HEADER MEMBRANE PROTEIN 13-SEP-24 9DMK TITLE HUMAN MUSCLE NACHR WITH ONE FAB1B-BOUND 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: FAB1B HEAVY CHAIN; COMPND 19 CHAIN: F; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: FAB1B 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 9DMK 0 JRNL AUTH H.LI,R.E.HIBBS JRNL TITL STRUCTURE OF HUMAN MUSCLE ACHR WITH ONE FAB1B-BOUND JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.46 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) : 2.460 REMARK 3 NUMBER OF PARTICLES : 96503 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 9DMK 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_1000288430. 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 : FEI TITAN 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 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 168 REMARK 465 LYS F 169 REMARK 465 SER F 170 REMARK 465 THR F 171 REMARK 465 SER F 172 REMARK 465 GLY F 173 REMARK 465 LYS F 254 REMARK 465 SER F 255 REMARK 465 CYS F 256 REMARK 465 GLY F 257 REMARK 465 SER F 258 REMARK 465 HIS F 259 REMARK 465 HIS F 260 REMARK 465 HIS F 261 REMARK 465 HIS F 262 REMARK 465 HIS F 263 REMARK 465 HIS F 264 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 GLY G 19 REMARK 465 GLY G 236 REMARK 465 GLU G 237 REMARK 465 CYS G 238 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 HZ1 LYS D 290 H13B POV D 501 1.08 REMARK 500 HA3 GLY B 236 H21E POV B 504 1.14 REMARK 500 O ASN D 187 HZ1 LYS D 224 1.48 REMARK 500 OE1 GLU B 89 HG1 THR B 150 1.57 REMARK 500 OD1 ASN B 432 H13A POV B 504 1.57 REMARK 500 OE1 GLU B 89 OG1 THR B 150 2.10 REMARK 500 OE2 GLU C 4 OG SER B 19 2.11 REMARK 500 OD1 ASN B 432 C13 POV B 504 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PHE A 325 CB - CA - C ANGL. DEV. = 17.4 DEGREES 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 57.11 -96.34 REMARK 500 ALA A 96 -61.87 -90.18 REMARK 500 PHE A 137 33.03 -96.81 REMARK 500 PHE A 326 -70.40 -132.76 REMARK 500 ASN C 42 147.40 -171.31 REMARK 500 ASN C 94 33.51 -96.91 REMARK 500 ASP C 97 20.77 -143.65 REMARK 500 PHE C 137 33.74 -99.09 REMARK 500 ASN C 169 32.66 -97.25 REMARK 500 MET C 324 -168.68 -129.88 REMARK 500 ASN E 94 33.86 -97.20 REMARK 500 ILE E 106 -129.46 54.58 REMARK 500 GLN E 119 70.03 -116.56 REMARK 500 GLN E 170 74.70 -103.45 REMARK 500 LYS E 190 59.36 -146.45 REMARK 500 VAL E 229 -55.19 -125.90 REMARK 500 LEU D 67 35.51 -99.65 REMARK 500 GLU D 91 97.55 -66.53 REMARK 500 ASN D 96 30.40 -92.54 REMARK 500 PHE D 139 30.74 -94.10 REMARK 500 THR D 154 -166.73 -110.06 REMARK 500 ARG D 195 66.22 -152.06 REMARK 500 ILE D 232 -56.24 -122.58 REMARK 500 ASN B 94 32.28 -94.23 REMARK 500 ASN B 170 52.00 -97.00 REMARK 500 CYS B 190 61.07 -157.11 REMARK 500 ILE B 227 -56.54 -121.37 REMARK 500 GLN B 310 30.47 -93.05 REMARK 500 ASP F 184 72.84 52.32 REMARK 500 ALA G 75 -9.74 74.07 REMARK 500 SER G 91 -169.55 -117.27 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 A 182 0.17 SIDE CHAIN REMARK 500 ARG A 301 0.28 SIDE CHAIN REMARK 500 ARG C 182 0.12 SIDE CHAIN REMARK 500 ARG E 480 0.09 SIDE CHAIN REMARK 500 ARG D 6 0.20 SIDE CHAIN REMARK 500 ARG G 132 0.12 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 D 501 REMARK 610 POV B 504 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-47008 RELATED DB: EMDB REMARK 900 HUMAN MUSCLE NACHR WITH ONE FAB1B-BOUND DBREF 9DMK A -19 437 UNP P02708 ACHA_HUMAN 1 457 DBREF 9DMK C -19 437 UNP P02708 ACHA_HUMAN 1 457 DBREF 9DMK E -22 478 UNP P11230 ACHB_HUMAN 1 501 DBREF 9DMK D -20 496 UNP Q07001 ACHD_HUMAN 1 517 DBREF 9DMK B -19 473 UNP Q04844 ACHE_HUMAN 1 493 DBREF 9DMK F 1 264 PDB 9DMK 9DMK 1 264 DBREF 9DMK G 1 238 PDB 9DMK 9DMK 1 238 SEQADV 9DMK SER E 479 UNP P11230 EXPRESSION TAG SEQADV 9DMK 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 264 MET ASP SER LYS GLY SER SER GLN LYS GLY SER ARG LEU SEQRES 2 F 264 LEU LEU LEU LEU VAL VAL SER ASN LEU LEU LEU CYS GLN SEQRES 3 F 264 GLY VAL VAL SER ALA GLN VAL GLN LEU VAL GLN SER GLY SEQRES 4 F 264 ALA GLU MET LYS LYS PRO GLY SER SER VAL LYS VAL SER SEQRES 5 F 264 CYS LYS ALA SER GLY GLY SER PHE GLY SER TYR GLY ILE SEQRES 6 F 264 ASP TRP VAL ARG GLN ALA PRO GLY GLN GLY LEU GLU TRP SEQRES 7 F 264 MET GLY GLY ILE MET PRO LYS PHE ASP ALA PRO LYS TYR SEQRES 8 F 264 ALA GLU LYS PHE GLN GLY ARG LEU THR ILE THR ALA ASP SEQRES 9 F 264 ARG ALA THR ASN THR ALA TYR MET GLU LEU SER SER LEU SEQRES 10 F 264 ARG PHE GLU ASP THR ALA ILE TYR TYR CYS ALA ARG ASP SEQRES 11 F 264 GLU GLN PRO PHE TYR ASP SER TRP ARG GLY LEU TYR TRP SEQRES 12 F 264 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 13 F 264 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 14 F 264 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 15 F 264 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 16 F 264 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 17 F 264 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 18 F 264 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 19 F 264 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 20 F 264 ASP LYS LYS VAL GLU PRO LYS SER CYS GLY SER HIS HIS SEQRES 21 F 264 HIS HIS HIS HIS SEQRES 1 G 238 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 G 238 ALA THR GLY VAL HIS GLY ASP ILE