HEADER MEMBRANE PROTEIN 14-SEP-24 9DMQ TITLE HUMAN MUSCLE NACHR WITH FAB3-BOUND CAVEAT 9DMQ NAG D 501 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT BETA; COMPND 7 CHAIN: E; 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; COMPND 15 CHAIN: B; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: FAB3 HEAVY CHAIN; COMPND 19 CHAIN: F; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: FAB3 LIGHT CHAIN; COMPND 23 CHAIN: G; COMPND 24 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_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: CHRNB1, ACHRB, CHRNB; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: CHRND, ACHRD; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 GENE: CHRNE, ACHRE; SOURCE 30 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 31 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 33 MOL_ID: 5; SOURCE 34 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 35 ORGANISM_COMMON: HUMAN; SOURCE 36 ORGANISM_TAXID: 9606; SOURCE 37 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 38 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 39 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 40 MOL_ID: 6; SOURCE 41 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 42 ORGANISM_COMMON: HUMAN; SOURCE 43 ORGANISM_TAXID: 9606; SOURCE 44 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 45 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 46 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS HUMAN MUSCLE, NICOTINIC ACETYLCHOLINE RECEPTOR, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR H.LI,R.E.HIBBS REVDAT 1 09-APR-25 9DMQ 0 JRNL AUTH H.LI,R.E.HIBBS JRNL TITL STRUCTURE OF HUMAN MUSCLE ACHR WITH FAB3-BOUND JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.060 REMARK 3 NUMBER OF PARTICLES : 339630 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9DMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288434. 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 MUSCLE NICOTINIC REMARK 245 ACETYLCHOLINE RECEPTOR WITH MG REMARK 245 FABS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : NULL 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: HEPTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, D, B, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -19 REMARK 465 GLU A -18 REMARK 465 PRO A -17 REMARK 465 TRP A -16 REMARK 465 PRO A -15 REMARK 465 LEU A -14 REMARK 465 LEU A -13 REMARK 465 LEU A -12 REMARK 465 LEU A -11 REMARK 465 PHE A -10 REMARK 465 SER A -9 REMARK 465 LEU A -8 REMARK 465 CYS A -7 REMARK 465 SER A -6 REMARK 465 ALA A -5 REMARK 465 GLY A -4 REMARK 465 LEU A -3 REMARK 465 VAL A -2 REMARK 465 LEU A -1 REMARK 465 GLY A 0 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 MET C -19 REMARK 465 GLU C -18 REMARK 465 PRO C -17 REMARK 465 TRP C -16 REMARK 465 PRO C -15 REMARK 465 LEU C -14 REMARK 465 LEU C -13 REMARK 465 LEU C -12 REMARK 465 LEU C -11 REMARK 465 PHE C -10 REMARK 465 SER C -9 REMARK 465 LEU C -8 REMARK 465 CYS C -7 REMARK 465 SER C -6 REMARK 465 ALA C -5 REMARK 465 GLY C -4 REMARK 465 LEU C -3 REMARK 465 VAL C -2 REMARK 465 LEU C -1 REMARK 465 GLY C 0 REMARK 465 ARG C 331 REMARK 465 PRO C 332 REMARK 465 SER C 333 REMARK 465 ARG C 334 REMARK 465 GLU C 335 REMARK 465 LYS C 336 REMARK 465 GLN C 337 REMARK 465 ASP C 338 REMARK 465 LYS C 339 REMARK 465 LYS C 340 REMARK 465 ILE C 341 REMARK 465 PHE C 342 REMARK 465 THR C 343 REMARK 465 GLU C 344 REMARK 465 ASP C 345 REMARK 465 ILE C 346 REMARK 465 ASP C 347 REMARK 465 ILE C 348 REMARK 465 SER C 349 REMARK 465 ASP C 350 REMARK 465 ILE C 351 REMARK 465 SER C 352 REMARK 465 GLY C 353 REMARK 465 LYS C 354 REMARK 465 PRO C 355 REMARK 465 GLY C 356 REMARK 465 PRO C 357 REMARK 465 PRO C 358 REMARK 465 PRO C 359 REMARK 465 MET C 360 REMARK 465 GLY C 361 REMARK 465 PHE C 362 REMARK 465 HIS C 363 REMARK 465 SER C 364 REMARK 465 PRO C 365 REMARK 465 GLY C 437 REMARK 465 MET E -22 REMARK 465 THR E -21 REMARK 465 PRO E -20 REMARK 465 GLY E -19 REMARK 465 ALA E -18 REMARK 465 LEU E -17 REMARK 465 LEU E -16 REMARK 465 MET E -15 REMARK 465 LEU E -14 REMARK 465 LEU E -13 REMARK 465 GLY E -12 REMARK 465 ALA E -11 REMARK 465 LEU E -10 REMARK 465 GLY E -9 REMARK 465 ALA E -8 REMARK 465 PRO E -7 REMARK 465 LEU E -6 REMARK 465 ALA E -5 REMARK 465 PRO E -4 REMARK 465 GLY E -3 REMARK 465 VAL E -2 REMARK 465 ARG E -1 REMARK 465 GLY E 0 REMARK 465 PRO E 164 REMARK 465 ASP E 165 REMARK 465 GLY E 166 REMARK 465 GLN E 167 REMARK 465 ASP E 200 REMARK 465 PRO E 201 REMARK 465 ARG E 202 REMARK 465 GLY E 203 REMARK 465 GLY E 204 REMARK 465 ARG E 205 REMARK 465 PRO E 342 REMARK 465 GLU E 343 REMARK 465 ARG E 344 REMARK 465 ASP E 345 REMARK 465 LEU E 346 REMARK 465 MET E 347 REMARK 465 PRO E 348 REMARK 465 GLU E 349 REMARK 465 PRO E 350 REMARK 465 PRO E 351 REMARK 465 HIS E 352 REMARK 465 CYS E 353 REMARK 465 SER E 354 REMARK 465 SER E 355 REMARK 465 PRO E 356 REMARK 465 GLY E 357 REMARK 465 SER E 358 REMARK 465 GLY E 359 REMARK 465 TRP E 360 REMARK 465 GLY E 361 REMARK 465 ARG E 362 REMARK 465 GLY