HEADER STRUCTURAL PROTEIN 20-FEB-15 4YCZ
TITLE Y-COMPLEX HUB (NUP85-NUP120-NUP145C-SEC13 COMPLEX) FROM M. THERMOPHILA
TITLE 2 (A.K.A. T. HETEROTHALLICA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUSION PROTEIN OF SEC13 AND NUP145C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: NUP85;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: NUP120;
COMPND 11 CHAIN: C;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THIELAVIA HETEROTHALLICA;
SOURCE 3 ORGANISM_TAXID: 573729;
SOURCE 4 STRAIN: ATCC 42464 / BCRC 31852 / DSM 1799;
SOURCE 5 GENE: MYCTH_2306744, MYCTH_2306912;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-LOBSTR;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: THIELAVIA HETEROTHALLICA;
SOURCE 11 ORGANISM_TAXID: 573729;
SOURCE 12 STRAIN: ATCC 42464 / BCRC 31852 / DSM 1799;
SOURCE 13 GENE: MYCTH_2059413;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21-LOBSTR;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: THIELAVIA HETEROTHALLICA;
SOURCE 19 ORGANISM_TAXID: 573729;
SOURCE 20 STRAIN: ATCC 42464 / BCRC 31852 / DSM 1799;
SOURCE 21 GENE: MYCTH_2296711;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: BL21-LOBSTR
KEYWDS STRUCTURAL PROTEIN COMPLEX, NUCLEAR PORE COMPLEX, MACROMOLECULAR
KEYWDS 2 ASSEMBLIES, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KELLEY,K.E.KNOCKENHAUER,T.U.SCHWARTZ
REVDAT 5 25-DEC-19 4YCZ 1 REMARK
REVDAT 4 20-SEP-17 4YCZ 1 SOURCE REMARK
REVDAT 3 27-MAY-15 4YCZ 1 JRNL
REVDAT 2 22-APR-15 4YCZ 1 JRNL
REVDAT 1 01-APR-15 4YCZ 0
JRNL AUTH K.KELLEY,K.E.KNOCKENHAUER,G.KABACHINSKI,T.U.SCHWARTZ
JRNL TITL ATOMIC STRUCTURE OF THE Y COMPLEX OF THE NUCLEAR PORE.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 22 425 2015
JRNL REFN ESSN 1545-9985
JRNL PMID 25822992
JRNL DOI 10.1038/NSMB.2998
REMARK 2
REMARK 2 RESOLUTION. 4.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1951)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 163.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 53648
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.322
REMARK 3 R VALUE (WORKING SET) : 0.319
REMARK 3 FREE R VALUE : 0.358
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.240
REMARK 3 FREE R VALUE TEST SET COUNT : 1975
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.810
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 10226
REMARK 3 ANGLE : 0.640 14023
REMARK 3 CHIRALITY : 0.027 1757
REMARK 3 PLANARITY : 0.004 1756
REMARK 3 DIHEDRAL : 9.003 3054
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4YCZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000207236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.23
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97890
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53692
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.100
REMARK 200 RESOLUTION RANGE LOW (A) : 163.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.19000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS-HCL PH 8.23, 0.7M AMMONIUM
REMARK 280 SULFATE, 20MM EDTA, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 52.49200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 106.01100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 52.49200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 106.01100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 77250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLY A 1
REMARK 465 PRO A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 MET A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 GLY A 8
REMARK 465 THR A 9
REMARK 465 GLN A 10
REMARK 465 VAL A 11
REMARK 465 ILE A 12
REMARK 465 ALA A 13
REMARK 465 ASN A 14
REMARK 465 SER A 15
REMARK 465 GLY A 16
REMARK 465 HIS A 17
REMARK 465 ASP A 18
REMARK 465 SER A 172
REMARK 465 SER A 173
REMARK 465 LYS A 174
REMARK 465 PRO A 175
REMARK 465 GLY A 176
REMARK 465 PRO A 177
REMARK 465 LYS A 178
REMARK 465 SER A 179
REMARK 465 THR A 180
REMARK 465 GLY A 181
REMARK 465 ASN A 182
REMARK 465 GLU A 240
REMARK 465 ASN A 263
REMARK 465 PHE A 264
REMARK 465 ASP A 265
REMARK 465 LYS A 1219
REMARK 465 THR A 1220
REMARK 465 ILE A 1221
REMARK 465 GLU A 1222
REMARK 465 GLU A 1223
REMARK 465 GLY A 1224
REMARK 465 GLY A 1225
REMARK 465 GLY A 1226
REMARK 465 GLY A 1227
REMARK 465 SER A 1228
REMARK 465 GLY A 1229
REMARK 465 GLY A 1230
REMARK 465 GLY A 1231
REMARK 465 GLY A 1232
REMARK 465 GLN A 1233
REMARK 465 ALA A 1234
REMARK 465 LYS A 1235
REMARK 465 GLY A 1236
REMARK 465 PRO A 1237
REMARK 465 THR A 1238
REMARK 465 GLN A 1239
REMARK 465 PRO A 1240
REMARK 465 GLU A 1241
REMARK 465 GLN A 1242
REMARK 465 ALA A 1243
REMARK 465 SER A 1244
REMARK 465 PRO A 1245
REMARK 465 ALA A 1246
REMARK 465 LYS A 1247
REMARK 465 GLY A 1248
REMARK 465 PHE A 1249
REMARK 465 VAL A 1250
REMARK 465 LYS A 1251
REMARK 465 TRP A 1252
REMARK 465 PRO A 1253
REMARK 465 TYR A 1254
REMARK 465 GLN A 1255
REMARK 465 GLN A 1256
REMARK 465 ARG A 1257
REMARK 465 PRO A 1258
REMARK 465 LYS A 1259
REMARK 465 ILE A 1260
REMARK 465 ASP A 1261
REMARK 465 GLN A 1262
REMARK 465 GLN A 1263
REMARK 465 GLU A 1264
REMARK 465 GLY A 1265
REMARK 465 PRO A 1266
REMARK 465 SER A 1267
REMARK 465 ILE A 1268
REMARK 465 PRO A 1269
REMARK 465 ARG A 1270
REMARK 465 SER A 1288
REMARK 465 LEU A 1289
REMARK 465 GLN A 1290
REMARK 465 PRO A 1291
REMARK 465 GLY A 1324
REMARK 465 GLN A 1325
REMARK 465 PRO A 1326
REMARK 465 ILE A 1327
REMARK 465 GLY A 1377
REMARK 465 LEU A 1378
REMARK 465 GLN A 1416
REMARK 465 ASP A 1417
REMARK 465 GLY A 1418
REMARK 465 ASP A 1419
REMARK 465 MET A 1420
REMARK 465 LYS A 1421
REMARK 465 ALA A 1422
REMARK 465 GLN A 1423
REMARK 465 LEU A 1424
REMARK 465 LYS A 1425
REMARK 465 ASP A 1426
REMARK 465 TRP A 1427
REMARK 465 ARG A 1428
REMARK 465 GLU A 1429
REMARK 465 SER A 1430
REMARK 465 ASN A 1431
REMARK 465 VAL A 1432
REMARK 465 LEU A 1433
REMARK 465 ALA A 1434
REMARK 465 GLU A 1435
REMARK 465 GLY A 1449
REMARK 465 ASN A 1450
REMARK 465 ALA A 1451
REMARK 465 GLY A 1452
REMARK 465 VAL A 1453
REMARK 465 CYS A 1454
REMARK 465 ALA A 1455
REMARK 465 GLY A 1456
REMARK 465 VAL A 1457
REMARK 465 LYS A 1458
REMARK 465 ASN A 1459
REMARK 465 VAL A 1460
REMARK 465 PRO A 1461
REMARK 465 ILE A 1462
REMARK 465 GLU A 1463
REMARK 465 ASN A 1464
REMARK 465 ARG A 1465
REMARK 465 VAL A 1466
REMARK 465 ASP A 1467
REMARK 465 SER A 1468
REMARK 465 PHE A 1469
REMARK 465 THR A 1470
REMARK 465 ILE A 1471
REMARK 465 SER A 1472
REMARK 465 GLN A 1473
REMARK 465 THR A 1537
REMARK 465 ARG A 1538
REMARK 465 LEU A 1539
REMARK 465 VAL A 1553
REMARK 465 SER A 1554
REMARK 465 PHE A 1555
REMARK 465 ILE A 1611
REMARK 465 GLY A 1612
REMARK 465 SER A 1613
REMARK 465 GLY A 1646
REMARK 465 ASP A 1647
REMARK 465 ILE A 1678
REMARK 465 ALA A 1679
REMARK 465 ARG A 1680
REMARK 465 LEU A 1699
REMARK 465 LYS A 1720
REMARK 465 GLN A 1785
REMARK 465 ALA A 1786
REMARK 465 LEU A 1787
REMARK 465 GLU A 1788
REMARK 465 VAL A 1789
REMARK 465 ILE A 1790
REMARK 465 CYS A 1791