VAL MET THR GLN SER SEQRES 3 G 238 PRO LEU SER LEU PRO VAL THR PRO GLY GLU PRO ALA SER SEQRES 4 G 238 ILE SER CYS ARG SER ASN GLN SER LEU LEU HIS THR LYS SEQRES 5 G 238 GLY TYR LYS TYR LEU ASN TRP TYR LEU GLN ARG PRO GLY SEQRES 6 G 238 GLN SER PRO GLN VAL LEU ILE TYR PHE ALA SER ASN ARG SEQRES 7 G 238 ALA PRO GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 8 G 238 GLY THR ASP PHE THR LEU LYS ILE SER ARG VAL GLU ALA SEQRES 9 G 238 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN GLY LEU GLN SEQRES 10 G 238 ILE PRO PHE THR PHE GLY PRO GLY THR LYS VAL ASP ILE SEQRES 11 G 238 LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO SEQRES 12 G 238 PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL SEQRES 13 G 238 VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS SEQRES 14 G 238 VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SEQRES 15 G 238 SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER SEQRES 16 G 238 THR TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA SEQRES 17 G 238 ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR SEQRES 18 G 238 HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN SEQRES 19 G 238 ARG GLY GLU 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 20 HET MAN I 4 21 HET NAG J 1 26 HET NAG J 2 26 HET BMA J 3 20 HET MAN J 4 21 HET NAG K 1 26 HET NAG K 2 26 HET BMA K 3 19 HET MAN K 4 21 HET MAN K 5 21 HET NAG L 1 26 HET NAG L 2 26 HET BMA L 3 21 HET POV E 501 134 HET POV D 501 92 HET NAG B 501 27 HET CLR B 502 74 HET CLR B 503 74 HET POV B 504 107 HET NAG G 301 27 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM POV (2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9- HETNAM 2 POV ENOYLOXY]PROPYL 2-(TRIMETHYLAMMONIO)ETHYL PHOSPHATE HETNAM CLR CHOLESTEROL 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 12(C8 H15 N O6) FORMUL 8 BMA 5(C6 H12 O6) FORMUL 8 MAN 6(C6 H12 O6) FORMUL 13 POV 3(C42 H82 N O8 P) FORMUL 16 CLR 2(C27 H46 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 GLU A 83 ILE A 85 5 3 HELIX 4 AA4 PRO A 211 VAL A 218 1 8 HELIX 5 AA5 VAL A 218 LEU A 231 1 14 HELIX 6 AA6 VAL A 232 LEU A 235 5 4 HELIX 7 AA7 PRO A 236 GLY A 240 5 5 HELIX 8 AA8 GLU A 241 ILE A 264 1 24 HELIX 9 AA9 PRO A 272 HIS A 300 1 29 HELIX 10 AB1 PRO A 309 ILE A 317 1 9 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 GLU C 83 ILE C 85 5 3 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 GLU C 241 ILE C 264 1 24 HELIX 20 AC2 PRO C 272 HIS C 300 1 29 HELIX 21 AC3 PRO C 309 ILE C 317 1 9 HELIX 22 AC4 ILE C 320 MET C 324 5 5 HELIX 23 AC5 HIS C 369 GLN C 436 1 68 HELIX 24 AC6 GLU E 2 PHE E 12 1 11 HELIX 