E 363 REMARK 465 THR E 364 REMARK 465 ASP E 365 REMARK 465 GLU E 366 REMARK 465 TYR E 367 REMARK 465 PHE E 368 REMARK 465 ILE E 369 REMARK 465 ARG E 370 REMARK 465 LYS E 371 REMARK 465 PRO E 372 REMARK 465 PRO E 373 REMARK 465 SER E 374 REMARK 465 ASP E 375 REMARK 465 PHE E 376 REMARK 465 LEU E 377 REMARK 465 PHE E 378 REMARK 465 PRO E 379 REMARK 465 LYS E 380 REMARK 465 PRO E 381 REMARK 465 ASN E 382 REMARK 465 ARG E 383 REMARK 465 PHE E 384 REMARK 465 GLN E 385 REMARK 465 PRO E 386 REMARK 465 GLU E 387 REMARK 465 LEU E 388 REMARK 465 SER E 389 REMARK 465 ALA E 390 REMARK 465 PRO E 391 REMARK 465 ASP E 392 REMARK 465 LEU E 393 REMARK 465 ARG E 394 REMARK 465 ARG E 395 REMARK 465 PHE E 396 REMARK 465 ILE E 397 REMARK 465 ASP E 398 REMARK 465 GLY E 399 REMARK 465 PRO E 400 REMARK 465 ASN E 401 REMARK 465 ARG E 402 REMARK 465 ALA E 403 REMARK 465 VAL E 404 REMARK 465 ALA E 405 REMARK 465 LEU E 406 REMARK 465 MET D -20 REMARK 465 GLU D -19 REMARK 465 GLY D -18 REMARK 465 PRO D -17 REMARK 465 VAL D -16 REMARK 465 LEU D -15 REMARK 465 THR D -14 REMARK 465 LEU D -13 REMARK 465 GLY D -12 REMARK 465 LEU D -11 REMARK 465 LEU D -10 REMARK 465 ALA D -9 REMARK 465 ALA D -8 REMARK 465 LEU D -7 REMARK 465 ALA D -6 REMARK 465 VAL D -5 REMARK 465 CYS D -4 REMARK 465 GLY D -3 REMARK 465 SER D -2 REMARK 465 TRP D -1 REMARK 465 GLY D 0 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 MET B -19 REMARK 465 ALA B -18 REMARK 465 ARG B -17 REMARK 465 ALA B -16 REMARK 465 PRO B -15 REMARK 465 LEU B -14 REMARK 465 GLY B -13 REMARK 465 VAL B -12 REMARK 465 LEU B -11 REMARK 465 LEU B -10 REMARK 465 LEU B -9 REMARK 465 LEU B -8 REMARK 465 GLY B -7 REMARK 465 LEU B -6 REMARK 465 LEU B -5 REMARK 465 GLY B -4 REMARK 465 ARG B -3 REMARK 465 GLY B -2 REMARK 465 VAL B -1 REMARK 465 GLY B 0 REMARK 465 GLY B 335 REMARK 465 SER B 336 REMARK 465 PRO B 337 REMARK 465 PRO B 338 REMARK 465 PRO B 339 REMARK 465 PRO B 340 REMARK 465 GLU B 341 REMARK 465 ALA B 342 REMARK 465 PRO B 343 REMARK 465 ARG B 344 REMARK 465 ALA B 345 REMARK 465 ALA B 346 REMARK 465 SER B 347 REMARK 465 PRO B 348 REMARK 465 PRO B 349 REMARK 465 ARG B 350 REMARK 465 ARG B 351 REMARK 465 ALA B 352 REMARK 465 SER B 353 REMARK 465 SER B 354 REMARK 465 VAL B 355 REMARK 465 GLY B 356 REMARK 465 LEU B 357 REMARK 465 LEU B 358 REMARK 465 LEU B 359 REMARK 465 ARG B 360 REMARK 465 ALA B 361 REMARK 465 GLU B 362 REMARK 465 GLU B 363 REMARK 465 LEU B 364 REMARK 465 ILE B 365 REMARK 465 LEU B 366 REMARK 465 LYS B 367 REMARK 465 LYS B 368 REMARK 465 PRO B 369 REMARK 465 ARG B 370 REMARK 465 SER B 371 REMARK 465 GLU B 372 REMARK 465 LEU B 373 REMARK 465 VAL B 374 REMARK 465 PHE B 375 REMARK 465 GLU B 376 REMARK 465 GLY B 377 REMARK 465 GLN B 378 REMARK 465 ARG B 379 REMARK 465 HIS B 380 REMARK 465 ARG B 381 REMARK 465 GLN B 382 REMARK 465 GLY B 383 REMARK 465 THR B 384 REMARK 465 TRP B 385 REMARK 465 THR B 386 REMARK 465 ALA B 387 REMARK 465 ALA B 388 REMARK 465 PHE B 389 REMARK 465 CYS B 390 REMARK 465 GLN B 391 REMARK 465 SER B 392 REMARK 465 LEU B 393 REMARK 465 GLY B 394 REMARK 465 ALA B 395 REMARK 465 ALA B 396 REMARK 465 MET F 1 REMARK 465 ASP F 2 REMARK 465 SER F 3 REMARK 465 LYS F 4 REMARK 465 GLY F 5 REMARK 465 SER F 6 REMARK 465 SER F 7 REMARK 465 GLN F 8 REMARK 465 LYS F 9 REMARK 465 GLY F 10 REMARK 465 SER F 11 REMARK 465 ARG F 12 REMARK 465 LEU F 13 REMARK 465 LEU F 14 REMARK 465 LEU F 15 REMARK 465 LEU F 16 REMARK 465 LEU F 17 REMARK 465 VAL F 18 REMARK 465 VAL F 19 REMARK 465 SER F 20 REMARK 465 ASN F 21 REMARK 465 LEU F 22 REMARK 465 LEU F 23 REMARK 465 LEU F 24 REMARK 465 CYS F 25 REMARK 465 GLN F 26 REMARK 465 GLY F 27 REMARK 465 VAL F 28 REMARK 465 VAL F 29 REMARK 465 SER F 30 REMARK 465 ALA F 31 REMARK 465 SER F 179 REMARK 465 LYS F 180 REMARK 465 SER F 181 REMARK 465 THR F 182 REMARK 465 SER F 183 REMARK 465 GLY F 184 REMARK 465 LYS F 265 REMARK 465 SER F 266 REMARK 465 CYS F 267 REMARK 465 GLY F 268 REMARK 465 SER F 269 REMARK 465 HIS F 270 REMARK 465 HIS F 271 REMARK 465 HIS F 272 REMARK 465 HIS F 273 REMARK 465 HIS F 274 REMARK 465 HIS F 275 REMARK 465 MET G 1 REMARK 465 GLY G 2 REMARK 465 TRP G 3 REMARK 465 SER G 4 REMARK 465 CYS G 5 REMARK 465 ILE G 6 REMARK 465 ILE G 7 REMARK 465 LEU G 8 REMARK 465 PHE G 9 REMARK 465 LEU G 10 REMARK 465 VAL G 11 REMARK 465 ALA G 12 REMARK 465 THR G 13 REMARK 465 ALA G 14 REMARK 465 THR G 15 REMARK 465 GLY G 16 REMARK 465 VAL G 17 REMARK 465 HIS G 18 REMARK 465 SER G 19 REMARK 465 GLY G 233 REMARK 465 GLU G 234 REMARK 465 CYS G 235 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 HD22 ASN A 297 H11A POV B 503 1.07 REMARK 500 HE1 TRP E 322 H13 POV E 502 1.15 REMARK 500 HZ1 LYS D 290 H12 POV D 506 1.26 REMARK 500 HE1 TRP E 322 C13 POV E 502 1.56 REMARK 500 HG11 VAL C 295 OD1 ASP C 407 1.57 REMARK 500 OH TYR B 242 HD21 ASN B 301 1.58 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 LEU A 65 71.03 -102.21 REMARK 500 ASN A 94 32.37 -92.74 REMARK 500 ALA A 96 -63.31 -94.35 REMARK 500 ASP A 97 33.35 -142.32 REMARK 500 PHE A 137 36.19 -99.92 REMARK 500 GLN A 436 30.46 -94.23 REMARK 500 ASN C 94 33.14 -96.41 REMARK 500 ASP C 97 10.17 -143.12 REMARK 500 PHE C 137 35.29 -98.25 REMARK 500 ASN E 94 30.68 -91.88 REMARK 500 ILE E 106 -141.34 44.93 REMARK 500 PHE E 137 34.04 -96.53 REMARK 500 LEU E 162 144.22 -170.13 REMARK 500 VAL E 229 -55.72 -126.77 REMARK 500 LEU D 67 35.89 -98.99 REMARK 500 ASN D 96 31.61 -95.84 REMARK 500 PHE D 139 34.11 -96.90 REMARK 500 ARG D 195 62.12 -150.18 REMARK 500 ILE D 232 -54.19 -127.67 REMARK 500 GLU D 332 -32.41 -130.72 REMARK 500 THR D 333 -61.96 -91.57 REMARK 500 PHE B 137 50.52 -92.79 REMARK 500 ASN B 170 54.68 -93.60 REMARK 500 CYS B 190 58.58 -152.46 REMARK 500 ILE B 227 -53.29 -125.05 REMARK 500 ARG F 147 58.51 -90.01 REMARK 500 ASP F 195 64.05 66.12 REMARK 500 ALA G 71 -12.71 72.59 REMARK 500 SER G 72 -14.37 -140.81 REMARK 500 ARG G 88 -95.14 59.97 REMARK 500 TYR G 111 24.12 -142.72 REMARK 500 SER G 114 164.87 65.56 REMARK 500 TYR G 161 126.66 -170.94 REMARK 500 LYS G 190 -75.56 -105.96 REMARK 500 SER G 192 45.28 71.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG C 182 0.16 SIDE CHAIN REMARK 500 ARG E 28 0.21 SIDE CHAIN REMARK 500 ARG E 480 0.28 SIDE CHAIN REMARK 500 ARG D 170 0.14 SIDE CHAIN REMARK 500 ARG B 461 0.17 SIDE CHAIN REMARK 500 ARG F 69 0.11 SIDE CHAIN REMARK 500 ARG G 129 0.16 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 POV E 502 REMARK 610 POV D 506 REMARK 610 POV B 503 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-47013 RELATED DB: EMDB REMARK 900 HUMAN MUSCLE NACHR WITH FAB3-BOUND DBREF 9DMQ A -19 437 UNP P02708 ACHA_HUMAN 1 457 DBREF 9DMQ C -19 437 UNP P02708 ACHA_HUMAN 1 457 DBREF 9DMQ E -22 478 UNP P11230 ACHB_HUMAN 1 501 DBREF 9DMQ D -20 496 UNP Q07001 ACHD_HUMAN 1 517 DBREF 9DMQ B -19 473 UNP Q04844 ACHE_HUMAN 1 493 DBREF 9DMQ F 1 275 PDB 9DMQ 9DMQ 1 275 DBREF 9DMQ G 1 235 PDB 9DMQ 9DMQ 1 235 SEQADV 9DMQ SER E 479 UNP P11230 EXPRESSION TAG SEQADV 9DMQ ARG E 480 UNP P11230 EXPRESSION TAG SEQRES 1 A 457 MET GLU PRO TRP PRO LEU LEU LEU LEU PHE SER LEU CYS SEQRES 2 A 457 SER ALA GLY LEU VAL LEU GLY SER GLU HIS GLU THR ARG SEQRES 3 A 457 LEU VAL ALA LYS LEU PHE LYS ASP TYR SER SER VAL VAL SEQRES 4 A 457 ARG PRO VAL GLU ASP HIS ARG GLN VAL VAL GLU VAL THR SEQRES 5 A 457 VAL GLY LEU GLN LEU ILE GLN LEU ILE ASN VAL ASP GLU SEQRES 6 A 457 VAL ASN GLN ILE VAL THR THR ASN VAL ARG LEU LYS GLN SEQRES 7 A 457 GLN TRP VAL ASP TYR ASN LEU LYS TRP ASN PRO ASP ASP SEQRES 8 A 457 TYR GLY GLY VAL LYS LYS ILE HIS ILE PRO SER GLU LYS SEQRES 9 A 457 ILE TRP ARG PRO ASP LEU VAL LEU TYR ASN ASN ALA ASP SEQRES 10 A 457 GLY ASP PHE ALA ILE VAL LYS PHE THR LYS VAL LEU LEU SEQRES 11 A 457 GLN TYR THR GLY HIS ILE THR TRP THR PRO PRO ALA ILE SEQRES 12 A 457 PHE LYS SER TYR CYS GLU ILE ILE VAL THR HIS PHE PRO SEQRES 13 A 457 PHE ASP GLU GLN ASN CYS SER MET LYS LEU GLY THR TRP SEQRES 14 A 457 THR TYR ASP GLY SER VAL VAL ALA ILE ASN PRO GLU SER SEQRES 15 A 457 ASP GLN PRO ASP LEU SER ASN PHE MET GLU SER GLY GLU SEQRES 16 A 457 TRP VAL ILE LYS GLU SER ARG GLY TRP LYS HIS SER VAL SEQRES 17 A 457 THR TYR SER CYS CYS PRO ASP THR PRO TYR LEU ASP ILE SEQRES 18 A 457 THR TYR HIS PHE VAL MET GLN ARG LEU PRO LEU TYR PHE SEQRES 19 A 457 ILE VAL ASN VAL ILE ILE PRO CYS LEU LEU PHE SER PHE SEQRES 20 A 457 LEU THR GLY LEU VAL PHE TYR LEU PRO THR ASP SER GLY SEQRES 21 A 457 GLU LYS MET THR LEU SER ILE SER VAL LEU LEU SER LEU SEQRES 22 A 457 THR VAL PHE LEU LEU VAL ILE VAL GLU LEU ILE PRO SER SEQRES 23 A 457 THR SER SER ALA VAL PRO LEU ILE GLY LYS TYR MET LEU SEQRES 24 A 457 PHE THR MET VAL PHE VAL ILE ALA SER ILE ILE ILE THR SEQRES 25 A 457 VAL ILE VAL ILE ASN THR HIS HIS ARG SER PRO SER THR SEQRES 26 A 457 HIS VAL MET PRO ASN TRP VAL ARG LYS VAL PHE ILE ASP SEQRES 27 A 457 THR ILE PRO ASN ILE MET PHE PHE SER THR MET LYS ARG SEQRES 28 A 457 PRO SER ARG GLU LYS GLN ASP LYS LYS ILE PHE THR GLU SEQRES 29 A 457 ASP ILE ASP ILE SER ASP ILE SER GLY LYS PRO GLY PRO SEQRES 30 A 457 PRO PRO MET GLY PHE HIS SER PRO LEU ILE LYS HIS PRO SEQRES 31 A 457 GLU VAL LYS SER ALA ILE GLU GLY ILE LYS TYR ILE ALA SEQRES 32 A 457 GLU THR MET LYS SER ASP GLN GLU SER ASN ASN ALA ALA SEQRES 33 A 457 ALA GLU TRP LYS TYR VAL ALA MET VAL MET ASP HIS ILE SEQRES 34 A 457 LEU LEU GLY VAL PHE MET LEU VAL CYS ILE ILE GLY THR SEQRES 35 A 457 LEU ALA VAL PHE ALA GLY ARG LEU ILE GLU LEU ASN GLN SEQRES 36 A 457 GLN GLY SEQRES 1 C 457 MET GLU PRO TRP PRO LEU LEU LEU LEU PHE SER LEU CYS SEQRES 2 C 457 SER ALA GLY LEU VAL LEU GLY SER GLU HIS GLU THR ARG SEQRES 3 C 457 LEU VAL ALA LYS LEU PHE LYS ASP TYR SER SER VAL VAL SEQRES 4 C 457 ARG PRO VAL GLU ASP HIS ARG GLN VAL VAL GLU VAL THR SEQRES 5 C 457 VAL GLY LEU GLN LEU ILE GLN LEU ILE ASN VAL ASP GLU SEQRES 6 C 457 VAL ASN GLN ILE VAL THR THR ASN VAL ARG LEU LYS GLN SEQRES 7 C 457 GLN TRP VAL ASP TYR ASN LEU LYS TRP ASN PRO ASP ASP SEQRES 8 C 457 TYR GLY GLY VAL LYS LYS ILE HIS ILE PRO SER GLU LYS SEQRES 9 C 457 ILE TRP ARG PRO ASP LEU VAL LEU TYR ASN ASN ALA ASP SEQRES 10 C 457 GLY ASP PHE ALA ILE VAL LYS