REMARK 465 GLY B 249
REMARK 465 PRO B 250
REMARK 465 GLY B 251
REMARK 465 SER B 252
REMARK 465 GLU B 253
REMARK 465 PHE B 254
REMARK 465 GLU B 255
REMARK 465 LEU B 256
REMARK 465 MSE B 257
REMARK 465 TRP B 258
REMARK 465 LEU B 259
REMARK 465 ASP B 260
REMARK 465 MSE B 261
REMARK 465 PRO B 262
REMARK 465 SER B 263
REMARK 465 THR B 264
REMARK 465 ALA B 265
REMARK 465 GLU B 266
REMARK 465 THR B 267
REMARK 465 GLY B 268
REMARK 465 ALA B 269
REMARK 465 ASP B 270
REMARK 465 GLN B 271
REMARK 465 PRO B 272
REMARK 465 ALA B 273
REMARK 465 ALA B 274
REMARK 465 GLY B 275
REMARK 465 GLU B 276
REMARK 465 VAL B 277
REMARK 465 SER B 278
REMARK 465 ASP B 279
REMARK 465 LEU B 280
REMARK 465 LEU B 281
REMARK 465 MSE B 282
REMARK 465 LEU B 283
REMARK 465 ALA B 284
REMARK 465 THR B 285
REMARK 465 PRO B 286
REMARK 465 ALA B 287
REMARK 465 ALA B 288
REMARK 465 THR B 289
REMARK 465 GLU B 290
REMARK 465 ARG B 291
REMARK 465 VAL B 292
REMARK 465 ARG B 293
REMARK 465 ARG B 294
REMARK 465 GLU B 295
REMARK 465 ALA B 296
REMARK 465 GLU B 297
REMARK 465 ASP B 298
REMARK 465 ILE B 299
REMARK 465 PHE B 300
REMARK 465 ARG B 301
REMARK 465 ALA B 302
REMARK 465 SER B 303
REMARK 465 SER B 304
REMARK 465 PHE B 305
REMARK 465 ARG B 306
REMARK 465 ALA B 307
REMARK 465 GLY B 308
REMARK 465 GLY B 309
REMARK 465 ALA B 310
REMARK 465 ALA B 311
REMARK 465 ARG B 312
REMARK 465 ARG B 313
REMARK 465 GLY B 355
REMARK 465 VAL B 356
REMARK 465 GLY B 357
REMARK 465 GLU B 358
REMARK 465 ALA B 359
REMARK 465 GLU B 360
REMARK 465 ASP B 361
REMARK 465 GLU B 362
REMARK 465 GLN B 363
REMARK 465 LEU B 387
REMARK 465 PRO B 388
REMARK 465 ARG B 389
REMARK 465 PRO B 390
REMARK 465 THR B 391
REMARK 465 GLU B 392
REMARK 465 ASP B 393
REMARK 465 HIS B 394
REMARK 465 ALA B 395
REMARK 465 ALA B 396
REMARK 465 GLU B 397
REMARK 465 ILE B 398
REMARK 465 GLY B 399
REMARK 465 PRO B 400
REMARK 465 GLY B 401
REMARK 465 PRO B 402
REMARK 465 HIS B 403
REMARK 465 ALA B 404
REMARK 465 THR B 423
REMARK 465 ARG B 424
REMARK 465 TYR B 425
REMARK 465 GLU B 426
REMARK 465 GLU B 427
REMARK 465 GLY B 428
REMARK 465 GLY B 429
REMARK 465 LEU B 430
REMARK 465 ILE B 431
REMARK 465 ARG B 432
REMARK 465 ALA B 433
REMARK 465 GLU B 434
REMARK 465 ASP B 449
REMARK 465 LEU B 480
REMARK 465 ARG B 481
REMARK 465 GLY B 482
REMARK 465 ARG B 500
REMARK 465 ARG B 501
REMARK 465 GLY B 502
REMARK 465 GLN B 503
REMARK 465 ARG B 504
REMARK 465 GLY B 505
REMARK 465 GLU B 506
REMARK 465 GLY B 511
REMARK 465 GLN B 512
REMARK 465 ALA B 513
REMARK 465 LEU B 514
REMARK 465 GLU B 515
REMARK 465 GLY B 533
REMARK 465 PHE B 534
REMARK 465 ASP B 535
REMARK 465 GLY B 536
REMARK 465 ASN B 537
REMARK 465 TRP B 538
REMARK 465 GLU B 539
REMARK 465 ILE B 540
REMARK 465 TRP B 541
REMARK 465 SER B 542
REMARK 465 SER B 543
REMARK 465 ASP B 544
REMARK 465 TRP B 545
REMARK 465 LYS B 566
REMARK 465 ASP B 567
REMARK 465 SER B 568
REMARK 465 ALA B 569
REMARK 465 PHE B 570
REMARK 465 GLY B 571
REMARK 465 ALA B 572
REMARK 465 SER B 573
REMARK 465 ALA B 574
REMARK 465 PHE B 575
REMARK 465 SER B 576
REMARK 465 ALA B 577
REMARK 465 SER B 578
REMARK 465 ALA B 579
REMARK 465 ALA B 580
REMARK 465 SER B 581
REMARK 465 ALA B 582
REMARK 465 GLN B 583
REMARK 465 SER B 584
REMARK 465 ARG B 585
REMARK 465 GLN B 586
REMARK 465 SER B 587
REMARK 465 MSE B 588
REMARK 465 ALA B 589
REMARK 465 GLY B 590
REMARK 465 LEU B 591
REMARK 465 ALA B 592
REMARK 465 ARG B 593
REMARK 465 ARG B 594
REMARK 465 ALA B 595
REMARK 465 GLU B 596
REMARK 465 SER B 597
REMARK 465 GLN B 598
REMARK 465 VAL B 599
REMARK 465 PRO B 600
REMARK 465 PHE B 636
REMARK 465 GLY B 637
REMARK 465 TRP B 638
REMARK 465 TRP B 639
REMARK 465 ASP B 640
REMARK 465 GLU B 641
REMARK 465 ARG B 642
REMARK 465 ALA B 643
REMARK 465 SER B 644
REMARK 465 ARG B 645
REMARK 465 THR B 646
REMARK 465 GLU B 647
REMARK 465 LYS B 648
REMARK 465 PRO B 649
REMARK 465 LEU B 650
REMARK 465 SER B 651
REMARK 465 THR B 652
REMARK 465 SER B 653
REMARK 465 GLN B 654
REMARK 465 SER B 655
REMARK 465 LEU B 656
REMARK 465 SER B 657
REMARK 465 ARG B 658
REMARK 465 SER B 659
REMARK 465 GLN B 660
REMARK 465 ALA B 661
REMARK 465 LEU B 662
REMARK 465 VAL B 663
REMARK 465 LEU B 664
REMARK 465 ALA B 665
REMARK 465 SER B 666
REMARK 465 ALA B 667
REMARK 465 PRO B 668
REMARK 465 HIS B 691
REMARK 465 PHE B 692
REMARK 465 ASN B 693
REMARK 465 SER B 694
REMARK 465 GLN B 695
REMARK 465 ASN B 696
REMARK 465 ALA B 697
REMARK 465 PRO B 739
REMARK 465 PRO B 740
REMARK 465 HIS B 741
REMARK 465 ARG B 742
REMARK 465 PRO B 743
REMARK 465 SER B 744
REMARK 465 GLY B 745
REMARK 465 VAL B 746
REMARK 465 TYR B 747
REMARK 465 GLY B 748
REMARK 465 LEU B 749
REMARK 465 GLU B 750
REMARK 465 ASP B 751
REMARK 465 LEU B 752
REMARK 465 ASP B 753
REMARK 465 MSE B 754
REMARK 465 ASP B 755
REMARK 465 ASP B 756
REMARK 465 LEU B 757
REMARK 465 GLU B 758
REMARK 465 VAL B 759
REMARK 465 LEU B 760
REMARK 465 GLY B 761
REMARK 465 MSE B 762
REMARK 465 ASP B 763
REMARK 465 PRO B 764
REMARK 465 GLY B 765
REMARK 465 ALA B 766
REMARK 465 PRO B 767
REMARK 465 ASP B 768
REMARK 465 SER B 798
REMARK 465 GLY B 799
REMARK 465 THR B 800
REMARK 465 SER B 801
REMARK 465 LYS B 802
REMARK 465 ASP B 816
REMARK 465 SER B 817
REMARK 465 SER B 909
REMARK 465 THR B 910
REMARK 465 ALA B 911
REMARK 465 PHE B 912
REMARK 465 ASP B 965
REMARK 465 ASN B 966
REMARK 465 GLU B 967
REMARK 465 ASP B 968
REMARK 465 ALA B 969
REMARK 465 LEU B 970
REMARK 465 ASN B 996
REMARK 465 ILE B 997
REMARK 465 ARG B 998
REMARK 465 GLY B 999
REMARK 465 GLY B 1000
REMARK 465 LEU B 1001
REMARK 465 TYR B 1002
REMARK 465 ASP B 1003
REMARK 465 GLN B 1004
REMARK 465 THR B 1005
REMARK 465 ARG B 1006
REMARK 465 ASP B 1007
REMARK 465 GLY B 1008
REMARK 465 ILE B 1009
REMARK 465 VAL B 1010
REMARK 465 SER B 1011
REMARK 465 ASP B 1030
REMARK 465 ASN B 1031
REMARK 465 THR B 1032
REMARK 465 ASN B 1033
REMARK 465 VAL B 1034
REMARK 465 HIS B 1035
REMARK 465 HIS B 1036
REMARK 465 GLY B 1037
REMARK 465 GLN B 1038
REMARK 465 LEU B 1039
REMARK 465 ALA B 1040
REMARK 465 THR B 1041
REMARK 465 PRO B 1042
REMARK 465 VAL B 1043
REMARK 465 ILE B 1044
REMARK 465 GLY B 1084
REMARK 465 LEU B 1085
REMARK 465 LYS B 1086
REMARK 465 GLY B 1087
REMARK 465 SER B 1088
REMARK 465 THR B 1089
REMARK 465 PRO B 1090
REMARK 465 ALA B 1091
REMARK 465 ASP B 1092
REMARK 465 LEU B 1093
REMARK 465 LEU B 1094
REMARK 465 LYS B 1095
REMARK 465 LYS B 1096
REMARK 465 SER B 1097
REMARK 465 ALA B 1098
REMARK 465 GLY B 1099
REMARK 465 PRO B 1100
REMARK 465 GLY B 1101
REMARK 465 PRO B 1102
REMARK 465 GLY B 1103
REMARK 465 GLY B 1104
REMARK 465 SER B 1105
REMARK 465 GLY B 1106
REMARK 465 ASN B 1107
REMARK 465 ALA B 1108
REMARK 465 MSE B 1109
REMARK 465 LEU B 1110
REMARK 465 ALA B 1111
REMARK 465 GLY B 1129
REMARK 465 GLY B 1130
REMARK 465 LEU B 1131
REMARK 465 GLY B 1132
REMARK 465 LYS B 1133
REMARK 465 VAL B 1134
REMARK 465 ALA B 1135
REMARK 465 VAL B 1136
REMARK 465 LYS B 1137
REMARK 465 ARG B 1138
REMARK 465 ARG B 1139
REMARK 465 GLY B 1140
