 VAL E 309N REMARK 465 ASN E 309O REMARK 465 GLY E 309P REMARK 465 HIS E 309Q REMARK 465 LYS E 309R REMARK 465 PHE E 309S REMARK 465 SER E 309T REMARK 465 VAL E 309U REMARK 465 SER E 309V REMARK 465 GLY E 309W REMARK 465 GLU E 309X REMARK 465 GLY E 309Y REMARK 465 GLU E 309Z REMARK 465 GLY E 310A REMARK 465 ASP E 310B REMARK 465 ALA E 310C REMARK 465 THR E 310D REMARK 465 TYR E 310E REMARK 465 GLY E 310F REMARK 465 LYS E 310G REMARK 465 LEU E 310H REMARK 465 THR E 310I REMARK 465 LEU E 310J REMARK 465 LYS E 310K REMARK 465 PHE E 310L REMARK 465 ILE E 310M REMARK 465 CYS E 310N REMARK 465 THR E 310O REMARK 465 THR E 310P REMARK 465 GLY E 310Q REMARK 465 LYS E 310R REMARK 465 LEU E 310S REMARK 465 PRO E 310T REMARK 465 VAL E 310U REMARK 465 PRO E 310V REMARK 465 TRP E 310W REMARK 465 PRO E 310X REMARK 465 THR E 310Y REMARK 465 LEU E 310Z REMARK 465 VAL E 311A REMARK 465 THR E 311B REMARK 465 THR E 311C REMARK 465 LEU E 311D REMARK 465 THR E 311E REMARK 465 TYR E 311F REMARK 465 GLY E 311G REMARK 465 VAL E 311H REMARK 465 GLN E 311I REMARK 465 CYS E 311J REMARK 465 PHE E 311K REMARK 465 SER E 311L REMARK 465 ARG E 311M REMARK 465 TYR E 311N REMARK 465 PRO E 311O REMARK 465 ASP E 311P REMARK 465 HIS E 311Q REMARK 465 MET E 311R REMARK 465 LYS E 311S REMARK 465 GLN E 311T REMARK 465 HIS E 311U REMARK 465 ASP E 311V REMARK 465 PHE E 311W REMARK 465 PHE E 311X REMARK 465 LYS E 311Y REMARK 465 SER E 311Z REMARK 465 ALA E 312A REMARK 465 MET E 312B REMARK 465 PRO E 312C REMARK 465 GLU E 312D REMARK 465 GLY E 312E REMARK 465 TYR E 312F REMARK 465 VAL E 312G REMARK 465 GLN E 312H REMARK 465 GLU E 312I REMARK 465 ARG E 312J REMARK 465 THR E 312K REMARK 465 ILE E 312L REMARK 465 PHE E 312M REMARK 465 PHE E 312N REMARK 465 LYS E 312O REMARK 465 ASP E 312P REMARK 465 ASP E 312Q REMARK 465 GLY E 312R REMARK 465 ASN E 312S REMARK 465 TYR E 312T REMARK 465 LYS E 312U REMARK 465 THR E 312V REMARK 465 ARG E 312W REMARK 465 ALA E 312X REMARK 465 GLU E 312Y REMARK 465 VAL E 312Z REMARK 465 LYS E 313A REMARK 465 PHE E 313B REMARK 465 GLU E 313C REMARK 465 GLY E 313D REMARK 465 ASP E 313E REMARK 465 THR E 313F REMARK 465 LEU E 313G REMARK 465 VAL E 313H REMARK 465 ASN E 313I REMARK 465 ARG E 313J REMARK 465 ILE E 313K REMARK 465 GLU E 313L REMARK 465 LEU E 313M REMARK 465 LYS E 313N REMARK 465 GLY E 313O REMARK 465 ILE E 313P REMARK 465 ASP E 313Q REMARK 465 PHE E 313R REMARK 465 LYS E 313S REMARK 465 GLU E 313T REMARK 465 ASP E 313U REMARK 465 GLY E 313V REMARK 465 ASN E 313W REMARK 465 ILE E 313X REMARK 465 LEU E 313Y REMARK 465 GLY E 313Z REMARK 465 HIS E 314A REMARK 465 LYS E 314B REMARK 465 LEU E 314C REMARK 465 GLU E 314D REMARK 465 TYR E 314E REMARK 465 ASN E 314F REMARK 465 TYR E 314G REMARK 465 ASN E 314H REMARK 465 SER E 314I REMARK 465 HIS E 314J REMARK 465 ASN E 314K REMARK 465 VAL E 314L REMARK 465 TYR E 314M REMARK 465 ILE E 314N REMARK 465 MET E 314O REMARK 465 ALA E 314P REMARK 465 ASP E 314Q REMARK 465 LYS E 314R REMARK 465 GLN E 314S REMARK 465 LYS E 314T REMARK 465 ASN E 314U REMARK 465 GLY E 314V REMARK 465 ILE E 314W REMARK 465 LYS E 314X REMARK 465 VAL E 314Y REMARK 465 ASN E 314Z REMARK 465 PHE E 315A REMARK 465 LYS E 315B REMARK 465 ILE E 315C REMARK 465 ARG E 315D REMARK 465 HIS E 315E REMARK 465 ASN E 315F REMARK 465 ILE E 315G REMARK 465 GLU E 315H REMARK 465 ASP E 315I REMARK 465 GLY E 315J REMARK 465 SER E 315K REMARK 465 VAL E 315L REMARK 465 GLN E 315M REMARK 465 LEU E 315N REMARK 465 ALA E 315O REMARK 465 ASP E 315P REMARK 465 HIS E 315Q REMARK 465 TYR E 315R REMARK 465 GLN E 315S REMARK 465 GLN E 315T REMARK 465 ASN E 315U REMARK 465 THR E 315V REMARK 465 PRO E 315W REMARK 465 ILE E 315X REMARK 465 GLY E 315Y REMARK 465 ASP E 315Z REMARK 465 GLY E 316A REMARK 465 PRO E 316B REMARK 465 VAL E 316C REMARK 465 LEU E 316D REMARK 465 LEU E 316E REMARK 465 PRO E 316F REMARK 465 ASP E 316G REMARK 465 ASN E 316H REMARK 465 HIS E 316I REMARK 465 TYR E 316J REMARK 465 LEU E 316K REMARK 465 SER E 316L REMARK 465 THR E 316M REMARK 465 GLN E 316N REMARK 465 SER E 316O REMARK 465 ALA E 316P REMARK 465 LEU E 316Q REMARK 465 SER E 316R REMARK 465 LYS E 316S REMARK 465 ASP E 316T REMARK 465 PRO E 316U REMARK 465 ASN E 316V REMARK 465 GLU E 316W REMARK 465 LYS E 316X REMARK 465 ARG E 316Y REMARK 465 ASP E 316Z REMARK 465 HIS E 317A REMARK 465 MET E 317B REMARK 465 VAL E 317C REMARK 465 LEU E 317D REMARK 465 LEU E 317E REMARK 465 GLU E 317F REMARK 465 PHE E 317G REMARK 465 VAL E 317H REMARK 465 THR E 317I REMARK 465 ALA E 317J REMARK 465 ALA E 317K REMARK 465 GLY E 317L REMARK 465 ILE E 317M REMARK 465 THR E 317N REMARK 465 LEU E 317O REMARK 465 GLY E 317P REMARK 465 MET E 317Q REMARK 465 ASP E 317R REMARK 465 GLU E 317S REMARK 465 LEU E 317T REMARK 465 TYR E 317U REMARK 465 LYS E 317V REMARK 465 ALA E 317W REMARK 465 PRO E 317X REMARK 465 ARG E 317Y REMARK 465 ALA E 317Z REMARK 465 ALA E 318A REMARK 465 SER E 318B REMARK 465 PRO E 318C REMARK 465 PRO E 318D REMARK 465 ARG E 318E REMARK 465 ARG E 318F REMARK 465 ALA E 318G REMARK 465 SER E 318H REMARK 465 SER E 318I REMARK 465 VAL E 318J REMARK 465 GLY E 318K REMARK 465 LEU E 318L REMARK 465 LEU E 318M REMARK 465 LEU E 318N REMARK 465 ARG E 318O REMARK 465 ALA E 318P REMARK 465 GLU E 318Q REMARK 465 GLU E 318R REMARK 465 LEU E 318S REMARK 465 ILE E 318T REMARK 465 LEU E 318U REMARK 465 LYS E 318V REMARK 465 LYS E 318W REMARK 465 PRO E 318X REMARK 465 ARG E 318Y REMARK 465 SER E 318Z REMARK 465 GLU E 319A REMARK 465 LEU E 319B REMARK 465 VAL E 319C REMARK 465 PHE E 319D REMARK 465 GLU E 319E REMARK 465 GLY E 319F REMARK 465 GLN E 319G REMARK 465 ARG E 319H REMARK 465 HIS E 319I REMARK 465 ARG E 319J REMARK 465 GLN E 319K REMARK 465 GLY E 319L REMARK 465 THR E 319M REMARK 465 TRP E 319N REMARK 465 THR E 319O REMARK 465 ALA E 319P REMARK 465 ALA E 319Q REMARK 465 PHE E 319R REMARK 465 CYS E 319S REMARK 465 GLN E 319T REMARK 465 SER E 319U REMARK 465 LEU E 319V REMARK 465 GLY E 319W REMARK 465 ALA E 319X REMARK 465 ALA E 319Y REMARK 465 ALA E 319Z REMARK 465 PRO E 320A REMARK 465 GLU E 320B REMARK 465 VAL E 320C REMARK 465 ARG E 320D REMARK 465 CYS E 320E REMARK 465 CYS E 320F REMARK 465 VAL E 320G REMARK 465 ASP E 320H REMARK 465 ALA E 320I REMARK 465 VAL E 320J REMARK 465 ASN E 320K REMARK 465 PHE E 320L REMARK 465 VAL E 320M REMARK 465 ALA E 320N REMARK 465 GLU E 320O REMARK 465 SER E 320P REMARK 465 THR E 320Q REMARK 465 ARG E 320R REMARK 465 ASP E 320S REMARK 465 GLN E 320T REMARK 465 GLU E 320U REMARK 465 ALA E 320V REMARK 465 THR E 320W REMARK 465 GLY E 320X REMARK 465 GLU E 320Y REMARK 465 GLU E 320Z REMARK 465 VAL E 321A REMARK 465 SER E 321B REMARK 465 ASP E 321C REMARK 465 TRP E 321D REMARK 465 VAL E 321E REMARK 465 ARG E 321F REMARK 465 MET E 321G REMARK 465 HIS L 299 REMARK 465 HIS L 300 REMARK 465 ARG L 301 REMARK 465 SER L 302 REMARK 465 PRO L 303 REMARK 465 SER L 304 REMARK 465 THR L 305 REMARK 465 HIS L 306 REMARK 465 VAL L 307 REMARK 465 MET L 308 REMARK 465 PRO L 309 REMARK 465 ASN L 310 REMARK 465 TRP L 311 REMARK 465 VAL L 312 REMARK 