HEADER MEMBRANE PROTEIN 18-SEP-24 9GU0 TITLE HUMAN ADULT MUSCLE NACHR IN RESTING STATE IN DETERGENT WITH ALPHA- TITLE 2 BUNGAROTOXIN 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: FAB35 LIGHT CHAIN; COMPND 11 CHAIN: C, G; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT DELTA; COMPND 15 CHAIN: D; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT EPSILON,GREEN FLUORESCENT COMPND 19 PROTEIN; COMPND 20 CHAIN: E; COMPND 21 ENGINEERED: YES; COMPND 22 MUTATION: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: FAB35 HEAVY CHAIN; COMPND 25 CHAIN: F, H; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 7; COMPND 28 MOLECULE: ALPHA-BUNGAROTOXIN; COMPND 29 CHAIN: J, I; COMPND 30 SYNONYM: ALPHA-BGTX,ALPHA-BTX,ALPHA-BUNGAROTOXIN,ISOFORM A31,ALPHA- COMPND 31 BTX A31,ALPHA-BGTX(A31),ALPHA-BUNGAROTOXIN (A31),BGTX A31,ALPHA- COMPND 32 ELAPITOXIN-BM2A,ALPHA-EPTX-BM2A,LONG NEUROTOXIN 1 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: RATTUS NORVEGICUS; SOURCE 23 ORGANISM_TAXID: 10116; SOURCE 24 EXPRESSION_SYSTEM: RATTUS NORVEGICUS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 10116; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA; SOURCE 27 EXPRESSION_SYSTEM_ATCC_NUMBER: TIB-175; SOURCE 28 MOL_ID: 4; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_COMMON: HUMAN; SOURCE 31 ORGANISM_TAXID: 9606; SOURCE 32 GENE: CHRND, ACHRD; SOURCE 33 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 35 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 36 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 37 EXPRESSION_SYSTEM_PLASMID: TLCV2; SOURCE 38 MOL_ID: 5; SOURCE 39 ORGANISM_SCIENTIFIC: HOMO SAPIENS, AEQUOREA VICTORIA; SOURCE 40 ORGANISM_COMMON: HUMAN, WATER JELLYFISH, MESONEMA VICTORIA; SOURCE 41 ORGANISM_TAXID: 9606, 6100; SOURCE 42 GENE: CHRNE, ACHRE, GFP; SOURCE 43 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 44 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 45 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 46 EXPRESSION_SYSTEM_VECTOR_TYPE: LENTIVIRUS; SOURCE 47 EXPRESSION_SYSTEM_PLASMID: TLCV2; 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; SOURCE 55 MOL_ID: 7; SOURCE 56 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS; SOURCE 57 ORGANISM_COMMON: MANY-BANDED KRAIT; SOURCE 58 ORGANISM_TAXID: 8616 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 9GU0 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 2 REMARK 2 RESOLUTION. 2.96 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, UCSF REMARK 3 CHIMERAX, COOT, ISOLDE, CRYOSPARC, REMARK 3 CRYOSPARC, 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) : 2.960 REMARK 3 NUMBER OF PARTICLES : 31022 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 REFINEMENT REMARK 4 REMARK 4 9GU0 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_1292141663. 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 RESTING STATE IN DETERGENT WITH REMARK 245 ALPHA-BUNGAROTOXIN REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.68 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT TIME 2S, BLOT FORCE -10 REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NACHR IN COMPLEX WITH ALPHA REMARK 245 -BUNGAROTOXIN AND FAB35 REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 18672 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) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 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 : OBJECTIVE APERTURE 70 UM 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: 11-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 11-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, J, L, REMARK 350 AND CHAINS: I, K, M, N, O, P, Q REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 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 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 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 GLY C 127 REMARK 465 GLY C 128 REMARK 465 ALA C 129 REMARK 465 CYS C 213 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 LEU E 333A REMARK 465 GLY E 333B REMARK 465 SER E 333C REMARK 465 PRO E 333D REMARK 465 PRO E 333E REMARK 465 PRO E 333F REMARK 465 PRO E 333G REMARK 465 GLU E 333H REMARK 465 ALA E 333I REMARK 465 PRO E 333J REMARK 465 ARG E 333K REMARK 465 ALA E 333L REMARK 465 PRO E 333M REMARK 465 PRO E 333N REMARK 465 VAL E 333O REMARK 465 ALA E 333P REMARK 465 THR E 333Q REMARK 465 MET E 333R REMARK 465 VAL E 333S REMARK 465 SER E 333T REMARK 465 LYS E 333U REMARK 465 GLY E 333V REMARK 465 GLU E 333W REMARK 465 GLU E 333X REMARK 465 LEU E 333Y REMARK 465 PHE E 333Z REMARK 465 THR E 334A REMARK 465 GLY E 334B REMARK 465 VAL E 334C REMARK 465 VAL E 334D REMARK 465 PRO E 334E REMARK 465 ILE E 334F REMARK 465 LEU E 334G REMARK 465 VAL E 334H REMARK 465 GLU E 334I REMARK 465 LEU E 334J REMARK 465 ASP E 334K REMARK 465 GLY E 334L REMARK 465 ASP E 334M REMARK 465 VAL E 334N REMARK 465 ASN E 334O REMARK 465 GLY E 334P REMARK 465 HIS E 334Q REMARK 465 LYS E 334R REMARK 465 PHE E 334S REMARK 465 SER E 334T REMARK 465 VAL E 334U REMARK 465 SER