HEADER TRANSFERASE/HYDROLASE 02-JAN-14 4CKB
TITLE VACCINIA VIRUS CAPPING ENZYME COMPLEXED WITH GTP AND SAH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MRNA-CAPPING ENZYME CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: VIRUS TERMINATION FACTOR LARGE SUBUNIT, VTF LARGE SUBUNIT,
COMPND 5 MRNA-CAPPING ENZYME 97 KDA SUBUNIT, MRNA-CAPPING ENZYME D1 SUBUNIT,
COMPND 6 MRNA-CAPPING ENZYME LARGE SUBUNIT, POLYNUCLEOTIDE 5'-TRIPHOSPHATASE,
COMPND 7 MRNA 5'-TRIPHOSPHATASE, TPASE, MRNA GUANYLYLTRANSFERASE, GTP--RNA
COMPND 8 GUANYLYLTRANSFERASE, GTASE, MRNA (GUANINE-N(7)-)-METHYLTRANSFERASE,
COMPND 9 MRNA CAP METHYLTRANSFERASE;
COMPND 10 EC: 3.1.3.33, 2.7.7.50, 2.1.1.56;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: MRNA-CAPPING ENZYME REGULATORY SUBUNIT;
COMPND 14 CHAIN: B, E;
COMPND 15 SYNONYM: VIRUS TERMINATION FACTOR SMALL SUBUNIT, VTF SMALL SUBUNIT,
COMPND 16 MRNA-CAPPING ENZYME 33 KDA SUBUNIT, MRNA-CAPPING ENZYME D12 SUBUNIT,
COMPND 17 MRNA-CAPPING ENZYME SMALL SUBUNIT;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS;
SOURCE 3 ORGANISM_TAXID: 10245;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: STAR PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-16B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: VACCINIA VIRUS;
SOURCE 12 ORGANISM_TAXID: 10245;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_VARIANT: STAR PLYSS;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: PET-16B
KEYWDS TRANSFERASE-HYDROLASE COMPLEX, TRIFUNCTIONAL VACCINIA VIRUS MRNA
KEYWDS 2 CAPPING ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR O.J.P.KYRIELEIS,J.CHANG,M.DE LA PENA,S.SHUMAN,S.CUSACK
REVDAT 2 20-DEC-23 4CKB 1 REMARK
REVDAT 1 19-MAR-14 4CKB 0
JRNL AUTH O.J.P.KYRIELEIS,J.CHANG,M.DE LA PENA,S.SHUMAN,S.CUSACK
JRNL TITL CRYSTAL STRUCTURE OF VACCINIA VIRUS MRNA CAPPING ENZYME
JRNL TITL 2 PROVIDES INSIGHTS INTO THE MECHANISM AND EVOLUTION OF THE
JRNL TITL 3 CAPPING APPARATUS.
JRNL REF STRUCTURE V. 22 452 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 24607143
JRNL DOI 10.1016/J.STR.2013.12.014
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 59782
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3184
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4316
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.3640
REMARK 3 BIN FREE R VALUE SET COUNT : 212
REMARK 3 BIN FREE R VALUE : 0.4270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17754
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 25
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.09000
REMARK 3 B22 (A**2) : -4.25000
REMARK 3 B33 (A**2) : -0.60000
REMARK 3 B12 (A**2) : -0.98000
REMARK 3 B13 (A**2) : 3.06000
REMARK 3 B23 (A**2) : -0.64000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.402
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.365
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.995
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 18193 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 17671 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24596 ; 1.126 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 40744 ; 0.700 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2176 ; 6.217 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 816 ;35.238 ;24.375