465 ARG L 313 REMARK 465 LYS L 314 REMARK 465 VAL L 315 REMARK 465 PHE L 316 REMARK 465 ILE L 317 REMARK 465 ASP L 318 REMARK 465 THR L 319 REMARK 465 ILE L 320 REMARK 465 PRO L 321 REMARK 465 ASN L 322 REMARK 465 ILE L 323 REMARK 465 MET L 324 REMARK 465 PHE L 325 REMARK 465 PHE L 326 REMARK 465 SER L 327 REMARK 465 THR L 328 REMARK 465 MET L 329 REMARK 465 LYS L 330 REMARK 465 ARG L 331 REMARK 465 PRO L 332 REMARK 465 SER L 333 REMARK 465 ARG L 334 REMARK 465 GLU L 335 REMARK 465 LYS L 336 REMARK 465 GLN L 337 REMARK 465 ASP L 338 REMARK 465 LYS L 339 REMARK 465 LYS L 340 REMARK 465 ILE L 341 REMARK 465 PHE L 342 REMARK 465 THR L 343 REMARK 465 GLU L 344 REMARK 465 ASP L 345 REMARK 465 ILE L 346 REMARK 465 ASP L 347 REMARK 465 ILE L 348 REMARK 465 SER L 349 REMARK 465 ASP L 350 REMARK 465 ILE L 351 REMARK 465 SER L 352 REMARK 465 GLY L 353 REMARK 465 LYS L 354 REMARK 465 PRO L 355 REMARK 465 GLY L 356 REMARK 465 PRO L 357 REMARK 465 PRO L 358 REMARK 465 PRO L 359 REMARK 465 MET L 360 REMARK 465 GLY L 361 REMARK 465 PHE L 362 REMARK 465 HIS L 363 REMARK 465 SER L 364 REMARK 465 PRO L 365 REMARK 465 LEU L 366 REMARK 465 ILE L 367 REMARK 465 LYS L 368 REMARK 465 HIS L 369 REMARK 465 PRO L 370 REMARK 465 GLU L 371 REMARK 465 VAL L 372 REMARK 465 LYS L 373 REMARK 465 SER L 374 REMARK 465 ALA L 375 REMARK 465 ILE L 376 REMARK 465 GLU L 377 REMARK 465 GLY L 378 REMARK 465 ILE L 379 REMARK 465 LYS L 380 REMARK 465 TYR L 381 REMARK 465 ILE L 382 REMARK 465 ALA L 383 REMARK 465 GLU L 384 REMARK 465 THR L 385 REMARK 465 MET L 386 REMARK 465 LYS L 387 REMARK 465 SER L 388 REMARK 465 ASP L 389 REMARK 465 GLN L 390 REMARK 465 GLU L 391 REMARK 465 SER L 392 REMARK 465 ASN L 393 REMARK 465 ASN L 394 REMARK 465 ALA L 395 REMARK 465 ALA L 396 REMARK 465 ALA L 397 REMARK 465 GLU L 398 REMARK 465 TRP L 399 REMARK 465 LYS L 400 REMARK 465 TYR L 401 REMARK 465 VAL L 402 REMARK 465 ALA L 403 REMARK 465 MET L 404 REMARK 465 VAL L 405 REMARK 465 ILE L 431 REMARK 465 GLU L 432 REMARK 465 LEU L 433 REMARK 465 ASN L 434 REMARK 465 GLN L 435 REMARK 465 GLN L 436 REMARK 465 GLY L 437 REMARK 465 CYS C 213 REMARK 465 CYS G 213 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ILE A 220 CG1 CG2 CD1 REMARK 470 LEU A 223 CG CD1 CD2 REMARK 470 LEU A 224 CG CD1 CD2 REMARK 470 PHE A 227 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 228 CG CD1 CD2 REMARK 470 LEU A 231 CG CD1 CD2 REMARK 470 PHE A 233 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR A 234 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 235 CG CD1 CD2 REMARK 470 ASP A 238 CG OD1 OD2 REMARK 470 SER A 239 OG REMARK 470 GLU A 241 CG CD OE1 OE2 REMARK 470 LEU A 245 CG CD1 CD2 REMARK 470 LEU A 250 CG CD1 CD2 REMARK 470 LEU A 251 CG CD1 CD2 REMARK 470 LEU A 253 CG CD1 CD2 REMARK 470 GLU A 262 CG CD OE1 OE2 REMARK 470 SER A 269 OG REMARK 470 TYR A 277 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 279 CG CD1 CD2 REMARK 470 PHE A 280 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET A 282 CG SD CE REMARK 470 PHE A 284 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE A 286 CG1 CG2 CD1 REMARK 470 SER A 288 OG REMARK 470 LEU A 411 CG CD1 CD2 REMARK 470 PHE A 414 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET A 415 CG SD CE REMARK 470 LEU A 416 CG CD1 CD2 REMARK 470 VAL A 417 CG1 CG2 REMARK 470 CYS A 418 SG REMARK 470 ILE A 419 CG1 CG2 CD1 REMARK 470 ILE A 420 CG1 CG2 CD1 REMARK 470 THR A 422 OG1 CG2 REMARK 470 LEU A 423 CG CD1 CD2 REMARK 470 VAL A 425 CG1 CG2 REMARK 470 PHE A 426 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP B 165 CG OD1 OD2 REMARK 470 LEU B 235 CG CD1 CD2 REMARK 470 ILE B 236 CG1 CG2 CD1 REMARK 470 LEU B 238 CG CD1 CD2 REMARK 470 LEU B 239 CG CD1 CD2 REMARK 470 ILE B 241 CG1 CG2 CD1 REMARK 470 PHE B 242 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 244 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR B 245 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU B 246 CG CD1 CD2 REMARK 470 ASP B 249 CG OD1 OD2 REMARK 470 GLU B 252 CG CD OE1 OE2 REMARK 470 LYS B 253 CG CD CE NZ REMARK 470 MET B 254 CG SD CE REMARK 470 LEU B 256 CG CD1 CD2 REMARK 470 SER B 257 OG REMARK 470 ILE B 258 CG1 CG2 CD1 REMARK 470 PHE B 259 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU B 261 CG CD1 CD2 REMARK 470 LEU B 262 CG CD1 CD2 REMARK 470 LEU B 264 CG CD1 CD2 REMARK 470 PHE B 267 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU B 269 CG CD1 CD2 REMARK 470 LEU B 271 CG CD1 CD2 REMARK 470 ASP B 273 CG OD1 OD2 REMARK 470 GLU B 277 CG CD OE1 OE2 REMARK 470 ILE B 285 CG1 CG2 CD1 REMARK 470 LYS B 287 CG CD CE NZ REMARK 470 TYR B 288 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 MET B 290 CG SD CE REMARK 470 PHE B 291 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET B 293 CG SD CE REMARK 470 VAL B 294 CG1 CG2 REMARK 470 LEU B 295 CG CD1 CD2 REMARK 470 VAL B 296 CG1 CG2 REMARK 470 PHE B 298 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER B 299 OG REMARK 470 VAL B 300 CG1 CG2 REMARK 470 ILE B 301 CG1 CG2 CD1 REMARK 470 LEU B 302 CG CD1 CD2 REMARK 470 SER B 303 OG REMARK 470 VAL B 306 CG1 CG2 REMARK 470 LEU B 307 CG CD1 CD2 REMARK 470 LEU B 309 CG CD1 CD2 REMARK 470 TRP B 437 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 437 CZ3 CH2 REMARK 470 GLN B 438 CG CD OE1 NE2 REMARK 470 PHE B 439 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL B 440 CG1 CG2 REMARK 470 MET B 442 CG SD CE REMARK 470 VAL B 443 CG1 CG2 REMARK 470 LEU B 447 CG CD1 CD2 REMARK 470 PHE B 448 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 452 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE B 453 CG1 CG2 CD1 REMARK 470 ILE B 454 CG1 CG2 CD1 REMARK 470 PHE B 455 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR B 456 OG1 CG2 REMARK 470 SER B 457 OG REMARK 470 VAL B 458 CG1 CG2 REMARK 470 THR B 460 OG1 CG2 REMARK 470 LEU B 461 CG CD1 CD2 REMARK 470 ILE B 463 CG1 CG2 CD1 REMARK 470 PHE B 464 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU B 465 CG CD1 CD2 REMARK 470 ASP B 466 CG OD1 OD2 REMARK 470 TYR B 469 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU D 168 CG CD OE1 OE2 REMARK 470 VAL D 234 CG1 CG2 REMARK 470 LEU D 238 CG CD1 CD2 REMARK 470 ILE D 239 CG1 CG2 CD1 REMARK 470 MET D 242 CG SD CE REMARK 470 VAL D 243 CG1 CG2 REMARK 470 LEU D 245 CG CD1 CD2 REMARK 470 VAL D 246 CG1 CG2 REMARK 470 LEU D 249 CG CD1 CD2 REMARK 470 ASP D 252 CG OD1 OD2 REMARK 470 GLU D 255 CG CD OE1 OE2 REMARK 470 SER D 258 OG REMARK 470 VAL D 259 CG1 CG2 REMARK 470 ILE D 261 CG1 CG2 CD1 REMARK 470 SER D 262 OG REMARK 470 VAL D 263 CG1 CG2 REMARK 470 LEU D 264 CG CD1 CD2 REMARK 470 LEU D 265 CG CD1 CD2 REMARK 470 GLN D 267 CG CD OE1 NE2 REMARK 470 VAL D 269 CG1 CG2 REMARK 470 PHE D 270 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS D 276 CG CD CE NZ REMARK 470 LEU D 287 CG CD1 CD2 REMARK 470 LYS D 290 CG CD CE NZ REMARK 470 MET D 296 CG SD CE REMARK 470 LEU D 298 CG CD1 CD2 REMARK 470 VAL D 299 CG1 CG2 REMARK 470 VAL D 302 CG1 CG2 REMARK 470 VAL D 303 CG1 CG2 REMARK 470 ILE D 305 