E 334V REMARK 465 GLY E 334W REMARK 465 GLU E 334X REMARK 465 GLY E 334Y REMARK 465 GLU E 334Z REMARK 465 GLY E 335A REMARK 465 ASP E 335B REMARK 465 ALA E 335C REMARK 465 THR E 335D REMARK 465 TYR E 335E REMARK 465 GLY E 335F REMARK 465 LYS E 335G REMARK 465 LEU E 335H REMARK 465 THR E 335I REMARK 465 LEU E 335J REMARK 465 LYS E 335K REMARK 465 PHE E 335L REMARK 465 ILE E 335M REMARK 465 CYS E 335N REMARK 465 THR E 335O REMARK 465 THR E 335P REMARK 465 GLY E 335Q REMARK 465 LYS E 335R REMARK 465 LEU E 335S REMARK 465 PRO E 335T REMARK 465 VAL E 335U REMARK 465 PRO E 335V REMARK 465 TRP E 335W REMARK 465 PRO E 335X REMARK 465 THR E 335Y REMARK 465 LEU E 335Z REMARK 465 VAL E 336A REMARK 465 THR E 336B REMARK 465 THR E 336C REMARK 465 LEU E 336D REMARK 465 THR E 336E REMARK 465 TYR E 336F REMARK 465 GLY E 336G REMARK 465 VAL E 336H REMARK 465 GLN E 336I REMARK 465 CYS E 336J REMARK 465 PHE E 336K REMARK 465 SER E 336L REMARK 465 ARG E 336M REMARK 465 TYR E 336N REMARK 465 PRO E 336O REMARK 465 ASP E 336P REMARK 465 HIS E 336Q REMARK 465 MET E 336R REMARK 465 LYS E 336S REMARK 465 GLN E 336T REMARK 465 HIS E 336U REMARK 465 ASP E 336V REMARK 465 PHE E 336W REMARK 465 PHE E 336X REMARK 465 LYS E 336Y REMARK 465 SER E 336Z REMARK 465 ALA E 337A REMARK 465 MET E 337B REMARK 465 PRO E 337C REMARK 465 GLU E 337D REMARK 465 GLY E 337E REMARK 465 TYR E 337F REMARK 465 VAL E 337G REMARK 465 GLN E 337H REMARK 465 GLU E 337I REMARK 465 ARG E 337J REMARK 465 THR E 337K REMARK 465 ILE E 337L REMARK 465 PHE E 337M REMARK 465 PHE E 337N REMARK 465 LYS E 337O REMARK 465 ASP E 337P REMARK 465 ASP E 337Q REMARK 465 GLY E 337R REMARK 465 ASN E 337S REMARK 465 TYR E 337T REMARK 465 LYS E 337U REMARK 465 THR E 337V REMARK 465 ARG E 337W REMARK 465 ALA E 337X REMARK 465 GLU E 337Y REMARK 465 VAL E 337Z REMARK 465 LYS E 338A REMARK 465 PHE E 338B REMARK 465 GLU E 338C REMARK 465 GLY E 338D REMARK 465 ASP E 338E REMARK 465 THR E 338F REMARK 465 LEU E 338G REMARK 465 VAL E 338H REMARK 465 ASN E 338I REMARK 465 ARG E 338J REMARK 465 ILE E 338K REMARK 465 GLU E 338L REMARK 465 LEU E 338M REMARK 465 LYS E 338N REMARK 465 GLY E 338O REMARK 465 ILE E 338P REMARK 465 ASP E 338Q REMARK 465 PHE E 338R REMARK 465 LYS E 338S REMARK 465 GLU E 338T REMARK 465 ASP E 338U REMARK 465 GLY E 338V REMARK 465 ASN E 338W REMARK 465 ILE E 338X REMARK 465 LEU E 338Y REMARK 465 GLY E 338Z REMARK 465 HIS E 339A REMARK 465 LYS E 339B REMARK 465 LEU E 339C REMARK 465 GLU E 339D REMARK 465 TYR E 339E REMARK 465 ASN E 339F REMARK 465 TYR E 339G REMARK 465 ASN E 339H REMARK 465 SER E 339I REMARK 465 HIS E 339J REMARK 465 ASN E 339K REMARK 465 VAL E 339L REMARK 465 TYR E 339M REMARK 465 ILE E 339N REMARK 465 MET E 339O REMARK 465 ALA E 339P REMARK 465 ASP E 339Q REMARK 465 LYS E 339R REMARK 465 GLN E 339S REMARK 465 LYS E 339T REMARK 465 ASN E 339U REMARK 465 GLY E 339V REMARK 465 ILE E 339W REMARK 465 LYS E 339X REMARK 465 VAL E 339Y REMARK 465 ASN E 339Z REMARK 465 PHE E 340A REMARK 465 LYS E 340B REMARK 465 ILE E 340C REMARK 465 ARG E 340D REMARK 465 HIS E 340E REMARK 465 ASN E 340F REMARK 465 ILE E 340G REMARK 465 GLU E 340H REMARK 465 ASP E 340I REMARK 465 GLY E 340J REMARK 465 SER E 340K REMARK 465 VAL E 340L REMARK 465 GLN E 340M REMARK 465 LEU E 340N REMARK 465 ALA E 340O REMARK 465 ASP E 340P REMARK 465 HIS E 340Q REMARK 465 TYR E 340R REMARK 465 GLN E 340S REMARK 465 GLN E 340T REMARK 465 ASN E 340U REMARK 465 THR E 340V REMARK 465 PRO E 340W REMARK 465 ILE E 340X REMARK 465 GLY E 340Y REMARK 465 ASP E 340Z REMARK 465 GLY E 341A REMARK 465 PRO E 341B REMARK 465 VAL E 341C REMARK 465 LEU E 341D REMARK 465 LEU E 341E REMARK 465 PRO E 341F REMARK 465 ASP E 341G REMARK 465 ASN E 341H REMARK 465 HIS E 341I REMARK 465 TYR E 341J REMARK 465 LEU E 341K REMARK 465 SER E 341L REMARK 465 THR E 341M REMARK 465 GLN E 341N REMARK 465 SER E 341O REMARK 465 ALA E 341P REMARK 465 LEU E 341Q REMARK 465 SER E 341R REMARK 465 LYS E 341S REMARK 465 ASP E 341T REMARK 465 PRO E 341U REMARK 465 ASN E 341V REMARK 465 GLU E 341W REMARK 465 LYS E 341X REMARK 465 ARG E 341Y REMARK 465 ASP E 341Z REMARK 465 HIS E 342A REMARK 465 MET E 342B REMARK 465 VAL E 342C REMARK 465 LEU E 342D REMARK 465 LEU E 342E REMARK 465 GLU E 342F REMARK 465 PHE E 342G REMARK 465 VAL E 342H REMARK 465 THR E 342I REMARK 465 ALA E 342J REMARK 465 ALA E 342K REMARK 465 GLY E 342L REMARK 465 ILE E 342M REMARK 465 THR E 342N REMARK 465 LEU E 342O REMARK 465 GLY E 342P REMARK 465 MET E 342Q REMARK 465 ASP E 342R REMARK 465 GLU E 342S REMARK 465 LEU E 342T REMARK 465 TYR E 342U REMARK 465 LYS E 342V REMARK 465 ALA E 342W REMARK 465 PRO E 342X REMARK 465 ARG E 342Y REMARK 465 ALA E 342Z REMARK 465 ALA E 343A REMARK 465 SER E 343B REMARK 465 PRO E 343C REMARK 465 PRO E 343D REMARK 465 ARG E 343E REMARK 465 ARG E 343F REMARK 465 ALA E 343G REMARK 465 SER E 343H REMARK 465 SER E 343I REMARK 465 VAL E 343J REMARK 465 GLY E 343K REMARK 465 LEU E 343L REMARK 465 LEU E 343M REMARK 465 LEU E 343N REMARK 465 ARG E 343O REMARK 465 ALA E 343P REMARK 465 GLU E 343Q REMARK 