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3372 ;16.935 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 92 ;17.359 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2816 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20011 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4065 ; 0.001 ; 0.020
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): 8755 ; 1.915 ; 4.538
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8754 ; 1.915 ; 4.538
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10914 ; 3.347 ; 6.797
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 10915 ; 3.347 ; 6.797
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9438 ; 1.735 ; 4.705
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 9426 ; 1.731 ; 4.698
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 13663 ; 3.076 ; 6.962
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 20022 ; 5.572 ;34.973
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 20015 ; 5.556 ;34.950
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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 197 1
REMARK 3 1 D 1 D 197 1
REMARK 3 2 A 204 A 221 1
REMARK 3 2 D 204 D 221 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 1 A (A**2): 3377 ; 14.48 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 3377 ; 14.48 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 222 A 320 2
REMARK 3 1 D 222 D 320 2
REMARK 3 2 A 324 A 407 2
REMARK 3 2 D 324 D 407 2
REMARK 3 3 A 413 A 527 2
REMARK 3 3 D 413 D 527 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 3027 ; 0.02 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 3027 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 2 A (A**2): 1744 ; 12.43 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 1744 ; 12.43 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 3027 ; 12.61 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 3027 ; 12.61 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 544 A 728 1
REMARK 3 1 D 544 D 728 1
REMARK 3 2 A 735 A 844 1
REMARK 3 2 D 735 D 844 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 3 A (A**2): 4587 ; 7.25 ; 0.50
REMARK 3 TIGHT THERMAL 3 D (A**2): 4587 ; 7.25 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 287 1
REMARK 3 1 E 1 E 287 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 4 B (A**2): 4630 ; 15.43 ; 0.50
REMARK 3 TIGHT THERMAL 4 E (A**2): 4630 ; 15.43 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
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 1 A 221
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2970 68.7030 20.0450
REMARK 3 T TENSOR
REMARK 3 T11: 0.7276 T22: 0.1109
REMARK 3 T33: 0.2315 T12: 0.1032
REMARK 3 T13: 0.2152 T23: -0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 0.5045 L22: 1.4771
REMARK 3 L33: 0.6033 L12: 0.4453
REMARK 3 L13: 0.4465 L23: 0.8200
REMARK 3 S TENSOR
REMARK 3 S11: -0.1143 S12: 0.0363 S13: 0.0273
REMARK 3 S21: 0.2858 S22: 0.0675 S23: 0.1266
REMARK 3 S31: -0.0909 S32: -0.0000 S33: 0.0468
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 : D 1 D 221