25 AC7 ASP E 68 HIS E 72 5 5 HELIX 26 AC8 GLU E 83 VAL E 85 5 3 HELIX 27 AC9 PRO E 222 VAL E 229 1 8 HELIX 28 AD1 VAL E 229 VAL E 243 1 15 HELIX 29 AD2 PHE E 244 LEU E 246 5 3 HELIX 30 AD3 PRO E 247 GLY E 251 5 5 HELIX 31 AD4 GLU E 252 ALA E 272 1 21 HELIX 32 AD5 PRO E 283 HIS E 311 1 29 HELIX 33 AD6 PRO E 320 HIS E 329 1 10 HELIX 34 AD7 LYS E 330 LEU E 335 1 6 HELIX 35 AD8 PRO E 408 TYR E 469 1 62 HELIX 36 AD9 ASN D 2 GLN D 13 1 12 HELIX 37 AE1 PRO D 83 VAL D 87 5 5 HELIX 38 AE2 PRO D 225 ILE D 232 1 8 HELIX 39 AE3 ILE D 232 MET D 242 1 11 HELIX 40 AE4 VAL D 243 TYR D 248 5 6 HELIX 41 AE5 GLU D 255 LYS D 276 1 22 HELIX 42 AE6 PRO D 286 PHE D 314 1 29 HELIX 43 AE7 SER D 323 GLU D 332 1 10 HELIX 44 AE8 GLU D 332 LEU D 338 1 7 HELIX 45 AE9 GLU D 409 TYR D 473 1 65 HELIX 46 AF1 ASN B 2 ASN B 13 1 12 HELIX 47 AF2 TYR B 63 ASN B 66 5 4 HELIX 48 AF3 PRO B 81 VAL B 85 5 5 HELIX 49 AF4 PRO B 220 ILE B 227 1 8 HELIX 50 AF5 ILE B 227 VAL B 238 1 12 HELIX 51 AF6 LEU B 239 LEU B 244 5 6 HELIX 52 AF7 GLN B 251 GLN B 272 1 22 HELIX 53 AF8 PRO B 282 GLN B 310 1 29 HELIX 54 AF9 SER B 319 LEU B 327 1 9 HELIX 55 AG1 GLU B 328 LEU B 334 1 7 HELIX 56 AG2 PRO B 398 PHE B 459 1 62 HELIX 57 AG3 GLU F 93 GLN F 96 5 4 HELIX 58 AG4 ARG F 118 THR F 122 5 5 HELIX 59 AG5 SER F 196 ALA F 198 5 3 HELIX 60 AG6 SER F 227 GLY F 230 5 4 HELIX 61 AG7 GLU G 147 SER G 151 5 5 HELIX 62 AG8 LYS G 207 HIS G 213 1 7 SHEET 1 AA1 5 LYS A 77 PRO A 81 0 SHEET 2 AA1 5 LYS A 107 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 SER A 126 N VAL A 50 SHEET 1 AA2 6 LYS A 77 PRO A 81 0 SHEET 2 AA2 6 LYS A 107 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 GLY A 34 O LYS A 57 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 GLU A 180 O VAL A 206 SHEET 1 AA4 5 LYS C 77 PRO C 81 0 SHEET 2 AA4 5 LYS C 107 GLN C 111 -1 O VAL C 108 N ILE C 80 SHEET 3 AA4 5 HIS C 115 TRP C 118 -1 O THR C 117 N LEU C 109 SHEET 4 AA4 5 ILE C 49 VAL C 61 -1 N TRP C 60 O ILE C 116 SHEET 5 AA4 5 PRO C 121 TYR C 127 -1 O SER C 126 N VAL C 50 SHEET 1 AA5 6 LYS C 77 PRO C 81 0 SHEET 2 AA5 6 LYS C 107 GLN C 111 -1 O VAL C 108 N ILE C 80 SHEET 3 AA5 6 HIS C 115 TRP C 118 -1 O THR C 117 N LEU C 109 SHEET 4 AA5 6 ILE C 49 VAL C 61 -1 N TRP C 60 O ILE C 116 SHEET 5 AA5 6 VAL C 29 ASP C 44 -1 N GLY C 34 O LYS C 57 SHEET 6 AA5 6 VAL C 156 PRO C 160 1 O ALA C 157 N VAL C 31 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 188 O TYR C 198 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 GLY E 122 N VAL E 54 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 SER E 32 O GLU E 59 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 