HEADER HYDROLASE 06-SEP-16 5GVU
TITLE CRYSTAL STRUCTURE OF BVDV NS3 HELICASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NS3 HELICASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 1939-2414;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOVINE VIRAL DIARRHEA VIRUS 1;
SOURCE 3 ORGANISM_COMMON: BVDV;
SOURCE 4 ORGANISM_TAXID: 11099;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HELICASE, NS3, BVDV, FLAVIVIRUS, PESTIVIRUS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LI,X.MAO
REVDAT 2 08-NOV-23 5GVU 1 REMARK
REVDAT 1 13-SEP-17 5GVU 0
JRNL AUTH J.SHI,M.HE,Y.NIE,S.LI,X.MAO
JRNL TITL CRYSTAL STRUCTURE OF BVDV NS3 HELICASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0124
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 41208
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.273
REMARK 3 R VALUE (WORKING SET) : 0.272
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2121
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3066
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9414
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 38
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.00000
REMARK 3 B22 (A**2) : 1.00000
REMARK 3 B33 (A**2) : -3.23000
REMARK 3 B12 (A**2) : 0.50000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.300
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.410
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.341
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.438
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.826
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.777
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9582 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12952 ; 1.361 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1171 ; 6.085 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 433 ;38.734 ;24.065
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1727 ;19.873 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;15.121 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1468 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7126 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4729 ; 0.783 ; 4.522
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5885 ; 1.479 ; 6.762
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4853 ; 0.317 ; 4.427
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 208 A 683
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9898 -65.0441 -47.3427
REMARK 3 T TENSOR
REMARK 3 T11: 0.1002 T22: 0.1545
REMARK 3 T33: 0.0882 T12: 0.1104
REMARK 3 T13: 0.0032 T23: -0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 0.1794 L22: 0.8236
REMARK 3 L33: 0.2521 L12: -0.2594
REMARK 3 L13: -0.0734 L23: 0.3595
REMARK 3 S TENSOR
REMARK 3 S11: 0.0425 S12: 0.0191 S13: -0.0314
REMARK 3 S21: -0.1762 S22: -0.0859 S23: -0.0343
REMARK 3 S31: -0.0922 S32: -0.0822 S33: 0.0433