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8410 -27.6430 -1.3130
REMARK 3 T TENSOR
REMARK 3 T11: 0.2935 T22: 0.3198
REMARK 3 T33: 0.3349 T12: 0.0252
REMARK 3 T13: -0.0201 T23: 0.0783
REMARK 3 L TENSOR
REMARK 3 L11: 1.5373 L22: 0.2652
REMARK 3 L33: 1.2409 L12: 0.0355
REMARK 3 L13: 0.4533 L23: -0.4600
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: 0.0389 S13: 0.0704
REMARK 3 S21: -0.1183 S22: -0.0685 S23: -0.0177
REMARK 3 S31: -0.0169 S32: 0.0286 S33: 0.0501
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 : A 222 A 528
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5290 49.7920 -6.2660
REMARK 3 T TENSOR
REMARK 3 T11: 0.5544 T22: 0.1314
REMARK 3 T33: 0.2120 T12: 0.0251
REMARK 3 T13: 0.0645 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.5533 L22: 1.0574
REMARK 3 L33: 0.5883 L12: 0.0944
REMARK 3 L13: 0.0491 L23: 0.3070
REMARK 3 S TENSOR
REMARK 3 S11: 0.1721 S12: 0.1020 S13: 0.0570
REMARK 3 S21: -0.2308 S22: -0.0408 S23: 0.0137
REMARK 3 S31: -0.0648 S32: -0.0696 S33: -0.1313
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 544 A 844
REMARK 3 RESIDUE RANGE : A 1845 A 1845
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4800 17.5550 9.5840
REMARK 3 T TENSOR
REMARK 3 T11: 0.3099 T22: 0.3573
REMARK 3 T33: 0.2661 T12: -0.0501
REMARK 3 T13: -0.0041 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 0.1377 L22: 1.6199
REMARK 3 L33: 1.8043 L12: 0.0626
REMARK 3 L13: -0.3794 L23: -0.2577
REMARK 3 S TENSOR
REMARK 3 S11: 0.0885 S12: -0.0442 S13: -0.1035
REMARK 3 S21: -0.0158 S22: -0.0028 S23: -0.0563
REMARK 3 S31: -0.3283 S32: 0.1650 S33: -0.0856
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 544 D 844
REMARK 3 RESIDUE RANGE : D 1845 D 1845
REMARK 3 ORIGIN FOR THE GROUP (A): -45.5660 -80.1670 9.1800
REMARK 3 T TENSOR
REMARK 3 T11: 0.3458 T22: 0.1556
REMARK 3 T33: 0.4179 T12: -0.1036
REMARK 3 T13: 0.1407 T23: -0.0755
REMARK 3 L TENSOR
REMARK 3 L11: 0.4104 L22: 1.4512
REMARK 3 L33: 1.9941 L12: -0.4620
REMARK 3 L13: -0.7842 L23: 0.4908
REMARK 3 S TENSOR
REMARK 3 S11: -0.1572 S12: 0.0954 S13: -0.1919
REMARK 3 S21: 0.1525 S22: -0.2598 S23: 0.2312
REMARK 3 S31: 0.0259 S32: -0.0608 S33: 0.4170
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 222 D 528
REMARK 3 RESIDUE RANGE : D 1846 D 1846
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4230 -46.1960 24.9440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2160 T22: 0.3640
REMARK 3 T33: 0.3408 T12: -0.0120
REMARK 3 T13: -0.0513 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 1.6418 L22: 0.4050
REMARK 3 L33: 0.5785 L12: -0.0763
REMARK 3 L13: 0.0482 L23: -0.3552
REMARK 3 S TENSOR
REMARK 3 S11: 0.0742 S12: -0.1960 S13: -0.1506
REMARK 3 S21: 0.0446 S22: -0.0523 S23: 0.0142
REMARK 3 S31: -0.0386 S32: 0.0369 S33: -0.0219
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 287
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7330 -2.1470 27.5390
REMARK 3 T TENSOR
REMARK 3 T11: 0.2540 T22: 0.4040
REMARK 3 T33: 0.2477 T12: 0.0342
REMARK 3 T13: -0.0486 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 1.8642 L22: 1.2461
REMARK 3 L33: 0.8986 L12: -1.0580