PHE THR LYS VAL LEU LEU SEQRES 11 C 457 GLN TYR THR GLY HIS ILE THR TRP THR PRO PRO ALA ILE SEQRES 12 C 457 PHE LYS SER TYR CYS GLU ILE ILE VAL THR HIS PHE PRO SEQRES 13 C 457 PHE ASP GLU GLN ASN CYS SER MET LYS LEU GLY THR TRP SEQRES 14 C 457 THR TYR ASP GLY SER VAL VAL ALA ILE ASN PRO GLU SER SEQRES 15 C 457 ASP GLN PRO ASP LEU SER ASN PHE MET GLU SER GLY GLU SEQRES 16 C 457 TRP VAL ILE LYS GLU SER ARG GLY TRP LYS HIS SER VAL SEQRES 17 C 457 THR TYR SER CYS CYS PRO ASP THR PRO TYR LEU ASP ILE SEQRES 18 C 457 THR TYR HIS PHE VAL MET GLN ARG LEU PRO LEU TYR PHE SEQRES 19 C 457 ILE VAL ASN VAL ILE ILE PRO CYS LEU LEU PHE SER PHE SEQRES 20 C 457 LEU THR GLY LEU VAL PHE TYR LEU PRO THR ASP SER GLY SEQRES 21 C 457 GLU LYS MET THR LEU SER ILE SER VAL LEU LEU SER LEU SEQRES 22 C 457 THR VAL PHE LEU LEU VAL ILE VAL GLU LEU ILE PRO SER SEQRES 23 C 457 THR SER SER ALA VAL PRO LEU ILE GLY LYS TYR MET LEU SEQRES 24 C 457 PHE THR MET VAL PHE VAL ILE ALA SER ILE ILE ILE THR SEQRES 25 C 457 VAL ILE VAL ILE ASN THR HIS HIS ARG SER PRO SER THR SEQRES 26 C 457 HIS VAL MET PRO ASN TRP VAL ARG LYS VAL PHE ILE ASP SEQRES 27 C 457 THR ILE PRO ASN ILE MET PHE PHE SER THR MET LYS ARG SEQRES 28 C 457 PRO SER ARG GLU LYS GLN ASP LYS LYS ILE PHE THR GLU SEQRES 29 C 457 ASP ILE ASP ILE SER ASP ILE SER GLY LYS PRO GLY PRO SEQRES 30 C 457 PRO PRO MET GLY PHE HIS SER PRO LEU ILE LYS HIS PRO SEQRES 31 C 457 GLU VAL LYS SER ALA ILE GLU GLY ILE LYS TYR ILE ALA SEQRES 32 C 457 GLU THR MET LYS SER ASP GLN GLU SER ASN ASN ALA ALA SEQRES 33 C 457 ALA GLU TRP LYS TYR VAL ALA MET VAL MET ASP HIS ILE SEQRES 34 C 457 LEU LEU GLY VAL PHE MET LEU VAL CYS ILE ILE GLY THR SEQRES 35 C 457 LEU ALA VAL PHE ALA GLY ARG LEU ILE GLU LEU ASN GLN SEQRES 36 C 457 GLN GLY SEQRES 1 E 503 MET THR PRO GLY ALA LEU LEU MET LEU LEU GLY ALA LEU SEQRES 2 E 503 GLY ALA PRO LEU ALA PRO GLY VAL ARG GLY SER GLU ALA SEQRES 3 E 503 GLU GLY ARG LEU ARG GLU LYS LEU PHE SER GLY TYR ASP SEQRES 4 E 503 SER SER VAL ARG PRO ALA ARG GLU VAL GLY ASP ARG VAL SEQRES 5 E 503 ARG VAL SER VAL GLY LEU ILE LEU ALA GLN LEU ILE SER SEQRES 6 E 503 LEU ASN GLU LYS ASP GLU GLU MET SER THR LYS VAL TYR SEQRES 7 E 503 LEU ASP LEU GLU TRP THR ASP TYR ARG LEU SER TRP ASP SEQRES 8 E 503 PRO ALA GLU HIS ASP GLY ILE ASP SER LEU ARG ILE THR SEQRES 9 E 503 ALA GLU SER VAL TRP LEU PRO ASP VAL VAL LEU LEU ASN SEQRES 10 E 503 ASN ASN ASP GLY ASN PHE ASP VAL ALA LEU ASP ILE SER SEQRES 11 E 503 VAL VAL VAL SER SER ASP GLY SER VAL ARG TRP GLN PRO SEQRES 12 E 503 PRO GLY ILE TYR ARG SER SER CYS SER ILE GLN VAL THR SEQRES 13 E 503 TYR PHE PRO PHE ASP TRP GLN ASN CYS THR MET VAL PHE SEQRES 14 E 503 SER SER TYR SER TYR ASP SER SER GLU VAL SER LEU GLN SEQRES 15 E 503 THR GLY LEU GLY PRO ASP GLY GLN GLY HIS GLN GLU ILE SEQRES 16 E 503 HIS ILE HIS GLU GLY THR PHE ILE GLU ASN GLY GLN TRP SEQRES 17 E 503 GLU ILE ILE HIS LYS PRO SER ARG LEU ILE GLN PRO PRO SEQRES 18 E 503 GLY ASP PRO ARG GLY GLY ARG GLU GLY GLN ARG GLN GLU SEQRES 19 E 503 VAL ILE PHE TYR LEU ILE ILE ARG ARG LYS PRO LEU PHE SEQRES 20 E 503 TYR LEU VAL ASN VAL ILE ALA PRO CYS ILE LEU ILE THR SEQRES 21 E 503 LEU LEU ALA ILE PHE VAL PHE TYR LEU PRO PRO ASP ALA SEQRES 22 E 503 GLY GLU LYS MET GLY LEU SER ILE PHE ALA LEU LEU THR SEQRES 23 E 503 LEU THR VAL PHE LEU LEU LEU LEU ALA ASP LYS VAL PRO SEQRES 24 E 503 GLU THR SER LEU SER VAL PRO ILE ILE ILE LYS TYR LEU SEQRES 25 E 503 MET PHE THR MET VAL LEU VAL THR PHE SER VAL ILE LEU SEQRES 26 E 503 SER VAL VAL VAL LEU ASN LEU HIS HIS ARG SER PRO HIS SEQRES 27 E 503 THR HIS GLN MET PRO LEU TRP VAL ARG GLN ILE PHE ILE SEQRES 28 E 503 HIS LYS LEU PRO LEU TYR LEU ARG LEU LYS ARG PRO LYS SEQRES 29 E 503 PRO GLU ARG ASP LEU MET PRO GLU PRO PRO HIS CYS SER SEQRES 30 E 503 SER PRO GLY SER GLY TRP GLY ARG GLY THR ASP GLU TYR SEQRES 31 E 503 PHE ILE ARG LYS PRO PRO SER ASP PHE LEU PHE PRO LYS SEQRES 32 E 503 PRO ASN ARG PHE GLN PRO GLU LEU SER ALA PRO ASP LEU SEQRES 33 E 503 ARG ARG PHE ILE ASP GLY PRO ASN ARG ALA VAL ALA LEU SEQRES 34 E 503 LEU PRO GLU LEU ARG GLU VAL VAL SER SER ILE SER TYR SEQRES 35 E 503 ILE ALA ARG GLN LEU GLN GLU GLN GLU ASP HIS ASP ALA SEQRES 36 E 503 LEU LYS GLU ASP TRP GLN PHE VAL ALA MET VAL VAL ASP SEQRES 37 E 503 ARG LEU PHE LEU TRP THR PHE ILE ILE PHE THR SER VAL SEQRES 38 E 503 GLY THR LEU VAL ILE PHE LEU ASP ALA THR TYR HIS LEU SEQRES 39 E 503 PRO PRO PRO ASP PRO PHE PRO SER ARG SEQRES 1 D 517 MET GLU GLY PRO VAL LEU THR LEU GLY LEU LEU ALA ALA SEQRES 2 D 517 LEU ALA VAL CYS GLY SER TRP GLY LEU ASN GLU GLU GLU SEQRES 3 D 517 ARG LEU ILE ARG HIS LEU PHE GLN GLU LYS GLY TYR ASN SEQRES 4 D 517 LYS GLU LEU ARG PRO VAL ALA HIS LYS GLU GLU SER VAL SEQRES 5 D 517 ASP VAL ALA LEU ALA LEU THR LEU SER ASN LEU ILE SER SEQRES 6 D 517 LEU LYS GLU VAL GLU GLU THR LEU THR THR ASN VAL TRP SEQRES 7 D 517 ILE GLU HIS GLY TRP THR ASP ASN ARG LEU LYS TRP ASN SEQRES 8 D 517 ALA GLU GLU PHE GLY ASN ILE SER VAL LEU ARG LEU PRO SEQRES 9 D 517 PRO ASP MET VAL TRP LEU PRO GLU ILE VAL LEU GLU ASN SEQRES 10 D 517 ASN ASN ASP GLY SER