465 GLU E 343R REMARK 465 LEU E 343S REMARK 465 ILE E 343T REMARK 465 LEU E 343U REMARK 465 LYS E 343V REMARK 465 LYS E 343W REMARK 465 PRO E 343X REMARK 465 ARG E 343Y REMARK 465 SER E 343Z REMARK 465 GLU E 344A REMARK 465 LEU E 344B REMARK 465 VAL E 344C REMARK 465 PHE E 344D REMARK 465 GLU E 344E REMARK 465 GLY E 344F REMARK 465 GLN E 344G REMARK 465 ARG E 344H REMARK 465 HIS E 344I REMARK 465 ARG E 344J REMARK 465 GLN E 344K REMARK 465 GLY E 344L REMARK 465 THR E 344M REMARK 465 TRP E 344N REMARK 465 THR E 344O REMARK 465 ALA E 344P REMARK 465 ALA E 344Q REMARK 465 PHE E 344R REMARK 465 CYS E 344S REMARK 465 GLN E 344T REMARK 465 SER E 344U REMARK 465 LEU E 344V REMARK 465 GLY E 344W REMARK 465 ALA E 344X REMARK 465 ALA E 344Y REMARK 465 ALA E 344Z REMARK 465 PRO E 345A REMARK 465 GLU E 345B REMARK 465 VAL E 345C REMARK 465 THR F 135 REMARK 465 ALA F 136 REMARK 465 LEU F 137 REMARK 465 LYS F 138 REMARK 465 SER F 139 REMARK 465 ASN F 140 REMARK 465 SER F 141 REMARK 465 MET F 142 REMARK 465 SER F 163 REMARK 465 GLY F 164 REMARK 465 ALA F 165 REMARK 465 LEU F 166 REMARK 465 SER F 167 REMARK 465 SER F 168 REMARK 465 THR F 189 REMARK 465 VAL F 190 REMARK 465 PRO F 191 REMARK 465 SER F 192 REMARK 465 SER F 193 REMARK 465 THR F 194 REMARK 465 TRP F 195 REMARK 465 PRO F 196 REMARK 465 SER F 197 REMARK 465 GLN F 198 REMARK 465 THR F 199 REMARK 465 LEU G 124 REMARK 465 ALA G 125 REMARK 465 THR G 126 REMARK 465 GLY G 127 REMARK 465 GLY G 128 REMARK 465 ALA G 129 REMARK 465 CYS G 213 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 LEU H 137 REMARK 465 LYS H 138 REMARK 465 SER H 139 REMARK 465 ASN H 140 REMARK 465 SER H 141 REMARK 465 SER H 163 REMARK 465 GLY H 164 REMARK 465 ALA H 165 REMARK 465 LEU H 166 REMARK 465 SER H 167 REMARK 465 SER H 168 REMARK 465 THR H 189 REMARK 465 VAL H 190 REMARK 465 PRO H 191 REMARK 465 SER H 192 REMARK 465 SER H 193 REMARK 465 THR H 194 REMARK 465 TRP H 195 REMARK 465 PRO H 196 REMARK 465 SER H 197 REMARK 465 GLN H 198 REMARK 465 THR H 199 REMARK 465 GLN H 209 REMARK 465 GLN H 210 REMARK 465 HIS H 211 REMARK 465 GLY J 74 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 GLN L 435 REMARK 465 GLN L 436 REMARK 465 GLY L 437 REMARK 465 GLY I 74 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 ASN A 310 CG OD1 ND2 REMARK 470 ASP A 318 CG OD1 OD2 REMARK 470 ILE A 320 CG1 CG2 CD1 REMARK 470 ILE A 323 CG1 CG2 CD1 REMARK 470 GLU A 371 CG CD OE1 OE2 REMARK 470 LYS A 373 CG CD CE NZ REMARK 470 LYS A 380 CG CD CE NZ REMARK 470 LYS A 387 CG CD CE NZ REMARK 470 GLU A 391 CG CD OE1 OE2 REMARK 470 ASP B 165 CG OD1 OD2 REMARK 470 ASP B 273 CG OD1 OD2 REMARK 470 GLU B 409 CG CD OE1 OE2 REMARK 470 ARG B 411 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 412 CG CD OE1 OE2 REMARK 470 GLU B 426 CG CD OE1 OE2 REMARK 470 GLU B 428 CG CD OE1 OE2 REMARK 470 LYS B 434 CG CD CE NZ REMARK 470 GLU B 435 CG CD OE1 OE2 REMARK 470 ASP B 436 CG OD1 OD2 REMARK 470 GLU C 81 CG CD OE1 OE2 REMARK 470 LEU C 83 CG CD1 CD2 REMARK 470 THR C 121 OG1 CG2 REMARK 470 GLN C 123 CG CD OE1 NE2 REMARK 470 LEU C 124 CG CD1 CD2 REMARK 470 THR C 126 OG1 CG2 REMARK 470 SER C 130 OG REMARK 470 VAL C 131 CG1 CG2 REMARK 470 ARG C 141 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 142 CG OD1 OD2 REMARK 470 ILE C 143 CG1 CG2 CD1 REMARK 470 SER C 144 OG REMARK 470 VAL C 145 CG1 CG2 REMARK 470 LYS C 146 CG CD CE NZ REMARK 470 TRP C 147 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 147 CZ3 CH2 REMARK 470 LYS C 148 CG CD CE NZ REMARK 470 ILE C 149 CG1 CG2 CD1 REMARK 470 ASP C 150 CG OD1 OD2 REMARK 470 THR C 152 OG1 CG2 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 VAL C 158 CG1 CG2 REMARK 470 LEU C 159 CG CD1 CD2 REMARK 470 ASP C 160 CG OD1 OD2 REMARK 470 ASP C 164 CG OD1 OD2 REMARK 470 LYS C 168 CG CD CE NZ REMARK 470 ASP C 169 CG OD1 OD2 REMARK 470 MET C 174 CG SD CE REMARK 470 THR C 177 OG1 CG2 REMARK 470 LEU C 178 CG CD1 CD2 REMARK 470 SER C 179 OG REMARK 470 LEU C 180 CG CD1 CD2 REMARK 470 THR C 181 OG1 CG2 REMARK 470 LYS C 182 CG CD CE NZ REMARK 470 ASP C 184 CG OD1 OD2 REMARK 470 TYR C 185 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU C 186 CG CD OE1 OE2 REMARK 470 SER C 187 OG REMARK 470 HIS C 188 CG ND1 CD2 CE1 NE2 REMARK 470 ASN C 189 CG OD1 ND2 REMARK 470 LEU C 190 CG CD1 CD2 REMARK 470 TYR C 191 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU C 194 CG CD OE1 OE2 REMARK 470 VAL C 195 CG1 CG2 REMARK 470 HIS C 197 CG ND1 CD2 CE1 NE2 REMARK 470 LYS C 198 CG CD CE NZ REMARK 470 THR C 199 OG1 CG2 REMARK 470 SER C 200 OG REMARK 470 SER C 201 OG REMARK 470 SER C 202 OG REMARK 470 VAL C 205 CG1 CG2 REMARK 470 GLU C 212 CG CD OE1 OE2 REMARK 470 GLU D 324 CG CD OE1 OE2 REMARK 470 LYS D 328 CG CD CE NZ REMARK 470 GLU D 332 CG CD OE1 OE2 REMARK 470 GLU D 336 CG CD OE1 OE2 REMARK 470 LYS D 415 CG CD CE NZ REMARK 470 VAL D 418 CG1 CG2 REMARK 470 ASN D 422 CG OD1 ND2 REMARK 470 PHE D 423 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG D 429 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 436 CG CD OE1 OE2 REMARK 470 LYS E 