REMARK 3 L13: -0.2901 L23: -0.4290
REMARK 3 S TENSOR
REMARK 3 S11: -0.0413 S12: 0.0934 S13: -0.1101
REMARK 3 S21: 0.0730 S22: 0.0102 S23: -0.0335
REMARK 3 S31: -0.0484 S32: -0.1720 S33: 0.0311
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 287
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1460 -97.1310 -8.8950
REMARK 3 T TENSOR
REMARK 3 T11: 0.4150 T22: 0.2746
REMARK 3 T33: 0.3311 T12: 0.0403
REMARK 3 T13: 0.2821 T23: 0.0708
REMARK 3 L TENSOR
REMARK 3 L11: 0.7378 L22: 2.0691
REMARK 3 L33: 1.2512 L12: 0.3796
REMARK 3 L13: -0.2338 L23: 0.8552
REMARK 3 S TENSOR
REMARK 3 S11: 0.0625 S12: -0.1112 S13: 0.1720
REMARK 3 S21: -0.1174 S22: -0.2030 S23: -0.1102
REMARK 3 S31: 0.2187 S32: 0.3059 S33: 0.1405
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4CKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1290059323.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62966
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 2.370
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.31
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.430
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2VDW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION AT 4 MG/ML IN 40 MM
REMARK 280 TRIS-HCL, PH 8.0, 200 MM NACL, 5 MM DTT WITH 100 MM GTP, 5 MM
REMARK 280 MANGANESE CHLORIDE, AND 5 MM ADOMET. RESERVOIR SOLUTION 0.1 M
REMARK 280 CITRIC ACID, PH 6.5, 1.2 M LICL, 6% PEG6000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 GLN A 27
REMARK 465 ARG A 28
REMARK 465 SER A 29
REMARK 465 THR A 30
REMARK 465 ALA A 31
REMARK 465 TYR A 32
REMARK 465 GLU A 33
REMARK 465 PRO A 320
REMARK 465 VAL A 321
REMARK 465 ASN A 322
REMARK 465 ALA A 323
REMARK 465 ILE A 324
REMARK 465 TYR A 409
REMARK 465 PHE A 529
REMARK 465 ASN A 530
REMARK 465 GLU A 531
REMARK 465 ASP A 532
REMARK 465 LYS A 533
REMARK 465 LEU A 534
REMARK 465 SER A 535
REMARK 465 ASP A 536
REMARK 465 VAL A 537
REMARK 465 GLY A 538
REMARK 465 HIS A 539
REMARK 465 GLN A 540
REMARK 465 TYR A 541
REMARK 465 ALA A 542
REMARK 465 ASN A 543
REMARK 465 SER A 554
REMARK 465 TYR A 555
REMARK 465 PHE A 556
REMARK 465 THR A 557
REMARK 465 ASN A 558
REMARK 465 LYS A 559
REMARK 465 ARG A 560
REMARK 465 ASN B 121
REMARK 465 HIS B 122
REMARK 465 LEU B 123
REMARK 465 ARG D 28
REMARK 465 SER D 29
REMARK 465 THR D 30
REMARK 465 ALA D 31
REMARK 465 TYR D 32
REMARK 465 GLU D 33
REMARK 465 ASN D 322
REMARK 465 ALA D 323
REMARK 465 PHE D 529
REMARK 465 ASN D 530
REMARK 465 GLU D 531
REMARK 465 ASP D 532
REMARK 465 LYS D 533
REMARK 465 LEU D 534
REMARK 465 SER D 535
REMARK 465 ASP D 536
REMARK 465 VAL D 537
REMARK 465 GLY D 538
REMARK 465 HIS D 539
REMARK 465 GLN D 540
REMARK 465 TYR D 541
REMARK 465 ALA D 542
REMARK 465 ASN D 543
REMARK 465 TYR D 555
REMARK 465 PHE D 556
REMARK 465 THR D 557
REMARK 465 ASN D 558
REMARK 465 LYS D 559
REMARK 465 ARG D 560
REMARK 465 THR D 561
REMARK 465 ASN E 121
REMARK 465 HIS E 122
REMARK 465 LEU E 123
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 HIS A 86 -64.51 -100.30
REMARK 500 LEU A 88 -26.83 -36.66
REMARK 500 ASP A 89 31.69 -66.34
REMARK 500 VAL A 110 -63.53 -93.53
REMARK 500 TYR A 137 32.21 -98.29
REMARK 500 LYS A 154 -56.38 70.28