REMARK 465 TRP B 1141
REMARK 465 ASP B 1142
REMARK 465 TRP B 1143
REMARK 465 ARG B 1144
REMARK 465 SER B 1145
REMARK 465 GLU B 1146
REMARK 465 VAL B 1147
REMARK 465 THR B 1148
REMARK 465 ALA B 1149
REMARK 465 LYS B 1150
REMARK 465 THR B 1151
REMARK 465 LYS B 1152
REMARK 465 ASP B 1177
REMARK 465 GLU B 1178
REMARK 465 MSE B 1179
REMARK 465 VAL B 1180
REMARK 465 TRP B 1181
REMARK 465 GLY C 943
REMARK 465 PRO C 944
REMARK 465 GLY C 945
REMARK 465 SER C 946
REMARK 465 GLU C 947
REMARK 465 PHE C 948
REMARK 465 GLU C 949
REMARK 465 LEU C 950
REMARK 465 MET C 951
REMARK 465 GLN C 952
REMARK 465 GLY C 953
REMARK 465 GLY C 954
REMARK 465 SER C 955
REMARK 465 SER C 956
REMARK 465 THR C 957
REMARK 465 ASN C 958
REMARK 465 HIS C 959
REMARK 465 GLU C 960
REMARK 465 THR C 961
REMARK 465 ALA C 962
REMARK 465 GLY C 963
REMARK 465 LEU C 964
REMARK 465 ARG C 965
REMARK 465 THR C 966
REMARK 465 GLU C 967
REMARK 465 ASP C 993
REMARK 465 ASP C 994
REMARK 465 GLU C 995
REMARK 465 ALA C 996
REMARK 465 ASP C 1043
REMARK 465 VAL C 1044
REMARK 465 LEU C 1045
REMARK 465 ASN C 1046
REMARK 465 GLY C 1047
REMARK 465 GLU C 1083
REMARK 465 GLY C 1084
REMARK 465 ASP C 1085
REMARK 465 LYS C 1086
REMARK 465 VAL C 1087
REMARK 465 ILE C 1088
REMARK 465 ALA C 1089
REMARK 465 ASN C 1090
REMARK 465 GLU C 1091
REMARK 465 HIS C 1092
REMARK 465 GLY C 1093
REMARK 465 ASN C 1094
REMARK 465 GLU C 1095
REMARK 465 ASP C 1096
REMARK 465 VAL C 1127
REMARK 465 LEU C 1128
REMARK 465 PRO C 1129
REMARK 465 GLY C 1130
REMARK 465 ASP C 1131
REMARK 465 GLY C 1132
REMARK 465 ARG C 1133
REMARK 465 GLY C 1134
REMARK 465 GLY C 1135
REMARK 465 ASP C 1136
REMARK 465 ASP C 1137
REMARK 465 ALA C 1138
REMARK 465 ASP C 1139
REMARK 465 GLY C 1140
REMARK 465 ASP C 1141
REMARK 465 ARG C 1142
REMARK 465 ASN C 1143
REMARK 465 GLY C 1144
REMARK 465 GLY C 1145
REMARK 465 LYS C 1146
REMARK 465 ALA C 1147
REMARK 465 GLY C 1148
REMARK 465 GLY C 1167
REMARK 465 ALA C 1168
REMARK 465 ASP C 1169
REMARK 465 ALA C 1170
REMARK 465 ALA C 1171
REMARK 465 LYS C 1172
REMARK 465 GLY C 1173
REMARK 465 ASP C 1174
REMARK 465 GLU C 1175
REMARK 465 MET C 1176
REMARK 465 ALA C 1177
REMARK 465 ALA C 1178
REMARK 465 GLU C 1179
REMARK 465 GLN C 1197
REMARK 465 ASN C 1198
REMARK 465 LEU C 1199
REMARK 465 PRO C 1200
REMARK 465 GLN C 1225
REMARK 465 ASN C 1226
REMARK 465 ASN C 1227
REMARK 465 GLN C 1228
REMARK 465 PHE C 1229
REMARK 465 GLY C 1230
REMARK 465 PHE C 1231
REMARK 465 GLY C 1232
REMARK 465 ALA C 1233
REMARK 465 GLU C 1234
REMARK 465 ASP C 1235
REMARK 465 ASP C 1236
REMARK 465 LEU C 1237
REMARK 465 MET C 1238
REMARK 465 ASP C 1239
REMARK 465 LEU C 1240
REMARK 465 ALA C 1241
REMARK 465 GLY C 1242
REMARK 465 GLY C 1243
REMARK 465 SER C 1244
REMARK 465 GLY C 1245
REMARK 465 HIS C 1246
REMARK 465 HIS C 1247
REMARK 465 HIS C 1248
REMARK 465 HIS C 1249
REMARK 465 HIS C 1250
REMARK 465 HIS C 1251
REMARK 465 HIS C 1252
REMARK 465 HIS C 1253
REMARK 465 HIS C 1254
REMARK 465 HIS C 1255
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 19 CG OD1 OD2
REMARK 470 GLU A 50 CG CD OE1 OE2
REMARK 470 ARG A 53 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 74 CG CD CE NZ
REMARK 470 GLN A 99 CG CD OE1 NE2
REMARK 470 ASN A 142 CG OD1 ND2
REMARK 470 SER A 143 OG
REMARK 470 PHE A 149 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 207 CG CD CE NZ
REMARK 470 ARG A 210 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 213 CG CD1 CD2
REMARK 470 ARG A 221 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 231 CG CD OE1 NE2
REMARK 470 LYS A 232 CG CD CE NZ
REMARK 470 ASP A 250 CG OD1 OD2
REMARK 470 ASN A 253 CG OD1 ND2
REMARK 470 LEU A 255 CG CD1 CD2
REMARK 470 GLN A 256 CG CD OE1 NE2
REMARK 470 TRP A 257 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 257 CZ3 CH2
REMARK 470 ASN A 258 CG OD1 ND2
REMARK 470 CYS A 259 SG
REMARK 470 LYS A 260 CG CD CE NZ
REMARK 470 VAL A 261 CG1 CG2
REMARK 470 LEU A 262 CG CD1 CD2
REMARK 470 VAL A 279 CG1 CG2
REMARK 470 ASN A 287 CG OD1 ND2
REMARK 470 LYS A 288 CG CD CE NZ
REMARK 470 VAL A 289 CG1 CG2
REMARK 470 LYS A 293 CG CD CE NZ
REMARK 470 GLU A 299 CG CD OE1 OE2
REMARK 470 GLU A 301 CG CD OE1 OE2
REMARK 470 THR A1271 OG1 CG2
REMARK 470 ASN A1272 CG OD1 ND2
REMARK 470 LEU A1278 CG CD1 CD2
REMARK 470 LEU A1279 CG CD1 CD2
REMARK 470 HIS A1283 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A1284 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A1286 CG CD OE1 OE2
REMARK 470 ASP A1293 CG OD1 OD2
REMARK 470 THR A1295 OG1 CG2
REMARK 470 GLU A1300 CG CD OE1 OE2
REMARK 470 GLU A1301 CG CD OE1 OE2
REMARK 470 GLU A1307 CG CD OE1 OE2
REMARK 470 ASN A1308 CG OD1 ND2
REMARK 470 LEU A1309 CG CD1 CD2
REMARK 470 ARG A1311 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1312 CG CD1 CD2
REMARK 470 GLN A1313 CG CD OE1 NE2
REMARK 470 ARG A1314 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1317 CG OD1 OD2
REMARK 470 SER A1318 OG
REMARK 470 VAL A1319 CG1 CG2
REMARK 470 SER A1320 OG
REMARK 470 PHE A1321 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A1322 CG CD CE NZ
REMARK 470 GLU A1323 CG CD OE1 OE2
REMARK 470 SER A1329 OG
REMARK 470 GLU A1331 CG CD OE1 OE2
REMARK 470 ARG A1333 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1334 CG CD OE1 OE2
REMARK 470 LEU A1335 CG CD1 CD2
REMARK 470 GLN A1337 CG CD OE1 NE2
REMARK 470 ASP A1339 CG OD1 OD2
REMARK 470 ASP A1351 CG OD1 OD2
REMARK 470 ASN A1352 CG OD1 ND2
REMARK 470 TYR A1354 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A1361 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1362 CG CD OE1 NE2
REMARK 470 LEU A1363 CG CD1 CD2
REMARK 470 SER A1365 OG
REMARK 470 GLU A1366 CG CD OE1 OE2
REMARK 470 THR A1368 OG1 CG2
REMARK 470 ASP A1369 CG OD1 OD2
REMARK 470 ARG A1370 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1374 CG CD OE1 NE2
REMARK 470 GLU A1375 CG CD OE1 OE2
REMARK 470 GLU A1379 CG CD OE1 OE2
REMARK 470 GLU A1380 CG CD OE1 OE2
REMARK 470 LYS A1381 CG CD CE NZ
REMARK 470 ILE A1384 CG1 CG2 CD1
REMARK 470 ASN A1389 CG OD1 ND2
REMARK 470 ARG A1390 CG CD NE CZ NH1 NH2
REMARK 470 VAL A1391 CG1 CG2
REMARK 470 ASP A1393 CG OD1 OD2
REMARK 470 ASN A1403 CG OD1 ND2
REMARK 470 PHE A1404 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A1405 CG CD NE CZ NH1 NH2
REMARK 470 THR A1408 OG1 CG2
REMARK 470 SER A1411 OG
REMARK 470 ILE A1413 CG1 CG2 CD1
REMARK 470 PHE A1436 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A1437 OG
REMARK 470 GLN A1438 CG CD OE1 NE2
REMARK 470 ARG A1441 CG CD NE CZ NH1 NH2
REMARK 470 ILE A1443 CG1 CG2 CD1
REMARK 470 TYR A1444 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A1445 CG CD OE1 OE2
REMARK 470 LEU A1446 CG CD1 CD2
REMARK 470 LEU A1447 CG CD1 CD2
REMARK 470 ARG A1474 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1475 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A1478 CG OD1 OD2
REMARK 470 TRP A1479 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1479 CZ3 CH2
REMARK 470 MET A1480 CG SD CE