1 CG CD CE NZ REMARK 470 GLU E 177 CG CD OE1 OE2 REMARK 470 THR E 202 OG1 CG2 REMARK 470 ASP E 203 CG OD1 OD2 REMARK 470 GLU E 276 CG CD OE1 OE2 REMARK 470 ARG E 321 CG CD NE CZ NH1 NH2 REMARK 470 HIS E 324 CG ND1 CD2 CE1 NE2 REMARK 470 LEU E 326 CG CD1 CD2 REMARK 470 GLU E 328 CG CD OE1 OE2 REMARK 470 LEU E 329 CG CD1 CD2 REMARK 470 LEU E 330 CG CD1 CD2 REMARK 470 ARG E 332 CG CD NE CZ NH1 NH2 REMARK 470 LEU E 333 CG CD1 CD2 REMARK 470 ARG E 401 CG CD NE CZ NH1 NH2 REMARK 470 CYS E 403 SG REMARK 470 VAL E 404 CG1 CG2 REMARK 470 ASP E 405 CG OD1 OD2 REMARK 470 VAL E 407 CG1 CG2 REMARK 470 ASN E 408 CG OD1 ND2 REMARK 470 PHE E 409 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU E 412 CG CD OE1 OE2 REMARK 470 SER E 413 OG REMARK 470 ARG E 461 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 1 CG CD OE1 OE2 REMARK 470 GLN F 5 CG CD OE1 NE2 REMARK 470 GLU F 6 CG CD OE1 OE2 REMARK 470 LYS F 43 CG CD CE NZ REMARK 470 ASP F 88 CG OD1 OD2 REMARK 470 GLN F 112 CG CD OE1 NE2 REMARK 470 GLU F 122 CG CD OE1 OE2 REMARK 470 THR F 124 OG1 CG2 REMARK 470 SER F 127 OG REMARK 470 VAL F 128 CG1 CG2 REMARK 470 TYR F 129 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU F 131 CG CD1 CD2 REMARK 470 VAL F 143 CG1 CG2 REMARK 470 THR F 144 OG1 CG2 REMARK 470 LEU F 145 CG CD1 CD2 REMARK 470 VAL F 149 CG1 CG2 REMARK 470 GLU F 155 CG CD OE1 OE2 REMARK 470 THR F 158 OG1 CG2 REMARK 470 VAL F 176 CG1 CG2 REMARK 470 GLN F 178 CG CD OE1 NE2 REMARK 470 GLN F 210 CG CD OE1 NE2 REMARK 470 HIS F 211 CG ND1 CD2 CE1 NE2 REMARK 470 GLN F 212 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 CYS F 219 SG REMARK 470 LYS G 45 CG CD CE NZ REMARK 470 ASP G 70 CG OD1 OD2 REMARK 470 GLU G 81 CG CD OE1 OE2 REMARK 470 LEU G 83 CG CD1 CD2 REMARK 470 GLU G 104 CG CD OE1 OE2 REMARK 470 LYS G 106 CG CD CE NZ REMARK 470 ASP G 109 CG OD1 OD2 REMARK 470 THR G 113 OG1 CG2 REMARK 470 THR G 121 OG1 CG2 REMARK 470 GLU G 122 CG CD OE1 OE2 REMARK 470 GLN G 123 CG CD OE1 NE2 REMARK 470 SER G 130 OG REMARK 470 VAL G 131 CG1 CG2 REMARK 470 LEU G 134 CG CD1 CD2 REMARK 470 MET G 135 CG SD CE REMARK 470 ASN G 137 CG OD1 ND2 REMARK 470 ARG G 141 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 142 CG OD1 OD2 REMARK 470 ILE G 143 CG1 CG2 CD1 REMARK 470 SER G 144 OG REMARK 470 VAL G 145 CG1 CG2 REMARK 470 LYS G 146 CG CD CE NZ REMARK 470 TRP G 147 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP G 147 CZ3 CH2 REMARK 470 LYS G 148 CG CD CE NZ REMARK 470 ILE G 149 CG1 CG2 CD1 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 VAL G 158 CG1 CG2 REMARK 470 LEU G 159 CG CD1 CD2 REMARK 470 ASP G 160 CG OD1 OD2 REMARK 470 ASP G 164 CG OD1 OD2 REMARK 470 LYS G 168 CG CD CE NZ REMARK 470 ASP G 169 CG OD1 OD2 REMARK 470 MET G 174 CG SD CE REMARK 470 THR G 177 OG1 CG2 REMARK 470 LEU G 178 CG CD1 CD2 REMARK 470 SER G 179 OG REMARK 470 LEU G 180 CG CD1 CD2 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 TYR G 185 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU G 186 CG CD OE1 OE2 REMARK 470 SER G 187 OG REMARK 470 HIS G 188 CG ND1 CD2 CE1 NE2 REMARK 470 ASN G 189 CG OD1 ND2 REMARK 470 LEU G 190 CG CD1 CD2 REMARK 470 TYR G 191 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU G 194 CG CD OE1 OE2 REMARK 470 VAL G 195 CG1 CG2 REMARK 470 HIS G 197 CG ND1 CD2 CE1 NE2 REMARK 470 LYS G 198 CG CD CE NZ REMARK 470 THR G 199 OG1 CG2 REMARK 470 SER G 200 OG REMARK 470 SER G 201 OG REMARK 470 SER G 202 OG REMARK 470 VAL G 205 CG1 CG2 REMARK 470 LYS G 206 CG CD CE NZ REMARK 470 ASN G 209 CG OD1 ND2 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 GLN H 3 CG CD OE1 NE2 REMARK 470 GLU H 6 CG CD OE1 OE2 REMARK 470 GLN H 13 CG CD OE1 NE2 REMARK 470 GLU H 16 CG CD OE1 OE2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 GLN H 86 CG CD OE1 NE2 REMARK 470 THR H 87 OG1 CG2 REMARK 470 ASP H 88 CG OD1 OD2 REMARK 470 GLN H 112 CG CD OE1 NE2 REMARK 470 GLU H 122 CG CD OE1 OE2 REMARK 470 THR H 124 OG1 CG2 REMARK 470 SER H 127 OG REMARK 470 VAL H 128 CG1 CG2 REMARK 470 TYR H 129 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU H 131 CG CD1 CD2 REMARK 470 MET H 142 CG SD CE REMARK 470 VAL H 143 CG1 CG2 REMARK 470 THR H 144 OG1 CG2 REMARK 470 LEU H 145 CG CD1 CD2 REMARK 470 LEU H 148 CG CD1 CD2 REMARK 470 VAL H 149 CG1 CG2 REMARK 470 LYS H 150 CG CD CE NZ REMARK 470 GLU H 155 CG CD OE1 OE2 REMARK 470 THR H 158 OG1 CG2 REMARK 470 HIS H 171 CG ND1 CD2 CE1 NE2 REMARK 470 VAL H 176 CG1 CG2 REMARK 470 GLN H 178 CG CD OE1 NE2 REMARK 470 THR H 185 OG1 CG2 REMARK 470 VAL H 188 CG1 CG2 REMARK 470 ASN H 203 CG OD1 ND2 REMARK 470 GLN H 212 CG CD OE1 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 470 LEU H 218 CG CD1 CD2 REMARK 470 CYS H 219 SG REMARK 470 ILE J 1 CG1 CG2 CD1 REMARK 470 VAL J 2 CG1 CG2 REMARK 470 THR J 15 OG1 CG2 REMARK 470 GLU J 20 CG CD OE1 OE2 REMARK 470 THR J 47 OG1 CG2 REMARK 470 SER J 50 OG REMARK 470 LYS J 51 CG CD CE NZ REMARK 470 LYS J 52 CG CD CE NZ REMARK 470 THR J 62 OG1 CG2 REMARK 470 LYS J 64 CG CD CE NZ REMARK 470 ARG J 72 CG CD NE CZ NH1 NH2 REMARK 470 VAL L 307 CG1 CG2 