PHE GLN ILE SER TYR SER CYS ASN SEQRES 11 D 517 VAL LEU VAL TYR HIS TYR GLY PHE VAL TYR TRP LEU PRO SEQRES 12 D 517 PRO ALA ILE PHE ARG SER SER CYS PRO ILE SER VAL THR SEQRES 13 D 517 TYR PHE PRO PHE ASP TRP GLN ASN CYS SER LEU LYS PHE SEQRES 14 D 517 SER SER LEU LYS TYR THR ALA LYS GLU ILE THR LEU SER SEQRES 15 D 517 LEU LYS GLN ASP ALA LYS GLU ASN ARG THR TYR PRO VAL SEQRES 16 D 517 GLU TRP ILE ILE ILE ASP PRO GLU GLY PHE THR GLU ASN SEQRES 17 D 517 GLY GLU TRP GLU ILE VAL HIS ARG PRO ALA ARG VAL ASN SEQRES 18 D 517 VAL ASP PRO ARG ALA PRO LEU ASP SER PRO SER ARG GLN SEQRES 19 D 517 ASP ILE THR PHE TYR LEU ILE ILE ARG ARG LYS PRO LEU SEQRES 20 D 517 PHE TYR ILE ILE ASN ILE LEU VAL PRO CYS VAL LEU ILE SEQRES 21 D 517 SER PHE MET VAL ASN LEU VAL PHE TYR LEU PRO ALA ASP SEQRES 22 D 517 SER GLY GLU LYS THR SER VAL ALA ILE SER VAL LEU LEU SEQRES 23 D 517 ALA GLN SER VAL PHE LEU LEU LEU ILE SER LYS ARG LEU SEQRES 24 D 517 PRO ALA THR SER MET ALA ILE PRO LEU ILE GLY LYS PHE SEQRES 25 D 517 LEU LEU PHE GLY MET VAL LEU VAL THR MET VAL VAL VAL SEQRES 26 D 517 ILE CYS VAL ILE VAL LEU ASN ILE HIS PHE ARG THR PRO SEQRES 27 D 517 SER THR HIS VAL LEU SER GLU GLY VAL LYS LYS LEU PHE SEQRES 28 D 517 LEU GLU THR LEU PRO GLU LEU LEU HIS MET SER ARG PRO SEQRES 29 D 517 ALA GLU ASP GLY PRO SER PRO GLY ALA LEU VAL ARG ARG SEQRES 30 D 517 SER SER SER LEU GLY TYR ILE SER LYS ALA GLU GLU TYR SEQRES 31 D 517 PHE LEU LEU LYS SER ARG SER ASP LEU MET PHE GLU LYS SEQRES 32 D 517 GLN SER GLU ARG HIS GLY LEU ALA ARG ARG LEU THR THR SEQRES 33 D 517 ALA ARG ARG PRO PRO ALA SER SER GLU GLN ALA GLN GLN SEQRES 34 D 517 GLU LEU PHE ASN GLU LEU LYS PRO ALA VAL ASP GLY ALA SEQRES 35 D 517 ASN PHE ILE VAL ASN HIS MET ARG ASP GLN ASN ASN TYR SEQRES 36 D 517 ASN GLU GLU LYS ASP SER TRP ASN ARG VAL ALA ARG THR SEQRES 37 D 517 VAL ASP ARG LEU CYS LEU PHE VAL VAL THR PRO VAL MET SEQRES 38 D 517 VAL VAL GLY THR ALA TRP ILE PHE LEU GLN GLY VAL TYR SEQRES 39 D 517 ASN GLN PRO PRO PRO GLN PRO PHE PRO GLY ASP PRO TYR SEQRES 40 D 517 SER TYR ASN VAL GLN ASP LYS ARG PHE ILE SEQRES 1 B 493 MET ALA ARG ALA PRO LEU GLY VAL LEU LEU LEU LEU GLY SEQRES 2 B 493 LEU LEU GLY ARG GLY VAL GLY LYS ASN GLU GLU LEU ARG SEQRES 3 B 493 LEU TYR HIS HIS LEU PHE ASN ASN TYR ASP PRO GLY SER SEQRES 4 B 493 ARG PRO VAL ARG GLU PRO GLU ASP THR VAL THR ILE SER SEQRES 5 B 493 LEU LYS VAL THR LEU THR ASN LEU ILE SER LEU ASN GLU SEQRES 6 B 493 LYS GLU GLU THR LEU THR THR SER VAL TRP ILE GLY ILE SEQRES 7 B 493 ASP TRP GLN ASP TYR ARG LEU ASN TYR SER LYS ASP ASP SEQRES 8 B 493 PHE GLY GLY ILE GLU THR LEU ARG VAL PRO SER GLU LEU SEQRES 9 B 493 VAL TRP LEU PRO GLU ILE VAL LEU GLU ASN ASN ILE ASP SEQRES 10 B 493 GLY GLN PHE GLY VAL ALA TYR ASP ALA ASN VAL LEU VAL SEQRES 11 B 493 TYR GLU GLY GLY SER VAL THR TRP LEU PRO PRO ALA ILE SEQRES 12 B 493 TYR ARG SER VAL CYS ALA VAL GLU VAL THR TYR PHE PRO SEQRES 13 B 493 PHE ASP TRP GLN ASN CYS SER LEU ILE PHE ARG SER GLN SEQRES 14 B 493 THR TYR ASN ALA GLU GLU VAL GLU PHE THR PHE ALA VAL SEQRES 15 B 493 ASP ASN ASP GLY LYS THR ILE ASN LYS ILE ASP ILE ASP SEQRES 16 B 493 THR GLU ALA TYR THR GLU ASN GLY GLU TRP ALA ILE ASP SEQRES 17 B 493 PHE CYS PRO GLY VAL ILE ARG ARG HIS HIS GLY GLY ALA SEQRES 18 B 493 THR ASP GLY PRO GLY GLU THR ASP VAL ILE TYR SER LEU SEQRES 19 B 493 ILE ILE ARG ARG LYS PRO LEU PHE TYR VAL ILE ASN ILE SEQRES 20 B 493 ILE VAL PRO CYS VAL LEU ILE SER GLY LEU VAL LEU LEU SEQRES 21 B 493 ALA TYR PHE LEU PRO ALA GLN ALA GLY GLY GLN LYS CYS SEQRES 22 B 493 THR VAL SER ILE ASN VAL LEU LEU ALA GLN THR VAL PHE SEQRES 23 B 493 LEU PHE LEU ILE ALA GLN LYS ILE PRO GLU THR SER LEU SEQRES 24 B 493 SER VAL PRO LEU LEU GLY ARG PHE LEU ILE PHE VAL MET SEQRES 25 B 493 VAL VAL ALA THR LEU ILE VAL MET ASN CYS VAL ILE VAL SEQRES 26 B 493 LEU ASN VAL SER GLN ARG THR PRO THR THR HIS ALA MET SEQRES 27 B 493 SER PRO ARG LEU ARG HIS VAL LEU LEU GLU LEU LEU PRO SEQRES 28 B 493 ARG LEU LEU GLY SER PRO PRO PRO PRO GLU ALA PRO ARG SEQRES 29 B 493 ALA ALA SER PRO PRO ARG ARG ALA SER SER VAL GLY LEU SEQRES 30 B 493 LEU LEU ARG ALA GLU GLU LEU ILE LEU LYS LYS PRO ARG SEQRES 31 B 493 SER GLU LEU VAL PHE GLU GLY GLN ARG HIS ARG GLN GLY SEQRES 32 B 493 THR TRP THR ALA ALA PHE CYS GLN SER LEU GLY ALA ALA SEQRES 33 B 493 ALA PRO GLU VAL ARG CYS CYS VAL ASP ALA VAL ASN PHE SEQRES 34 B 493 VAL ALA GLU SER THR ARG ASP GLN GLU ALA THR GLY GLU SEQRES 35 B 493 GLU VAL SER ASP TRP VAL ARG MET GLY ASN ALA LEU ASP SEQRES 36 B 493 ASN ILE CYS PHE TRP ALA ALA LEU VAL LEU PHE SER VAL SEQRES 37 B 493 GLY SER SER LEU ILE PHE LEU GLY ALA TYR PHE ASN ARG SEQRES 38 B 493 VAL PRO ASP LEU PRO TYR ALA PRO CYS ILE GLN PRO SEQRES 1 F 275 MET ASP SER LYS GLY SER SER GLN LYS GLY SER ARG LEU SEQRES 2 F 275 LEU LEU LEU LEU VAL VAL SER ASN LEU LEU LEU CYS GLN SEQRES 3 F 275 GLY VAL VAL SER ALA GLU VAL GLN LEU VAL GLN TRP GLY SEQRES 4 F 275 ALA GLY LEU LEU LYS PRO SER GLU THR LEU SER LEU THR SEQRES 5 F 275 CYS THR VAL PHE GLY GLY SER LEU ARG ALA ASN TYR TRP SEQRES 6 F 275 SER TRP ILE ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP SEQRES 7 F 275 ILE GLY GLU ILE ASN HIS ASN GLY HIS THR ASN TYR ASN SEQRES 8 F 275 PRO SER LEU LYS SER ARG ALA THR ILE SER VAL ASP THR SEQRES 9 F 275 SER LYS ASN GLN PHE SER LEU ARG LEU SER SER VAL THR SEQRES 10 F 275 ALA ALA ASP THR ALA LEU TYR TYR CYS ALA ARG GLY SER SEQRES 11 F 275 ARG PHE PHE TYR TYR GLY ALA GLY ILE TYR TYR ASN ALA SEQRES 12 F 275 ARG ARG ASP ARG ASP ASN TYR PHE ASP PRO TRP GLY GLN SEQRES 13 F 275 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 14 F 275 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 15 F 275 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 16 F 275 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 17 F 275 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 18 F 275 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 19 F 275 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 20 F 275 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 21 F 275 LYS VAL GLU PRO LYS SER CYS GLY SER HIS HIS HIS HIS SEQRES 22 F 275 HIS HIS SEQRES 1 G 235 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 G 235 ALA THR GLY VAL HIS SER ASP ILE VAL MET THR GLN SER SEQRES 3 G 235 PRO GLY THR LEU SER LEU SER PRO GLY GLU ARG ALA THR SEQRES 4 G 235 LEU SER CYS ARG ALA SER GLN HIS VAL THR GLY ASN CYS SEQRES 5 G 235 LEU ALA TRP TYR GLN GLN LYS PRO ASP GLN ALA PRO ARG SEQRES 6 G 235 LEU LEU ILE TYR ASP ALA SER THR ARG ALA THR GLY VAL SEQRES 7 G 235 PRO ASP ARG PHE SER GLY SER GLY SER ARG THR ASP PHE SEQRES 8 G 235 THR LEU THR ILE SER ARG LEU GLU PRO GLU ASP PHE ALA SEQRES 9 G 235 VAL TYR HIS CYS GLN GLN TYR GLY ASP SER PRO PRO TRP SEQRES 10 G 235 THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR SEQRES 11 G 235 VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP SEQRES 12 G 235 GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU SEQRES 13 G 235 LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP SEQRES 14 G 235 LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SEQRES 15 G 235 SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER SEQRES 16 G 235 LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU SEQRES 17 G 235 LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY SEQRES 18 G 235 LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU SEQRES 19 G 235 CYS HET NAG H 1 26 HET NAG H 2 26 HET BMA H 3 19 HET MAN H 4 21 HET MAN H 5 21 HET NAG I 1 26 HET NAG I 2 26 HET BMA I 3 19 HET MAN I 4 19 HET MAN I 5 21 HET MAN I 6 21 HET MAN I 7 21 HET NAG J 1 26 HET NAG J 2 26 HET BMA J 3 19 HET MAN J 4 20 HET MAN J 5 21 HET MAN J 6 21 HET NAG K 1 26 HET NAG K 2 27 HET NAG L 1 26 HET NAG L 2 26 HET BMA L 3 19 HET MAN L 4 20 HET MAN L 5 21 HET MAN L 6 21 HET NAG M 1 26 HET NAG M 2 27 HET NAG N 1 26 HET NAG N 2 26 HET BMA N 3 19 HET MAN N 4 21 HET MAN N 5 21 HET ACH A 501 26 HET CLR E 501 74 HET POV E 502 86 HET NAG D 501 27 HET CLR D 502 74 HET POV D 503 134 HET CLR D 504 74 HET CLR D 505 74 HET POV D 506 92 HET CLR B 501 74 HET CLR B 502 74 HET POV B 503 107 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM ACH ACETYLCHOLINE HETNAM CLR CHOLESTEROL HETNAM POV (2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9- HETNAM 2 POV ENOYLOXY]PROPYL 2-(TRIMETHYLAMMONIO)ETHYL PHOSPHATE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN POV POPC FORMUL 8 NAG 15(C8 H15 N O6) FORMUL 8 BMA 5(C6 H12 O6) FORMUL 8 MAN 14(C6 H12 O6) FORMUL 15 ACH C7 H16 N O2 1+ FORMUL 16 CLR 6(C27 H46 O) FORMUL 17 POV 4(C42 H82 N O8 P) FORMUL 27 HOH *(H2 O) HELIX 1 AA1 SER A 1 PHE A 12 1 12 HELIX 2 AA2 ASN A 68 GLY A 73 5 6 HELIX 3 AA3 PRO A 81 ILE A 85 5 5 HELIX 4 AA4 PRO A 211 VAL A 218 1 8 HELIX 5 AA5 VAL A 218 GLY A 230 1 13 HELIX 6 AA6 LEU A 231 LEU A 235 5 5 HELIX 7 AA7 PRO A 236 GLY A 240 5 5 HELIX 8 AA8 GLU A 241 LEU A 263 1 23 HELIX 9 AA9 PRO A 272 HIS A 300 1 29 HELIX 10 AB1 PRO A 309 PHE A 316 1 8 HELIX 11 AB2 THR A 319 MET A 324 1 6 HELIX 12 AB3 HIS A 369 GLN A 436 1 68 HELIX 13 AB4 GLU C 2 PHE C 12 1 11 HELIX 14 AB5 ASN C 68 GLY C 73 5 6 HELIX 15 AB6 PRO C 81 ILE C 85 5 5 HELIX 16 AB7 PRO C 211 VAL C 218 1 8 HELIX 17 AB8 VAL C 218 LEU C 231 1 14 HELIX 18 AB9 VAL C 232 LEU C 235 5 4 HELIX 19 AC1 PRO C 236 GLY C 240 5 5 HELIX 20 AC2 GLU C 241 ILE C 264 1 24 HELIX 21 AC3 PRO C 272 HIS C 300 1 29 HELIX 22 AC4 PRO C 309 ILE C 317 1 9 HELIX 23 AC5 ASP C 318 ILE C 323 1 6 HELIX 24 AC6 HIS C 369 GLN C 436 1 68 HELIX 25 AC7 GLU E 2 PHE E 12 1 11 HELIX 26 AC8 ASP E 68 HIS E 72 5 5 HELIX 27 AC9 GLU E 83 VAL E 85 5 3 HELIX 28 AD1 PRO E 222 VAL E 229 1 8 HELIX 29 AD2 VAL E 229 VAL E 243 1 15 HELIX 30 AD3 PHE E 244 LEU E 246 5 3 HELIX 31 AD4 PRO E 247 GLY E 251 5 5 HELIX 32 AD5 GLU E 252 ASP E 273 1 22 HELIX 33 AD6 PRO E 283 HIS E 311 1 29 HELIX 34 AD7 PRO E 320 HIS E 329 1 10 HELIX 35 AD8 HIS E 329 LEU E 335 1 7 HELIX 36 AD9 PRO E 408 TYR E 469 1 62 HELIX 37 AE1 ASN D 2 GLN D 13 1 12 HELIX 38 AE2 ASN D 70 GLY D 75 5 6 HELIX 39 AE3 PRO D 83 VAL D 87 5 5 HELIX 40 AE4 PRO D 225 ILE D 232 1 8 HELIX 41 AE5 ILE D 232 MET D 242 1 11 HELIX 42 AE6 VAL D 243 LEU