REMARK 500 ASP A 199 155.00 95.53
REMARK 500 ASP A 307 72.87 -168.29
REMARK 500 LYS A 308 -60.61 71.22
REMARK 500 SER A 420 13.72 -142.52
REMARK 500 ASN A 448 -110.56 -101.47
REMARK 500 ASN A 455 -10.92 76.16
REMARK 500 ASP A 545 56.58 -140.89
REMARK 500 GLU A 552 78.27 40.52
REMARK 500 LEU A 586 -133.32 -90.08
REMARK 500 TYR A 668 -70.99 -57.09
REMARK 500 ALA A 680 -22.36 -166.16
REMARK 500 THR A 711 -163.07 -170.05
REMARK 500 SER A 734 -31.76 -32.29
REMARK 500 ASP A 784 119.65 -163.69
REMARK 500 LYS A 823 77.54 -68.68
REMARK 500 ASN B 26 60.75 -166.96
REMARK 500 ILE B 47 -48.43 -136.27
REMARK 500 ASN B 85 -65.48 -95.76
REMARK 500 SER B 93 49.84 -100.59
REMARK 500 VAL B 148 -87.76 -145.44
REMARK 500 ASP B 192 42.20 -94.08
REMARK 500 ASP B 200 84.86 61.47
REMARK 500 ILE B 232 -39.22 -160.77
REMARK 500 SER B 269 130.23 -18.41
REMARK 500 HIS D 86 -64.91 -99.06
REMARK 500 LEU D 88 -25.11 -37.62
REMARK 500 ASP D 89 32.95 -68.12
REMARK 500 VAL D 110 -61.59 -94.81
REMARK 500 TYR D 137 32.36 -97.40
REMARK 500 LYS D 154 -56.89 69.72
REMARK 500 ASP D 199 167.30 106.23
REMARK 500 ASP D 307 71.87 -167.19
REMARK 500 LYS D 308 -58.94 71.37
REMARK 500 GLU D 319 98.20 55.65
REMARK 500 PRO D 320 -159.71 -88.31
REMARK 500 ASP D 340 46.74 39.98
REMARK 500 SER D 420 13.99 -142.59
REMARK 500 ASN D 448 -110.47 -98.82
REMARK 500 ASN D 455 -10.35 76.35
REMARK 500 ASP D 545 57.08 -141.13
REMARK 500 GLU D 552 79.22 40.85
REMARK 500 VAL D 553 68.98 -159.98
REMARK 500 LEU D 586 -132.26 -89.35
REMARK 500 TYR D 668 -71.22 -55.94
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1845
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH D 1845
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP D 1846
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CKC RELATED DB: PDB
REMARK 900 VACCINIA VIRUS CAPPING ENZYME COMPLEXED WITH SAH (MONOCLINIC FORM)
REMARK 900 RELATED ID: 4CKE RELATED DB: PDB
REMARK 900 VACCINIA VIRUS CAPPING ENZYME COMPLEXED WITH SAH IN P1 FORM
DBREF 4CKB A 1 844 UNP P04298 MCEL_VACCW 1 844
DBREF 4CKB B 1 287 UNP P04318 MCES_VACCW 1 287
DBREF 4CKB D 1 844 UNP P04298 MCEL_VACCW 1 844
DBREF 4CKB E 1 287 UNP P04318 MCES_VACCW 1 287
SEQRES 1 A 844 MET ASP ALA ASN VAL VAL SER SER SER THR ILE ALA THR
SEQRES 2 A 844 TYR ILE ASP ALA LEU ALA LYS ASN ALA SER GLU LEU GLU
SEQRES 3 A 844 GLN ARG SER THR ALA TYR GLU ILE ASN ASN GLU LEU GLU
SEQRES 4 A 844 LEU VAL PHE ILE LYS PRO PRO LEU ILE THR LEU THR ASN
SEQRES 5 A 844 VAL VAL ASN ILE SER THR ILE GLN GLU SER PHE ILE ARG
SEQRES 6 A 844 PHE THR VAL THR ASN LYS GLU GLY VAL LYS ILE ARG THR
SEQRES 7 A 844 LYS ILE PRO LEU SER LYS VAL HIS GLY LEU ASP VAL LYS
SEQRES 8 A 844 ASN VAL GLN LEU VAL ASP ALA ILE ASP ASN ILE VAL TRP
SEQRES 9 A 844 GLU LYS LYS SER LEU VAL THR GLU ASN ARG LEU HIS LYS
SEQRES 10 A 844 GLU CYS LEU LEU ARG LEU SER THR GLU GLU ARG HIS ILE
SEQRES 11 A 844 PHE LEU ASP TYR LYS LYS TYR GLY SER SER ILE ARG LEU
SEQRES 12 A 844 GLU LEU VAL ASN LEU ILE GLN ALA LYS THR LYS ASN PHE
SEQRES 13 A 844 THR ILE ASP PHE LYS LEU LYS TYR PHE LEU GLY SER GLY
SEQRES 14 A 844 ALA GLN SER LYS SER SER LEU LEU HIS ALA ILE ASN HIS
SEQRES 15 A 844 PRO LYS SER ARG PRO ASN THR SER LEU GLU ILE GLU PHE