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 208 B 683
REMARK 3 ORIGIN FOR THE GROUP (A): -40.7285 -29.7712 -12.1173
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0831
REMARK 3 T33: 0.1405 T12: 0.0100
REMARK 3 T13: 0.0080 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 0.7686 L22: 1.0466
REMARK 3 L33: 0.7635 L12: 0.8315
REMARK 3 L13: -0.4798 L23: -0.2621
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: -0.0425 S13: -0.0299
REMARK 3 S21: -0.0143 S22: 0.0055 S23: -0.0137
REMARK 3 S31: 0.0270 S32: 0.0895 S33: 0.0144
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 208 C 683
REMARK 3 ORIGIN FOR THE GROUP (A): -49.0259 -88.4564 -8.9006
REMARK 3 T TENSOR
REMARK 3 T11: 0.0610 T22: 0.1321
REMARK 3 T33: 0.1004 T12: -0.0023
REMARK 3 T13: -0.0146 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.3925 L22: 0.1064
REMARK 3 L33: 1.1706 L12: 0.1832
REMARK 3 L13: 0.3564 L23: 0.0562
REMARK 3 S TENSOR
REMARK 3 S11: -0.0801 S12: 0.0508 S13: 0.1175
REMARK 3 S21: -0.0460 S22: -0.0280 S23: 0.0711
REMARK 3 S31: 0.0773 S32: 0.2877 S33: 0.1081
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 5GVU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1300001489.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41208
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.820
REMARK 200 RESOLUTION RANGE LOW (A) : 50.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 15.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.30
REMARK 200 R MERGE FOR SHELL (I) : 0.45100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 4CBG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM FORMATE, 15% W/V PEG
REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.14733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.57367
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 PRO A 353
REMARK 465 ALA A 354
REMARK 465 GLY A 355
REMARK 465 SER A 356
REMARK 465 VAL A 357
REMARK 465 THR A 358
REMARK 465 THR A 359
REMARK 465 THR A 360
REMARK 465 GLY A 361
REMARK 465 GLN A 362
REMARK 465 LYS A 363
REMARK 465 LEU A 380
REMARK 465 GLY A 381
REMARK 465 SER A 382
REMARK 465 TYR A 427
REMARK 465 SER A 430
REMARK 465 GLY A 431
REMARK 465 GLU A 432
REMARK 465 ASP A 433
REMARK 465 SER A 456
REMARK 465 GLY A 457
REMARK 465 VAL A 458
REMARK 465 PRO B 353
REMARK 465 ALA B 354
REMARK 465 GLY B 355
REMARK 465 SER B 356
REMARK 465 VAL B 357
REMARK 465 THR B 358
REMARK 465 THR B 359
REMARK 465 THR B 360
REMARK 465 GLY B 361
REMARK 465 GLN B 362
REMARK 465 LYS B 363
REMARK 465 HIS B 364
REMARK 465 PRO B 365
REMARK 465 ILE B 366
REMARK 465 GLU B 367
REMARK 465 GLU B 368
REMARK 465 PHE B 369
REMARK 465 ILE B 370
REMARK 465 ALA B 371
REMARK 465 PRO B 372
REMARK 465 GLU B 373
REMARK 465 VAL B 374
REMARK 465 MET B 375
REMARK 465 LYS B 376
REMARK 465 GLY B 377
REMARK 465 GLU B 378
REMARK 465 ASP B 379
REMARK 465 LEU B 380
REMARK 465 GLY B 381