D 249 5 7 HELIX 43 AE7 PRO D 250 GLY D 254 5 5 HELIX 44 AE8 GLU D 255 LYS D 276 1 22 HELIX 45 AE9 PRO D 286 PHE D 314 1 29 HELIX 46 AF1 SER D 323 THR D 333 1 11 HELIX 47 AF2 THR D 333 HIS D 339 1 7 HELIX 48 AF3 GLU D 409 TYR D 473 1 65 HELIX 49 AF4 ASN B 2 ASN B 13 1 12 HELIX 50 AF5 TYR B 63 ASN B 66 5 4 HELIX 51 AF6 SER B 68 GLY B 73 5 6 HELIX 52 AF7 GLU B 83 VAL B 85 5 3 HELIX 53 AF8 ASP B 175 TYR B 179 5 5 HELIX 54 AF9 GLY B 200 GLY B 204 5 5 HELIX 55 AG1 PRO B 220 ILE B 227 1 8 HELIX 56 AG2 ILE B 227 LEU B 237 1 11 HELIX 57 AG3 VAL B 238 LEU B 244 5 7 HELIX 58 AG4 GLN B 251 GLN B 272 1 22 HELIX 59 AG5 PRO B 282 GLN B 310 1 29 HELIX 60 AG6 SER B 319 GLU B 328 1 10 HELIX 61 AG7 GLU B 328 LEU B 334 1 7 HELIX 62 AG8 PRO B 398 PHE B 459 1 62 HELIX 63 AG9 SER F 59 ARG F 61 5 3 HELIX 64 AH1 THR F 117 THR F 121 5 5 HELIX 65 AH2 ALA F 137 TYR F 141 5 5 HELIX 66 AH3 SER F 207 ALA F 209 5 3 HELIX 67 AH4 SER F 238 GLY F 241 5 4 HELIX 68 AH5 LYS F 252 ASN F 255 5 4 HELIX 69 AH6 VAL G 48 ASN G 51 5 4 HELIX 70 AH7 GLU G 99 PHE G 103 5 5 HELIX 71 AH8 SER G 142 SER G 148 1 7 HELIX 72 AH9 LYS G 204 LYS G 209 1 6 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 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 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 TRP A 60 O ILE A 116 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 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 LYS C 77 ILE C 80 0 SHEET 2 AA4 5 VAL C 108 GLN C 111 -1 O VAL C 108 N ILE C 80 SHEET 3 AA4 5 HIS C 115 TRP C 118 -1 O HIS C 115 N GLN C 111 SHEET 4 AA4 5 ILE C 49 VAL C 61 -1 N GLN C 58 O TRP C 118 SHEET 5 AA4 5 PRO C 121 TYR C 127 -1 O ALA C 122 N VAL C 54 SHEET 1 AA5 6 LYS C 77 ILE C 80 0 SHEET 2 AA5 6 VAL C 108 GLN C 111 -1 O VAL C 108 N ILE C 80 SHEET 3 AA5 6 HIS C 115 TRP C 118 -1 O HIS C 115 N GLN C 111 SHEET 4 AA5 6 ILE C 49 VAL C 61 -1 N GLN C 58 O TRP C 118 SHEET 5 AA5 6 VAL C 29 ASP C 44 -1 N ASP C 44 O ILE C 49 SHEET 6 AA5 6 VAL C 156 PRO C 160 1 O ALA C 157 N VAL C 29 SHEET 1 AA6 4 LEU C 90 LEU C 92 0 SHEET 2 AA6 4 GLU C 139 THR C 148 -1 O GLY C 147 N VAL C 91 SHEET 3 AA6 4 TYR C 198 ARG C 209 -1 O ILE C 201 N LEU C 146 SHEET 4 AA6 4 TRP C 176 VAL C 188 -1 N VAL C 177 O GLN C 208 SHEET 1 AA7 5 SER E 77 THR E 81 0 SHEET 2 AA7 5 SER E 107 SER E 111 -1 O VAL E 108 N ILE E 80 SHEET 3 AA7 5 ASP E 113 TRP E 118 -1 O ARG E 117 N VAL E 109 SHEET 4 AA7 5 GLU E 49 SER E 66 -1 N TRP E 60 O VAL E 116 SHEET 5 AA7 5 PRO E 121 SER E 127 -1 O SER E 126 N MET E 50 SHEET 1 AA8 6 SER E 77 THR E 81 0 SHEET 2 AA8 6 SER E 107 SER E 111 -1 O VAL E 108 N ILE E 80 SHEET 3 AA8 6 ASP E 113 TRP E 118 -1 O ARG E 117 N VAL E 109 SHEET 4 AA8 6 GLU E 49 SER E 66 -1 N TRP E 60 O VAL E 116 SHEET 5 AA8 6 VAL E 29 ASN E 44 -1 N GLN E 39 O LYS E 53 SHEET 6 AA8 6 VAL E 156 THR E 160 1 O SER E 157 N VAL E 31 SHEET 1 AA9 4 VAL E 90 LEU E 92 0 SHEET 2 AA9 4 TRP E 139 SER E 148 -1 O SER E 147 N VAL E 91 SHEET 3 AA9 4 GLU E 211 ARG E 220 -1 O VAL E 212 N PHE E 146 SHEET 4 AA9 4 TRP E 185 HIS E 189 -1 N ILE E 188 O ILE E 217 SHEET 1 AB1 4 VAL E 90 LEU E 92 0 SHEET 2 AB1 4 TRP E 139 SER E 148 -1 O SER E 147 N VAL E 91 SHEET 3 AB1 4 GLU E 211 ARG E 220 -1 O VAL E 212 N PHE E 146 SHEET 4 AB1 4 SER E 192 ILE E 195 -1 N ILE E 195 O GLU E 211 SHEET 1 AB2 5 VAL D 79 LEU D 82 0 SHEET 2 AB2 5 VAL D 110 TYR D 113 -1 O VAL D 112 N LEU D 80 SHEET 3 AB2 5 TYR D 115 TRP D 120 -1 O TYR D 119 N LEU D 111 SHEET 4 AB2 5 THR D 51 LYS D 68 -1 N HIS D 60 O TRP D 120 SHEET 5 AB2 5 PRO D 123 SER D 129 -1 O SER D 128 N LEU D 52 SHEET 1 AB3 6 VAL D 79 LEU D 82 0 SHEET 2 AB3 6 VAL D 110 TYR D 113 -1 O VAL D 112 N LEU D 80 SHEET 3 AB3 6 TYR D 115 TRP D 120 -1 O TYR D 119 N LEU D 111 SHEET 4 AB3 6 THR D 51 LYS D 68 -1 N HIS D 60 O TRP D 120 SHEET 5 AB3 6 VAL D 31 LYS D 46 -1 N ALA D 34 O GLY D 61 SHEET 6 AB3 6 ILE D 158 LEU D 162 1 O THR D 159 N VAL D 31 SHEET 1 AB4 4 ILE D 92 LEU D 94 0 SHEET 2 AB4 4 TRP D 141 SER D 150 -1 O SER D 149 N VAL D 93 SHEET 3 AB4 4 GLN D 213 ARG D 223 -1 O ILE D 215 N PHE D 148 SHEET 4 AB4 4 TRP D 190 HIS D 194 -1 N VAL D 193 O ILE D 220 SHEET 1 AB5 4 ILE D 92 LEU D 94 0 SHEET 2 AB5 4 TRP D 141 SER D 150 -1 O SER D 149 N VAL D 93 SHEET 3 AB5 4 GLN D 213 ARG D 223 -1 O ILE D 215 N PHE D 148 SHEET 4 AB5 4 ALA D 197 VAL D 201 -1 N ARG D 198 O THR D 216 SHEET 1 AB6 2 GLN D 164 ASP D 165 0 SHEET 2 AB6 2 TYR D 172 PRO D 173 -1 O TYR D 172 N ASP D 165 SHEET 1 AB7 5 THR B 77 PRO B 81 0 SHEET 2 AB7 5 ASN B 107 TYR B 111 -1 O VAL B 110 N LEU B 78 SHEET 3 AB7 5 SER B 115 TRP B 118 -1 O SER B 115 N TYR B 111 SHEET 4 AB7 5 THR B 49 GLN B 61 -1 N TRP B 60 O VAL B 116 SHEET 5 AB7 5 PRO B 121 VAL B 127 -1 O ALA B 122 N VAL B 54 SHEET 1 AB8 6 THR B 77 PRO B 81 0 SHEET 2 AB8 6 ASN B 107 TYR B 111 -1 O VAL B 110 N LEU B 78 SHEET 3 AB8 6 SER B 115 TRP B 118 -1 O SER B 115 N TYR B 111 SHEET 4 AB8 6 THR B 49 GLN B 61 -1 N TRP B 60 O VAL B 116 SHEET 5 AB8 6 VAL B 29 ASN B 44 -1 N ASN B 39 O SER B 53 SHEET 6 AB8 6 VAL B 156 PHE B 160 1 O THR B 159 N LEU B 33 SHEET 1 AB9 4 ILE B 90 LEU B 92 0 