REMARK 470 LYS L 314 CG CD CE NZ REMARK 470 ILE L 323 CG1 CG2 CD1 REMARK 470 MET L 324 CG SD CE REMARK 470 LYS L 373 CG CD CE NZ REMARK 470 ILE L 376 CG1 CG2 CD1 REMARK 470 LYS L 387 CG CD CE NZ REMARK 470 GLU L 391 CG CD OE1 OE2 REMARK 470 ILE I 1 CG1 CG2 CD1 REMARK 470 VAL I 2 CG1 CG2 REMARK 470 ILE I 11 CG1 CG2 CD1 REMARK 470 SER I 12 OG REMARK 470 VAL I 14 CG1 CG2 REMARK 470 THR I 15 OG1 CG2 REMARK 470 GLU I 20 CG CD OE1 OE2 REMARK 470 ASN I 21 CG OD1 ND2 REMARK 470 LYS I 26 CG CD CE NZ REMARK 470 SER I 34 OG REMARK 470 SER I 35 OG REMARK 470 LYS I 38 CG CD CE NZ REMARK 470 GLU I 41 CG CD OE1 OE2 REMARK 470 THR I 47 OG1 CG2 REMARK 470 SER I 50 OG REMARK 470 LYS I 51 CG CD CE NZ REMARK 470 LYS I 52 CG CD CE NZ REMARK 470 TYR I 54 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU I 55 CG CD OE1 OE2 REMARK 470 GLU I 56 CG CD OE1 OE2 REMARK 470 SER I 61 OG REMARK 470 THR I 62 OG1 CG2 REMARK 470 ASP I 63 CG OD1 OD2 REMARK 470 LYS I 64 CG CD CE NZ REMARK 470 ARG I 72 CG CD NE CZ NH1 NH2 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 43.85 -81.08 REMARK 500 ASP A 89 58.48 -96.41 REMARK 500 ASN A 94 35.73 -97.24 REMARK 500 ASP A 97 18.75 -145.49 REMARK 500 VAL A 218 -55.35 -128.05 REMARK 500 PRO B 21 49.93 -85.17 REMARK 500 LEU B 65 38.28 -96.78 REMARK 500 VAL B 229 -55.99 -126.98 REMARK 500 ARG B 336 19.55 59.43 REMARK 500 THR C 51 -11.96 68.86 REMARK 500 SER C 60 1.76 -67.46 REMARK 500 TYR C 91 27.45 -142.23 REMARK 500 SER C 170 7.85 58.85 REMARK 500 ASN D 96 30.29 -92.05 REMARK 500 ARG D 195 57.69 -151.02 REMARK 500 ILE D 232 -53.18 -127.03 REMARK 500 ALA D 280 49.58 -80.14 REMARK 500 GLU D 332 -56.50 -121.04 REMARK 500 ASP D 492 58.10 -97.93 REMARK 500 ASN E 94 33.90 -99.00 REMARK 500 ARG E 125 75.67 -102.35 REMARK 500 ASN E 141 65.16 -102.83 REMARK 500 ASN E 170 49.28 -86.27 REMARK 500 CYS E 190 53.99 -147.84 REMARK 500 ILE E 227 -54.44 -127.57 REMARK 500 GLU E 328 -50.78 -122.72 REMARK 500 ASN E 460 36.56 -98.58 REMARK 500 SER F 15 -2.27 68.90 REMARK 500 ARG F 102 -118.76 52.89 REMARK 500 GLN F 209 18.77 -141.55 REMARK 500 THR G 51 -12.42 68.42 REMARK 500 ASN G 52 -37.49 -134.39 REMARK 500 TYR G 91 34.80 -141.91 REMARK 500 ARG G 154 171.84 63.25 REMARK 500 SER G 170 10.84 59.33 REMARK 500 ARG H 102 -122.49 50.85 REMARK 500 ASN J 21 -34.32 -134.04 REMARK 500 SER J 35 -36.80 -131.84 REMARK 500 ASP L 89 57.11 -93.49 REMARK 500 ASN L 94 33.22 -92.47 REMARK 500 ASP L 97 23.08 -143.49 REMARK 500 LYS L 125 70.14 -100.98 REMARK 500 VAL L 218 -54.71 -124.60 REMARK 500 HIS L 306 170.83 68.20 REMARK 500 ASP L 318 -61.48 -94.38 REMARK 500 ASN I 21 -33.08 -134.25 REMARK 500 SER I 35 -30.90 -133.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-51568 RELATED DB: EMDB REMARK 900 HUMAN ADULT MUSCLE NACHR IN RESTING STATE IN DETERGENT WITH ALPHA- REMARK 900 BUNGAROTOXIN DBREF 9GU0 A 1 437 UNP P02708 ACHA_HUMAN 21 457 DBREF 9GU0 B 1 478 UNP P11230 ACHB_HUMAN 24 501 DBREF 9GU0 C 1 213 PDB 9GU0 9GU0 1 213 DBREF 9GU0 D 1 496 UNP Q07001 ACHD_HUMAN 22 517 DBREF 9GU0 E 1 333K UNP Q04844 ACHE_HUMAN 21 364 DBREF 9GU0 E 333T 342V UNP P42212 GFP_AEQVI 2 238 DBREF 9GU0 E 342W 473 UNP Q04844 ACHE_HUMAN 362 493 DBREF 9GU0 F 1 219 PDB 9GU0 9GU0 1 219 DBREF 9GU0 G 1 213 PDB 9GU0 9GU0 1 213 DBREF 9GU0 H 1 219 PDB 9GU0 9GU0 1 219 DBREF 9GU0 J 1 74 UNP P60615 3L21A_BUNMU 22 95 DBREF 9GU0 L 1 437 UNP P02708 ACHA_HUMAN 21 457 DBREF 9GU0 I 1 74 UNP P60615 3L21A_BUNMU 22 95 SEQADV 9GU0 ALA E 333L UNP Q04844 LINKER SEQADV 9GU0 PRO E 333M UNP Q04844 LINKER SEQADV 9GU0 PRO E 333N UNP Q04844 LINKER SEQADV 9GU0 VAL E 333O UNP Q04844 LINKER SEQADV 9GU0 ALA E 333P UNP Q04844 LINKER SEQADV 9GU0 THR E 333Q UNP Q04844 LINKER SEQADV 9GU0 MET E 333R UNP Q04844 LINKER SEQADV 9GU0 VAL E 333S UNP Q04844 LINKER SEQADV 9GU0 LEU E 336D UNP P42212 PHE 64 CONFLICT SEQADV 9GU0 THR E 336E UNP P42212 SER 65 CONFLICT SEQADV 9GU0 LEU E 342O 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 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 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 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 SEQRES 1 J 74 ILE VAL CYS HIS THR THR ALA THR SER PRO ILE SER ALA SEQRES 2 J 74 VAL THR CYS PRO PRO GLY GLU ASN LEU CYS TYR ARG LYS SEQRES 3 J 74 MET TRP CYS ASP ALA PHE CYS SER SER ARG GLY LYS VAL SEQRES 4 J 74 VAL GLU LEU GLY CYS ALA ALA THR CYS PRO SER LYS LYS SEQRES 5 J 74 PRO TYR GLU GLU VAL THR CYS CYS SER THR ASP LYS CYS SEQRES 6 J 74 ASN PRO HIS PRO LYS GLN ARG PRO GLY 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 I 74 ILE VAL CYS HIS THR THR ALA THR SER PRO ILE SER ALA SEQRES 2 I 74 VAL THR CYS PRO PRO GLY GLU ASN LEU CYS TYR ARG LYS SEQRES 3 I 74 MET TRP CYS ASP ALA PHE CYS SER SER ARG GLY LYS VAL SEQRES 4 I 74 VAL GLU LEU GLY CYS ALA ALA THR CYS PRO SER LYS LYS SEQRES 5 I 74 PRO TYR GLU GLU VAL THR CYS CYS SER THR ASP LYS CYS SEQRES 6 I 74 ASN PRO HIS PRO LYS GLN ARG PRO GLY HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET MAN K 4 11 HET MAN K 5 11 HET MAN K 6 11 HET MAN K 7 11 HET NAG M 1 14 HET NAG M 2 14 HET BMA M 3 11 HET MAN