CG1 CG2 CD1 REMARK 470 CYS D 306 SG REMARK 470 VAL D 307 CG1 CG2 REMARK 470 LEU D 310 CG CD1 CD2 REMARK 470 ARG D 446 CG CD NE CZ NH1 NH2 REMARK 470 THR D 447 OG1 CG2 REMARK 470 ARG D 450 CG CD NE CZ NH1 NH2 REMARK 470 VAL D 461 CG1 CG2 REMARK 470 ILE D 467 CG1 CG2 CD1 REMARK 470 PHE D 468 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU D 469 CG CD1 CD2 REMARK 470 TYR D 473 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS E 1 CG CD CE NZ REMARK 470 LYS E 46 CE NZ REMARK 470 HIS E 198 CG ND1 CD2 CE1 NE2 REMARK 470 THR E 202 OG1 CG2 REMARK 470 ASP E 203 CG OD1 OD2 REMARK 470 ILE E 225 CG1 CG2 CD1 REMARK 470 LEU E 233 CG CD1 CD2 REMARK 470 ILE E 234 CG1 CG2 CD1 REMARK 470 LEU E 237 CG CD1 CD2 REMARK 470 VAL E 238 CG1 CG2 REMARK 470 LEU E 240 CG CD1 CD2 REMARK 470 GLN E 247 CG CD OE1 NE2 REMARK 470 GLN E 251 CG CD OE1 NE2 REMARK 470 LYS E 252 CG CD CE NZ REMARK 470 CYS E 253 SG REMARK 470 THR E 254 OG1 CG2 REMARK 470 SER E 256 OG REMARK 470 ILE E 257 CG1 CG2 CD1 REMARK 470 ASN E 258 CG OD1 ND2 REMARK 470 GLN E 263 CG CD OE1 NE2 REMARK 470 VAL E 265 CG1 CG2 REMARK 470 GLN E 272 CG CD OE1 NE2 REMARK 470 LYS E 273 CG CD CE NZ REMARK 470 GLU E 276 CG CD OE1 OE2 REMARK 470 THR E 277 OG1 CG2 REMARK 470 LEU E 288 CG CD1 CD2 REMARK 470 VAL E 291 CG1 CG2 REMARK 470 MET E 292 CG SD CE REMARK 470 VAL E 294 CG1 CG2 REMARK 470 THR E 296 OG1 CG2 REMARK 470 ILE E 298 CG1 CG2 CD1 REMARK 470 VAL E 299 CG1 CG2 REMARK 470 ASN E 301 CG OD1 ND2 REMARK 470 CYS E 302 SG REMARK 470 ASN E 432 CG OD1 ND2 REMARK 470 LEU E 434 CG CD1 CD2 REMARK 470 ASP E 435 CG OD1 OD2 REMARK 470 ILE E 437 CG1 CG2 CD1 REMARK 470 LEU E 443 CG CD1 CD2 REMARK 470 VAL E 444 CG1 CG2 REMARK 470 LEU E 445 CG CD1 CD2 REMARK 470 PHE E 446 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER E 447 OG REMARK 470 VAL E 448 CG1 CG2 REMARK 470 SER E 450 OG REMARK 470 SER E 451 OG REMARK 470 LEU E 452 CG CD1 CD2 REMARK 470 ILE E 453 CG1 CG2 CD1 REMARK 470 PHE E 454 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU E 455 CG CD1 CD2 REMARK 470 TYR E 458 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG E 461 CG CD NE CZ NH1 NH2 REMARK 470 ILE L 220 CG1 CG2 CD1 REMARK 470 LEU L 223 CG CD1 CD2 REMARK 470 LEU L 224 CG CD1 CD2 REMARK 470 PHE L 225 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE L 227 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU L 228 CG CD1 CD2 REMARK 470 LEU L 231 CG CD1 CD2 REMARK 470 ASP L 238 CG OD1 OD2 REMARK 470 GLU L 241 CG CD OE1 OE2 REMARK 470 MET L 243 CG SD CE REMARK 470 THR L 244 OG1 CG2 REMARK 470 LEU L 245 CG CD1 CD2 REMARK 470 SER L 246 OG REMARK 470 ILE L 247 CG1 CG2 CD1 REMARK 470 SER L 248 OG REMARK 470 LEU L 250 CG CD1 CD2 REMARK 470 SER L 252 OG REMARK 470 LEU L 253 CG CD1 CD2 REMARK 470 PHE L 256 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU L 257 CG CD1 CD2 REMARK 470 GLU L 262 CG CD OE1 OE2 REMARK 470 SER L 269 OG REMARK 470 LEU L 273 CG CD1 CD2 REMARK 470 LEU L 279 CG CD1 CD2 REMARK 470 PHE L 280 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR L 281 OG1 CG2 REMARK 470 MET L 282 CG SD CE REMARK 470 PHE L 284 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL L 285 CG1 CG2 REMARK 470 ILE L 286 CG1 CG2 CD1 REMARK 470 SER L 288 OG REMARK 470 ILE L 289 CG1 CG2 CD1 REMARK 470 ILE L 291 CG1 CG2 CD1 REMARK 470 THR L 292 OG1 CG2 REMARK 470 VAL L 293 CG1 CG2 REMARK 470 MET L 406 CG SD CE REMARK 470 HIS L 408 CG ND1 CD2 CE1 NE2 REMARK 470 ILE L 409 CG1 CG2 CD1 REMARK 470 LEU L 410 CG CD1 CD2 REMARK 470 LEU L 411 CG CD1 CD2 REMARK 470 VAL L 413 CG1 CG2 REMARK 470 PHE L 414 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET L 415 CG SD CE REMARK 470 LEU L 416 CG CD1 CD2 REMARK 470 VAL L 417 CG1 CG2 REMARK 470 CYS L 418 SG REMARK 470 ILE L 419 CG1 CG2 CD1 REMARK 470 ILE L 420 CG1 CG2 CD1 REMARK 470 THR L 422 OG1 CG2 REMARK 470 LEU L 423 CG CD1 CD2 REMARK 470 VAL L 425 CG1 CG2 REMARK 470 PHE L 426 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG L 429 CG CD NE CZ NH1 NH2 REMARK 470 LEU L 430 CG CD1 CD2 REMARK 470 GLU C 104 CG CD OE1 OE2 REMARK 470 LYS C 146 CG CD CE NZ REMARK 470 LYS C 148 CG CD CE NZ REMARK 470 GLU C 153 CG CD OE1 OE2 REMARK 470 ARG C 154 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 155 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 156 CG OD1 OD2 REMARK 470 LEU C 159 CG CD1 CD2 REMARK 470 ASP C 160 CG OD1 OD2 REMARK 470 LYS C 168 CG CD CE NZ REMARK 470 SER C 179 OG REMARK 470 LYS C 182 CG CD CE NZ REMARK 470 ASP C 184 CG OD1 OD2 REMARK 470 GLU C 194 CG CD OE1 OE2 REMARK 470 LYS C 198 CG CD CE NZ REMARK 470 SER C 200 OG REMARK 470 SER C 201 OG REMARK 470 SER C 202 OG REMARK 470 ARG C 210 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 212 CG CD OE1 OE2 REMARK 470 GLU F 1 CG CD OE1 OE2 REMARK 470 GLU F 122 CG CD OE1 OE2 REMARK 470 LEU F 137 CG CD1 CD2 REMARK 470 LYS F 138 CG CD CE NZ REMARK 470 SER F 139 OG REMARK 470 ASN F 140 CG OD1 ND2 REMARK 470 SER F 141 OG REMARK 470 MET F 142 CG SD CE REMARK 470 GLN F 178 CG CD OE1 NE2 REMARK 470 SER F 179 OG REMARK 470 SER F 192 OG REMARK 470 SER F 193 OG REMARK 470 GLN F 210 CG CD OE1 NE2 REMARK 470 ARG F 213 CG CD NE CZ NH1 NH2 REMARK 470 TRP F 214 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 214 CZ3 CH2 REMARK 470 ARG F 216 CG CD NE CZ NH1 NH2 REMARK 470 LEU F 218 CG CD1 CD2 REMARK 470 GLU G 104 CG CD OE1 OE2 REMARK 470 THR G 121 OG1 CG2 REMARK 470 THR G 126 OG1 CG2 REMARK 470 ASP G 150 CG OD1 OD2 REMARK 470 THR G 152 OG1 CG2 REMARK 470 GLU G 153 CG CD OE1 OE2 REMARK 470 ARG G 154 CG CD NE CZ NH1 NH2 REMARK 470 ARG G 155 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 156 CG OD1 OD2 REMARK 470 LEU G 159 CG CD1 CD2 REMARK 470 ASP G 160 CG OD1 OD2 REMARK 470 LYS G 168 CG CD CE NZ REMARK 470 SER G 179 OG REMARK 470 THR G 181 OG1 CG2 REMARK 470 LYS G 182 CG CD CE NZ REMARK 470 ASP G 184 CG OD1 OD2 REMARK 470 GLU G 186 CG CD OE1 OE2 REMARK 470 SER G 187 OG REMARK 470 GLU G 194 CG CD OE1 OE2 REMARK 470 VAL G 195 CG1 CG2 REMARK 470 VAL G 196 CG1 CG2 REMARK 470 LYS G 198 CG CD CE NZ REMARK 470 SER G 200 OG REMARK 470 SER G 201 OG REMARK 470 SER G 202 OG REMARK 470 ARG G 210 CG CD NE CZ NH1 NH2 REMARK 470 GLU G 212 CG CD OE1 OE2 REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 GLU H 122 CG CD OE1 OE2 REMARK 470 LEU H 137 CG CD1 CD2 REMARK 470 LYS H 138 CG CD CE NZ REMARK 470 SER H 139 OG REMARK 470 ASN H 140 CG OD1 ND2 REMARK 470 SER H 141 OG REMARK 470 MET H 142 CG SD CE REMARK 470 SER H 168 OG REMARK 470 GLN H 178 CG CD OE1 NE2 REMARK 470 SER H 192 OG REMARK 470 SER H 193 OG REMARK 470 SER H 197 OG REMARK 470 THR H 199 OG1 CG2 REMARK 470 GLN H 210 CG CD OE1 NE2 REMARK 470 HIS H 211 CG ND1 CD2 CE1 NE2 REMARK 470 ARG H 213 CG CD NE CZ NH1 NH2 REMARK 470 TRP H 214 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 214 CZ3 CH2 REMARK 470 ARG H 216 CG CD NE CZ NH1 NH2 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 OG SER C 7 OG1 THR C 22 2.12 REMARK 500 OG SER G 7 OG1 THR G 22 2.13 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 PRO A 21 46.12 -84.10 