GLU E 186 O ARG E 219 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 TRP D 62 O VAL D 118 SHEET 5 AB2 5 PRO D 123 SER D 129 -1 O ALA D 124 N VAL D 56 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 TRP D 62 O VAL D 118 SHEET 5 AB3 6 VAL D 31 LYS D 46 -1 N THR D 38 O TRP D 57 SHEET 6 AB3 6 ILE D 158 LEU D 162 1 O THR D 159 N VAL D 31 SHEET 1 AB4 4 VAL D 93 LEU D 94 0 SHEET 2 AB4 4 TRP D 141 SER D 149 -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 GLU D 191 O ARG D 222 SHEET 1 AB5 4 VAL D 93 LEU D 94 0 SHEET 2 AB5 4 TRP D 141 SER D 149 -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 ALA D 166 0 SHEET 2 AB6 2 THR D 171 PRO D 173 -1 O TYR D 172 N ASP D 165 SHEET 1 AB7 5 THR B 77 VAL B 80 0 SHEET 2 AB7 5 VAL B 108 TYR B 111 -1 O VAL B 110 N LEU B 78 SHEET 3 AB7 5 SER B 115 TRP B 118 -1 O THR B 117 N LEU B 109 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 VAL B 80 0 SHEET 2 AB8 6 VAL B 108 TYR B 111 -1 O VAL B 110 N LEU B 78 SHEET 3 AB8 6 SER B 115 TRP B 118 -1 O THR B 117 N LEU B 109 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 LYS B 34 O GLY B 57 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 GLN F 37 0 SHEET 2 AC2 4 VAL F 49 SER F 56 -1 O LYS F 54 N VAL F 36 SHEET 3 AC2 4 THR F 109 LEU F 114 -1 O MET F 112 N VAL F 51 SHEET 4 AC2 4 LEU F 99 ASP F 104 -1 N ASP F 104 O THR F 109 SHEET 1 AC3 6 GLU F 41 LYS F 43 0 SHEET 2 AC3 6 THR F 147 VAL F 151 1 O THR F 150 N LYS F 43 SHEET 3 AC3 6 ALA F 123 ARG F 129 -1 N TYR F 125 O THR F 147 SHEET 4 AC3 6 ILE F 65 GLN F 70 -1 N VAL F 68 O TYR F 126 SHEET 5 AC3 6 LEU F 76 ILE F 82 -1 O MET F 79 N TRP F 67 SHEET 6 AC3 6 PRO F 89 TYR F 91 -1 O LYS F 90 N GLY F 81 SHEET 1 AC4 4 GLU F 41 LYS F 43 0 SHEET 2 AC4 4 THR F 147 VAL F 151 1 O THR F 150 N LYS F 43 SHEET 3 AC4 4 ALA F 123 ARG F 129 -1 N TYR F 125 O THR F 147 SHEET 4 AC4 4 TYR F 142 TRP F 143 -1 O TYR F 142 N ARG F 129 SHEET 1 AC5 4 SER F 160 LEU F 164 0 SHEET 2 AC5 4 THR F 175 TYR F 185 -1 O LEU F 181 N PHE F 162 SHEET 3 AC5 4 TYR F 216 PRO F 225 -1 O LEU F 218 N VAL F 182 SHEET 4 AC5 4 HIS F 204 THR F 205 -1 N HIS F 204 O VAL F 221 SHEET 1 AC6 4 SER F 160 LEU F 164 0 SHEET 2 AC6 4 THR F 175 TYR F 185 -1 O LEU F 181 N PHE F 162 SHEET 3 AC6 4 TYR F 216 PRO F 225 -1 O LEU F 218 N VAL F 182 SHEET 4 AC6 4 VAL F 209 LEU F 210 -1 N VAL F 209 O SER F 217 SHEET 1 AC7 3 VAL F 190 TRP F 194 0 SHEET 2 AC7 3 ILE F 235 HIS F 240 -1 O ASN F 237 N SER F 193 SHEET 3 AC7 3 THR F 245 LYS F 250 -1 O VAL F 247 N VAL F 238 SHEET 1 AC8 4 MET G 23 SER G 26 0 SHEET 2 AC8 4 ALA G 38 SER G 44 -1 O ARG G 43 N THR G 24 SHEET 3 AC8 4 ASP G 94 ILE G 99 -1 O LEU