REMARK 470 LEU A1485 CG CD1 CD2
REMARK 470 THR A1490 OG1 CG2
REMARK 470 THR A1491 OG1 CG2
REMARK 470 THR A1494 OG1 CG2
REMARK 470 ASN A1496 CG OD1 ND2
REMARK 470 GLU A1499 CG CD OE1 OE2
REMARK 470 ARG A1502 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1505 CG CD OE1 NE2
REMARK 470 GLU A1509 CG CD OE1 OE2
REMARK 470 GLN A1510 CG CD OE1 NE2
REMARK 470 ASP A1511 CG OD1 OD2
REMARK 470 LYS A1512 CG CD CE NZ
REMARK 470 GLU A1513 CG CD OE1 OE2
REMARK 470 ASP A1517 CG OD1 OD2
REMARK 470 SER A1518 OG
REMARK 470 LEU A1520 CG CD1 CD2
REMARK 470 TRP A1521 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1521 CZ3 CH2
REMARK 470 SER A1522 OG
REMARK 470 ASN A1529 CG OD1 ND2
REMARK 470 ASP A1533 CG OD1 OD2
REMARK 470 TRP A1534 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1534 CZ3 CH2
REMARK 470 SER A1535 OG
REMARK 470 ASP A1536 CG OD1 OD2
REMARK 470 LEU A1542 CG CD1 CD2
REMARK 470 THR A1544 OG1 CG2
REMARK 470 LYS A1545 CG CD CE NZ
REMARK 470 ILE A1547 CG1 CG2 CD1
REMARK 470 LYS A1552 CG CD CE NZ
REMARK 470 ASP A1558 CG OD1 OD2
REMARK 470 GLU A1561 CG CD OE1 OE2
REMARK 470 LYS A1562 CG CD CE NZ
REMARK 470 LYS A1565 CG CD CE NZ
REMARK 470 SER A1567 OG
REMARK 470 TYR A1570 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A1572 OG
REMARK 470 LEU A1574 CG CD1 CD2
REMARK 470 THR A1575 OG1 CG2
REMARK 470 GLN A1579 CG CD OE1 NE2
REMARK 470 THR A1584 OG1 CG2
REMARK 470 LEU A1588 CG CD1 CD2
REMARK 470 GLN A1589 CG CD OE1 NE2
REMARK 470 SER A1591 OG
REMARK 470 ASP A1592 CG OD1 OD2
REMARK 470 SER A1595 OG
REMARK 470 ARG A1596 CG CD NE CZ NH1 NH2
REMARK 470 HIS A1607 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A1609 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1610 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1615 CG CD NE CZ NH1 NH2
REMARK 470 ASN A1616 CG OD1 ND2
REMARK 470 ASN A1618 CG OD1 ND2
REMARK 470 SER A1622 OG
REMARK 470 SER A1623 OG
REMARK 470 ARG A1625 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1626 CG CD CE NZ
REMARK 470 PHE A1627 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A1631 CG CD OE1 OE2
REMARK 470 THR A1632 OG1 CG2
REMARK 470 GLU A1636 CG CD OE1 OE2
REMARK 470 LYS A1638 CG CD CE NZ
REMARK 470 ARG A1645 CG CD NE CZ NH1 NH2
REMARK 470 SER A1648 OG
REMARK 470 GLN A1649 CG CD OE1 NE2
REMARK 470 GLN A1650 CG CD OE1 NE2
REMARK 470 GLU A1651 CG CD OE1 OE2
REMARK 470 GLN A1659 CG CD OE1 NE2
REMARK 470 ASN A1660 CG OD1 ND2
REMARK 470 TYR A1661 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A1663 CG CD OE1 OE2
REMARK 470 ASN A1665 CG OD1 ND2
REMARK 470 GLN A1666 CG CD OE1 NE2
REMARK 470 PHE A1668 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A1671 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1675 CG OD1 OD2
REMARK 470 VAL A1677 CG1 CG2
REMARK 470 ASP A1681 CG OD1 OD2
REMARK 470 PHE A1682 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A1683 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1693 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A1694 CG CD CE NZ
REMARK 470 LYS A1698 CG CD CE NZ
REMARK 470 GLN A1700 CG CD OE1 NE2
REMARK 470 ASP A1701 CG OD1 OD2
REMARK 470 TRP A1702 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1702 CZ3 CH2
REMARK 470 ARG A1704 CG CD NE CZ NH1 NH2
REMARK 470 TYR A1709 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A1716 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1717 CG CD1 CD2
REMARK 470 GLN A1721 CG CD OE1 NE2
REMARK 470 LYS A1726 CG CD CE NZ
REMARK 470 PHE A1727 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A1728 CG OD1 OD2
REMARK 470 HIS A1729 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A1730 CG CD OE1 NE2
REMARK 470 ASP A1733 CG OD1 OD2
REMARK 470 VAL A1736 CG1 CG2
REMARK 470 ARG A1739 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1741 CG CD OE1 NE2
REMARK 470 THR A1742 OG1 CG2
REMARK 470 ARG A1747 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1748 CG CD OE1 NE2
REMARK 470 GLU A1749 CG CD OE1 OE2
REMARK 470 CYS A1762 SG
REMARK 470 ARG A1763 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1766 CG OD1 OD2
REMARK 470 ARG A1768 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1772 CG CD1 CD2
REMARK 470 ASP A1776 CG OD1 OD2
REMARK 470 ARG A1778 CG CD NE CZ NH1 NH2
REMARK 470 SER A1779 OG
REMARK 470 LYS A1780 CG CD CE NZ
REMARK 470 TYR A1781 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A1782 CG SD CE
REMARK 470 ARG A1783 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 315 CG CD OE1 OE2
REMARK 470 ARG B 317 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 323 CG CD CE NZ
REMARK 470 ASP B 324 CG OD1 OD2
REMARK 470 GLN B 327 CG CD OE1 NE2
REMARK 470 GLN B 328 CG CD OE1 NE2
REMARK 470 GLU B 336 CG CD OE1 OE2
REMARK 470 GLN B 339 CG CD OE1 NE2
REMARK 470 GLU B 345 CG CD OE1 OE2
REMARK 470 ASP B 346 CG OD1 OD2
REMARK 470 ARG B 350 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 352 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 353 CG OD1 OD2
REMARK 470 GLU B 354 CG CD OE1 OE2
REMARK 470 LYS B 364 CG CD CE NZ
REMARK 470 ASP B 366 CG OD1 OD2
REMARK 470 ASP B 367 CG OD1 OD2
REMARK 470 ASP B 385 CG OD1 OD2
REMARK 470 GLU B 386 CG CD OE1 OE2
REMARK 470 GLU B 408 CG CD OE1 OE2
REMARK 470 LYS B 409 CG CD CE NZ
REMARK 470 HIS B 422 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 442 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 445 CG OD1 ND2
REMARK 470 GLU B 446 CG CD OE1 OE2
REMARK 470 HIS B 448 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 456 CG OD1 OD2
REMARK 470 ASP B 457 CG OD1 OD2
REMARK 470 ARG B 460 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 462 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 483 CG CD CE NZ
REMARK 470 ASP B 486 CG OD1 OD2
REMARK 470 ARG B 489 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 492 CG OD1 OD2
REMARK 470 GLN B 493 CG CD OE1 NE2
REMARK 470 HIS B 498 CG ND1 CD2 CE1 NE2
REMARK 470 ASN B 516 CG OD1 ND2
REMARK 470 GLN B 518 CG CD OE1 NE2
REMARK 470 ARG B 519 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 522 CG OD1 OD2
REMARK 470 GLU B 523 CG CD OE1 OE2
REMARK 470 GLU B 529 CG CD OE1 OE2
REMARK 470 ARG B 549 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 551 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 553 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 557 CG CD OE1 OE2
REMARK 470 ARG B 560 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 561 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 564 CG CD OE1 OE2
REMARK 470 GLU B 605 CG CD OE1 OE2
REMARK 470 ASN B 608 CG OD1 ND2
REMARK 470 GLN B 617 CG CD OE1 NE2
REMARK 470 GLN B 618 CG CD OE1 NE2
REMARK 470 GLU B 623 CG CD OE1 OE2
REMARK 470 GLN B 626 CG CD OE1 NE2
REMARK 470 ASN B 670 CG OD1 ND2
REMARK 470 ASP B 676 CG OD1 OD2
REMARK 470 ARG B 680 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 683 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 687 CG CD OE1 OE2
REMARK 470 ASP B 689 CG OD1 OD2
REMARK 470 GLU B 699 CG CD OE1 OE2