REMARK 500 ASN A 94 32.34 -94.62 REMARK 500 ASP A 97 18.63 -142.32 REMARK 500 LYS A 125 74.46 -100.78 REMARK 500 VAL A 218 -55.96 -127.11 REMARK 500 PRO B 21 48.73 -80.95 REMARK 500 ILE B 188 -60.14 -103.02 REMARK 500 LYS B 190 52.58 -142.37 REMARK 500 VAL B 229 -58.91 -122.24 REMARK 500 ASN D 96 31.50 -94.48 REMARK 500 ASN D 143 75.62 -101.45 REMARK 500 ARG D 195 57.99 -146.02 REMARK 500 ASP D 492 43.57 -108.57 REMARK 500 PHE E 137 32.17 -94.49 REMARK 500 ASN E 170 49.44 -87.78 REMARK 500 CYS E 190 53.43 -149.76 REMARK 500 ILE E 227 -55.23 -126.04 REMARK 500 GLN E 251 30.78 -91.54 REMARK 500 ASN L 94 32.06 -92.96 REMARK 500 ASP L 97 13.74 -142.26 REMARK 500 LYS L 125 76.71 -102.31 REMARK 500 VAL L 218 -55.55 -126.04 REMARK 500 THR C 51 -16.81 72.81 REMARK 500 ASN C 52 -3.95 -144.97 REMARK 500 ARG C 210 -167.68 57.70 REMARK 500 SER F 15 -1.08 67.79 REMARK 500 ARG F 102 -117.46 54.87 REMARK 500 SER F 139 21.34 -140.13 REMARK 500 SER F 163 -113.37 54.89 REMARK 500 SER F 167 179.14 62.15 REMARK 500 THR G 51 -17.44 72.20 REMARK 500 ARG G 210 -170.72 59.30 REMARK 500 SER H 15 -1.07 68.00 REMARK 500 ARG H 102 -121.85 52.64 REMARK 500 SER H 163 -112.29 54.61 REMARK 500 SER H 167 176.45 62.28 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-51571 RELATED DB: EMDB REMARK 900 HUMAN ADULT MUSCLE NACHR IN DESENSITISED STATE IN NANODISC WITH 1 REMARK 900 MM ACETYLCHOLINE DBREF 9GU3 A 1 437 UNP P02708 ACHA_HUMAN 21 457 DBREF 9GU3 B 1 478 UNP P11230 ACHB_HUMAN 24 501 DBREF 9GU3 D 1 496 UNP Q07001 ACHD_HUMAN 22 517 DBREF 9GU3 E 1 308K UNP Q04844 ACHE_HUMAN 21 364 DBREF 9GU3 E 308T 317V UNP P42212 GFP_AEQVI 2 238 DBREF 9GU3 E 317W 473 UNP Q04844 ACHE_HUMAN 362 493 DBREF 9GU3 L 1 437 UNP P02708 ACHA_HUMAN 21 457 DBREF 9GU3 C 1 213 PDB 9GU3 9GU3 1 213 DBREF 9GU3 F 1 219 PDB 9GU3 9GU3 1 219 DBREF 9GU3 G 1 213 PDB 9GU3 9GU3 1 213 DBREF 9GU3 H 1 219 PDB 9GU3 9GU3 1 219 SEQADV 9GU3 ALA E 308L UNP Q04844 LINKER SEQADV 9GU3 PRO E 308M UNP Q04844 LINKER SEQADV 9GU3 PRO E 308N UNP Q04844 LINKER SEQADV 9GU3 VAL E 308O UNP Q04844 LINKER SEQADV 9GU3 ALA E 308P UNP Q04844 LINKER SEQADV 9GU3 THR E 308Q UNP Q04844 LINKER SEQADV 9GU3 MET E 308R UNP Q04844 LINKER SEQADV 9GU3 VAL E 308S UNP Q04844 LINKER SEQADV 9GU3 LEU E 311D UNP P42212 PHE 64 CONFLICT SEQADV 9GU3 THR E 311E UNP P42212 SER 65 CONFLICT SEQADV 9GU3 LEU E 317O UNP P42212 HIS 231 CONFLICT SEQRES 1 A 437 SER GLU HIS GLU THR ARG LEU VAL ALA LYS LEU PHE LYS SEQRES 2 A 437 ASP TYR SER SER VAL VAL ARG PRO VAL GLU ASP HIS ARG SEQRES 3 A 437 GLN VAL VAL GLU VAL THR VAL GLY LEU GLN LEU ILE GLN SEQRES 4 A 437 LEU ILE ASN VAL ASP GLU VAL ASN GLN ILE VAL THR THR SEQRES 5 A 437 ASN VAL ARG LEU LYS GLN GLN TRP VAL ASP TYR ASN LEU SEQRES 6 A 437 LYS TRP ASN PRO ASP ASP TYR GLY GLY VAL LYS LYS ILE SEQRES 7 A 437 HIS ILE PRO SER GLU LYS ILE TRP ARG PRO ASP LEU VAL SEQRES 8 A 437 LEU TYR ASN ASN ALA ASP GLY ASP PHE ALA ILE VAL LYS SEQRES 9 A 437 PHE THR LYS VAL LEU LEU GLN TYR THR GLY HIS ILE THR SEQRES 10 A 437 TRP THR PRO PRO ALA ILE PHE LYS SER TYR CYS GLU ILE SEQRES 11 A 437 ILE VAL THR HIS PHE PRO PHE ASP GLU GLN ASN CYS SER SEQRES 12 A 437 MET LYS LEU GLY THR TRP THR TYR ASP GLY SER VAL VAL SEQRES 13 A 437 ALA ILE ASN PRO GLU SER ASP GLN PRO ASP LEU SER ASN SEQRES 14 A 437 PHE MET GLU SER GLY GLU TRP VAL ILE LYS GLU SER ARG SEQRES 15 A 437 GLY TRP LYS HIS SER VAL THR TYR SER CYS CYS PRO ASP SEQRES 16 A 437 THR PRO TYR LEU ASP ILE THR TYR HIS PHE VAL MET GLN SEQRES 17 A 437 ARG LEU PRO LEU TYR PHE ILE VAL ASN VAL ILE ILE PRO SEQRES 18 A 437 CYS LEU LEU PHE SER PHE LEU THR GLY LEU VAL PHE TYR SEQRES 19 A 437 LEU PRO THR ASP SER GLY GLU LYS MET THR LEU SER ILE SEQRES 20 A 437 SER VAL LEU LEU SER LEU THR VAL PHE LEU LEU VAL ILE SEQRES 21 A 437 VAL GLU LEU ILE PRO SER THR SER SER ALA VAL PRO LEU SEQRES 22 A 437 ILE GLY LYS TYR MET LEU PHE THR MET VAL PHE VAL ILE SEQRES 23 A 437 ALA SER ILE ILE ILE THR VAL ILE VAL ILE ASN THR HIS SEQRES 24 A 437 HIS ARG SER PRO SER THR HIS VAL MET PRO ASN TRP VAL SEQRES 25 A 437 ARG LYS VAL PHE ILE ASP THR ILE PRO ASN ILE MET PHE SEQRES 26 A 437 PHE SER THR MET LYS ARG PRO SER ARG GLU LYS GLN ASP SEQRES 27 A 437 LYS LYS ILE PHE THR GLU ASP ILE ASP ILE SER ASP ILE SEQRES 28 A 437 SER GLY LYS PRO GLY PRO PRO PRO MET GLY PHE HIS SER SEQRES 29 A 437 PRO LEU ILE LYS HIS PRO GLU VAL LYS SER ALA ILE GLU SEQRES 30 A 437 GLY ILE LYS TYR ILE ALA GLU THR MET LYS SER ASP GLN SEQRES 31 A 437 GLU SER ASN ASN ALA ALA ALA GLU TRP LYS TYR VAL ALA SEQRES 32 A 437 MET VAL MET ASP HIS ILE LEU LEU GLY VAL PHE MET LEU SEQRES 33 A 437 VAL CYS ILE ILE GLY THR LEU ALA VAL PHE ALA GLY ARG SEQRES 34 A 437 LEU ILE GLU LEU ASN GLN GLN GLY SEQRES 1 B 478 SER GLU ALA GLU GLY ARG LEU ARG GLU LYS LEU PHE SER SEQRES 2 B 478 GLY TYR ASP SER SER VAL ARG PRO ALA ARG GLU VAL GLY SEQRES 3 B 478 ASP ARG VAL ARG VAL SER VAL GLY LEU ILE LEU ALA GLN SEQRES 4 B 478 LEU ILE SER LEU ASN GLU LYS ASP GLU GLU MET SER THR SEQRES 5 B 478 LYS VAL TYR LEU ASP LEU GLU TRP THR ASP TYR ARG LEU SEQRES 6 B 478 SER TRP ASP PRO ALA GLU HIS ASP GLY ILE ASP SER LEU SEQRES 7 B 478 ARG ILE THR ALA GLU SER VAL TRP LEU PRO ASP VAL VAL SEQRES 8 B 478 LEU LEU ASN ASN ASN ASP GLY ASN PHE ASP VAL ALA LEU SEQRES 9 B 478 ASP ILE SER VAL VAL VAL SER SER ASP GLY SER VAL ARG SEQRES 10 B 478 TRP GLN PRO PRO GLY ILE TYR ARG SER SER CYS SER ILE SEQRES 11 B 478 GLN VAL THR TYR PHE PRO PHE ASP TRP GLN ASN CYS THR SEQRES 12 B 478 MET VAL PHE SER SER TYR SER TYR ASP SER SER GLU VAL SEQRES 13 B 478 SER LEU GLN THR GLY LEU GLY PRO ASP GLY GLN GLY HIS SEQRES 14 B 478 GLN GLU ILE HIS ILE HIS GLU GLY THR PHE ILE GLU ASN SEQRES 15 B 478 GLY GLN TRP GLU ILE ILE HIS LYS PRO SER ARG LEU ILE SEQRES 16 B 478 GLN PRO PRO GLY ASP PRO ARG GLY GLY ARG GLU GLY GLN SEQRES 17 B 478 ARG GLN GLU VAL ILE PHE TYR LEU ILE ILE ARG ARG LYS SEQRES 18 B 478 PRO LEU PHE TYR LEU VAL ASN VAL ILE ALA PRO CYS ILE SEQRES 19 B 478 LEU ILE THR LEU LEU ALA ILE PHE VAL PHE TYR LEU PRO SEQRES 20 B 478 PRO ASP ALA GLY GLU LYS MET GLY LEU SER ILE PHE ALA SEQRES 21 B 478 LEU LEU THR LEU THR VAL PHE LEU LEU LEU LEU ALA ASP SEQRES 22 B 478 LYS VAL PRO GLU THR SER LEU SER VAL PRO ILE ILE ILE SEQRES 23 B 478 LYS TYR LEU MET PHE THR MET VAL LEU VAL THR PHE SER SEQRES 24 B 478 VAL ILE LEU SER VAL VAL VAL LEU ASN LEU HIS HIS ARG SEQRES 25 B 478 SER PRO HIS THR HIS GLN MET PRO LEU TRP VAL ARG GLN SEQRES 26 B 478 ILE PHE ILE HIS LYS LEU PRO LEU TYR LEU ARG LEU LYS SEQRES 27 B 478 ARG PRO LYS PRO GLU ARG ASP LEU MET PRO GLU PRO PRO SEQRES 28 B 478 HIS CYS SER SER PRO GLY SER GLY TRP GLY ARG GLY THR SEQRES 29 B 478 ASP GLU TYR PHE ILE ARG LYS PRO PRO SER ASP PHE LEU SEQRES 30 B 478 PHE PRO LYS PRO ASN ARG PHE GLN PRO GLU LEU SER ALA SEQRES 31 B 478 PRO ASP LEU ARG ARG PHE ILE ASP GLY PRO ASN ARG ALA SEQRES 32 B 478 VAL ALA LEU LEU PRO GLU LEU ARG GLU VAL VAL SER SER SEQRES 33 B 478 ILE SER TYR ILE ALA ARG GLN LEU GLN GLU GLN GLU ASP SEQRES 34 B 478 HIS ASP ALA LEU LYS GLU ASP TRP GLN PHE VAL ALA MET SEQRES 35 B 478 VAL VAL ASP ARG LEU PHE LEU TRP THR PHE ILE ILE PHE SEQRES 