G 97 N ILE G 40 SHEET 4 AC8 4 PHE G 86 GLY G 90 -1 N SER G 89 O THR G 96 SHEET 1 AC9 6 SER G 29 VAL G 32 0 SHEET 2 AC9 6 THR G 126 ILE G 130 1 O ASP G 129 N VAL G 32 SHEET 3 AC9 6 VAL G 109 GLN G 114 -1 N TYR G 110 O THR G 126 SHEET 4 AC9 6 LEU G 57 GLN G 62 -1 N ASN G 58 O MET G 113 SHEET 5 AC9 6 PRO G 68 TYR G 73 -1 O GLN G 69 N LEU G 61 SHEET 6 AC9 6 ASN G 77 ARG G 78 -1 O ASN G 77 N TYR G 73 SHEET 1 AD1 4 SER G 29 VAL G 32 0 SHEET 2 AD1 4 THR G 126 ILE G 130 1 O ASP G 129 N VAL G 32 SHEET 3 AD1 4 VAL G 109 GLN G 114 -1 N TYR G 110 O THR G 126 SHEET 4 AD1 4 THR G 121 PHE G 122 -1 O THR G 121 N GLN G 114 SHEET 1 AD2 4 SER G 138 PHE G 142 0 SHEET 2 AD2 4 THR G 153 PHE G 163 -1 O LEU G 159 N PHE G 140 SHEET 3 AD2 4 TYR G 197 SER G 206 -1 O LEU G 199 N LEU G 160 SHEET 4 AD2 4 SER G 183 VAL G 187 -1 N SER G 186 O SER G 200 SHEET 1 AD3 3 TRP G 172 LYS G 173 0 SHEET 2 AD3 3 ALA G 217 VAL G 220 -1 O ALA G 217 N LYS G 173 SHEET 3 AD3 3 VAL G 229 LYS G 231 -1 O VAL G 229 N VAL G 220 SSBOND 1 CYS A 128 CYS A 142 1555 1555 2.04 SSBOND 2 CYS C 128 CYS C 142 1555 1555 2.03 SSBOND 3 CYS E 128 CYS E 142 1555 1555 2.04 SSBOND 4 CYS D 130 CYS D 144 1555 1555 2.04 SSBOND 5 CYS B 128 CYS B 142 1555 1555 2.04 SSBOND 6 CYS B 190 CYS B 470 1555 1555 2.03 SSBOND 7 CYS F 53 CYS F 127 1555 1555 2.03 SSBOND 8 CYS F 180 CYS F 236 1555 1555 2.04 SSBOND 9 CYS G 42 CYS G 112 1555 1555 2.04 SSBOND 10 CYS G 158 CYS G 218 1555 1555 2.04 LINK ND2 ASN A 141 C1 NAG H 1 1555 1555 1.56 LINK ND2 ASN C 141 C1 NAG I 1 1555 1555 1.58 LINK ND2 ASN E 141 C1 NAG J 1 1555 1555 1.58 LINK ND2 ASN D 143 C1 NAG K 1 1555 1555 1.58 LINK ND2 ASN B 66 C1 NAG B 501 1555 1555 1.58 LINK ND2 ASN B 141 C1 NAG L 1 1555 1555 1.59 LINK ND2 ASN G 45 C1 NAG G 301 1555 1555 1.45 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 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44 LINK O6 BMA I 3 C1 MAN I 4 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44 LINK O6 BMA J 3 C1 MAN J 4 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O3 BMA K 3 C1 MAN K 4 1555 1555 1.44 LINK O6 BMA K 3 C1 MAN K 5 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44 LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.44 CISPEP 1 PHE A 135 PRO A 136 0 3.74 CISPEP 2 PHE C 135 PRO C 136 0 3.95 CISPEP 3 PHE E 135 PRO E 136 0 -1.71 CISPEP 4 PHE D 137 PRO D 138 0 5.84 CISPEP 5 PHE B 135 PRO B 136 0 2.90 CISPEP 6 PHE F 186 PRO F 187 0 -4.34 CISPEP 7 GLU F 188 PRO F 189 0 -5.61 CISPEP 8 SER G 26 PRO G 27 0 -1.41 CISPEP 9 ILE G 118 PRO G 119 0 -1.96 CISPEP 10 TYR G 164 PRO G 165 0 3.70 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