SEQRES 16 A 844 THR PRO ARG ASP ASN GLU THR VAL PRO TYR ASP GLU LEU
SEQRES 17 A 844 ILE LYS GLU LEU THR THR LEU SER ARG HIS ILE PHE MET
SEQRES 18 A 844 ALA SER PRO GLU ASN VAL ILE LEU SER PRO PRO ILE ASN
SEQRES 19 A 844 ALA PRO ILE LYS THR PHE MET LEU PRO LYS GLN ASP ILE
SEQRES 20 A 844 VAL GLY LEU ASP LEU GLU ASN LEU TYR ALA VAL THR LYS
SEQRES 21 A 844 THR ASP GLY ILE PRO ILE THR ILE ARG VAL THR SER ASN
SEQRES 22 A 844 GLY LEU TYR CYS TYR PHE THR HIS LEU GLY TYR ILE ILE
SEQRES 23 A 844 ARG TYR PRO VAL LYS ARG ILE ILE ASP SER GLU VAL VAL
SEQRES 24 A 844 VAL PHE GLY GLU ALA VAL LYS ASP LYS ASN TRP THR VAL
SEQRES 25 A 844 TYR LEU ILE LYS LEU ILE GLU PRO VAL ASN ALA ILE ASN
SEQRES 26 A 844 ASP ARG LEU GLU GLU SER LYS TYR VAL GLU SER LYS LEU
SEQRES 27 A 844 VAL ASP ILE CYS ASP ARG ILE VAL PHE LYS SER LYS LYS
SEQRES 28 A 844 TYR GLU GLY PRO PHE THR THR THR SER GLU VAL VAL ASP
SEQRES 29 A 844 MET LEU SER THR TYR LEU PRO LYS GLN PRO GLU GLY VAL
SEQRES 30 A 844 ILE LEU PHE TYR SER LYS GLY PRO LYS SER ASN ILE ASP
SEQRES 31 A 844 PHE LYS ILE LYS LYS GLU ASN THR ILE ASP GLN THR ALA
SEQRES 32 A 844 ASN VAL VAL PHE ARG TYR MET SER SER GLU PRO ILE ILE
SEQRES 33 A 844 PHE GLY GLU SER SER ILE PHE VAL GLU TYR LYS LYS PHE
SEQRES 34 A 844 SER ASN ASP LYS GLY PHE PRO LYS GLU TYR GLY SER GLY
SEQRES 35 A 844 LYS ILE VAL LEU TYR ASN GLY VAL ASN TYR LEU ASN ASN
SEQRES 36 A 844 ILE TYR CYS LEU GLU TYR ILE ASN THR HIS ASN GLU VAL
SEQRES 37 A 844 GLY ILE LYS SER VAL VAL VAL PRO ILE LYS PHE ILE ALA
SEQRES 38 A 844 GLU PHE LEU VAL ASN GLY GLU ILE LEU LYS PRO ARG ILE
SEQRES 39 A 844 ASP LYS THR MET LYS TYR ILE ASN SER GLU ASP TYR TYR
SEQRES 40 A 844 GLY ASN GLN HIS ASN ILE ILE VAL GLU HIS LEU ARG ASP
SEQRES 41 A 844 GLN SER ILE LYS ILE GLY ASP ILE PHE ASN GLU ASP LYS
SEQRES 42 A 844 LEU SER ASP VAL GLY HIS GLN TYR ALA ASN ASN ASP LYS
SEQRES 43 A 844 PHE ARG LEU ASN PRO GLU VAL SER TYR PHE THR ASN LYS
SEQRES 44 A 844 ARG THR ARG GLY PRO LEU GLY ILE LEU SER ASN TYR VAL
SEQRES 45 A 844 LYS THR LEU LEU ILE SER MET TYR CYS SER LYS THR PHE
SEQRES 46 A 844 LEU ASP ASP SER ASN LYS ARG LYS VAL LEU ALA ILE ASP
SEQRES 47 A 844 PHE GLY ASN GLY ALA ASP LEU GLU LYS TYR PHE TYR GLY
SEQRES 48 A 844 GLU ILE ALA LEU LEU VAL ALA THR ASP PRO ASP ALA ASP
SEQRES 49 A 844 ALA ILE ALA ARG GLY ASN GLU ARG TYR ASN LYS LEU ASN
SEQRES 50 A 844 SER GLY ILE LYS THR LYS TYR TYR LYS PHE ASP TYR ILE
SEQRES 51 A 844 GLN GLU THR ILE ARG SER ASP THR PHE VAL SER SER VAL
SEQRES 52 A 844 ARG GLU VAL PHE TYR PHE GLY LYS PHE ASN ILE ILE ASP
SEQRES 53 A 844 TRP GLN PHE ALA ILE HIS TYR SER PHE HIS PRO ARG HIS
SEQRES 54 A 844 TYR ALA THR VAL MET ASN ASN LEU SER GLU LEU THR ALA
SEQRES 55 A 844 SER GLY GLY LYS VAL LEU ILE THR THR MET ASP GLY ASP
SEQRES 56 A 844 LYS LEU SER LYS LEU THR ASP LYS LYS THR PHE ILE ILE
SEQRES 57 A 844 HIS LYS ASN LEU PRO SER SER GLU ASN TYR MET SER VAL
SEQRES 58 A 844 GLU LYS ILE ALA ASP ASP ARG ILE VAL VAL TYR ASN PRO
SEQRES 59 A 844 SER THR MET SER THR PRO MET THR GLU TYR ILE ILE LYS
SEQRES 60 A 844 LYS ASN ASP ILE VAL ARG VAL PHE ASN GLU TYR GLY PHE
SEQRES 61 A 844 VAL LEU VAL ASP ASN VAL ASP PHE ALA THR ILE ILE GLU