SHEET 2 AB9 4 TRP B 139 SER B 148 -1 O ARG B 147 N VAL B 91 SHEET 3 AB9 4 GLU B 207 ARG B 218 -1 O VAL B 210 N PHE B 146 SHEET 4 AB9 4 TRP B 185 PHE B 189 -1 N ALA B 186 O ARG B 217 SHEET 1 AC1 4 ILE B 90 LEU B 92 0 SHEET 2 AC1 4 TRP B 139 SER B 148 -1 O ARG B 147 N VAL B 91 SHEET 3 AC1 4 GLU B 207 ARG B 218 -1 O VAL B 210 N PHE B 146 SHEET 4 AC1 4 GLY B 192 HIS B 197 -1 N HIS B 197 O GLU B 207 SHEET 1 AC2 4 GLN F 34 TRP F 38 0 SHEET 2 AC2 4 LEU F 49 PHE F 56 -1 O THR F 54 N VAL F 36 SHEET 3 AC2 4 GLN F 108 LEU F 113 -1 O PHE F 109 N CYS F 53 SHEET 4 AC2 4 ALA F 98 ASP F 103 -1 N ASP F 103 O GLN F 108 SHEET 1 AC3 6 LEU F 42 LEU F 43 0 SHEET 2 AC3 6 THR F 158 VAL F 162 1 O THR F 161 N LEU F 43 SHEET 3 AC3 6 ALA F 122 TYR F 135 -1 N TYR F 124 O THR F 158 SHEET 4 AC3 6 ASN F 63 GLN F 70 -1 N TYR F 64 O GLY F 129 SHEET 5 AC3 6 LEU F 76 ILE F 82 -1 O ILE F 79 N TRP F 67 SHEET 6 AC3 6 THR F 88 TYR F 90 -1 O ASN F 89 N GLU F 81 SHEET 1 AC4 4 LEU F 42 LEU F 43 0 SHEET 2 AC4 4 THR F 158 VAL F 162 1 O THR F 161 N LEU F 43 SHEET 3 AC4 4 ALA F 122 TYR F 135 -1 N TYR F 124 O THR F 158 SHEET 4 AC4 4 ASN F 142 ARG F 145 -1 O ASN F 142 N TYR F 135 SHEET 1 AC5 4 SER F 171 LEU F 175 0 SHEET 2 AC5 4 THR F 186 TYR F 196 -1 O LEU F 192 N PHE F 173 SHEET 3 AC5 4 TYR F 227 PRO F 236 -1 O TYR F 227 N TYR F 196 SHEET 4 AC5 4 VAL F 214 THR F 216 -1 N HIS F 215 O VAL F 232 SHEET 1 AC6 4 SER F 171 LEU F 175 0 SHEET 2 AC6 4 THR F 186 TYR F 196 -1 O LEU F 192 N PHE F 173 SHEET 3 AC6 4 TYR F 227 PRO F 236 -1 O TYR F 227 N TYR F 196 SHEET 4 AC6 4 VAL F 220 LEU F 221 -1 N VAL F 220 O SER F 228 SHEET 1 AC7 3 THR F 202 TRP F 205 0 SHEET 2 AC7 3 ILE F 246 HIS F 251 -1 O ASN F 248 N SER F 204 SHEET 3 AC7 3 THR F 256 LYS F 261 -1 O VAL F 258 N VAL F 249 SHEET 1 AC8 4 MET G 23 GLN G 25 0 SHEET 2 AC8 4 ALA G 38 ALA G 44 -1 O ARG G 43 N THR G 24 SHEET 3 AC8 4 ASP G 90 ILE G 95 -1 O LEU G 93 N LEU G 40 SHEET 4 AC8 4 PHE G 82 SER G 87 -1 N SER G 83 O THR G 94 SHEET 1 AC9 6 THR G 29 LEU G 32 0 SHEET 2 AC9 6 THR G 123 ILE G 127 1 O LYS G 124 N LEU G 30 SHEET 3 AC9 6 VAL G 105 GLN G 110 -1 N TYR G 106 O THR G 123 SHEET 4 AC9 6 LEU G 53 GLN G 58 -1 N ALA G 54 O GLN G 109 SHEET 5 AC9 6 ARG G 65 TYR G 69 -1 O ARG G 65 N GLN G 57 SHEET 6 AC9 6 THR G 73 ARG G 74 -1 O THR G 73 N TYR G 69 SHEET 1 AD1 4 THR G 29 LEU G 32 0 SHEET 2 AD1 4 THR G 123 ILE G 127 1 O LYS G 124 N LEU G 30 SHEET 3 AD1 4 VAL G 105 GLN G 110 -1 N TYR G 106 O THR G 123 SHEET 4 AD1 4 THR G 118 PHE G 119 -1 O THR G 118 N GLN G 110 SHEET 1 AD2 4 SER G 135 PHE G 139 0 SHEET 2 AD2 4 THR G 150 PHE G 160 -1 O ASN G 158 N SER G 135 SHEET 3 AD2 4 TYR G 194 SER G 203 -1 O LEU G 196 N LEU G 157 SHEET 4 AD2 4 SER G 180 VAL G 184 -1 N SER G 183 O SER G 197 SHEET 1 AD3 4 ALA G 174 LEU G 175 0 SHEET 2 AD3 4 LYS G 166 VAL G 171 -1 N VAL G 171 O ALA G 174 SHEET 3 AD3 4 VAL G 212 THR G 218 -1 O GLU G 216 N GLN G 168 SHEET 4 AD3 4 VAL G 226 ASN G 231 -1 O VAL G 226 N VAL G 217 SSBOND 1 CYS C 128 CYS C 142 1555 1555 2.05 SSBOND 2 CYS E 128 CYS E 142 1555 1555 2.05 SSBOND 3 CYS D 130 CYS D 144 1555 1555 2.04 SSBOND 4 CYS B 128 CYS B 142 1555 1555 2.04 SSBOND 5 CYS B 190 CYS B 470 1555 1555 2.03 SSBOND 6 CYS F 53 CYS F 126 1555 1555 2.04 SSBOND 7 CYS F 191 CYS F 247 1555 1555 2.04 SSBOND 8 CYS G 42 CYS G 108 1555 1555 2.04 SSBOND 9 CYS G 155 CYS G 215 1555 1555 2.06 LINK ND2 ASN A 141 C1 NAG H 1 1555 1555 1.57 LINK ND2 ASN C 141 C1 NAG I 1 1555 1555 1.56 LINK ND2 ASN E 141 C1 NAG J 1 1555 1555 1.57 LINK ND2 ASN D 76 C1 NAG D 501 1555 1555 1.58 LINK ND2 ASN D 143 C1 NAG L 1 1555 1555 1.58 LINK ND2 ASN D 169 C1 NAG K 1 1555 1555 1.59 LINK ND2 ASN B 66 C1 NAG M 1 1555 1555 1.55 LINK ND2 ASN B 141 C1 NAG N 1 1555 1555 1.59 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.43 LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44 LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.44 LINK O6 BMA H 3 C1 MAN H 5 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.43 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 7 1555 1555 1.44 LINK O3 MAN I 4 C1 MAN I 5 1555 1555 1.44 LINK O6 MAN I 4 C1 MAN I 6 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.43 LINK O6 BMA J 3 C1 MAN J 4 1555 1555 1.44 LINK O3 BMA J 3 C1 MAN J 6 1555 1555 1.44 LINK O3 MAN J 4 C1 MAN J 5 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.43 LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.44 LINK O6 BMA L 3 C1 MAN L 4 1555 1555 1.44 LINK O3 BMA L 3 C1 MAN L 6 1555 1555 1.44 LINK O3 MAN L 4 C1 MAN L 5 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.45 LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.45 LINK O6 BMA N 3 C1 MAN N 5 1555 1555 1.44 CISPEP 1 PHE A 135 PRO A 136 0 4.24 CISPEP 2 PHE C 135 PRO C 136 0 4.17 CISPEP 3 PHE E 135 PRO E 136 0 -1.69 CISPEP 4 PHE D 137 PRO D 138 0 4.28 CISPEP 5 PHE B 135 PRO B 136 0 4.91 CISPEP 6 PHE F 197 PRO F 198 0 -10.89 CISPEP 7 GLU F 199 PRO F 200 0 0.53 CISPEP 8 PRO G 115 PRO G 116 0 3.21 CISPEP 9 TYR G 161 PRO G 162 0 22.21 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