M 4 11 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET MAN N 4 11 HET NAG N 5 14 HET MAN N 6 11 HET MAN N 7 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 NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET MAN Q 4 11 HET MAN Q 5 11 HET MAN Q 6 11 HET MAN Q 7 11 HET NAG D 501 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE 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 12 NAG 14(C8 H15 N O6) FORMUL 12 BMA 5(C6 H12 O6) FORMUL 12 MAN 12(C6 H12 O6) 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 232 1 22 HELIX 5 AA5 PHE A 233 LEU A 235 5 3 HELIX 6 AA6 PRO A 236 GLY A 240 5 5 HELIX 7 AA7 GLU A 241 ILE A 264 1 24 HELIX 8 AA8 PRO A 272 HIS A 300 1 29 HELIX 9 AA9 PRO A 309 ILE A 317 1 9 HELIX 10 AB1 ASP A 318 ILE A 323 1 6 HELIX 11 AB2 GLU A 371 GLN A 435 1 65 HELIX 12 AB3 GLU B 2 PHE B 12 1 11 HELIX 13 AB4 TYR B 63 SER B 66 5 4 HELIX 14 AB5 ASP B 68 HIS B 72 5 5 HELIX 15 AB6 THR B 81 VAL B 85 5 5 HELIX 16 AB7 GLN B 131 PHE B 135 5 5 HELIX 17 AB8 PRO B 222 VAL B 229 1 8 HELIX 18 AB9 VAL B 229 VAL B 243 1 15 HELIX 19 AC1 PHE B 244 LEU B 246 5 3 HELIX 20 AC2 PRO B 247 GLY B 251 5 5 HELIX 21 AC3 GLU B 252 ASP B 273 1 22 HELIX 22 AC4 PRO B 283 HIS B 311 1 29 HELIX 23 AC5 PRO B 320 LEU B 335 1 16 HELIX 24 AC6 GLU B 409 HIS B 470 1 62 HELIX 25 AC7 HIS C 79 LEU C 83 5 5 HELIX 26 AC8 SER C 120 THR C 126 1 7 HELIX 27 AC9 THR C 181 HIS C 188 1 8 HELIX 28 AD1 ASN D 2 GLN D 13 1 12 HELIX 29 AD2 ASN D 65 LYS D 68 5 4 HELIX 30 AD3 ASN D 70 GLY D 75 5 6 HELIX 31 AD4 PRO D 225 ILE D 232 1 8 HELIX 32 AD5 ILE D 232 MET D 242 1 11 HELIX 33 AD6 ASN D 244 LEU D 249 1 6 HELIX 34 AD7 PRO D 250 GLY D 254 5 5 HELIX 35 AD8 GLU D 255 LYS D 276 1 22 HELIX 36 AD9 PRO D 286 PHE D 314 1 29 HELIX 37 AE1 SER D 323 GLU D 332 1 10 HELIX 38 AE2 GLU D 332 LEU D 338 1 7 HELIX 39 AE3 PRO D 416 TYR D 473 1 58 HELIX 40 AE4 ASN E 2 ASN E 13 1 12 HELIX 41 AE5 TYR E 63 ASN E 66 5 4 HELIX 42 AE6 SER E 68 GLY E 73 5 6 HELIX 43 AE7 PRO E 81 VAL E 85 5 5 HELIX 44 AE8 GLU E 131 PHE E 135 5 5 HELIX 45 AE9 PRO E 220 ILE E 227 1 8 HELIX 46 AF1 ILE E 227 LEU E 239 1 13 HELIX 47 AF2 LEU E 240 LEU E 244 5 5 HELIX 48 AF3 GLN E 251 ILE E 274 1 24 HELIX 49 AF4 PRO E 282 GLN E 310 1 29 HELIX 50 AF5 SER E 319 GLU E 328 1 10 HELIX 51 AF6 GLU E 328 LEU E 333 1 6 HELIX 52 AF7 CYS E 402 ASN E 460 1 59 HELIX 53 AF8 GLN F 86 ASP F 89 5 4 HELIX 54 AF9 HIS G 79 LEU G 83 5 5 HELIX 55 AG1 ALA G 183 HIS G 188 5 6 HELIX 56 AG2 GLN H 86 ASP H 89 5 4 HELIX 57 AG3 ASP J 30 SER J 35 5 6 HELIX 58 AG4 GLU L 2 LYS L 13 1 12 HELIX 59 AG5 TYR L 63 LYS L 66 5 4 HELIX 60 AG6 ASN L 68 GLY L 73 5 6 HELIX 61 AG7 PRO L 211 VAL L 218 1 8 HELIX 62 AG8 VAL L 218 VAL L 232 1 15 HELIX 63 AG9 PRO L 236 SER L 239 5 4 HELIX 64 AH1 GLY L 240 ILE L 264 1 25 HELIX 65 AH2 PRO L 272 HIS L 300 1 29 HELIX 66 AH3 SER L 302 HIS L 306 5 5 HELIX 67 AH4 PRO L 309 ILE L 317 1 9 HELIX 68 AH5 ASP L 318 ILE L 323 1 6 HELIX 69 AH6 GLU L 371 ASN L 434 1 64 SHEET 1 AA1 5 LYS A 77 ILE A 80 0 SHEET 2 AA1 5 VAL A 108 GLN A 111 -1 O LEU A 110 N ILE A 78 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 GLN A 58 O TRP A 118 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 ILE A 80 0 SHEET 2 AA2 6 VAL A 108 GLN A 111 -1 O LEU A 110 N ILE A 78 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 GLN A 58 O TRP A 118 SHEET 5 AA2 6 VAL A 29 ASP A 44 -1 N ASP A 44 O ILE A 49 SHEET 6 AA2 6 VAL A 156 PRO A 160 1 O ALA A 157 N VAL A 29 SHEET 1 AA3 7 LEU A 90 LEU A 92 0 SHEET 2 AA3 7 GLU A 139 THR A 148 -1 O GLY A 147 N VAL A 91 SHEET 3 AA3 7 CYS A 193 ARG A 209 -1 O ILE A 201 N LEU A 146 SHEET 4 AA3 7 TRP A 176 TYR A 190 -1 N HIS A 186 O ASP A 200 SHEET 5 AA3 7 VAL I 39 ALA I 45 -1 O VAL I 40 N THR A 189 SHEET 6 AA3 7 LEU I 22 TRP I 28 -1 N TRP I 28 O VAL I 39 SHEET 7 AA3 7 GLU I 56 CYS I 60 -1 O THR I 58 N ARG I 25 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 LEU B 58 O TRP B 118 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 LEU B 58 O TRP B 118 SHEET 5 AA5 6 VAL B 29 ASN B 44 -1 N ASN B 44 O GLU B 49 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 4 ILE C 4 SER C 7 0 SHEET 2 AA8 4 VAL C 19 GLY C 25 -1 O LYS C 24 N THR C 5 SHEET 3 AA8 4 ASP C 70 ILE C 75 -1 O LEU C 73 N LEU C 21 SHEET 4 AA8 4 PHE C 62 SER C 67 -1 N SER C 65 O THR C 72 SHEET 1 AA9 6 LEU C 10 ALA C 13 0 SHEET 2 AA9 6 THR C 101 LEU C 105 1 O GLU C 104 N ALA C 13 SHEET 3 AA9 6 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 101 SHEET 4 AA9 6 LEU C 33 GLN C 38 -1 N ALA C 34 O TYR C 89 SHEET 5 AA9 6 LYS C 45 TYR C 49 -1 O LYS C 45 N GLN C 37 SHEET 6 AA9 6 SER C 53 LEU C 54 -1 O SER C 53 N TYR C 49 SHEET 1 AB1 4 LEU C 10 ALA C 13 0 SHEET 2 AB1 4 THR C 101 LEU C 105 1 O GLU C 104 N ALA C 13 SHEET 3 AB1 4 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 101 SHEET 4 AB1 4 THR C 96 PHE C 97 -1 O THR C 96 N GLN C 90 SHEET 1 AB2 4 THR C 113 PHE C 117 0 SHEET 2 AB2 4 VAL C 131 PHE C 138 -1 O ASN C 136 N THR C 113 SHEET 3 AB2 4 TYR C 172 LEU C 178 -1 O SER C 176 N CYS C 133 SHEET 4 AB2 4 LEU C 159 VAL C 162 -1 N SER C 161 O SER C 175 SHEET 1 AB3 4 THR