SEQRES 62 A 844 ARG SER LYS LYS PHE ILE ASN GLY ALA SER THR MET GLU
SEQRES 63 A 844 ASP ARG PRO SER THR ARG ASN PHE PHE GLU LEU ASN ARG
SEQRES 64 A 844 GLY ALA ILE LYS CYS GLU GLY LEU ASP VAL GLU ASP LEU
SEQRES 65 A 844 LEU SER TYR TYR VAL VAL TYR VAL PHE SER LYS ARG
SEQRES 1 B 287 MET ASP GLU ILE VAL LYS ASN ILE ARG GLU GLY THR HIS
SEQRES 2 B 287 VAL LEU LEU PRO PHE TYR GLU THR LEU PRO GLU LEU ASN
SEQRES 3 B 287 LEU SER LEU GLY LYS SER PRO LEU PRO SER LEU GLU TYR
SEQRES 4 B 287 GLY ALA ASN TYR PHE LEU GLN ILE SER ARG VAL ASN ASP
SEQRES 5 B 287 LEU ASN ARG MET PRO THR ASP MET LEU LYS LEU PHE THR
SEQRES 6 B 287 HIS ASP ILE MET LEU PRO GLU SER ASP LEU ASP LYS VAL
SEQRES 7 B 287 TYR GLU ILE LEU LYS ILE ASN SER VAL LYS TYR TYR GLY
SEQRES 8 B 287 ARG SER THR LYS ALA ASP ALA VAL VAL ALA ASP LEU SER
SEQRES 9 B 287 ALA ARG ASN LYS LEU PHE LYS ARG GLU ARG ASP ALA ILE
SEQRES 10 B 287 LYS SER ASN ASN HIS LEU THR GLU ASN ASN LEU TYR ILE
SEQRES 11 B 287 SER ASP TYR LYS MET LEU THR PHE ASP VAL PHE ARG PRO
SEQRES 12 B 287 LEU PHE ASP PHE VAL ASN GLU LYS TYR CYS ILE ILE LYS
SEQRES 13 B 287 LEU PRO THR LEU PHE GLY ARG GLY VAL ILE ASP THR MET
SEQRES 14 B 287 ARG ILE TYR CYS SER LEU PHE LYS ASN VAL ARG LEU LEU
SEQRES 15 B 287 LYS CYS VAL SER ASP SER TRP LEU LYS ASP SER ALA ILE
SEQRES 16 B 287 MET VAL ALA SER ASP VAL CYS LYS LYS ASN LEU ASP LEU
SEQRES 17 B 287 PHE MET SER HIS VAL LYS SER VAL THR LYS SER SER SER
SEQRES 18 B 287 TRP LYS ASP VAL ASN SER VAL GLN PHE SER ILE LEU ASN
SEQRES 19 B 287 ASN PRO VAL ASP THR GLU PHE ILE ASN LYS PHE LEU GLU
SEQRES 20 B 287 PHE SER ASN ARG VAL TYR GLU ALA LEU TYR TYR VAL HIS
SEQRES 21 B 287 SER LEU LEU TYR SER SER MET THR SER ASP SER LYS SER
SEQRES 22 B 287 ILE GLU ASN LYS HIS GLN ARG ARG LEU VAL LYS LEU LEU
SEQRES 23 B 287 LEU
SEQRES 1 D 844 MET ASP ALA ASN VAL VAL SER SER SER THR ILE ALA THR
SEQRES 2 D 844 TYR ILE ASP ALA LEU ALA LYS ASN ALA SER GLU LEU GLU
SEQRES 3 D 844 GLN ARG SER THR ALA TYR GLU ILE ASN ASN GLU LEU GLU
SEQRES 4 D 844 LEU VAL PHE ILE LYS PRO PRO LEU ILE THR LEU THR ASN
SEQRES 5 D 844 VAL VAL ASN ILE SER THR ILE GLN GLU SER PHE ILE ARG
SEQRES 6 D 844 PHE THR VAL THR ASN LYS GLU GLY VAL LYS ILE ARG THR
SEQRES 7 D 844 LYS ILE PRO LEU SER LYS VAL HIS GLY LEU ASP VAL LYS
SEQRES 8 D 844 ASN VAL GLN LEU VAL ASP ALA ILE ASP ASN ILE VAL TRP
SEQRES 9 D 844 GLU LYS LYS SER LEU VAL THR GLU ASN ARG LEU HIS LYS
SEQRES 10 D 844 GLU CYS LEU LEU ARG LEU SER THR GLU GLU ARG HIS ILE
SEQRES 11 D 844 PHE LEU ASP TYR LYS LYS TYR GLY SER SER ILE ARG LEU
SEQRES 12 D 844 GLU LEU VAL ASN LEU ILE GLN ALA LYS THR LYS ASN PHE
SEQRES 13 D 844 THR ILE ASP PHE LYS LEU LYS TYR PHE LEU GLY SER GLY
SEQRES 14 D 844 ALA GLN SER LYS SER SER LEU LEU HIS ALA ILE ASN HIS
SEQRES 15 D 844 PRO LYS SER ARG PRO ASN THR SER LEU GLU ILE GLU PHE
SEQRES 16 D 844 THR PRO ARG ASP ASN GLU THR VAL PRO TYR ASP GLU LEU
SEQRES 17 D 844 ILE LYS GLU LEU THR THR LEU SER ARG HIS ILE PHE MET
SEQRES 18 D 844 ALA SER PRO GLU ASN VAL ILE LEU SER PRO PRO ILE ASN
SEQRES 19 D 844 ALA PRO ILE LYS THR PHE MET LEU PRO LYS GLN ASP ILE
SEQRES 20 D 844 VAL GLY LEU ASP LEU GLU ASN LEU TYR ALA VAL THR LYS
SEQRES 21 D 844 THR ASP GLY ILE PRO ILE THR ILE ARG VAL THR SER ASN