REMARK 470 GLU B 707 CG CD OE1 OE2
REMARK 470 LYS B 711 CG CD CE NZ
REMARK 470 ARG B 718 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 730 CG CD OE1 OE2
REMARK 470 SER B 733 OG
REMARK 470 LYS B 736 CG CD CE NZ
REMARK 470 TRP B 737 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 737 CZ3 CH2
REMARK 470 LEU B 738 CG CD1 CD2
REMARK 470 GLU B 769 CG CD OE1 OE2
REMARK 470 VAL B 770 CG1 CG2
REMARK 470 ASP B 771 CG OD1 OD2
REMARK 470 LYS B 774 CG CD CE NZ
REMARK 470 ASP B 775 CG OD1 OD2
REMARK 470 GLN B 780 CG CD OE1 NE2
REMARK 470 GLN B 783 CG CD OE1 NE2
REMARK 470 ASP B 787 CG OD1 OD2
REMARK 470 TYR B 788 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 789 CG CD OE1 OE2
REMARK 470 LEU B 791 CG CD1 CD2
REMARK 470 SER B 792 OG
REMARK 470 SER B 793 OG
REMARK 470 VAL B 794 CG1 CG2
REMARK 470 GLN B 795 CG CD OE1 NE2
REMARK 470 ASP B 796 CG OD1 OD2
REMARK 470 ARG B 797 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 803 CG OD1 OD2
REMARK 470 ARG B 814 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 819 CG CD OE1 OE2
REMARK 470 ARG B 820 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 822 CG CD OE1 OE2
REMARK 470 GLU B 823 CG CD OE1 OE2
REMARK 470 ARG B 826 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 827 CG OD1 OD2
REMARK 470 GLU B 830 CG CD OE1 OE2
REMARK 470 GLN B 834 CG CD OE1 NE2
REMARK 470 GLN B 835 CG CD OE1 NE2
REMARK 470 HIS B 837 CG ND1 CD2 CE1 NE2
REMARK 470 VAL B 838 CG1 CG2
REMARK 470 ASP B 839 CG OD1 OD2
REMARK 470 ASN B 841 CG OD1 ND2
REMARK 470 ASP B 845 CG OD1 OD2
REMARK 470 ARG B 846 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 852 CG OD1 ND2
REMARK 470 GLU B 853 CG CD OE1 OE2
REMARK 470 GLU B 858 CG CD OE1 OE2
REMARK 470 GLU B 861 CG CD OE1 OE2
REMARK 470 ASP B 862 CG OD1 OD2
REMARK 470 GLU B 865 CG CD OE1 OE2
REMARK 470 ARG B 877 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 880 CG CD OE1 OE2
REMARK 470 ARG B 890 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 892 CG OD1 ND2
REMARK 470 LYS B 893 CG CD CE NZ
REMARK 470 ARG B 895 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 896 CG CD OE1 OE2
REMARK 470 ASN B 899 CG OD1 ND2
REMARK 470 GLN B 908 CG CD OE1 NE2
REMARK 470 ASP B 917 CG OD1 OD2
REMARK 470 ASP B 919 CG OD1 OD2
REMARK 470 ASP B 920 CG OD1 OD2
REMARK 470 TYR B 921 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 924 CG CD CE NZ
REMARK 470 ASN B 927 CG OD1 ND2
REMARK 470 ARG B 929 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 930 CG CD CE NZ
REMARK 470 GLU B 934 CG CD OE1 OE2
REMARK 470 GLN B 935 CG CD OE1 NE2
REMARK 470 GLN B 939 CG CD OE1 NE2
REMARK 470 GLU B 942 CG CD OE1 OE2
REMARK 470 GLU B 945 CG CD OE1 OE2
REMARK 470 LYS B 949 CG CD CE NZ
REMARK 470 ARG B 958 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 959 CG CD OE1 NE2
REMARK 470 ASP B 962 CG OD1 OD2
REMARK 470 ARG B 964 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 972 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 978 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 979 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 980 CG CD CE NZ
REMARK 470 GLN B 981 CG CD OE1 NE2
REMARK 470 ASP B 994 CG OD1 OD2
REMARK 470 ASP B 995 CG OD1 OD2
REMARK 470 GLU B1012 CG CD OE1 OE2
REMARK 470 ASP B1013 CG OD1 OD2
REMARK 470 ASP B1028 CG OD1 OD2
REMARK 470 ASP B1047 CG OD1 OD2
REMARK 470 GLN B1048 CG CD OE1 NE2
REMARK 470 ASP B1050 CG OD1 OD2
REMARK 470 LYS B1054 CG CD CE NZ
REMARK 470 GLU B1057 CG CD OE1 OE2
REMARK 470 ASP B1058 CG OD1 OD2
REMARK 470 ASN B1068 CG OD1 ND2
REMARK 470 ASP B1071 CG OD1 OD2
REMARK 470 GLU B1072 CG CD OE1 OE2
REMARK 470 GLN B1075 CG CD OE1 NE2
REMARK 470 GLN B1119 CG CD OE1 NE2
REMARK 470 GLN B1121 CG CD OE1 NE2
REMARK 470 ARG B1122 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1154 CG CD OE1 OE2
REMARK 470 ASP B1155 CG OD1 OD2
REMARK 470 ARG B1158 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1159 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1166 CG CD CE NZ
REMARK 470 ASP B1167 CG OD1 OD2
REMARK 470 MET C 968 CG SD CE
REMARK 470 ARG C 971 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 981 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 983 CG CD OE1 OE2
REMARK 470 GLU C 984 CG CD OE1 OE2
REMARK 470 HIS C 986 CG ND1 CD2 CE1 NE2
REMARK 470 MET C 992 CG SD CE
REMARK 470 MET C 997 CG SD CE
REMARK 470 ARG C1003 CG CD NE CZ NH1 NH2
REMARK 470 ARG C1004 CG CD NE CZ NH1 NH2
REMARK 470 GLU C1007 CG CD OE1 OE2
REMARK 470 MET C1009 CG SD CE
REMARK 470 GLU C1011 CG CD OE1 OE2
REMARK 470 GLU C1017 CG CD OE1 OE2
REMARK 470 PHE C1023 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C1029 CG CD CE NZ
REMARK 470 GLU C1036 CG CD OE1 OE2
REMARK 470 LYS C1037 CG CD CE NZ
REMARK 470 ARG C1042 CG CD NE CZ NH1 NH2
REMARK 470 HIS C1051 CG ND1 CD2 CE1 NE2
REMARK 470 GLN C1052 CG CD OE1 NE2
REMARK 470 ARG C1058 CG CD NE CZ NH1 NH2
REMARK 470 ASP C1073 CG OD1 OD2
REMARK 470 GLN C1076 CG CD OE1 NE2
REMARK 470 ARG C1079 CG CD NE CZ NH1 NH2
REMARK 470 ARG C1080 CG CD NE CZ NH1 NH2
REMARK 470 ASP C1099 CG OD1 OD2
REMARK 470 THR C1100 OG1 CG2
REMARK 470 GLN C1101 CG CD OE1 NE2
REMARK 470 ARG C1104 CG CD NE CZ NH1 NH2
REMARK 470 GLN C1105 CG CD OE1 NE2
REMARK 470 ASN C1111 CG OD1 ND2
REMARK 470 GLU C1120 CG CD OE1 OE2
REMARK 470 GLU C1125 CG CD OE1 OE2
REMARK 470 ASP C1149 CG OD1 OD2
REMARK 470 ASP C1150 CG OD1 OD2
REMARK 470 GLU C1152 CG CD OE1 OE2
REMARK 470 ASP C1154 CG OD1 OD2
REMARK 470 ASP C1156 CG OD1 OD2
REMARK 470 GLU C1157 CG CD OE1 OE2
REMARK 470 LYS C1160 CG CD CE NZ
REMARK 470 LYS C1161 CG CD CE NZ
REMARK 470 GLU C1180 CG CD OE1 OE2
REMARK 470 ASP C1181 CG OD1 OD2
REMARK 470 GLU C1186 CG CD OE1 OE2
REMARK 470 LYS C1187 CG CD CE NZ
REMARK 470 LYS C1189 CG CD CE NZ
REMARK 470 ARG C1190 CG CD NE CZ NH1 NH2
REMARK 470 ARG C1194 CG CD NE CZ NH1 NH2
REMARK 470 ASN C1195 CG OD1 ND2
REMARK 470 ARG C1203 CG CD NE CZ NH1 NH2
REMARK 470 ASP C1209 CG OD1 OD2
REMARK 470 ARG C1211 CG CD NE CZ NH1 NH2
REMARK 470 GLN C1213 CG CD OE1 NE2
REMARK 470 GLN C1215 CG CD OE1 NE2
REMARK 470 GLN C1216 CG CD OE1 NE2
REMARK 470 GLU C1217 CG CD OE1 OE2
REMARK 470 ASP C1219 CG OD1 OD2
REMARK 470 ARG C1220 CG CD NE CZ NH1 NH2
REMARK 470 ILE C1221 CG1 CG2 CD1
REMARK 470 VAL C1222 CG1 CG2
REMARK 470 ILE C1224 CG1 CG2 CD1
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 ARG A 31 -18.51 -141.42
REMARK 500 ASP A 39 35.29 -92.62
REMARK 500 THR A 55 -69.41 -120.57
REMARK 500 ILE A 101 -66.46 -90.43
REMARK 500 LEU A 106 48.78 -151.87
REMARK 500 CYS A 123 79.27 -112.79
REMARK 500 LEU A 125 105.36 -161.83
REMARK 500 SER A 130 53.45 -92.05
REMARK 500 ASN A 142 -80.39 -99.50
REMARK 500 TRP A 144 138.97 -19.76
REMARK 500 ALA A 151 -157.73 -124.75
REMARK 500 THR A 165 79.07 -107.12
REMARK 500 SER A 169 -56.14 -123.58
REMARK 500 THR A 205 -159.47 -131.87
REMARK 500 THR A 214 70.93 47.91
REMARK 500 PRO A 251 56.66 -61.26
REMARK 500 ALA A 252 -159.78 -170.76
REMARK 500 SER A 276 43.54 -141.64