C 152 GLU C 153 0 SHEET 2 AB3 4 ILE C 143 ILE C 149 -1 N ILE C 149 O THR C 152 SHEET 3 AB3 4 LEU C 190 HIS C 197 -1 O GLU C 194 N LYS C 146 SHEET 4 AB3 4 VAL C 204 ASN C 209 -1 O LYS C 206 N CYS C 193 SHEET 1 AB4 6 VAL D 79 LEU D 82 0 SHEET 2 AB4 6 VAL D 110 TYR D 113 -1 O VAL D 112 N LEU D 80 SHEET 3 AB4 6 PHE D 117 TRP D 120 -1 O TYR D 119 N LEU D 111 SHEET 4 AB4 6 THR D 51 THR D 63 -1 N HIS D 60 O TRP D 120 SHEET 5 AB4 6 VAL D 31 LYS D 46 -1 N ALA D 34 O GLY D 61 SHEET 6 AB4 6 ILE D 158 LEU D 162 1 O THR D 159 N VAL D 33 SHEET 1 AB5 4 PRO D 123 SER D 129 0 SHEET 2 AB5 4 THR D 51 THR D 63 -1 N VAL D 56 O ALA D 124 SHEET 3 AB5 4 VAL D 31 LYS D 46 -1 N ALA D 34 O GLY D 61 SHEET 4 AB5 4 ILE D 178 ILE D 179 1 O ILE D 178 N LEU D 39 SHEET 1 AB6 4 ILE D 92 LEU D 94 0 SHEET 2 AB6 4 TRP D 141 SER D 150 -1 O SER D 149 N VAL D 93 SHEET 3 AB6 4 GLN D 213 ARG D 223 -1 O PHE D 217 N LEU D 146 SHEET 4 AB6 4 TRP D 190 HIS D 194 -1 N VAL D 193 O ILE D 220 SHEET 1 AB7 4 ILE D 92 LEU D 94 0 SHEET 2 AB7 4 TRP D 141 SER D 150 -1 O SER D 149 N VAL D 93 SHEET 3 AB7 4 GLN D 213 ARG D 223 -1 O PHE D 217 N LEU D 146 SHEET 4 AB7 4 ALA D 197 VAL D 201 -1 N ASN D 200 O ASP D 214 SHEET 1 AB8 2 GLN D 164 LYS D 167 0 SHEET 2 AB8 2 ARG D 170 PRO D 173 -1 O ARG D 170 N LYS D 167 SHEET 1 AB9 6 THR E 77 VAL E 80 0 SHEET 2 AB9 6 VAL E 108 TYR E 111 -1 O VAL E 110 N LEU E 78 SHEET 3 AB9 6 SER E 115 TRP E 118 -1 O SER E 115 N TYR E 111 SHEET 4 AB9 6 THR E 49 GLN E 61 -1 N ILE E 58 O TRP E 118 SHEET 5 AB9 6 VAL E 29 ASN E 44 -1 N LYS E 34 O GLY E 57 SHEET 6 AB9 6 VAL E 156 PHE E 160 1 O GLU E 157 N ILE E 31 SHEET 1 AC1 4 PRO E 121 VAL E 127 0 SHEET 2 AC1 4 THR E 49 GLN E 61 -1 N LEU E 50 O SER E 126 SHEET 3 AC1 4 VAL E 29 ASN E 44 -1 N LYS E 34 O GLY E 57 SHEET 4 AC1 4 ASP E 173 ILE E 174 1 O ASP E 173 N LEU E 37 SHEET 1 AC2 4 ILE E 90 LEU E 92 0 SHEET 2 AC2 4 TRP E 139 SER E 148 -1 O ARG E 147 N VAL E 91 SHEET 3 AC2 4 GLU E 207 ARG E 218 -1 O VAL E 210 N PHE E 146 SHEET 4 AC2 4 TRP E 185 PHE E 189 -1 N ALA E 186 O ARG E 217 SHEET 1 AC3 4 ILE E 90 LEU E 92 0 SHEET 2 AC3 4 TRP E 139 SER E 148 -1 O ARG E 147 N VAL E 91 SHEET 3 AC3 4 GLU E 207 ARG E 218 -1 O VAL E 210 N PHE E 146 SHEET 4 AC3 4 GLY E 192 HIS E 197 -1 N ARG E 195 O ASP E 209 SHEET 1 AC4 4 GLN F 3 SER F 7 0 SHEET 2 AC4 4 LEU F 18 SER F 25 -1 O THR F 23 N GLN F 5 SHEET 3 AC4 4 GLN F 77 MET F 82 -1 O MET F 82 N LEU F 18 SHEET 4 AC4 4 LEU F 67 ASP F 72 -1 N SER F 70 O PHE F 79 SHEET 1 AC5 6 LEU F 11 VAL F 12 0 SHEET 2 AC5 6 THR F 114 VAL F 118 1 O THR F 117 N VAL F 12 SHEET 3 AC5 6 GLY F 91 ILE F 101 -1 N GLY F 91 O VAL F 116 SHEET 4 AC5 6 SER F 33 PRO F 40 -1 N LEU F 37 O TYR F 94 SHEET 5 AC5 6 GLU F 46 MET F 51 -1 O MET F 51 N VAL F 34 SHEET 6 AC5 6 THR F 57 TYR F 59 -1 O VAL F 58 N ARG F 50 SHEET 1 AC6 4 LEU F 11 VAL F 12 0 SHEET 2 AC6 4 THR F 114 VAL F 118 1 O THR F 117 N VAL F 12 SHEET 3 AC6 4 GLY F 91 ILE F 101 -1 N GLY F 91 O VAL F 116 SHEET 4 AC6 4 ILE F 104 TRP F 110 -1 O ALA F 108 N ARG F 97 SHEET 1 AC7 4 TYR F 129 LEU F 131 0 SHEET 2 AC7 4 LEU F 145 TYR F 152 -1 O LEU F 148 N TYR F 129 SHEET 3 AC7 4 TYR F 182 VAL F 188 -1 O SER F 186 N CYS F 147 SHEET 4 AC7 4 HIS F 171 THR F 172 -1 N HIS F 171 O SER F 187 SHEET 1 AC8 4 TYR F 129 LEU F 131 0 SHEET 2 AC8 4 LEU F 145 TYR F 152 -1 O LEU F 148 N TYR F 129 SHEET 3 AC8 4 TYR F 182 VAL F 188 -1 O SER F 186 N CYS F 147 SHEET 4 AC8 4 VAL F 176 LEU F 177 -1 N VAL F 176 O THR F 183 SHEET 1 AC9 3 THR F 158 TRP F 161 0 SHEET 2 AC9 3 THR F 201 HIS F 206 -1 O ALA F 205 N THR F 158 SHEET 3 AC9 3 HIS F 211 ARG F 216 -1 O ARG F 213 N VAL F 204 SHEET 1 AD1 4 ILE G 4 SER G 7 0 SHEET 2 AD1 4 VAL G 19 GLY G 25 -1 O LYS G 24 N THR G 5 SHEET 3 AD1 4 ASP G 70 ILE G 75 -1 O LEU G 73 N LEU G 21 SHEET 4 AD1 4 PHE G 62 SER G 67 -1 N SER G 65 O THR G 72 SHEET 1 AD2 6 LEU G 10 ALA G 13 0 SHEET 2 AD2 6 THR G 101 LEU G 105 1 O GLU G 104 N LEU G 11 SHEET 3 AD2 6 THR G 85 GLN G 90 -1 N TYR G 86 O THR G 101 SHEET 4 AD2 6 LEU G 33 GLN G 38 -1 N ALA G 34 O TYR G 89 SHEET 5 AD2 6 LYS G 45 TYR G 49 -1 O LYS G 45 N GLN G 37 SHEET 6 AD2 6 SER G 53 LEU G 54 -1 O SER G 53 N TYR G 49 SHEET 1 AD3 4 LEU G 10 ALA G 13 0 SHEET 2 AD3 4 THR G 101 LEU G 105 1 O GLU G 104 N LEU G 11 SHEET 3 AD3 4 THR G 85 GLN G 90 -1 N TYR G 86 O THR G 101 SHEET 4 AD3 4 THR G 96 PHE G 97 -1 O THR G 96 N GLN G 90 SHEET 1 AD4 4 SER G 115 PHE G 117 0 SHEET 2 AD4 4 VAL G 131 PHE G 138 -1 O LEU G 134 N SER G 115 SHEET 3 AD4 4 TYR G 172 THR G 181 -1 O SER G 176 N CYS G 133 SHEET 4 AD4 4 LEU G 159 VAL G 162 -1 N SER G 161 O SER G 175 SHEET 1 AD5 4 THR G 152 GLU G 153 0 SHEET 2 AD5 4 SER G 144 ILE G 149 -1 N ILE G 149 O THR G 152 SHEET 3 AD5 4 TYR G 191 HIS G 197 -1 O GLU G 194 N LYS G 146 SHEET 4 AD5 4 SER G 200 PHE G 208 -1 O LYS G 206 N CYS G 193 SHEET 1 AD6 4 GLN H 3 SER H 7 0 SHEET 2 AD6 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AD6 4 GLN H 77 MET H 82 -1 O VAL H 78 N CYS H 22 SHEET 4 AD6 4 LEU H 67 ASP H 72 -1 N SER H 70 O PHE H 79 SHEET 1 AD7 6 LEU H 11 VAL H 12 0 SHEET 2 AD7 6 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AD7 