36 B 478 THR SER VAL GLY THR LEU VAL ILE PHE LEU ASP ALA THR SEQRES 37 B 478 TYR HIS LEU PRO PRO PRO ASP PRO PHE PRO SEQRES 1 D 496 LEU ASN GLU GLU GLU ARG LEU ILE ARG HIS LEU PHE GLN SEQRES 2 D 496 GLU LYS GLY TYR ASN LYS GLU LEU ARG PRO VAL ALA HIS SEQRES 3 D 496 LYS GLU GLU SER VAL ASP VAL ALA LEU ALA LEU THR LEU SEQRES 4 D 496 SER ASN LEU ILE SER LEU LYS GLU VAL GLU GLU THR LEU SEQRES 5 D 496 THR THR ASN VAL TRP ILE GLU HIS GLY TRP THR ASP ASN SEQRES 6 D 496 ARG LEU LYS TRP ASN ALA GLU GLU PHE GLY ASN ILE SER SEQRES 7 D 496 VAL LEU ARG LEU PRO PRO ASP MET VAL TRP LEU PRO GLU SEQRES 8 D 496 ILE VAL LEU GLU ASN ASN ASN ASP GLY SER PHE GLN ILE SEQRES 9 D 496 SER TYR SER CYS ASN VAL LEU VAL TYR HIS TYR GLY PHE SEQRES 10 D 496 VAL TYR TRP LEU PRO PRO ALA ILE PHE ARG SER SER CYS SEQRES 11 D 496 PRO ILE SER VAL THR TYR PHE PRO PHE ASP TRP GLN ASN SEQRES 12 D 496 CYS SER LEU LYS PHE SER SER LEU LYS TYR THR ALA LYS SEQRES 13 D 496 GLU ILE THR LEU SER LEU LYS GLN ASP ALA LYS GLU ASN SEQRES 14 D 496 ARG THR TYR PRO VAL GLU TRP ILE ILE ILE ASP PRO GLU SEQRES 15 D 496 GLY PHE THR GLU ASN GLY GLU TRP GLU ILE VAL HIS ARG SEQRES 16 D 496 PRO ALA ARG VAL ASN VAL ASP PRO ARG ALA PRO LEU ASP SEQRES 17 D 496 SER PRO SER ARG GLN ASP ILE THR PHE TYR LEU ILE ILE SEQRES 18 D 496 ARG ARG LYS PRO LEU PHE TYR ILE ILE ASN ILE LEU VAL SEQRES 19 D 496 PRO CYS VAL LEU ILE SER PHE MET VAL ASN LEU VAL PHE SEQRES 20 D 496 TYR LEU PRO ALA ASP SER GLY GLU LYS THR SER VAL ALA SEQRES 21 D 496 ILE SER VAL LEU LEU ALA GLN SER VAL PHE LEU LEU LEU SEQRES 22 D 496 ILE SER LYS ARG LEU PRO ALA THR SER MET ALA ILE PRO SEQRES 23 D 496 LEU ILE GLY LYS PHE LEU LEU PHE GLY MET VAL LEU VAL SEQRES 24 D 496 THR MET VAL VAL VAL ILE CYS VAL ILE VAL LEU ASN ILE SEQRES 25 D 496 HIS PHE ARG THR PRO SER THR HIS VAL LEU SER GLU GLY SEQRES 26 D 496 VAL LYS LYS LEU PHE LEU GLU THR LEU PRO GLU LEU LEU SEQRES 27 D 496 HIS MET SER ARG PRO ALA GLU ASP GLY PRO SER PRO GLY SEQRES 28 D 496 ALA LEU VAL ARG ARG SER SER SER LEU GLY TYR ILE SER SEQRES 29 D 496 LYS ALA GLU GLU TYR PHE LEU LEU LYS SER ARG SER ASP SEQRES 30 D 496 LEU MET PHE GLU LYS GLN SER GLU ARG HIS GLY LEU ALA SEQRES 31 D 496 ARG ARG LEU THR THR ALA ARG ARG PRO PRO ALA SER SER SEQRES 32 D 496 GLU GLN ALA GLN GLN GLU LEU PHE ASN GLU LEU LYS PRO SEQRES 33 D 496 ALA VAL ASP GLY ALA ASN PHE ILE VAL ASN HIS MET ARG SEQRES 34 D 496 ASP GLN ASN ASN TYR ASN GLU GLU LYS ASP SER TRP ASN SEQRES 35 D 496 ARG VAL ALA ARG THR VAL ASP ARG LEU CYS LEU PHE VAL SEQRES 36 D 496 VAL THR PRO VAL MET VAL VAL GLY THR ALA TRP ILE PHE SEQRES 37 D 496 LEU GLN GLY VAL TYR ASN GLN PRO PRO PRO GLN PRO PHE SEQRES 38 D 496 PRO GLY ASP PRO TYR SER TYR ASN VAL GLN ASP LYS ARG SEQRES 39 D 496 PHE ILE SEQRES 1 E 721 LYS ASN GLU GLU LEU ARG LEU TYR HIS HIS LEU PHE ASN SEQRES 2 E 721 ASN TYR ASP PRO GLY SER ARG PRO VAL ARG GLU PRO GLU SEQRES 3 E 721 ASP THR VAL THR ILE SER LEU LYS VAL THR LEU THR ASN SEQRES 4 E 721 LEU ILE SER LEU ASN GLU LYS GLU GLU THR LEU THR THR SEQRES 5 E 721 SER VAL TRP ILE GLY ILE ASP TRP GLN ASP TYR ARG LEU SEQRES 6 E 721 ASN TYR SER LYS ASP ASP PHE GLY GLY ILE GLU THR LEU SEQRES 7 E 721 ARG VAL PRO SER GLU LEU VAL TRP LEU PRO GLU ILE VAL SEQRES 8 E 721 LEU GLU ASN ASN ILE ASP GLY GLN PHE GLY VAL ALA TYR SEQRES 9 E 721 ASP ALA ASN VAL LEU VAL TYR GLU GLY GLY SER VAL THR SEQRES 10 E 721 TRP LEU PRO PRO ALA ILE TYR ARG SER VAL CYS ALA VAL SEQRES 11 E 721 GLU VAL THR TYR PHE PRO PHE ASP TRP GLN ASN CYS SER SEQRES 12 E 721 LEU ILE PHE ARG SER GLN THR TYR ASN ALA GLU GLU VAL SEQRES 13 E 721 GLU PHE THR PHE ALA VAL ASP ASN ASP GLY LYS THR ILE SEQRES 14 E 721 ASN LYS ILE ASP ILE ASP THR GLU ALA TYR THR GLU ASN SEQRES 15 E 721 GLY GLU TRP ALA ILE ASP PHE CYS PRO GLY VAL ILE ARG SEQRES 16 E 721 ARG HIS HIS GLY GLY ALA THR ASP GLY PRO GLY GLU THR SEQRES 17 E 721 ASP VAL ILE TYR SER LEU ILE ILE ARG ARG LYS PRO LEU SEQRES 18 E 721 PHE TYR VAL ILE ASN ILE ILE VAL PRO CYS VAL LEU ILE SEQRES 19 E 721 SER GLY LEU VAL LEU LEU ALA TYR PHE LEU PRO ALA GLN SEQRES 20 E 721 ALA GLY GLY GLN LYS CYS THR VAL SER ILE ASN VAL LEU SEQRES 21 E 721 LEU ALA GLN THR VAL PHE LEU PHE LEU ILE ALA GLN LYS SEQRES 22 E 721 ILE PRO GLU THR SER LEU SER VAL PRO LEU LEU GLY ARG SEQRES 23 E 721 PHE LEU ILE PHE VAL MET VAL VAL ALA THR LEU ILE VAL SEQRES 24 E 721 MET ASN CYS VAL ILE VAL LEU ASN VAL SER GLN ARG THR SEQRES 25 E 721 PRO THR THR HIS ALA MET SER PRO ARG LEU ARG HIS VAL SEQRES 26 E 721 LEU LEU GLU LEU LEU PRO ARG LEU LEU GLY SER PRO PRO SEQRES 27 E 721 PRO PRO GLU ALA PRO ARG ALA PRO PRO VAL ALA THR MET SEQRES 28 E 721 VAL SER LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO SEQRES 29 E 721 ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS SEQRES 30 E 721 PHE SER VAL SER GLY GLU GLY GLU GLY ASP ALA THR TYR SEQRES 31 E 721 GLY LYS LEU THR LEU LYS PHE ILE CYS THR THR GLY LYS SEQRES 32 E 721 LEU PRO VAL PRO TRP PRO THR LEU VAL THR THR LEU THR SEQRES 33 E 721 TYR GLY VAL GLN CYS PHE SER ARG TYR PRO ASP HIS MET SEQRES 34 E 721 LYS GLN HIS ASP PHE PHE LYS SER ALA MET PRO GLU GLY SEQRES 35 E 721 TYR VAL GLN GLU ARG THR ILE PHE PHE LYS ASP ASP GLY SEQRES 36 E 721 ASN TYR LYS THR ARG ALA GLU VAL LYS PHE GLU GLY ASP SEQRES 37 E 721 THR LEU VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE SEQRES 38 E 721 LYS GLU ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR SEQRES 39 E 721 ASN TYR ASN SER HIS ASN VAL TYR ILE MET ALA ASP LYS SEQRES 40 E 721 GLN LYS ASN GLY ILE LYS VAL ASN PHE LYS ILE ARG HIS SEQRES 41 E 721 ASN ILE GLU ASP GLY SER VAL GLN LEU ALA ASP HIS TYR SEQRES 42 E 721 GLN GLN ASN THR PRO ILE GLY ASP GLY PRO VAL LEU LEU SEQRES 43 E 721 PRO ASP ASN HIS TYR LEU SER THR GLN SER ALA LEU SER SEQRES 44 E 721 LYS ASP PRO ASN GLU LYS ARG ASP HIS MET VAL LEU LEU SEQRES 45 E 721 GLU PHE VAL THR ALA ALA GLY ILE THR LEU GLY MET ASP SEQRES 46 E 721 GLU LEU TYR LYS ALA PRO ARG ALA ALA SER PRO PRO ARG SEQRES 47 E 721 ARG ALA SER SER VAL GLY LEU LEU LEU ARG ALA GLU GLU SEQRES 48 E 721 LEU ILE LEU LYS LYS PRO ARG SER GLU LEU VAL PHE GLU SEQRES 49 E 721 GLY GLN ARG HIS ARG GLN GLY THR TRP THR ALA ALA PHE SEQRES 50 E 721 CYS GLN SER LEU GLY ALA ALA ALA PRO GLU VAL ARG CYS SEQRES 51 E 721 CYS VAL ASP ALA VAL ASN PHE VAL ALA GLU SER THR ARG SEQRES 52 E 721 ASP GLN GLU ALA THR GLY GLU GLU VAL SER ASP TRP VAL SEQRES 53 E 721 ARG MET GLY ASN ALA LEU ASP ASN ILE CYS PHE TRP ALA SEQRES 54 E 721 ALA LEU VAL LEU PHE SER VAL GLY SER SER LEU ILE PHE SEQRES 55 E 721 LEU GLY ALA TYR PHE ASN ARG VAL PRO ASP LEU PRO TYR SEQRES 56 E 721 ALA PRO CYS ILE GLN PRO SEQRES 1 L 437 SER GLU HIS GLU THR ARG LEU VAL ALA LYS LEU PHE LYS SEQRES 2 L 437 ASP TYR SER SER VAL VAL ARG PRO VAL GLU ASP HIS ARG SEQRES 3 L 437 GLN VAL VAL GLU VAL THR VAL GLY LEU GLN LEU ILE GLN SEQRES 4 L 437 LEU ILE ASN VAL ASP GLU VAL ASN GLN ILE VAL THR THR SEQRES 5 L 437 ASN VAL ARG LEU LYS GLN GLN TRP VAL ASP TYR ASN LEU SEQRES 6 L 437 LYS TRP ASN PRO ASP ASP TYR GLY GLY VAL LYS LYS ILE SEQRES 7 L 437 HIS ILE PRO SER GLU LYS ILE TRP ARG PRO ASP LEU VAL SEQRES 8 L 437 LEU TYR ASN