REMARK 465 SER B 382
REMARK 465 GLN B 383
REMARK 465 PHE B 384
REMARK 465 LEU B 385
REMARK 465 ASP B 386
REMARK 465 ILE B 387
REMARK 465 ALA B 388
REMARK 465 GLY B 389
REMARK 465 LEU B 390
REMARK 465 LYS B 391
REMARK 465 ILE B 392
REMARK 465 PRO B 393
REMARK 465 VAL B 394
REMARK 465 ASP B 395
REMARK 465 GLU B 396
REMARK 465 MET B 397
REMARK 465 LYS B 398
REMARK 465 GLY B 399
REMARK 465 ASN B 400
REMARK 465 MET B 401
REMARK 465 LEU B 402
REMARK 465 VAL B 403
REMARK 465 ASN B 409
REMARK 465 MET B 410
REMARK 465 ALA B 411
REMARK 465 VAL B 412
REMARK 465 GLU B 413
REMARK 465 VAL B 414
REMARK 465 ALA B 415
REMARK 465 LYS B 416
REMARK 465 LYS B 417
REMARK 465 LEU B 418
REMARK 465 LYS B 419
REMARK 465 ALA B 420
REMARK 465 LYS B 421
REMARK 465 GLY B 422
REMARK 465 TYR B 423
REMARK 465 ASN B 424
REMARK 465 SER B 425
REMARK 465 GLY B 426
REMARK 465 TYR B 427
REMARK 465 TYR B 428
REMARK 465 TYR B 429
REMARK 465 SER B 430
REMARK 465 GLY B 431
REMARK 465 GLU B 432
REMARK 465 ASP B 433
REMARK 465 PRO B 434
REMARK 465 ALA B 435
REMARK 465 ASN B 436
REMARK 465 LEU B 437
REMARK 465 ARG B 438
REMARK 465 VAL B 439
REMARK 465 VAL B 440
REMARK 465 THR B 441
REMARK 465 SER B 442
REMARK 465 GLN B 443
REMARK 465 SER B 444
REMARK 465 PRO B 445
REMARK 465 TYR B 446
REMARK 465 VAL B 447
REMARK 465 ILE B 448
REMARK 465 VAL B 449
REMARK 465 ALA B 450
REMARK 465 THR B 451
REMARK 465 ASN B 452
REMARK 465 ALA B 453
REMARK 465 ILE B 454
REMARK 465 GLU B 455
REMARK 465 SER B 456
REMARK 465 GLY B 457
REMARK 465 VAL B 458
REMARK 465 THR B 459
REMARK 465 LEU B 460
REMARK 465 PRO B 461
REMARK 465 ASP B 462
REMARK 465 LEU B 463
REMARK 465 ASP B 464
REMARK 465 THR B 465
REMARK 465 VAL B 466
REMARK 465 ILE B 467
REMARK 465 ARG B 506
REMARK 465 VAL B 507
REMARK 465 GLY B 508
REMARK 465 ARG B 509
REMARK 465 VAL B 510
REMARK 465 LYS B 511
REMARK 465 PRO B 512
REMARK 465 GLY B 513
REMARK 465 ARG B 514
REMARK 465 TYR B 515
REMARK 465 TYR B 516
REMARK 465 ALA C 354
REMARK 465 GLY C 355
REMARK 465 SER C 356
REMARK 465 VAL C 357
REMARK 465 THR C 358
REMARK 465 THR C 359
REMARK 465 THR C 360
REMARK 465 GLY C 361
REMARK 465 GLN C 362
REMARK 465 LYS C 363
REMARK 465 HIS C 364
REMARK 465 PRO C 365
REMARK 465 ILE C 366
REMARK 465 GLU C 367
REMARK 465 GLU C 368
REMARK 465 PHE C 369
REMARK 465 ILE C 370
REMARK 465 ALA C 371
REMARK 465 PRO C 372
REMARK 465 GLU C 373
REMARK 465 VAL C 374
REMARK 465 MET C 375
REMARK 465 LYS C 376
REMARK 465 GLY C 377
REMARK 465 GLU C 378
REMARK 465 ASP C 379
REMARK 465 LEU C 380
REMARK 465 GLY C 381
REMARK 465 SER C 382
REMARK 465 GLN C 383
REMARK 465 PHE C 384
REMARK 465 LEU C 385
REMARK 465 ASP C 386
REMARK 465 ILE C 387
REMARK 465 ALA C 388
REMARK 465 GLY C 389
REMARK 465 LEU C 390
REMARK 465 LYS C 391
REMARK 465 ILE C 392
REMARK 465 PRO C 393
REMARK 465 VAL C 394
REMARK 465 ASP C 395
REMARK 465 GLU C 396
REMARK 465 MET C 397