REMARK 500 TRP A1273 -81.75 -123.34
REMARK 500 THR A1295 73.12 -153.59
REMARK 500 PHE A1321 -35.87 -138.69
REMARK 500 GLN A1337 -124.62 58.78
REMARK 500 ASP A1351 80.80 -63.54
REMARK 500 TYR A1354 44.84 -96.19
REMARK 500 ASN A1403 -123.21 58.84
REMARK 500 THR A1491 -163.53 -102.60
REMARK 500 ASP A1517 76.33 53.12
REMARK 500 ASN A1529 73.32 55.40
REMARK 500 GLN A1530 87.00 -66.59
REMARK 500 GLU A1531 -158.47 -141.77
REMARK 500 ASP A1533 -74.20 -125.71
REMARK 500 THR A1550 -90.19 -87.33
REMARK 500 ASP A1558 -63.57 71.75
REMARK 500 ALA A1559 56.24 -66.58
REMARK 500 GLN A1577 41.17 -94.37
REMARK 500 GLN A1589 52.07 -110.65
REMARK 500 ALA A1620 -51.06 -120.43
REMARK 500 TYR A1661 -60.66 -94.36
REMARK 500 SER A1662 -104.28 55.50
REMARK 500 PHE A1727 -3.28 -140.89
REMARK 500 HIS A1743 -136.47 -79.96
REMARK 500 ARG A1763 -158.49 -109.77
REMARK 500 PRO A1767 -154.29 -83.77
REMARK 500 PHE A1770 -82.21 -118.32
REMARK 500 TYR B 451 -26.59 -166.12
REMARK 500 LEU B 470 35.26 -97.49
REMARK 500 GLN B 493 55.31 -109.14
REMARK 500 TRP B 496 -136.55 55.15
REMARK 500 GLU B 529 39.47 -90.88
REMARK 500 SER B 530 -60.32 -91.59
REMARK 500
REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4YCZ A 5 1223 UNP G2QES5 G2QES5_THIHA 1 304
DBREF 4YCZ A 1224 1414 PDB 4YCZ 4YCZ 1224 1414
DBREF 4YCZ A 1415 1791 UNP G2QEZ2 G2QEZ2_THIHA 1 377
DBREF 4YCZ B 257 1181 UNP G2Q7J4 G2Q7J4_THIHA 257 1181
DBREF 4YCZ C 952 1241 UNP G2Q2S2 G2Q2S2_THIHA 952 1241
SEQADV 4YCZ GLY A 1 UNP G2QES5 EXPRESSION TAG
SEQADV 4YCZ PRO A 2 UNP G2QES5 EXPRESSION TAG
SEQADV 4YCZ GLY A 3 UNP G2QES5 EXPRESSION TAG
SEQADV 4YCZ SER A 4 UNP G2QES5 EXPRESSION TAG
SEQADV 4YCZ GLY B 249 UNP G2Q7J4 EXPRESSION TAG
SEQADV 4YCZ PRO B 250 UNP G2Q7J4 EXPRESSION TAG
SEQADV 4YCZ GLY B 251 UNP G2Q7J4 EXPRESSION TAG
SEQADV 4YCZ SER B 252 UNP G2Q7J4 EXPRESSION TAG
SEQADV 4YCZ GLU B 253 UNP G2Q7J4 EXPRESSION TAG
SEQADV 4YCZ PHE B 254 UNP G2Q7J4 EXPRESSION TAG
SEQADV 4YCZ GLU B 255 UNP G2Q7J4 EXPRESSION TAG
SEQADV 4YCZ LEU B 256 UNP G2Q7J4 EXPRESSION TAG
SEQADV 4YCZ GLY C 943 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ PRO C 944 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ GLY C 945 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ SER C 946 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ GLU C 947 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ PHE C 948 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ GLU C 949 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ LEU C 950 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ MET C 951 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ GLY C 1242 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ GLY C 1243 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ SER C 1244 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ GLY C 1245 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1246 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1247 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1248 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1249 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1250 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1251 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1252 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1253 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1254 UNP G2Q2S2 EXPRESSION TAG
SEQADV 4YCZ HIS C 1255 UNP G2Q2S2 EXPRESSION TAG
SEQRES 1 A 876 GLY PRO GLY SER MET ALA ALA GLY THR GLN VAL ILE ALA
SEQRES 2 A 876 ASN SER GLY HIS ASP ASP MET ILE HIS ASP ALA VAL LEU
SEQRES 3 A 876 ASP TYR TYR GLY ARG ARG LEU ALA THR CYS SER SER ASP
SEQRES 4 A 876 ARG THR ILE LYS ILE PHE GLU ILE GLU GLY GLU THR GLN
SEQRES 5 A 876 ARG LEU THR GLU THR LEU LYS GLY HIS ASP GLY ALA VAL
SEQRES 6 A 876 TRP CYS VAL SER TRP ALA HIS PRO LYS TYR GLY ASN ILE
SEQRES 7 A 876 LEU ALA SER ALA GLY TYR ASP GLY LYS VAL LEU ILE TRP
SEQRES 8 A 876 ARG GLU LEU ASN GLY ALA TRP GLN ARG ILE PHE ASP PHE
SEQRES 9 A 876 ALA LEU HIS LYS ALA SER VAL ASN VAL VAL SER TRP SER
SEQRES 10 A 876 PRO HIS GLU ALA GLY CYS LEU LEU ALA CYS ALA SER SER
SEQRES 11 A 876 ASP GLY ASN VAL SER VAL LEU GLU PHE ARG ASP ASN SER
SEQRES 12 A 876 TRP GLU HIS SER ILE PHE HIS ALA HIS GLY LEU GLY VAL
SEQRES 13 A 876 ASN SER VAL SER TRP ALA PRO ALA THR SER PRO GLY SER
SEQRES 14 A 876 ILE VAL SER SER LYS PRO GLY PRO LYS SER THR GLY ASN
SEQRES 15 A 876 ARG ARG PHE VAL THR GLY GLY SER ASP ASN ALA LEU LYS
SEQRES 16 A 876 ILE TRP ALA TYR ASP PRO ALA THR ASN THR TYR LYS LEU
SEQRES 17 A 876 GLU ARG GLU PRO LEU THR GLY HIS THR ASP TRP VAL ARG
SEQRES 18 A 876 ASP VAL ALA TRP SER PRO THR VAL LEU GLN LYS SER TYR
SEQRES 19 A 876 ILE ALA SER ALA SER GLU ASP ARG THR VAL ARG ILE TRP
SEQRES 20 A 876 THR SER ASP PRO ALA ASN PRO LEU GLN TRP ASN CYS LYS
SEQRES 21 A 876 VAL LEU ASN PHE ASP ALA ALA VAL TRP ARG VAL SER TRP
SEQRES 22 A 876 SER LEU SER GLY ASN VAL LEU ALA ALA SER GLY GLY ASP
SEQRES 23 A 876 ASN LYS VAL THR LEU TRP LYS GLU ASN LEU LYS GLY GLU
SEQRES 24 A 876 TRP GLU CYS VAL LYS THR ILE GLU GLU GLY GLY GLY GLY
SEQRES 25 A 876 SER GLY GLY GLY GLY GLN ALA LYS GLY PRO THR GLN PRO
SEQRES 26 A 876 GLU GLN ALA SER PRO ALA LYS GLY PHE VAL LYS TRP PRO
SEQRES 27 A 876 TYR GLN GLN ARG PRO LYS ILE ASP GLN GLN GLU GLY PRO
SEQRES 28 A 876 SER ILE PRO ARG THR ASN TRP GLY PRO ASN GLY LEU LEU
SEQRES 29 A 876 VAL THR THR HIS HIS GLY GLU PRO SER LEU GLN PRO ALA
SEQRES 30 A 876 ASP GLY THR LEU ALA ALA SER GLU GLU SER VAL GLY SER
SEQRES 31 A 876 PRO GLU ASN LEU ALA ARG LEU GLN ARG TYR ILE ASP SER
SEQRES 32 A 876 VAL SER PHE LYS GLU GLY GLN PRO ILE ALA SER PRO GLU
SEQRES 33 A 876 PHE ARG GLU LEU ALA GLN GLY ASP PRO SER TRP GLU LEU
SEQRES 34 A 876 ALA SER LEU LEU PHE ASP ASP ASN GLY TYR GLY LEU PRO
SEQRES 35 A 876 ALA PHE TRP ARG GLN LEU VAL SER GLU ALA THR ASP ARG
SEQRES 36 A 876 ALA LEU ALA GLN GLU PRO GLY LEU GLU GLU LYS ALA ILE
SEQRES 37 A 876 ILE CYS LEU ALA GLY ASN ARG VAL ALA ASP ALA CYS GLY
SEQRES 38 A 876 TYR LEU LEU ALA ALA GLY ASN PHE ARG LEU ALA THR LEU
SEQRES 39 A 876 VAL SER GLY ILE GLY MET GLN ASP GLY ASP MET LYS ALA
SEQRES 40 A 876 GLN LEU LYS ASP TRP ARG GLU SER ASN VAL LEU ALA GLU
SEQRES 41 A 876 PHE SER GLN PRO VAL ARG ALA ILE TYR GLU LEU LEU ALA
SEQRES 42 A 876 GLY ASN ALA GLY VAL CYS ALA GLY VAL LYS ASN VAL PRO
SEQRES 43 A 876 ILE GLU ASN ARG VAL ASP SER PHE THR ILE SER GLN ARG
SEQRES 44 A 876 PHE GLY LEU ASP TRP MET ARG SER PHE GLY LEU ARG LEU
SEQRES 45 A 876 PHE TYR THR THR GLY ALA THR ALA ASN VAL ALA GLU ALA
SEQRES 46 A 876 VAL ARG SER PHE GLN ALA ASP ILE GLU GLN ASP LYS GLU
SEQRES 47 A 876 PRO GLU PRO ASP SER ALA LEU TRP SER LEU LEU LYS ALA
SEQRES 48 A 876 PHE ALA ASN GLN GLU PHE ASP TRP SER ASP THR ARG LEU
SEQRES 49 A 876 GLY TRP LEU LEU THR LYS ALA ILE TYR ALA THR GLY LYS
SEQRES 50 A 876 VAL SER PHE GLY GLN ASP ALA ALA GLU LYS LEU ASP LYS
SEQRES 51 A 876 ALA SER LEU ALA TYR ALA SER ALA LEU THR ALA GLN SER
SEQRES 52 A 876 GLN TRP VAL PRO ALA THR PHE VAL LEU LEU GLN LEU SER