ASN ALA ASP GLY ASP PHE ALA ILE VAL LYS SEQRES 9 L 437 PHE THR LYS VAL LEU LEU GLN TYR THR GLY HIS ILE THR SEQRES 10 L 437 TRP THR PRO PRO ALA ILE PHE LYS SER TYR CYS GLU ILE SEQRES 11 L 437 ILE VAL THR HIS PHE PRO PHE ASP GLU GLN ASN CYS SER SEQRES 12 L 437 MET LYS LEU GLY THR TRP THR TYR ASP GLY SER VAL VAL SEQRES 13 L 437 ALA ILE ASN PRO GLU SER ASP GLN PRO ASP LEU SER ASN SEQRES 14 L 437 PHE MET GLU SER GLY GLU TRP VAL ILE LYS GLU SER ARG SEQRES 15 L 437 GLY TRP LYS HIS SER VAL THR TYR SER CYS CYS PRO ASP SEQRES 16 L 437 THR PRO TYR LEU ASP ILE THR TYR HIS PHE VAL MET GLN SEQRES 17 L 437 ARG LEU PRO LEU TYR PHE ILE VAL ASN VAL ILE ILE PRO SEQRES 18 L 437 CYS LEU LEU PHE SER PHE LEU THR GLY LEU VAL PHE TYR SEQRES 19 L 437 LEU PRO THR ASP SER GLY GLU LYS MET THR LEU SER ILE SEQRES 20 L 437 SER VAL LEU LEU SER LEU THR VAL PHE LEU LEU VAL ILE SEQRES 21 L 437 VAL GLU LEU ILE PRO SER THR SER SER ALA VAL PRO LEU SEQRES 22 L 437 ILE GLY LYS TYR MET LEU PHE THR MET VAL PHE VAL ILE SEQRES 23 L 437 ALA SER ILE ILE ILE THR VAL ILE VAL ILE ASN THR HIS SEQRES 24 L 437 HIS ARG SER PRO SER THR HIS VAL MET PRO ASN TRP VAL SEQRES 25 L 437 ARG LYS VAL PHE ILE ASP THR ILE PRO ASN ILE MET PHE SEQRES 26 L 437 PHE SER THR MET LYS ARG PRO SER ARG GLU LYS GLN ASP SEQRES 27 L 437 LYS LYS ILE PHE THR GLU ASP ILE ASP ILE SER ASP ILE SEQRES 28 L 437 SER GLY LYS PRO GLY PRO PRO PRO MET GLY PHE HIS SER SEQRES 29 L 437 PRO LEU ILE LYS HIS PRO GLU VAL LYS SER ALA ILE GLU SEQRES 30 L 437 GLY ILE LYS TYR ILE ALA GLU THR MET LYS SER ASP GLN SEQRES 31 L 437 GLU SER ASN ASN ALA ALA ALA GLU TRP LYS TYR VAL ALA SEQRES 32 L 437 MET VAL MET ASP HIS ILE LEU LEU GLY VAL PHE MET LEU SEQRES 33 L 437 VAL CYS ILE ILE GLY THR LEU ALA VAL PHE ALA GLY ARG SEQRES 34 L 437 LEU ILE GLU LEU ASN GLN GLN GLY SEQRES 1 C 213 ASP ILE VAL ILE THR GLN SER PRO SER LEU LEU SER ALA SEQRES 2 C 213 SER VAL GLY ASP ARG VAL THR LEU THR CYS LYS GLY SER SEQRES 3 C 213 GLN ASN ILE ASP ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 C 213 LEU GLY GLU ALA PRO LYS LEU LEU ILE TYR LYS THR ASN SEQRES 5 C 213 SER LEU GLN THR GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 C 213 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 C 213 HIS SER GLU ASP LEU ALA THR TYR TYR CYS TYR GLN TYR SEQRES 8 C 213 ILE ASN GLY TYR THR PHE GLY THR GLY THR LYS LEU GLU SEQRES 9 C 213 LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 C 213 PRO PRO SER THR GLU GLN LEU ALA THR GLY GLY ALA SER SEQRES 11 C 213 VAL VAL CYS LEU MET ASN ASN PHE TYR PRO ARG ASP ILE SEQRES 12 C 213 SER VAL LYS TRP LYS ILE ASP GLY THR GLU ARG ARG ASP SEQRES 13 C 213 GLY VAL LEU ASP SER VAL THR ASP GLN ASP SER LYS ASP SEQRES 14 C 213 SER THR TYR SER MET SER SER THR LEU SER LEU THR LYS SEQRES 15 C 213 ALA ASP TYR GLU SER HIS ASN LEU TYR THR CYS GLU VAL SEQRES 16 C 213 VAL HIS LYS THR SER SER SER PRO VAL VAL LYS SER PHE SEQRES 17 C 213 ASN ARG ASN GLU CYS SEQRES 1 F 219 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL GLN SEQRES 2 F 219 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 F 219 PHE SER LEU THR SER TYR SER VAL SER TRP LEU ARG GLN SEQRES 4 F 219 PRO SER GLY LYS GLY PRO GLU TRP MET GLY ARG MET TRP SEQRES 5 F 219 ASP ASP GLY GLY THR VAL TYR ASN SER GLY LEU LYS SER SEQRES 6 F 219 ARG LEU SER ILE SER ARG ASP THR SER LYS ASN GLN VAL SEQRES 7 F 219 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR GLY SEQRES 8 F 219 THR TYR TYR CYS THR ARG ASP GLU ARG ILE ARG ALA ILE SEQRES 9 F 219 ASN TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 F 219 VAL SER SER ALA GLU THR THR ALA PRO SER VAL TYR PRO SEQRES 11 F 219 LEU ALA PRO GLY THR ALA LEU LYS SER ASN SER MET VAL SEQRES 12 F 219 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO SEQRES 13 F 219 VAL THR VAL THR TRP ASN SER GLY ALA LEU SER SER GLY SEQRES 14 F 219 VAL HIS THR PHE PRO ALA VAL LEU GLN SER GLY LEU TYR SEQRES 15 F 219 THR LEU THR SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 F 219 PRO SER GLN THR VAL THR CYS ASN VAL ALA HIS PRO GLY SEQRES 17 F 219 GLN GLN HIS GLN ARG TRP THR ARG LYS LEU CYS SEQRES 1 G 213 ASP ILE VAL ILE THR GLN SER PRO SER LEU LEU SER ALA SEQRES 2 G 213 SER VAL GLY ASP ARG VAL THR LEU THR CYS LYS GLY SER SEQRES 3 G 213 GLN ASN ILE ASP ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 G 213 LEU GLY GLU ALA PRO LYS LEU LEU ILE TYR LYS THR ASN SEQRES 5 G 213 SER LEU GLN THR GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 G 213 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 G 213 HIS SER GLU ASP LEU ALA THR TYR TYR CYS TYR GLN TYR SEQRES 8 G 213 ILE ASN GLY TYR THR PHE GLY THR GLY THR LYS LEU GLU SEQRES 9 G 213 LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 G 213 PRO PRO SER THR GLU GLN LEU ALA THR GLY GLY ALA SER SEQRES 11 G 213 VAL VAL CYS LEU MET ASN ASN PHE TYR PRO ARG ASP ILE SEQRES 12 G 213 SER VAL LYS TRP LYS ILE ASP GLY THR GLU ARG ARG ASP SEQRES 13 G 213 GLY VAL LEU ASP SER VAL THR ASP GLN ASP SER LYS ASP SEQRES 14 G 213 SER THR TYR SER MET SER SER THR LEU SER LEU THR LYS SEQRES 15 G 213 ALA ASP TYR GLU SER HIS ASN LEU TYR THR CYS GLU VAL SEQRES 16 G 213 VAL HIS LYS THR SER SER SER PRO VAL VAL LYS SER PHE SEQRES 17 G 213 ASN ARG ASN GLU CYS SEQRES 1 H 219 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL GLN SEQRES 2 H 219 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 219 PHE SER LEU THR SER TYR SER VAL SER TRP LEU ARG GLN SEQRES 4 H 219 PRO SER GLY LYS GLY PRO GLU TRP MET GLY ARG MET TRP SEQRES 5 H 219 ASP ASP GLY GLY THR VAL TYR ASN SER GLY LEU LYS SER SEQRES 6 H 219 ARG LEU SER ILE SER ARG ASP THR SER LYS ASN GLN VAL SEQRES 7 H 219 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR GLY SEQRES 8 H 219 THR TYR TYR CYS THR ARG ASP GLU ARG ILE ARG ALA ILE SEQRES 9 H 219 ASN TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 219 VAL SER SER ALA GLU THR THR ALA PRO SER VAL TYR PRO SEQRES 11 H 219 LEU ALA PRO GLY THR ALA LEU LYS SER ASN SER MET VAL SEQRES 12 H 219 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO SEQRES 13 H 219 VAL THR VAL THR TRP ASN SER GLY ALA LEU SER SER GLY SEQRES 14 H 219 VAL HIS THR PHE PRO ALA VAL LEU GLN SER GLY LEU TYR SEQRES 15 H 219 THR LEU THR SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 H 219 PRO SER GLN THR VAL THR CYS ASN VAL ALA HIS PRO GLY SEQRES 17 H 219 GLN GLN HIS GLN ARG TRP THR ARG LYS LEU CYS 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 MAN J 4 11 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET MAN K 4 11 HET NAG K 5 14 HET MAN K 6 11 HET MAN K 7 11 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET MAN N 4 11 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET MAN O 4 11 HET MAN O 5 11 HET MAN O 6 11 HET ACH A 500 10 HET NAG D 501 14 HET ACH L 500 10 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM ACH ACETYLCHOLINE 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 FORMUL 10 NAG 14(C8 H15 N O6) FORMUL 10 BMA 5(C6 H12 O6) FORMUL 10 MAN 11(C6 H12 O6) FORMUL 16 ACH 2(C7 H16 N O2 1+) HELIX 1 AA1 SER A 1 PHE A 12 1 12 HELIX 2 AA2 TYR A 63 LYS