REMARK 465 LYS C 398
REMARK 465 GLY C 399
REMARK 465 ASN C 400
REMARK 465 MET C 401
REMARK 465 GLY C 422
REMARK 465 TYR C 423
REMARK 465 ASN C 424
REMARK 465 SER C 425
REMARK 465 GLY C 426
REMARK 465 TYR C 427
REMARK 465 TYR C 428
REMARK 465 TYR C 429
REMARK 465 SER C 430
REMARK 465 GLY C 431
REMARK 465 GLU C 432
REMARK 465 ASP C 433
REMARK 465 PRO C 434
REMARK 465 ALA C 435
REMARK 465 ASN C 436
REMARK 465 LEU C 437
REMARK 465 ARG C 438
REMARK 465 VAL C 439
REMARK 465 VAL C 440
REMARK 465 THR C 441
REMARK 465 SER C 442
REMARK 465 GLN C 443
REMARK 465 SER C 444
REMARK 465 PRO C 445
REMARK 465 TYR C 446
REMARK 465 VAL C 447
REMARK 465 ILE C 448
REMARK 465 ALA C 453
REMARK 465 ILE C 454
REMARK 465 GLU C 455
REMARK 465 SER C 456
REMARK 465 GLY C 457
REMARK 465 VAL C 458
REMARK 465 THR C 459
REMARK 465 LEU C 460
REMARK 465 PRO C 461
REMARK 465 ASP C 462
REMARK 465 LEU C 463
REMARK 465 ASP C 464
REMARK 465 THR C 465
REMARK 465 VAL C 466
REMARK 465 ILE C 467
REMARK 465 VAL C 507
REMARK 465 GLY C 508
REMARK 465 ARG C 509
REMARK 465 VAL C 510
REMARK 465 LYS C 511
REMARK 465 PRO C 512
REMARK 465 GLY C 513
REMARK 465 ARG C 514
REMARK 465 TYR C 515
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 NH2 ARG B 635 O ASP B 640 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 461 97.10 -61.28
REMARK 500 GLN A 519 47.99 -87.34
REMARK 500 THR B 234 -57.63 -120.88
REMARK 500 MET B 283 108.14 -52.51
REMARK 500 MET B 288 24.20 -143.23
REMARK 500 GLN B 519 49.08 -90.85
REMARK 500 GLU C 243 -62.14 -107.02
REMARK 500 LYS C 270 -54.09 -130.18
REMARK 500 PHE C 404 78.41 -116.97
REMARK 500 THR C 451 -169.26 -124.22
REMARK 500 PRO C 583 159.93 -47.55
REMARK 500 ASP C 624 42.71 -100.11
REMARK 500 LEU C 658 2.13 -66.90
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5GVU A 208 683 UNP Q9IFH8 Q9IFH8_BVDV 1939 2414
DBREF 5GVU B 208 683 UNP Q9IFH8 Q9IFH8_BVDV 1939 2414
DBREF 5GVU C 208 683 UNP Q9IFH8 Q9IFH8_BVDV 1939 2414
SEQRES 1 A 476 GLU MET VAL LYS LYS ILE THR SER MET ASN ARG GLY ASP
SEQRES 2 A 476 PHE LYS GLN ILE THR LEU ALA THR GLY ALA GLY LYS THR
SEQRES 3 A 476 THR GLU LEU PRO LYS ALA VAL ILE GLU GLU ILE GLY ARG
SEQRES 4 A 476 HIS LYS ARG VAL LEU VAL LEU ILE PRO LEU ARG ALA ALA
SEQRES 5 A 476 ALA GLU SER VAL TYR GLN TYR MET ARG LEU LYS HIS PRO
SEQRES 6 A 476 SER ILE SER PHE ASN LEU ARG ILE GLY ASP MET LYS GLU
SEQRES 7 A 476 GLY ASP MET ALA THR GLY ILE THR TYR ALA SER TYR GLY
SEQRES 8 A 476 TYR PHE CYS GLN MET PRO GLN PRO LYS LEU ARG ALA ALA
SEQRES 9 A 476 MET VAL GLU TYR SER TYR ILE PHE LEU ASP GLU TYR HIS
SEQRES 10 A 476 CYS ALA THR PRO GLU GLN LEU ALA ILE ILE GLY LYS ILE
SEQRES 11 A 476 HIS ARG PHE SER GLU SER ILE ARG VAL VAL ALA MET THR
SEQRES 12 A 476 ALA THR PRO ALA GLY SER VAL THR THR THR GLY GLN LYS
SEQRES 13 A 476 HIS PRO ILE GLU GLU PHE ILE ALA PRO GLU VAL MET LYS
SEQRES 14 A 476 GLY GLU ASP LEU GLY SER GLN PHE LEU ASP ILE ALA GLY