6 GLY H 91 ILE H 101 -1 N GLY H 91 O VAL H 116 SHEET 4 AD7 6 VAL H 34 PRO H 40 -1 N LEU H 37 O TYR H 94 SHEET 5 AD7 6 GLU H 46 MET H 51 -1 O MET H 51 N VAL H 34 SHEET 6 AD7 6 THR H 57 TYR H 59 -1 O VAL H 58 N ARG H 50 SHEET 1 AD8 4 LEU H 11 VAL H 12 0 SHEET 2 AD8 4 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AD8 4 GLY H 91 ILE H 101 -1 N GLY H 91 O VAL H 116 SHEET 4 AD8 4 ILE H 104 TRP H 110 -1 O ALA H 108 N ARG H 97 SHEET 1 AD9 4 SER H 127 PRO H 130 0 SHEET 2 AD9 4 LEU H 145 TYR H 152 -1 O LYS H 150 N SER H 127 SHEET 3 AD9 4 TYR H 182 VAL H 188 -1 O LEU H 184 N VAL H 149 SHEET 4 AD9 4 HIS H 171 THR H 172 -1 N HIS H 171 O SER H 187 SHEET 1 AE1 4 SER H 127 PRO H 130 0 SHEET 2 AE1 4 LEU H 145 TYR H 152 -1 O LYS H 150 N SER H 127 SHEET 3 AE1 4 TYR H 182 VAL H 188 -1 O LEU H 184 N VAL H 149 SHEET 4 AE1 4 VAL H 176 LEU H 177 -1 N VAL H 176 O THR H 183 SHEET 1 AE2 3 THR H 158 TRP H 161 0 SHEET 2 AE2 3 THR H 201 ALA H 205 -1 O ASN H 203 N THR H 160 SHEET 3 AE2 3 ARG H 213 ARG H 216 -1 O THR H 215 N CYS H 202 SHEET 1 AE3 2 VAL J 2 THR J 5 0 SHEET 2 AE3 2 SER J 12 THR J 15 -1 O VAL J 14 N CYS J 3 SHEET 1 AE4 7 GLU J 55 CYS J 60 0 SHEET 2 AE4 7 LEU J 22 TRP J 28 -1 N MET J 27 O GLU J 56 SHEET 3 AE4 7 VAL J 39 ALA J 45 -1 O VAL J 39 N TRP J 28 SHEET 4 AE4 7 TRP L 176 TYR L 190 -1 O THR L 189 N VAL J 40 SHEET 5 AE4 7 CYS L 193 ARG L 209 -1 O VAL L 206 N GLU L 180 SHEET 6 AE4 7 GLU L 139 THR L 148 -1 N MET L 144 O TYR L 203 SHEET 7 AE4 7 LEU L 90 LEU L 92 -1 N VAL L 91 O GLY L 147 SHEET 1 AE5 5 LYS L 77 PRO L 81 0 SHEET 2 AE5 5 LYS L 107 GLN L 111 -1 O LEU L 110 N ILE L 78 SHEET 3 AE5 5 HIS L 115 TRP L 118 -1 O THR L 117 N LEU L 109 SHEET 4 AE5 5 ILE L 49 VAL L 61 -1 N GLN L 58 O TRP L 118 SHEET 5 AE5 5 PRO L 121 TYR L 127 -1 O ALA L 122 N VAL L 54 SHEET 1 AE6 6 LYS L 77 PRO L 81 0 SHEET 2 AE6 6 LYS L 107 GLN L 111 -1 O LEU L 110 N ILE L 78 SHEET 3 AE6 6 HIS L 115 TRP L 118 -1 O THR L 117 N LEU L 109 SHEET 4 AE6 6 ILE L 49 VAL L 61 -1 N GLN L 58 O TRP L 118 SHEET 5 AE6 6 VAL L 29 ASP L 44 -1 N ASP L 44 O ILE L 49 SHEET 6 AE6 6 VAL L 156 PRO L 160 1 O ALA L 157 N VAL L 31 SHEET 1 AE7 2 VAL I 2 THR I 5 0 SHEET 2 AE7 2 SER I 12 THR I 15 -1 O VAL I 14 N CYS I 3 SSBOND 1 CYS A 128 CYS A 142 1555 1555 2.03 SSBOND 2 CYS A 192 CYS A 193 1555 1555 2.04 SSBOND 3 CYS B 128 CYS B 142 1555 1555 2.03 SSBOND 4 CYS C 23 CYS C 88 1555 1555 2.04 SSBOND 5 CYS C 133 CYS C 193 1555 1555 2.03 SSBOND 6 CYS D 130 CYS D 144 1555 1555 2.03 SSBOND 7 CYS E 128 CYS E 142 1555 1555 2.03 SSBOND 8 CYS E 190 CYS E 470 1555 1555 2.03 SSBOND 9 CYS F 22 CYS F 95 1555 1555 2.03 SSBOND 10 CYS F 147 CYS F 202 1555 1555 2.03 SSBOND 11 CYS G 23 CYS G 88 1555 1555 2.03 SSBOND 12 CYS G 133 CYS G 193 1555 1555 2.03 SSBOND 13 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 14 CYS H 147 CYS H 202 1555 1555 2.03 SSBOND 15 CYS J 3 CYS J 23 1555 1555 2.03 SSBOND 16 CYS J 16 CYS J 44 1555 1555 2.03 SSBOND 17 CYS J 29 CYS J 33 1555 1555 2.03 SSBOND 18 CYS J 48 CYS J 59 1555 1555 2.03 SSBOND 19 CYS J 60 CYS J 65 1555 1555 2.03 SSBOND 20 CYS L 128 CYS L 142 1555 1555 2.03 SSBOND 21 CYS L 192 CYS L 193 1555 1555 2.04 SSBOND 22 CYS I 3 CYS I 23 1555 1555 2.03 SSBOND 23 CYS I 16 CYS I 44 1555 1555 2.03 SSBOND 24 CYS I 29 CYS I 33 1555 1555 2.03 SSBOND 25 CYS I 48 CYS I 59 1555 1555 2.03 SSBOND 26 CYS I 60 CYS I 65 1555 1555 2.03 LINK ND2 ASN A 141 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN B 141 C1 NAG M 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 N 1 1555 1555 1.44 LINK ND2 ASN E 66 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN E 141 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN L 141 C1 NAG Q 1 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 O6 BMA K 3 C1 MAN K 4 1555 1555 1.44 LINK O3 BMA K 3 C1 MAN K 7 1555 1555 1.44 LINK O3 MAN K 4 C1 MAN K 5 1555 1555 1.44 LINK O6 MAN K 4 C1 MAN K 6 1555 1555 1.46 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.44 LINK O6 BMA M 3 C1 MAN M 4 1555 1555 1.45 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 O3 BMA N 3 C1 MAN N 4 1555 1555 1.45 LINK O6 BMA N 3 C1 MAN N 6 1555 1555 1.44 LINK O2 MAN N 4 C1 NAG N 5 1555 1555 1.45 LINK O3 MAN N 6 C1 MAN N 7 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.46 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.44 LINK O6 BMA Q 3 C1 MAN Q 4 1555 1555 1.45 LINK O3 BMA Q 3 C1 MAN Q 7 1555 1555 1.44 LINK O3 MAN Q 4 C1 MAN Q 5 1555 1555 1.44 LINK O6 MAN Q 4 C1 MAN Q 6 1555 1555 1.44 CISPEP 1 PHE A 135 PRO A 136 0 5.95 CISPEP 2 PHE B 135 PRO B 136 0 3.73 CISPEP 3 SER C 7 PRO C 8 0 -10.64 CISPEP 4 TYR C 139 PRO C 140 0 -1.33 CISPEP 5 PHE D 137 PRO D 138 0 6.57 CISPEP 6 PHE E 135 PRO E 136 0 0.78 CISPEP 7 PHE F 153 PRO F 154 0 -14.13 CISPEP 8 GLU F 155 PRO F 156 0 -1.68 CISPEP 9 SER G 7 PRO G 8 0 -2.87 CISPEP 10 TYR G 139 PRO G 140 0 -5.41 CISPEP 11 PHE H 153 PRO H 154 0 -17.25 CISPEP 12 GLU H 155 PRO H 156 0 -0.87 CISPEP 13 SER J 9 PRO J 10 0 -5.76 CISPEP 14 PHE L 135 PRO L 136 0 5.34 CISPEP 15 SER I 9 PRO I 10 0 -3.44 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