A 66 5 4 HELIX 3 AA3 ASN A 68 GLY A 73 5 6 HELIX 4 AA4 PRO A 211 VAL A 218 1 8 HELIX 5 AA5 VAL A 218 VAL A 232 1 15 HELIX 6 AA6 PHE A 233 LEU A 235 5 3 HELIX 7 AA7 PRO A 236 GLY A 240 5 5 HELIX 8 AA8 GLU A 241 ILE A 264 1 24 HELIX 9 AA9 PRO A 272 ASN A 297 1 26 HELIX 10 AB1 ALA A 403 PHE A 426 1 24 HELIX 11 AB2 GLU B 2 SER B 13 1 12 HELIX 12 AB3 TYR B 63 SER B 66 5 4 HELIX 13 AB4 ASP B 68 ASP B 73 5 6 HELIX 14 AB5 THR B 81 VAL B 85 5 5 HELIX 15 AB6 PRO B 222 VAL B 229 1 8 HELIX 16 AB7 VAL B 229 VAL B 243 1 15 HELIX 17 AB8 PHE B 244 LEU B 246 5 3 HELIX 18 AB9 PRO B 247 GLY B 251 5 5 HELIX 19 AC1 GLU B 252 VAL B 275 1 24 HELIX 20 AC2 PRO B 283 LEU B 309 1 27 HELIX 21 AC3 GLN B 438 HIS B 470 1 33 HELIX 22 AC4 ASN D 2 GLN D 13 1 12 HELIX 23 AC5 ASN D 65 LYS D 68 5 4 HELIX 24 AC6 ASN D 70 GLY D 75 5 6 HELIX 25 AC7 PRO D 225 ILE D 232 1 8 HELIX 26 AC8 ILE D 232 VAL D 243 1 12 HELIX 27 AC9 ASN D 244 TYR D 248 5 5 HELIX 28 AD1 PRO D 250 GLY D 254 5 5 HELIX 29 AD2 GLU D 255 LEU D 278 1 24 HELIX 30 AD3 PRO D 286 ILE D 312 1 27 HELIX 31 AD4 ARG D 446 TYR D 473 1 28 HELIX 32 AD5 ASN D 489 LYS D 493 5 5 HELIX 33 AD6 ASN E 2 ASN E 13 1 12 HELIX 34 AD7 TYR E 63 ASN E 66 5 4 HELIX 35 AD8 SER E 68 PHE E 72 5 5 HELIX 36 AD9 PRO E 81 VAL E 85 5 5 HELIX 37 AE1 PRO E 220 ILE E 227 1 8 HELIX 38 AE2 ILE E 227 LEU E 239 1 13 HELIX 39 AE3 LEU E 240 LEU E 244 5 5 HELIX 40 AE4 GLN E 251 ILE E 274 1 24 HELIX 41 AE5 PRO E 282 ASN E 307 1 26 HELIX 42 AE6 ASN E 432 ASN E 460 1 29 HELIX 43 AE7 GLU L 2 PHE L 12 1 11 HELIX 44 AE8 TYR L 63 LYS L 66 5 4 HELIX 45 AE9 ASN L 68 GLY L 73 5 6 HELIX 46 AF1 GLU L 83 ILE L 85 5 3 HELIX 47 AF2 PRO L 211 VAL L 218 1 8 HELIX 48 AF3 VAL L 218 LEU L 235 1 18 HELIX 49 AF4 PRO L 236 SER L 239 5 4 HELIX 50 AF5 GLY L 240 ILE L 264 1 25 HELIX 51 AF6 PRO L 272 THR L 298 1 27 HELIX 52 AF7 ASP L 407 LEU L 430 1 24 HELIX 53 AF8 HIS C 79 LEU C 83 5 5 HELIX 54 AF9 SER C 120 THR C 126 1 7 HELIX 55 AG1 THR C 181 SER C 187 1 7 HELIX 56 AG2 GLN F 86 ASP F 89 5 4 HELIX 57 AG3 SER F 163 SER F 167 5 5 HELIX 58 AG4 HIS G 79 LEU G 83 5 5 HELIX 59 AG5 SER G 120 THR G 126 1 7 HELIX 60 AG6 THR G 181 SER G 187 1 7 HELIX 61 AG7 GLN H 86 ASP H 89 5 4 HELIX 62 AG8 SER H 163 SER H 167 5 5 SHEET 1 AA1 5 LYS A 77 PRO A 81 0 SHEET 2 AA1 5 LYS A 107 GLN A 111 -1 O VAL A 108 N ILE A 80 SHEET 3 AA1 5 HIS A 115 TRP A 118 -1 O THR A 117 N LEU A 109 SHEET 4 AA1 5 ILE A 49 VAL A 61 -1 N TRP A 60 O ILE A 116 SHEET 5 AA1 5 PRO A 121 TYR A 127 -1 O ALA A 122 N VAL A 54 SHEET 1 AA2 6 LYS A 77 PRO A 81 0 SHEET 2 AA2 6 LYS A 107 GLN A 111 -1 O VAL A 108 N ILE A 80 SHEET 3 AA2 6 HIS A 115 TRP A 118 -1 O THR A 117 N LEU A 109 SHEET 4 AA2 6 ILE A 49 VAL A 61 -1 N TRP A 60 O ILE A 116 SHEET 5 AA2 6 VAL A 29 ASP A 44 -1 N GLN A 39 O ASN A 53 SHEET 6 AA2 6 VAL A 156 PRO A 160 1 O ALA A 157 N VAL A 31 SHEET 1 AA3 4 LEU A 90 LEU A 92 0 SHEET 2 AA3 4 GLU A 139 THR A 148 -1 O GLY A 147 N VAL A 91 SHEET 3 AA3 4 TYR A 198 ARG A 209 -1 O ILE A 201 N LEU A 146 SHEET 4 AA3 4 TRP A 176 VAL A 188 -1 N VAL A 177 O GLN A 208 SHEET 1 AA4 5 SER B 77 ILE B 80 0 SHEET 2 AA4 5 VAL B 108 SER B 111 -1 O VAL B 110 N LEU B 78 SHEET 3 AA4 5 SER B 115 TRP B 118 -1 O SER B 115 N SER B 111 SHEET 4 AA4 5 GLU B 49 THR B 61 -1 N TRP B 60 O VAL B 116 SHEET 5 AA4 5 PRO B 121 SER B 127 -1 O GLY B 122 N VAL B 54 SHEET 1 AA5 6 SER B 77 ILE B 80 0 SHEET 2 AA5 6 VAL B 108 SER B 111 -1 O VAL B 110 N LEU B 78 SHEET 3 AA5 6 SER B 115 TRP B 118 -1 O SER B 115 N SER B 111 SHEET 4 AA5 6 GLU B 49 THR B 61 -1 N TRP B 60 O VAL B 116 SHEET 5 AA5 6 VAL B 29 ASN B 44 -1 N GLN B 39 O LYS B 53 SHEET 6 AA5 6 VAL B 156 THR B 160 1 O GLN B 159 N VAL B 33 SHEET 1 AA6 4 VAL B 90 LEU B 92 0 SHEET 2 AA6 4 TRP B 139 SER B 148 -1 O SER B 147 N VAL B 91 SHEET 3 AA6 4 GLU B 211 ARG B 220 -1 O ILE B 218 N GLN B 140 SHEET 4 AA6 4 TRP B 185 HIS B 189 -1 N ILE B 188 O ILE B 217 SHEET 1 AA7 4 VAL B 90 LEU B 92 0 SHEET 2 AA7 4 TRP B 139 SER B 148 -1 O SER B 147 N VAL B 91 SHEET 3 AA7 4 GLU B 211 ARG B 220 -1 O ILE B 218 N GLN B 140 SHEET 4 AA7 4 SER B 192 ILE B 195 -1 N ILE B 195 O GLU B 211 SHEET 1 AA8 5 VAL D 79 LEU D 82 0 SHEET 2 AA8 5 VAL D 110 TYR D 113 -1 O VAL D 112 N LEU D 80 SHEET 3 AA8 5 PHE D 117 TRP D 120 -1 O TYR D 119 N LEU D 111 SHEET 4 AA8 5 THR D 51 THR D 63 -1 N TRP D 62 O VAL D 118 SHEET 5 AA8 5 PRO D 123 SER D 129 -1 O ALA D 124 N VAL D 56 SHEET 1 AA9 6 VAL D 79 LEU D 82 0 SHEET 2 AA9 6 VAL D 110 TYR D 113 -1 O VAL D 112 N LEU D 80 SHEET 3 AA9 6 PHE D 117 TRP D 120 -1 O TYR D 119 N LEU D 111 SHEET 4 AA9 6 THR D 51 THR D 63 -1 N TRP D 62 O VAL D 118 SHEET 5 AA9 6 VAL D 31 LYS D 46 -1 N ASN D 41 O ASN D 55 SHEET 6 AA9 6 ILE D 158 LEU D 162 1 O THR D 159 N VAL D 33 SHEET 1 AB1 4 ILE D 92 LEU D 94 0 SHEET 2 AB1 4 TRP D 141 SER D 150 -1 O SER D 149 N VAL D 93 SHEET 3 AB1 4 GLN D 213 ARG D 223 -1 O ILE D 215 N PHE D 148 SHEET 4 AB1 4 TRP D 190 HIS D 194 -1 N GLU D 191 O ARG D 222 SHEET 1 AB2 4 ILE D 92 LEU D 94 0 SHEET 2 AB2 4 TRP D 141 SER D 150 -1 O SER D 149 N VAL D 93 SHEET 3 AB2 4 GLN D 213 ARG D 223 -1 O ILE D 215 N PHE D 148 SHEET 4 AB2 4 ALA D 197 VAL D 201 -1 N ARG D 198 O THR D 216 SHEET 1 AB3 2 GLN D 164 LYS D 167 0 SHEET 2 AB3 2 ARG D 170 PRO D 173 -1 O TYR D 172 N ASP D 165 SHEET 1 AB4 5 THR E 77 VAL E 80 0 SHEET 2 AB4 5 VAL E 108 TYR E 111 -1 O VAL E 110 N LEU E 78 SHEET 3 AB4 5 SER E 115 TRP E 118 -1 O THR E 117 N LEU E 109 SHEET 4 AB4 5 THR E 49 GLN E 61 -1 N TRP E 60 O VAL E 116 SHEET 5 AB4 5 PRO E 121 VAL E 127 -1 O TYR E 124 N THR E 52 SHEET 1 AB5 6 THR E 77 VAL E 80 0 SHEET 2 AB5 6 VAL E 108 TYR E 111 -1 O VAL E 110 N LEU E 78 SHEET 3 AB5 6 SER E 115 TRP E 118 -1 O THR E 117 N LEU E 109 SHEET 4 AB5 6 THR E 49 GLN E 61 -1 N TRP E 60 O VAL E 116 SHEET 5 AB5 6 VAL E 29 ASN E 44 -1 N ASN E 44 O THR E 49 SHEET 6 AB5 6 VAL E 156 PHE E 160 1 O GLU E 157 N ILE E 31 SHEET 1 AB6 4 ILE E 90 LEU E 92 0 SHEET 2 AB6 4 TRP E 139 SER E 148 -1 O ARG E 147 N VAL E 91 SHEET 3 AB6 4 GLU E 207 ARG E 218 -1 O VAL E 210 N PHE E 146 SHEET 4 AB6 4 TRP E 185 PHE E 189 -1 N ALA E 186 O ARG E 217 SHEET 1 AB7 4 ILE E 90 LEU E 92 0 SHEET 2 AB7 4 TRP E 139 SER E 148 -1 O ARG E 147 N VAL E 91 SHEET 3 AB7 4 GLU E 207 ARG E 218 -1 O VAL E 210 N PHE E 146 SHEET 4 AB7 4 GLY E 192 HIS E 197 -1 N VAL E 193 O ILE E 211 SHEET 1 AB8 5 LYS L 77 PRO L 81 0 SHEET 2 AB8 5 LYS L 107 GLN L 111 -1 O VAL L 108 N ILE L 80 SHEET 3 AB8 5 HIS L 115 TRP L 118 -1 O THR L 117 N LEU L 109 SHEET 4 AB8 5 ILE L 49 VAL L 61 -1 N TRP L 60 O ILE L 116 SHEET 5 AB8 5 PRO L 121 TYR L 127 -1 O ALA L 122 N VAL L 54 SHEET 1 AB9 6 LYS L 77 PRO L 81 0 SHEET 2 AB9 6 LYS L 107 GLN L 111 -1 O VAL L 108 N ILE L 80 SHEET 3 AB9 6 HIS L 115 TRP L 118 -1 O THR L 117 N LEU L 109 SHEET 4 AB9 6 ILE L 49 VAL L 61 -1 N TRP L 60 O ILE L 116 SHEET 5 AB9 6 VAL L 29 ASP L 44 -1 N GLN L 39 O ASN L 53 SHEET 6 AB9 6 VAL L 156 PRO L 160 1 O ASN L 159 N VAL L 31 SHEET 1 AC1 4 LEU L 90 LEU L 92 0 SHEET 2 AC1 4 GLU L 139 THR L 148 -1 O GLY L 147 N VAL L 91 SHEET 3 AC1 4 TYR L 198 ARG L 209 -1 O ILE L 201 N LEU L 146 SHEET 4 AC1 4 TRP L 176 VAL L 188 -1 N VAL L 