SEQRES 53 A 876 ASP ALA ALA SER ARG GLU ALA ALA VAL ARG ASP HIS LEU
SEQRES 54 A 876 GLY ARG HIS ALA ARG ARG ILE GLY SER PRO ARG ASN PRO
SEQRES 55 A 876 ASN SER ALA PHE SER SER LEU ARG LYS PHE GLY VAL PRO
SEQRES 56 A 876 GLU THR TRP ILE TRP GLU ALA LYS ALA LEU ASP PHE ARG
SEQRES 57 A 876 ALA ARG GLY ASP SER GLN GLN GLU PHE LEU ALA LEU VAL
SEQRES 58 A 876 TRP ALA GLN ASN TYR SER GLU ALA ASN GLN ALA PHE VAL
SEQRES 59 A 876 HIS ARG VAL GLY PRO ASP LEU VAL ILE ALA ARG ASP PHE
SEQRES 60 A 876 ARG ARG LEU PHE ARG PHE ALA GLN LEU LEU PHE LYS VAL
SEQRES 61 A 876 LYS GLY LYS LEU GLN ASP TRP ASP ARG GLY ALA ALA VAL
SEQRES 62 A 876 TYR LEU LEU TYR PRO MET ALA ARG LEU GLN GLY LYS GLN
SEQRES 63 A 876 HIS GLY LEU ASP LYS PHE ASP HIS GLN LEU PHE ASP GLY
SEQRES 64 A 876 LEU VAL ALA LEU ARG GLY GLN THR HIS GLY ASP ILE ARG
SEQRES 65 A 876 GLN GLU ALA ALA ILE ALA ASP MET ALA GLU ASP LEU ILE
SEQRES 66 A 876 ARG CYS ARG GLY GLY ASP PRO ARG LEU PHE GLY LEU LEU
SEQRES 67 A 876 PRO GLU ASP VAL ARG SER LYS TYR MET ARG ALA GLN ALA
SEQRES 68 A 876 LEU GLU VAL ILE CYS
SEQRES 1 B 933 GLY PRO GLY SER GLU PHE GLU LEU MSE TRP LEU ASP MSE
SEQRES 2 B 933 PRO SER THR ALA GLU THR GLY ALA ASP GLN PRO ALA ALA
SEQRES 3 B 933 GLY GLU VAL SER ASP LEU LEU MSE LEU ALA THR PRO ALA
SEQRES 4 B 933 ALA THR GLU ARG VAL ARG ARG GLU ALA GLU ASP ILE PHE
SEQRES 5 B 933 ARG ALA SER SER PHE ARG ALA GLY GLY ALA ALA ARG ARG
SEQRES 6 B 933 SER GLU TYR ARG TYR ALA ALA LEU ALA LYS ASP ALA TYR
SEQRES 7 B 933 GLN GLN MSE GLY THR ALA PRO VAL THR GLU PRO PRO GLN
SEQRES 8 B 933 VAL ILE LEU GLY THR GLU ASP LEU LEU SER ARG LEU TYR
SEQRES 9 B 933 ASP GLU GLY VAL GLY GLU ALA GLU ASP GLU GLN LYS MSE
SEQRES 10 B 933 ASP ASP THR LEU ALA THR ALA ALA ALA GLN LEU ALA ALA
SEQRES 11 B 933 LEU TRP ARG GLU HIS VAL ASP GLU LEU PRO ARG PRO THR
SEQRES 12 B 933 GLU ASP HIS ALA ALA GLU ILE GLY PRO GLY PRO HIS ALA
SEQRES 13 B 933 THR PRO PHE GLU LYS ALA ASN TYR LEU ALA ASN LEU ALA
SEQRES 14 B 933 LEU GLN ILE HIS HIS THR ARG TYR GLU GLU GLY GLY LEU
SEQRES 15 B 933 ILE ARG ALA GLU PRO LEU PRO GLN THR LEU PHE ARG TRP
SEQRES 16 B 933 LEU ASN GLU TYR HIS ASP MSE TYR GLY SER GLN VAL ASP
SEQRES 17 B 933 ASP ILE LEU ARG HIS ARG PRO SER PRO ALA CYS HIS SER
SEQRES 18 B 933 LEU PHE TRP GLN ALA VAL PHE ILE ALA LEU LEU ARG GLY
SEQRES 19 B 933 LYS VAL GLY ASP ALA ALA ARG LEU LEU ASP GLN ALA GLY
SEQRES 20 B 933 TRP GLY HIS VAL ARG ARG GLY GLN ARG GLY GLU TYR ALA
SEQRES 21 B 933 TYR VAL GLY GLN ALA LEU GLU ASN VAL GLN ARG ALA VAL
SEQRES 22 B 933 ASP GLU THR ILE ALA VAL LEU GLU SER CYS PRO GLY PHE
SEQRES 23 B 933 ASP GLY ASN TRP GLU ILE TRP SER SER ASP TRP THR LEU
SEQRES 24 B 933 PHE ARG VAL ARG ALA ARG GLY LEU LEU GLU HIS LEU ARG
SEQRES 25 B 933 ARG PHE ALA GLU GLY LYS ASP SER ALA PHE GLY ALA SER
SEQRES 26 B 933 ALA PHE SER ALA SER ALA ALA SER ALA GLN SER ARG GLN
SEQRES 27 B 933 SER MSE ALA GLY LEU ALA ARG ARG ALA GLU SER GLN VAL
SEQRES 28 B 933 PRO TRP GLU ILE TYR GLU ASN LEU ASN ILE VAL PHE ASP
SEQRES 29 B 933 ILE VAL LEU GLY GLN GLN GLY ALA ILE LEU GLU ALA ALA
SEQRES 30 B 933 GLN ASP TRP LEU GLU ALA THR VAL GLY LEU PHE GLY TRP
SEQRES 31 B 933 TRP ASP GLU ARG ALA SER ARG THR GLU LYS PRO LEU SER
SEQRES 32 B 933 THR SER GLN SER LEU SER ARG SER GLN ALA LEU VAL LEU
SEQRES 33 B 933 ALA SER ALA PRO ALA ASN SER GLU SER TYR LEU ASP ARG
SEQRES 34 B 933 LEU ALA ARG ALA PHE HIS THR ALA VAL GLU SER ASP PHE
SEQRES 35 B 933 HIS PHE ASN SER GLN ASN ALA VAL GLU ILE GLY MSE ALA
SEQRES 36 B 933 CYS VAL PHE GLU ASP ASN ILE LYS GLY VAL ILE GLY LEU
SEQRES 37 B 933 LEU ARG GLY TRP SER LEU PRO ILE ALA ALA ALA VAL ALA
SEQRES 38 B 933 GLU ILE ALA SER LEU GLY LYS TRP LEU PRO PRO HIS ARG
SEQRES 39 B 933 PRO SER GLY VAL TYR GLY LEU GLU ASP LEU ASP MSE ASP
SEQRES 40 B 933 ASP LEU GLU VAL LEU GLY MSE ASP PRO GLY ALA PRO ASP
SEQRES 41 B 933 GLU VAL ASP GLY ILE LYS ASP SER THR LEU VAL GLN TYR
SEQRES 42 B 933 ALA GLN ALA LEU ALA ASP TYR GLU GLY LEU SER SER VAL
SEQRES 43 B 933 GLN ASP ARG SER GLY THR SER LYS ASP GLY TRP GLU LEU
SEQRES 44 B 933 SER ILE SER VAL LEU GLY ARG MSE ASP SER PRO GLU ARG
SEQRES 45 B 933 SER GLU GLU MSE VAL ARG ASP LEU VAL GLU HIS LEU VAL
SEQRES 46 B 933 GLN GLN LEU HIS VAL ASP SER ASN ALA THR VAL ASP ARG
SEQRES 47 B 933 LEU TRP PHE LEU LEU ASN GLU LEU GLY MSE ILE GLU PHE
SEQRES 48 B 933 ALA GLU ASP THR THR GLU THR TYR GLY ASP ILE LEU ALA
SEQRES 49 B 933 ARG ASP SER HIS ARG TYR GLY GLU ALA MSE TRP TYR TYR
SEQRES 50 B 933 ALA LEU ALA HIS ARG PRO ASN LYS VAL ARG GLU VAL MSE
SEQRES 51 B 933 ASN LEU LEU THR SER TYR SER LEU ILE GLN SER THR ALA
SEQRES 52 B 933 PHE PRO PRO ALA ASN ASP LEU ASP ASP TYR LEU TYR LYS
SEQRES 53 B 933 LEU LEU ASN ASP ARG LYS ASN THR LEU GLU GLN CYS ALA
SEQRES 54 B 933 SER GLN ASP MSE GLU ALA ALA GLU LEU LEU GLY LYS MSE
SEQRES 55 B 933 LEU SER GLY TYR ALA SER LEU ARG GLN PHE TYR ASP ILE
SEQRES 56 B 933 ARG ASP ASN GLU ASP ALA LEU PRO HIS ALA THR PRO LEU
SEQRES 57 B 933 SER ARG ARG LYS GLN ALA ALA THR ALA LEU ILE SER VAL
SEQRES 58 B 933 ILE ALA SER SER ASP ASP ASN ILE ARG GLY GLY LEU TYR
SEQRES 59 B 933 ASP GLN THR ARG ASP GLY ILE VAL SER GLU ASP PHE LEU
SEQRES 60 B 933 LEU ALA LEU LEU GLY GLU ALA LEU VAL PHE VAL SER ASP
SEQRES 61 B 933 PRO ASP ASN THR ASN VAL HIS HIS GLY GLN LEU ALA THR
SEQRES 62 B 933 PRO VAL ILE THR LEU ASP GLN ILE ASP VAL LEU LEU LYS
SEQRES 63 B 933 ALA ILE GLU ASP LEU GLN ALA VAL GLY SER ARG VAL TYR
SEQRES 64 B 933 ASN ALA CYS ASP GLU PHE LEU GLN LEU VAL LEU ALA SER
SEQRES 65 B 933 ALA PRO GLY GLY LEU LYS GLY SER THR PRO ALA ASP LEU
SEQRES 66 B 933 LEU LYS LYS SER ALA GLY PRO GLY PRO GLY GLY SER GLY
SEQRES 67 B 933 ASN ALA MSE LEU ALA GLY SER SER LEU VAL ALA SER GLN
SEQRES 68 B 933 LEU GLN ARG SER LEU SER GLY THR GLY GLY GLY LEU GLY
SEQRES 69 B 933 LYS VAL ALA VAL LYS ARG ARG GLY TRP ASP TRP ARG SER
SEQRES 70 B 933 GLU VAL THR ALA LYS THR LYS GLY GLU ASP ILE MSE ARG
SEQRES 71 B 933 ARG LEU ARG LEU GLY LEU ALA LYS ASP LEU ALA GLY LEU
SEQRES 72 B 933 TRP LEU ALA GLU ALA ASP GLU MSE VAL TRP
SEQRES 1 C 313 GLY PRO GLY SER GLU PHE GLU LEU MET GLN GLY GLY SER
SEQRES 2 C 313 SER THR ASN HIS GLU THR ALA GLY LEU ARG THR GLU MET
SEQRES 3 C 313 LEU SER ARG LEU PHE THR ALA ALA THR SER ILE SER HIS
SEQRES 4 C 313 PHE GLU GLU ALA HIS SER ALA LEU LEU SER MET ASP ASP
SEQRES 5 C 313 GLU ALA MET GLN LYS SER TYR LEU ARG ARG LEU VAL GLU
SEQRES 6 C 313 LYS MET CYS GLU THR GLY GLN SER SER GLU LEU ILE THR
SEQRES 7 C 313 LEU PRO PHE SER GLY LEU GLN THR LYS VAL ASP ASP ILE
SEQRES 8 C 313 LEU VAL GLU LYS CYS ARG ALA THR ARG ASP VAL LEU ASN
SEQRES 9 C 313 GLY VAL PRO TYR HIS GLN ILE LEU TYR ALA TRP ARG ILE
SEQRES 10 C 313 ASN HIS ASN ASP TYR ARG GLY GLY ALA ALA ILE LEU LEU
SEQRES 11 C 313 ASP ARG LEU GLN LYS LEU ARG ARG ALA GLY GLU GLY ASP
SEQRES 12 C 313 LYS VAL ILE ALA ASN GLU HIS GLY ASN GLU ASP ALA LEU
SEQRES 13 C 313 ASP THR GLN VAL THR ARG GLN TYR LEU LEU LEU ILE ASN
SEQRES 14 C 313 ALA LEU SER CYS VAL PRO PRO GLN GLU ALA TYR ILE LEU