SEQRES 15 A 476 LEU LYS ILE PRO VAL ASP GLU MET LYS GLY ASN MET LEU
SEQRES 16 A 476 VAL PHE VAL PRO THR ARG ASN MET ALA VAL GLU VAL ALA
SEQRES 17 A 476 LYS LYS LEU LYS ALA LYS GLY TYR ASN SER GLY TYR TYR
SEQRES 18 A 476 TYR SER GLY GLU ASP PRO ALA ASN LEU ARG VAL VAL THR
SEQRES 19 A 476 SER GLN SER PRO TYR VAL ILE VAL ALA THR ASN ALA ILE
SEQRES 20 A 476 GLU SER GLY VAL THR LEU PRO ASP LEU ASP THR VAL ILE
SEQRES 21 A 476 ASP THR GLY LEU LYS CYS GLU LYS ARG VAL ARG VAL SER
SEQRES 22 A 476 SER LYS ILE PRO PHE ILE VAL THR GLY LEU LYS ARG MET
SEQRES 23 A 476 ALA VAL THR VAL GLY GLU GLN ALA GLN ARG ARG GLY ARG
SEQRES 24 A 476 VAL GLY ARG VAL LYS PRO GLY ARG TYR TYR ARG SER GLN
SEQRES 25 A 476 GLU THR ALA THR GLY SER LYS ASP TYR HIS TYR ASP LEU
SEQRES 26 A 476 LEU GLN ALA GLN ARG TYR GLY ILE GLU ASP GLY ILE ASN
SEQRES 27 A 476 VAL THR LYS SER PHE ARG GLU MET ASN TYR ASP TRP SER
SEQRES 28 A 476 LEU TYR GLU GLU ASP SER LEU LEU ILE THR GLN LEU GLU
SEQRES 29 A 476 ILE LEU ASN ASN LEU LEU ILE SER GLU ASP LEU PRO ALA
SEQRES 30 A 476 ALA VAL LYS ASN ILE MET ALA ARG THR ASP HIS PRO GLU
SEQRES 31 A 476 PRO ILE GLN LEU ALA TYR ASN SER TYR GLU VAL GLN VAL
SEQRES 32 A 476 PRO VAL LEU PHE PRO LYS ILE ARG ASN GLY GLU VAL THR
SEQRES 33 A 476 ASP THR TYR GLU ASN TYR SER PHE LEU ASN ALA ARG LYS
SEQRES 34 A 476 LEU GLY GLU ASP VAL PRO VAL TYR ILE TYR ALA THR GLU
SEQRES 35 A 476 ASP GLU ASP LEU ALA VAL ASP LEU LEU GLY LEU ASP TRP
SEQRES 36 A 476 PRO ASP PRO GLY ASN GLN GLN VAL VAL GLU THR GLY LYS
SEQRES 37 A 476 ALA LEU LYS GLN VAL THR GLY LEU
SEQRES 1 B 476 GLU MET VAL LYS LYS ILE THR SER MET ASN ARG GLY ASP
SEQRES 2 B 476 PHE LYS GLN ILE THR LEU ALA THR GLY ALA GLY LYS THR
SEQRES 3 B 476 THR GLU LEU PRO LYS ALA VAL ILE GLU GLU ILE GLY ARG
SEQRES 4 B 476 HIS LYS ARG VAL LEU VAL LEU ILE PRO LEU ARG ALA ALA
SEQRES 5 B 476 ALA GLU SER VAL TYR GLN TYR MET ARG LEU LYS HIS PRO
SEQRES 6 B 476 SER ILE SER PHE ASN LEU ARG ILE GLY ASP MET LYS GLU
SEQRES 7 B 476 GLY ASP MET ALA THR GLY ILE THR TYR ALA SER TYR GLY
SEQRES 8 B 476 TYR PHE CYS GLN MET PRO GLN PRO LYS LEU ARG ALA ALA
SEQRES 9 B 476 MET VAL GLU TYR SER TYR ILE PHE LEU ASP GLU TYR HIS
SEQRES 10 B 476 CYS ALA THR PRO GLU GLN LEU ALA ILE ILE GLY LYS ILE
SEQRES 11 B 476 HIS ARG PHE SER GLU SER ILE ARG VAL VAL ALA MET THR
SEQRES 12 B 476 ALA THR PRO ALA GLY SER VAL THR THR THR GLY GLN LYS
SEQRES 13 B 476 HIS PRO ILE GLU GLU PHE ILE ALA PRO GLU VAL MET LYS
SEQRES 14 B 476 GLY GLU ASP LEU GLY SER GLN PHE LEU ASP ILE ALA GLY
SEQRES 15 B 476 LEU LYS ILE PRO VAL ASP GLU MET LYS GLY ASN MET LEU
SEQRES 16 B 476 VAL PHE VAL PRO THR ARG ASN MET ALA VAL GLU VAL ALA
SEQRES 17 B 476 LYS LYS LEU LYS ALA LYS GLY TYR ASN SER GLY TYR TYR
SEQRES 18 B 476 TYR SER GLY GLU ASP PRO ALA ASN LEU ARG VAL VAL THR
SEQRES 19 B 476 SER GLN SER PRO TYR VAL ILE VAL ALA THR ASN ALA ILE
SEQRES 20 B 476 GLU SER GLY VAL THR LEU PRO ASP LEU ASP THR VAL ILE