177 O GLN L 208 SHEET 1 AC2 4 ILE C 4 SER C 7 0 SHEET 2 AC2 4 VAL C 19 GLY C 25 -1 O LYS C 24 N THR C 5 SHEET 3 AC2 4 ASP C 70 ILE C 75 -1 O TYR C 71 N CYS C 23 SHEET 4 AC2 4 PHE C 62 SER C 67 -1 N SER C 65 O THR C 72 SHEET 1 AC3 6 LEU C 10 ALA C 13 0 SHEET 2 AC3 6 THR C 101 LEU C 105 1 O GLU C 104 N LEU C 11 SHEET 3 AC3 6 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 101 SHEET 4 AC3 6 LEU C 33 GLN C 38 -1 N GLN C 38 O THR C 85 SHEET 5 AC3 6 LYS C 45 TYR C 49 -1 O LYS C 45 N GLN C 37 SHEET 6 AC3 6 SER C 53 LEU C 54 -1 O SER C 53 N TYR C 49 SHEET 1 AC4 4 LEU C 10 ALA C 13 0 SHEET 2 AC4 4 THR C 101 LEU C 105 1 O GLU C 104 N LEU C 11 SHEET 3 AC4 4 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 101 SHEET 4 AC4 4 THR C 96 PHE C 97 -1 O THR C 96 N GLN C 90 SHEET 1 AC5 4 THR C 113 PHE C 117 0 SHEET 2 AC5 4 VAL C 131 PHE C 138 -1 O VAL C 132 N PHE C 117 SHEET 3 AC5 4 TYR C 172 LEU C 178 -1 O TYR C 172 N PHE C 138 SHEET 4 AC5 4 VAL C 158 VAL C 162 -1 N LEU C 159 O THR C 177 SHEET 1 AC6 4 THR C 152 ARG C 154 0 SHEET 2 AC6 4 ILE C 143 ILE C 149 -1 N ILE C 149 O THR C 152 SHEET 3 AC6 4 LEU C 190 HIS C 197 -1 O GLU C 194 N LYS C 146 SHEET 4 AC6 4 VAL C 204 ASN C 209 -1 O VAL C 204 N VAL C 195 SHEET 1 AC7 4 GLN F 3 SER F 7 0 SHEET 2 AC7 4 LEU F 18 SER F 25 -1 O SER F 25 N GLN F 3 SHEET 3 AC7 4 GLN F 77 MET F 82 -1 O VAL F 78 N CYS F 22 SHEET 4 AC7 4 LEU F 67 ASP F 72 -1 N ASP F 72 O GLN F 77 SHEET 1 AC8 6 LEU F 11 VAL F 12 0 SHEET 2 AC8 6 THR F 114 VAL F 118 1 O THR F 117 N VAL F 12 SHEET 3 AC8 6 GLY F 91 ILE F 101 -1 N GLY F 91 O VAL F 116 SHEET 4 AC8 6 SER F 33 PRO F 40 -1 N LEU F 37 O TYR F 94 SHEET 5 AC8 6 GLU F 46 MET F 51 -1 O GLU F 46 N ARG F 38 SHEET 6 AC8 6 THR F 57 TYR F 59 -1 O VAL F 58 N ARG F 50 SHEET 1 AC9 4 LEU F 11 VAL F 12 0 SHEET 2 AC9 4 THR F 114 VAL F 118 1 O THR F 117 N VAL F 12 SHEET 3 AC9 4 GLY F 91 ILE F 101 -1 N GLY F 91 O VAL F 116 SHEET 4 AC9 4 ILE F 104 TRP F 110 -1 O TYR F 109 N ARG F 97 SHEET 1 AD1 4 SER F 127 LEU F 131 0 SHEET 2 AD1 4 VAL F 143 LYS F 150 -1 O LEU F 148 N TYR F 129 SHEET 3 AD1 4 LEU F 181 VAL F 190 -1 O LEU F 184 N VAL F 149 SHEET 4 AD1 4 VAL F 170 GLN F 178 -1 N GLN F 178 O LEU F 181 SHEET 1 AD2 3 THR F 158 TRP F 161 0 SHEET 2 AD2 3 THR F 201 HIS F 206 -1 O ALA F 205 N THR F 158 SHEET 3 AD2 3 HIS F 211 ARG F 216 -1 O THR F 215 N CYS F 202 SHEET 1 AD3 4 ILE G 4 SER G 7 0 SHEET 2 AD3 4 VAL G 19 GLY G 25 -1 O LYS G 24 N THR G 5 SHEET 3 AD3 4 ASP G 70 ILE G 75 -1 O TYR G 71 N CYS G 23 SHEET 4 AD3 4 PHE G 62 SER G 67 -1 N SER G 63 O THR G 74 SHEET 1 AD4 6 LEU G 10 ALA G 13 0 SHEET 2 AD4 6 THR G 101 LEU G 105 1 O LYS G 102 N LEU G 11 SHEET 3 AD4 6 THR G 85 GLN G 90 -1 N TYR G 86 O THR G 101 SHEET 4 AD4 6 LEU G 33 GLN G 38 -1 N GLN G 38 O THR G 85 SHEET 5 AD4 6 LYS G 45 TYR G 49 -1 O LYS G 45 N GLN G 37 SHEET 6 AD4 6 SER G 53 LEU G 54 -1 O SER G 53 N TYR G 49 SHEET 1 AD5 4 LEU G 10 ALA G 13 0 SHEET 2 AD5 4 THR G 101 LEU G 105 1 O LYS G 102 N LEU G 11 SHEET 3 AD5 4 THR G 85 GLN G 90 -1 N TYR G 86 O THR G 101 SHEET 4 AD5 4 THR G 96 PHE G 97 -1 O THR G 96 N GLN G 90 SHEET 1 AD6 4 THR G 113 PHE G 117 0 SHEET 2 AD6 4 VAL G 131 PHE G 138 -1 O VAL G 132 N PHE G 117 SHEET 3 AD6 4 TYR G 172 LEU G 178 -1 O TYR G 172 N PHE G 138 SHEET 4 AD6 4 VAL G 158 VAL G 162 -1 N SER G 161 O SER G 175 SHEET 1 AD7 4 THR G 152 ARG G 154 0 SHEET 2 AD7 4 ILE G 143 ILE G 149 -1 N ILE G 149 O THR G 152 SHEET 3 AD7 4 LEU G 190 HIS G 197 -1 O GLU G 194 N LYS G 146 SHEET 4 AD7 4 VAL G 204 ASN G 209 -1 O VAL G 204 N VAL G 195 SHEET 1 AD8 4 GLN H 3 SER H 7 0 SHEET 2 AD8 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AD8 4 GLN H 77 MET H 82 -1 O VAL H 78 N CYS H 22 SHEET 4 AD8 4 LEU H 67 ASP H 72 -1 N SER H 68 O LYS H 81 SHEET 1 AD9 6 LEU H 11 VAL H 12 0 SHEET 2 AD9 6 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AD9 6 GLY H 91 ILE H 101 -1 N GLY H 91 O VAL H 116 SHEET 4 AD9 6 SER H 33 PRO H 40 -1 N LEU H 37 O TYR H 94 SHEET 5 AD9 6 GLU H 46 MET H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AD9 6 THR H 57 TYR H 59 -1 O VAL H 58 N ARG H 50 SHEET 1 AE1 4 LEU H 11 VAL H 12 0 SHEET 2 AE1 4 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AE1 4 GLY H 91 ILE H 101 -1 N GLY H 91 O VAL H 116 SHEET 4 AE1 4 ILE H 104 TRP H 110 -1 O ILE H 104 N ILE H 101 SHEET 1 AE2 4 SER H 127 LEU H 131 0 SHEET 2 AE2 4 VAL H 143 TYR H 152 -1 O LYS H 150 N SER H 127 SHEET 3 AE2 4 LEU H 181 VAL H 190 -1 O TYR H 182 N TYR H 152 SHEET 4 AE2 4 VAL H 170 GLN H 178 -1 N GLN H 178 O LEU H 181 SHEET 1 AE3 3 THR H 158 TRP H 161 0 SHEET 2 AE3 3 THR H 201 HIS H 206 -1 O ALA H 205 N THR H 158 SHEET 3 AE3 3 HIS H 211 ARG H 216 -1 O THR H 215 N CYS H 202 SSBOND 1 CYS A 128 CYS A 142 1555 1555 2.03 SSBOND 2 CYS A 192 CYS A 193 1555 1555 2.05 SSBOND 3 CYS B 128 CYS B 142 1555 1555 2.03 SSBOND 4 CYS D 130 CYS D 144 1555 1555 2.03 SSBOND 5 CYS E 128 CYS E 142 1555 1555 2.03 SSBOND 6 CYS E 190 CYS E 470 1555 1555 2.03 SSBOND 7 CYS L 128 CYS L 142 1555 1555 2.03 SSBOND 8 CYS L 192 CYS L 193 1555 1555 2.05 SSBOND 9 CYS C 23 CYS C 88 1555 1555 2.03 SSBOND 10 CYS C 133 CYS C 193 1555 1555 2.04 SSBOND 11 CYS F 22 CYS F 95 1555 1555 2.03 SSBOND 12 CYS F 147 CYS F 202 1555 1555 2.03 SSBOND 13 CYS G 23 CYS G 88 1555 1555 2.03 SSBOND 14 CYS G 133 CYS G 193 1555 1555 2.03 SSBOND 15 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 16 CYS H 147 CYS H 202 1555 1555 2.03 LINK ND2 ASN A 141 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN B 141 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN D 76 C1 NAG D 501 1555 1555 1.44 LINK ND2 ASN D 143 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN E 66 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN E 141 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN L 141 C1 NAG O 1 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44 LINK O6 BMA I 3 C1 MAN I 4 1555 1555 1.44 LINK O3 BMA I 3 C1 MAN I 6 1555 1555 1.45 LINK O3 MAN I 4 C1 MAN I 5 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44 LINK O6 BMA J 3 C1 MAN J 4 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O3 BMA K 3 C1 MAN K 4 1555 1555 1.44 LINK O6 BMA K 3 C1 MAN K 6 1555 1555 1.44 LINK O2 MAN K 4 C1 NAG K 5 1555 1555 1.44 LINK O3 MAN K 6 C1 MAN K 7 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.46 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.44 LINK O6 BMA N 3 C1 MAN N 4 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O6 BMA O 3 C1 MAN O 4 1555 1555 1.44 LINK O3 BMA O 3 C1 MAN O 6 1555 1555 1.44 LINK O3 MAN O 4 C1 MAN O 5 1555 1555 1.44 CISPEP 1 PHE A 135 PRO A 136 0 0.51 CISPEP 2 PHE B 135 PRO B 136 0 -1.14 CISPEP 3 PHE D 137 PRO D 138 0 2.61 CISPEP 4 PHE E 135 PRO E 136 0 0.48 CISPEP 5 PHE L 135 PRO L 136 0 1.66 CISPEP 6 SER C 7 PRO C 8 0 -11.00 CISPEP 7 TYR C 139 PRO C 140 0 -4.06 CISPEP 8 PHE F 153 PRO F 154 0 -13.74 CISPEP 9 GLU F 155 PRO F 156 0 -1.86 CISPEP 10 SER G 7 PRO G 8 0 -9.84 CISPEP 11 TYR G 139 PRO G 140 0 -3.70 CISPEP 12 PHE H 153 PRO H 154 0 -13.01 CISPEP 13 GLU H 155 PRO H 156 0 -4.54 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