SEQRES 15 C 313 GLU ASP VAL LEU PRO GLY ASP GLY ARG GLY GLY ASP ASP
SEQRES 16 C 313 ALA ASP GLY ASP ARG ASN GLY GLY LYS ALA GLY ASP ASP
SEQRES 17 C 313 LEU GLU ALA ASP ILE ASP GLU LEU GLU LYS LYS LEU ASP
SEQRES 18 C 313 VAL GLU GLY GLY ALA ASP ALA ALA LYS GLY ASP GLU MET
SEQRES 19 C 313 ALA ALA GLU GLU ASP ALA ALA LEU ILE GLU LYS MET LYS
SEQRES 20 C 313 ARG PHE SER THR ARG ASN GLY GLN ASN LEU PRO ALA ARG
SEQRES 21 C 313 ARG LEU LEU MET LEU ALA ASP LEU ARG LYS GLN TYR GLN
SEQRES 22 C 313 GLN GLU LEU ASP ARG ILE VAL ALA ILE GLN ASN ASN GLN
SEQRES 23 C 313 PHE GLY PHE GLY ALA GLU ASP ASP LEU MET ASP LEU ALA
SEQRES 24 C 313 GLY GLY SER GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 25 C 313 HIS
MODRES 4YCZ MSE B 329 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 365 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 450 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 702 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 815 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 824 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 856 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 882 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 898 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 941 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 950 MET MODIFIED RESIDUE
MODRES 4YCZ MSE B 1157 MET MODIFIED RESIDUE
HET MSE B 329 8
HET MSE B 365 8
HET MSE B 450 8
HET MSE B 702 8
HET MSE B 815 8
HET MSE B 824 8
HET MSE B 856 8
HET MSE B 882 8
HET MSE B 898 8
HET MSE B 941 8
HET MSE B 950 8
HET MSE B1157 8
HETNAM MSE SELENOMETHIONINE
FORMUL 2 MSE 12(C5 H11 N O2 SE)
HELIX 1 AA1 HIS A 72 GLY A 76 5 5
HELIX 2 AA2 PRO A 118 GLY A 122 5 5
HELIX 3 AA3 SER A 1305 SER A 1318 1 14
HELIX 4 AA4 ASP A 1339 LEU A 1347 1 9
HELIX 5 AA5 GLY A 1355 GLU A 1366 1 12
HELIX 6 AA6 GLU A 1380 ALA A 1387 1 8
HELIX 7 AA7 VAL A 1391 ALA A 1401 1 11
HELIX 8 AA8 GLY A 1402 PHE A 1404 5 3
HELIX 9 AA9 ARG A 1405 ILE A 1413 1 9
HELIX 10 AB1 SER A 1437 ALA A 1448 1 12
HELIX 11 AB2 ARG A 1481 TYR A 1489 1 9
HELIX 12 AB3 VAL A 1497 GLN A 1510 1 14
HELIX 13 AB4 SER A 1518 ALA A 1526 1 9
HELIX 14 AB5 TRP A 1541 THR A 1550 1 10
HELIX 15 AB6 ALA A 1559 ALA A 1576 1 18
HELIX 16 AB7 TRP A 1580 LEU A 1588 1 9
HELIX 17 AB8 ASP A 1592 ARG A 1610 1 19
HELIX 18 AB9 PRO A 1617 LYS A 1626 1 10
HELIX 19 AC1 THR A 1632 ARG A 1645 1 14
HELIX 20 AC2 GLN A 1650 TRP A 1657 1 8
HELIX 21 AC3 SER A 1662 ALA A 1667 1 6
HELIX 22 AC4 PHE A 1668 GLY A 1673 1 6
HELIX 23 AC5 PRO A 1674 LEU A 1676 5 3
HELIX 24 AC6 PHE A 1682 VAL A 1695 1 14
HELIX 25 AC7 TRP A 1702 ALA A 1707 1 6
HELIX 26 AC8 ALA A 1707 GLY A 1719 1 13
HELIX 27 AC9 PHE A 1727 THR A 1742 1 16
HELIX 28 AD1 ASP A 1745 ASP A 1758 1 14
HELIX 29 AD2 GLY A 1771 ARG A 1783 1 13
HELIX 30 AD3 GLU B 315 ASP B 324 1 10
HELIX 31 AD4 GLU B 336 TYR B 352 1 17
HELIX 32 AD5 MSE B 365 GLU B 386 1 22
HELIX 33 AD6 PRO B 406 HIS B 422 1 17
HELIX 34 AD7 LEU B 436 ASN B 445 1 10
HELIX 35 AD8 GLN B 454 ARG B 460 1 7
HELIX 36 AD9 PHE B 471 LEU B 479 1 9
HELIX 37 AE1 VAL B 484 GLN B 493 1 10
HELIX 38 AE2 VAL B 517 GLU B 529 1 13
HELIX 39 AE3 LEU B 547 GLY B 565 1 19
HELIX 40 AE4 GLU B 602 GLY B 616 1 15
HELIX 41 AE5 GLN B 617 LEU B 622 1 6
HELIX 42 AE6 ASP B 627 GLY B 634 1 8
HELIX 43 AE7 ASN B 670 ARG B 680 1 11
HELIX 44 AE8 GLU B 699 GLU B 707 1 9
HELIX 45 AE9 ILE B 710 TRP B 720 1 11
HELIX 46 AF1 PRO B 723 SER B 733 1 11
HELIX 47 AF2 ASP B 775 ALA B 786 1 12
HELIX 48 AF3 TRP B 805 GLY B 813 1 9
HELIX 49 AF4 SER B 821 GLN B 834 1 14
HELIX 50 AF5 SER B 840 ASN B 852 1 13
HELIX 51 AF6 MSE B 856 LEU B 871 1 16
HELIX 52 AF7 TYR B 878 LEU B 887 1 10
HELIX 53 AF8 ARG B 890 GLN B 908 1 19
HELIX 54 AF9 ASP B 919 LEU B 925 1 7
HELIX 55 AG1 LYS B 930 ALA B 937 1 8
HELIX 56 AG2 ASP B 940 LYS B 949 1 10
HELIX 57 AG3 LEU B 951 ARG B 964 1 14
HELIX 58 AG4 ALA B 973 ILE B 990 1 18
HELIX 59 AG5 PHE B 1014 SER B 1027 1 14
HELIX 60 AG6 LEU B 1046 ASP B 1058 1 13
HELIX 61 AG7 SER B 1064 LEU B 1076 1 13
HELIX 62 AG8 SER B 1113 ARG B 1122 1 10
HELIX 63 AG9 GLU B 1154 LEU B 1171 1 18
HELIX 64 AH1 LEU C 969 SER C 978 1 10
HELIX 65 AH2 GLU C 984 MET C 992 1 9
HELIX 66 AH3 TYR C 1001 THR C 1012 1 12
HELIX 67 AH4 SER C 1015 THR C 1020 1 6
HELIX 68 AH5 PHE C 1023 LYS C 1037 1 15
HELIX 69 AH6 HIS C 1051 ASP C 1063 1 13
HELIX 70 AH7 TYR C 1064 ALA C 1081 1 18
HELIX 71 AH8 LEU C 1098 VAL C 1116 1 19
HELIX 72 AH9 LEU C 1151 ASP C 1163 1 13
HELIX 73 AI1 ASP C 1181 ASN C 1195 1 15
HELIX 74 AI2 MET C 1206 ALA C 1223 1 18
SHEET 1 AA1 4 ALA A 24 LEU A 26 0
SHEET 2 AA1 4 LEU A 33 THR A 35 -1 O ALA A 34 N VAL A 25
SHEET 3 AA1 4 THR A 41 GLU A 48 -1 O PHE A 45 N LEU A 33
SHEET 4 AA1 4 THR A 51 LYS A 59 -1 O LEU A 58 N ILE A 42
SHEET 1 AA2 4 VAL A 65 CYS A 67 0
SHEET 2 AA2 4 ILE A 78 GLY A 83 -1 O ALA A 82 N TRP A 66
SHEET 3 AA2 4 LYS A 87 GLU A 93 -1 O LEU A 89 N SER A 81
SHEET 4 AA2 4 TRP A 98 ALA A 105 -1 O GLN A 99 N ARG A 92
SHEET 1 AA3 2 VAL A 111 TRP A 116 0
SHEET 2 AA3 2 LEU A 125 SER A 129 -1 O ALA A 128 N VAL A 113
SHEET 1 AA4 2 VAL A 136 GLU A 138 0
SHEET 2 AA4 2 GLU A 145 SER A 147 -1 O GLU A 145 N GLU A 138
SHEET 1 AA5 4 VAL A 159 ALA A 162 0
SHEET 2 AA5 4 ARG A 184 THR A 187 -1 O ARG A 184 N ALA A 162
SHEET 3 AA5 4 LYS A 195 ASP A 200 -1 O LYS A 195 N THR A 187
SHEET 4 AA5 4 THR A 205 LEU A 208 -1 O LYS A 207 N ALA A 198
SHEET 1 AA6 3 ASP A 222 TRP A 225 0
SHEET 2 AA6 3 SER A 233 ALA A 238 -1 O ALA A 238 N ASP A 222
SHEET 3 AA6 3 ARG A 245 SER A 249 -1 O ARG A 245 N SER A 237
SHEET 1 AA7 4 VAL A 268 SER A 274 0
SHEET 2 AA7 4 VAL A 279 GLY A 284 -1 O ALA A 281 N SER A 272
SHEET 3 AA7 4 VAL A 289 GLU A 294 -1 O THR A 290 N ALA A 282
SHEET 4 AA7 4 TRP A 300 VAL A 303 -1 O GLU A 301 N LYS A 293
LINK C GLN B 328 N MSE B 329 1555 1555 1.33
LINK C MSE B 329 N GLY B 330 1555 1555 1.33
LINK C LYS B 364 N MSE B 365 1555 1555 1.33
LINK C MSE B 365 N ASP B 366 1555 1555 1.33
LINK C MSE B 450 N TYR B 451 1555 1555 1.33
LINK C GLY B 701 N MSE B 702 1555 1555 1.33
LINK C MSE B 702 N ALA B 703 1555 1555 1.33
LINK C ARG B 814 N MSE B 815 1555 1555 1.33
LINK C GLU B 823 N MSE B 824 1555 1555 1.33
LINK C MSE B 824 N VAL B 825 1555 1555 1.33
LINK C GLY B 855 N MSE B 856 1555 1555 1.33
LINK C MSE B 856 N ILE B 857 1555 1555 1.33
LINK C ALA B 881 N MSE B 882 1555 1555 1.33
LINK C MSE B 882 N TRP B 883 1555 1555 1.33
LINK C VAL B 897 N MSE B 898 1555 1555 1.33
LINK C MSE B 898 N ASN B 899 1555 1555 1.33
LINK C ASP B 940 N MSE B 941 1555 1555 1.33
LINK C MSE B 941 N GLU B 942 1555 1555 1.33
LINK C LYS B 949 N MSE B 950 1555 1555 1.33
LINK C MSE B 950 N LEU B 951 1555 1555 1.33
LINK C ILE B1156 N MSE B1157 1555 1555 1.33
LINK C MSE B1157 N ARG B1158 1555 1555 1.33
CRYST1 104.984 212.022 170.643 90.00 107.21 90.00 C 1 2 1 4
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 0.009525 0.000000 0.002950 0.00000
SCALE2 0.000000 0.004716 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006135 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