SEQRES 21 B 476 ASP THR GLY LEU LYS CYS GLU LYS ARG VAL ARG VAL SER
SEQRES 22 B 476 SER LYS ILE PRO PHE ILE VAL THR GLY LEU LYS ARG MET
SEQRES 23 B 476 ALA VAL THR VAL GLY GLU GLN ALA GLN ARG ARG GLY ARG
SEQRES 24 B 476 VAL GLY ARG VAL LYS PRO GLY ARG TYR TYR ARG SER GLN
SEQRES 25 B 476 GLU THR ALA THR GLY SER LYS ASP TYR HIS TYR ASP LEU
SEQRES 26 B 476 LEU GLN ALA GLN ARG TYR GLY ILE GLU ASP GLY ILE ASN
SEQRES 27 B 476 VAL THR LYS SER PHE ARG GLU MET ASN TYR ASP TRP SER
SEQRES 28 B 476 LEU TYR GLU GLU ASP SER LEU LEU ILE THR GLN LEU GLU
SEQRES 29 B 476 ILE LEU ASN ASN LEU LEU ILE SER GLU ASP LEU PRO ALA
SEQRES 30 B 476 ALA VAL LYS ASN ILE MET ALA ARG THR ASP HIS PRO GLU
SEQRES 31 B 476 PRO ILE GLN LEU ALA TYR ASN SER TYR GLU VAL GLN VAL
SEQRES 32 B 476 PRO VAL LEU PHE PRO LYS ILE ARG ASN GLY GLU VAL THR
SEQRES 33 B 476 ASP THR TYR GLU ASN TYR SER PHE LEU ASN ALA ARG LYS
SEQRES 34 B 476 LEU GLY GLU ASP VAL PRO VAL TYR ILE TYR ALA THR GLU
SEQRES 35 B 476 ASP GLU ASP LEU ALA VAL ASP LEU LEU GLY LEU ASP TRP
SEQRES 36 B 476 PRO ASP PRO GLY ASN GLN GLN VAL VAL GLU THR GLY LYS
SEQRES 37 B 476 ALA LEU LYS GLN VAL THR GLY LEU
SEQRES 1 C 476 GLU MET VAL LYS LYS ILE THR SER MET ASN ARG GLY ASP
SEQRES 2 C 476 PHE LYS GLN ILE THR LEU ALA THR GLY ALA GLY LYS THR
SEQRES 3 C 476 THR GLU LEU PRO LYS ALA VAL ILE GLU GLU ILE GLY ARG
SEQRES 4 C 476 HIS LYS ARG VAL LEU VAL LEU ILE PRO LEU ARG ALA ALA
SEQRES 5 C 476 ALA GLU SER VAL TYR GLN TYR MET ARG LEU LYS HIS PRO
SEQRES 6 C 476 SER ILE SER PHE ASN LEU ARG ILE GLY ASP MET LYS GLU
SEQRES 7 C 476 GLY ASP MET ALA THR GLY ILE THR TYR ALA SER TYR GLY
SEQRES 8 C 476 TYR PHE CYS GLN MET PRO GLN PRO LYS LEU ARG ALA ALA
SEQRES 9 C 476 MET VAL GLU TYR SER TYR ILE PHE LEU ASP GLU TYR HIS
SEQRES 10 C 476 CYS ALA THR PRO GLU GLN LEU ALA ILE ILE GLY LYS ILE
SEQRES 11 C 476 HIS ARG PHE SER GLU SER ILE ARG VAL VAL ALA MET THR
SEQRES 12 C 476 ALA THR PRO ALA GLY SER VAL THR THR THR GLY GLN LYS
SEQRES 13 C 476 HIS PRO ILE GLU GLU PHE ILE ALA PRO GLU VAL MET LYS
SEQRES 14 C 476 GLY GLU ASP LEU GLY SER GLN PHE LEU ASP ILE ALA GLY
SEQRES 15 C 476 LEU LYS ILE PRO VAL ASP GLU MET LYS GLY ASN MET LEU
SEQRES 16 C 476 VAL PHE VAL PRO THR ARG ASN MET ALA VAL GLU VAL ALA
SEQRES 17 C 476 LYS LYS LEU LYS ALA LYS GLY TYR ASN SER GLY TYR TYR
SEQRES 18 C 476 TYR SER GLY GLU ASP PRO ALA ASN LEU ARG VAL VAL THR
SEQRES 19 C 476 SER GLN SER PRO TYR VAL ILE VAL ALA THR ASN ALA ILE
SEQRES 20 C 476 GLU SER GLY VAL THR LEU PRO ASP LEU ASP THR VAL ILE
SEQRES 21 C 476 ASP THR GLY LEU LYS CYS GLU LYS ARG VAL ARG VAL SER
SEQRES 22 C 476 SER LYS ILE PRO PHE ILE VAL THR GLY LEU LYS ARG MET
SEQRES 23 C 476 ALA VAL THR VAL GLY GLU GLN ALA GLN ARG ARG GLY ARG
SEQRES 24 C 476 VAL GLY ARG VAL LYS PRO GLY ARG TYR TYR ARG SER GLN
SEQRES 25 C 476 GLU THR ALA THR GLY SER LYS ASP TYR HIS TYR ASP LEU
SEQRES 26 C 476 LEU GLN ALA GLN ARG TYR GLY ILE GLU ASP GLY ILE ASN
SEQRES 27 C 476 VAL THR LYS SER PHE ARG GLU MET ASN TYR ASP TRP SER
SEQRES 28 C 476 LEU TYR GLU GLU ASP SER LEU LEU ILE THR GLN LEU GLU
SEQRES 29 C 476 ILE LEU ASN ASN LEU LEU ILE SER GLU ASP LEU PRO ALA
SEQRES 30 C 476 ALA VAL LYS ASN ILE MET ALA ARG THR ASP HIS PRO GLU
SEQRES 31 C 476 PRO ILE GLN LEU ALA TYR ASN SER TYR GLU VAL GLN VAL
SEQRES 32 C 476 PRO VAL LEU PHE PRO LYS ILE ARG ASN GLY GLU VAL THR
SEQRES 33 C 476 ASP THR TYR GLU ASN TYR SER PHE LEU ASN ALA ARG LYS
SEQRES 34 C 476 LEU GLY GLU ASP VAL PRO VAL TYR ILE TYR ALA THR GLU
SEQRES 35 C 476 ASP GLU ASP LEU ALA VAL ASP LEU LEU GLY LEU ASP TRP
SEQRES 36 C 476 PRO ASP PRO GLY ASN GLN GLN VAL VAL GLU THR GLY LYS
SEQRES 37 C 476 ALA LEU LYS GLN VAL THR GLY LEU
FORMUL 4 HOH *38(H2 O)
HELIX 1 AA1 MET A 209 THR A 214 1 6
HELIX 2 AA2 GLY A 231 GLY A 245 1 15
HELIX 3 AA3 LEU A 256 HIS A 271 1 16
HELIX 4 AA4 TYR A 297 CYS A 301 1 5
HELIX 5 AA5 PRO A 304 VAL A 313 1 10
HELIX 6 AA6 GLU A 322 ALA A 326 5 5
HELIX 7 AA7 THR A 327 HIS A 338 1 12
HELIX 8 AA8 ARG A 339 ILE A 344 5 6
HELIX 9 AA9 PRO A 393 LYS A 398 5 6
HELIX 10 AB1 ASN A 409 ALA A 420 1 12
HELIX 11 AB2 ALA A 435 SER A 442 1 8
HELIX 12 AB3 THR A 496 GLY A 505 1 10
HELIX 13 AB4 TYR A 528 GLN A 536 1 9
HELIX 14 AB5 ARG A 537 ILE A 540 5 4
HELIX 15 AB6 ASN A 545 TRP A 557 1 13
HELIX 16 AB7 ASP A 563 ILE A 578 1 16
HELIX 17 AB8 PRO A 583 THR A 593 1 11
HELIX 18 AB9 PRO A 598 SER A 605 1 8
HELIX 19 AC1 GLU A 649 LEU A 658 1 10
HELIX 20 AC2 ASN A 667 LEU A 683 1 17
HELIX 21 AC3 MET B 209 SER B 215 1 7
HELIX 22 AC4 THR B 234 GLY B 245 1 12
HELIX 23 AC5 LEU B 256 HIS B 271 1 16
HELIX 24 AC6 TYR B 297 GLN B 302 1 6
HELIX 25 AC7 PRO B 304 VAL B 313 1 10
HELIX 26 AC8 TYR B 323 ALA B 326 5 4
HELIX 27 AC9 THR B 327 ILE B 337 1 11
HELIX 28 AD1 PHE B 340 ILE B 344 5 5
HELIX 29 AD2 GLN B 500 GLY B 505 1 6
HELIX 30 AD3 TYR B 528 GLN B 536 1 9
HELIX 31 AD4 ARG B 537 ILE B 540 5 4
HELIX 32 AD5 ASN B 545 SER B 558 1 14
HELIX 33 AD6 ASP B 563 ILE B 578 1 16
HELIX 34 AD7 PRO B 583 THR B 593 1 11
HELIX 35 AD8 PRO B 598 SER B 605 1 8
HELIX 36 AD9 GLU B 649 LEU B 658 1 10
HELIX 37 AE1 ASN B 667 GLY B 682 1 16
HELIX 38 AE2 MET C 209 SER C 215 1 7
HELIX 39 AE3 GLY C 231 GLU C 242 1 12
HELIX 40 AE4 ARG C 257 LEU C 269 1 13
HELIX 41 AE5 TYR C 297 CYS C 301 1 5
HELIX 42 AE6 PRO C 304 VAL C 313 1 10
HELIX 43 AE7 TYR C 323 ALA C 326 5 4
HELIX 44 AE8 THR C 327 HIS C 338 1 12
HELIX 45 AE9 ARG C 339 SER C 343 5 5
HELIX 46 AF1 THR C 407 LYS C 417 1 11
HELIX 47 AF2 THR C 496 GLN C 502 1 7
HELIX 48 AF3 TYR C 528 GLN C 536 1 9
HELIX 49 AF4 ARG C 537 ILE C 540 5 4
HELIX 50 AF5 ASN C 545 SER C 558 1 14
HELIX 51 AF6 ASP C 563 ILE C 578 1 16
HELIX 52 AF7 PRO C 583 THR C 593 1 11
HELIX 53 AF8 PRO C 598 SER C 605 1 8
HELIX 54 AF9 GLU C 649 LEU C 658 1 10
HELIX 55 AG1 ASN C 667 GLY C 682 1 16
SHEET 1 AA1 6 PHE A 221 ILE A 224 0
SHEET 2 AA1 6 VAL A 346 MET A 349 1 O ALA A 348 N LYS A 222
SHEET 3 AA1 6 TYR A 317 LEU A 320 1 N LEU A 320 O VAL A 347
SHEET 4 AA1 6 VAL A 250 ILE A 254 1 N LEU A 251 O PHE A 319
SHEET 5 AA1 6 ILE A 292 SER A 296 1 O THR A 293 N VAL A 250
SHEET 6 AA1 6 PHE A 276 ARG A 279 1 N ASN A 277 O TYR A 294
SHEET 1 AA2 5 ILE A 366 ILE A 370 0
SHEET 2 AA2 5 GLY A 513 ARG A 517 1 O TYR A 515 N GLU A 367
SHEET 3 AA2 5 THR A 465 ASP A 468 1 N ASP A 468 O TYR A 516
SHEET 4 AA2 5 MET A 401 PHE A 404 1 N LEU A 402 O ILE A 467
SHEET 5 AA2 5 VAL A 447 ALA A 450 1 O ILE A 448 N VAL A 403
SHEET 1 AA3 2 LEU A 385 ILE A 387 0
SHEET 2 AA3 2 LEU A 390 ILE A 392 -1 O ILE A 392 N LEU A 385
SHEET 1 AA4 3 LEU A 471 VAL A 479 0
SHEET 2 AA4 3 ILE A 486 ALA A 494 -1 O VAL A 487 N ARG A 478
SHEET 3 AA4 3 TYR A 646 THR A 648 1 O ALA A 647 N ILE A 486
SHEET 1 AA5 2 VAL A 612 LEU A 613 0
SHEET 2 AA5 2 ARG A 635 LYS A 636 1 O ARG A 635 N LEU A 613
SHEET 1 AA6 2 ILE A 617 ARG A 618 0
SHEET 2 AA6 2 GLU A 621 VAL A 622 -1 O GLU A 621 N ARG A 618
SHEET 1 AA7 6 PHE B 221 ILE B 224 0
SHEET 2 AA7 6 VAL B 346 MET B 349 1 O ALA B 348 N ILE B 224
SHEET 3 AA7 6 TYR B 317 ASP B 321 1 N LEU B 320 O VAL B 347
SHEET 4 AA7 6 VAL B 250 ILE B 254 1 N LEU B 251 O TYR B 317
SHEET 5 AA7 6 ILE B 292 SER B 296 1 O ALA B 295 N ILE B 254
SHEET 6 AA7 6 PHE B 276 ARG B 279 1 N ASN B 277 O TYR B 294
SHEET 1 AA8 3 CYS B 473 VAL B 479 0
SHEET 2 AA8 3 ILE B 486 ARG B 492 -1 O LYS B 491 N GLU B 474
SHEET 3 AA8 3 TYR B 646 THR B 648 1 O ALA B 647 N ILE B 486
SHEET 1 AA9 2 VAL B 612 LEU B 613 0
SHEET 2 AA9 2 ARG B 635 LYS B 636 1 O ARG B 635 N LEU B 613
SHEET 1 AB1 2 ILE B 617 ARG B 618 0
SHEET 2 AB1 2 GLU B 621 VAL B 622 -1 O GLU B 621 N ARG B 618
SHEET 1 AB2 6 ASP C 220 ILE C 224 0
SHEET 2 AB2 6 ARG C 345 MET C 349 1 O VAL C 346 N ASP C 220
SHEET 3 AB2 6 TYR C 317 ASP C 321 1 N ILE C 318 O VAL C 347
SHEET 4 AB2 6 VAL C 250 ILE C 254 1 N LEU C 251 O PHE C 319
SHEET 5 AB2 6 ILE C 292 SER C 296 1 O THR C 293 N VAL C 252
SHEET 6 AB2 6 PHE C 276 ARG C 279 1 N ASN C 277 O ILE C 292
SHEET 1 AB3 3 LEU C 471 VAL C 479 0
SHEET 2 AB3 3 ILE C 486 ALA C 494 -1 O MET C 493 N LYS C 472
SHEET 3 AB3 3 TYR C 646 THR C 648 1 O ALA C 647 N ILE C 486
SHEET 1 AB4 2 VAL C 612 LEU C 613 0
SHEET 2 AB4 2 ARG C 635 LYS C 636 1 O ARG C 635 N LEU C 613
SHEET 1 AB5 2 PRO C 615 ARG C 618 0
SHEET 2 AB5 2 GLU C 621 TYR C 626 -1 O THR C 625 N LYS C 616
CISPEP 1 SER A 444 PRO A 445 0 -0.23
CISPEP 2 ILE A 483 PRO A 484 0 3.50
CISPEP 3 ILE B 483 PRO B 484 0 12.87
CISPEP 4 VAL B 497 GLY B 498 0 4.44
CISPEP 5 ILE C 483 PRO C 484 0 6.63
CRYST1 121.100 121.100 109.721 90.00 90.00 120.00 P 32 9
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 0.008258 0.004768 0.000000 0.00000
SCALE2 0.000000 0.009535 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009114 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