SEQRES 22 D 844 GLY LEU TYR CYS TYR PHE THR HIS LEU GLY TYR ILE ILE
SEQRES 23 D 844 ARG TYR PRO VAL LYS ARG ILE ILE ASP SER GLU VAL VAL
SEQRES 24 D 844 VAL PHE GLY GLU ALA VAL LYS ASP LYS ASN TRP THR VAL
SEQRES 25 D 844 TYR LEU ILE LYS LEU ILE GLU PRO VAL ASN ALA ILE ASN
SEQRES 26 D 844 ASP ARG LEU GLU GLU SER LYS TYR VAL GLU SER LYS LEU
SEQRES 27 D 844 VAL ASP ILE CYS ASP ARG ILE VAL PHE LYS SER LYS LYS
SEQRES 28 D 844 TYR GLU GLY PRO PHE THR THR THR SER GLU VAL VAL ASP
SEQRES 29 D 844 MET LEU SER THR TYR LEU PRO LYS GLN PRO GLU GLY VAL
SEQRES 30 D 844 ILE LEU PHE TYR SER LYS GLY PRO LYS SER ASN ILE ASP
SEQRES 31 D 844 PHE LYS ILE LYS LYS GLU ASN THR ILE ASP GLN THR ALA
SEQRES 32 D 844 ASN VAL VAL PHE ARG TYR MET SER SER GLU PRO ILE ILE
SEQRES 33 D 844 PHE GLY GLU SER SER ILE PHE VAL GLU TYR LYS LYS PHE
SEQRES 34 D 844 SER ASN ASP LYS GLY PHE PRO LYS GLU TYR GLY SER GLY
SEQRES 35 D 844 LYS ILE VAL LEU TYR ASN GLY VAL ASN TYR LEU ASN ASN
SEQRES 36 D 844 ILE TYR CYS LEU GLU TYR ILE ASN THR HIS ASN GLU VAL
SEQRES 37 D 844 GLY ILE LYS SER VAL VAL VAL PRO ILE LYS PHE ILE ALA
SEQRES 38 D 844 GLU PHE LEU VAL ASN GLY GLU ILE LEU LYS PRO ARG ILE
SEQRES 39 D 844 ASP LYS THR MET LYS TYR ILE ASN SER GLU ASP TYR TYR
SEQRES 40 D 844 GLY ASN GLN HIS ASN ILE ILE VAL GLU HIS LEU ARG ASP
SEQRES 41 D 844 GLN SER ILE LYS ILE GLY ASP ILE PHE ASN GLU ASP LYS
SEQRES 42 D 844 LEU SER ASP VAL GLY HIS GLN TYR ALA ASN ASN ASP LYS
SEQRES 43 D 844 PHE ARG LEU ASN PRO GLU VAL SER TYR PHE THR ASN LYS
SEQRES 44 D 844 ARG THR ARG GLY PRO LEU GLY ILE LEU SER ASN TYR VAL
SEQRES 45 D 844 LYS THR LEU LEU ILE SER MET TYR CYS SER LYS THR PHE
SEQRES 46 D 844 LEU ASP ASP SER ASN LYS ARG LYS VAL LEU ALA ILE ASP
SEQRES 47 D 844 PHE GLY ASN GLY ALA ASP LEU GLU LYS TYR PHE TYR GLY
SEQRES 48 D 844 GLU ILE ALA LEU LEU VAL ALA THR ASP PRO ASP ALA ASP
SEQRES 49 D 844 ALA ILE ALA ARG GLY ASN GLU ARG TYR ASN LYS LEU ASN
SEQRES 50 D 844 SER GLY ILE LYS THR LYS TYR TYR LYS PHE ASP TYR ILE
SEQRES 51 D 844 GLN GLU THR ILE ARG SER ASP THR PHE VAL SER SER VAL
SEQRES 52 D 844 ARG GLU VAL PHE TYR PHE GLY LYS PHE ASN ILE ILE ASP
SEQRES 53 D 844 TRP GLN PHE ALA ILE HIS TYR SER PHE HIS PRO ARG HIS
SEQRES 54 D 844 TYR ALA THR VAL MET ASN ASN LEU SER GLU LEU THR ALA
SEQRES 55 D 844 SER GLY GLY LYS VAL LEU ILE THR THR MET ASP GLY ASP
SEQRES 56 D 844 LYS LEU SER LYS LEU THR ASP LYS LYS THR PHE ILE ILE
SEQRES 57 D 844 HIS LYS ASN LEU PRO SER SER GLU ASN TYR MET SER VAL
SEQRES 58 D 844 GLU LYS ILE ALA ASP ASP ARG ILE VAL VAL TYR ASN PRO
SEQRES 59 D 844 SER THR MET SER THR PRO MET THR GLU TYR ILE ILE LYS
SEQRES 60 D 844 LYS ASN ASP ILE VAL ARG VAL PHE ASN GLU TYR GLY PHE
SEQRES 61 D 844 VAL LEU VAL ASP ASN VAL ASP PHE ALA THR ILE ILE GLU
SEQRES 62 D 844 ARG SER LYS LYS PHE ILE ASN GLY ALA SER THR MET GLU
SEQRES 63 D 844 ASP ARG PRO SER THR ARG ASN PHE PHE GLU LEU ASN ARG
SEQRES 64 D 844 GLY ALA ILE LYS CYS GLU GLY LEU ASP VAL GLU ASP LEU
SEQRES 65 D 844 LEU SER TYR TYR VAL VAL TYR VAL PHE SER LYS ARG
SEQRES 1 E 287 MET ASP GLU ILE VAL LYS ASN ILE ARG GLU GLY THR HIS
SEQRES 2 E 287 VAL LEU LEU PRO PHE TYR GLU THR LEU PRO GLU LEU ASN
SEQRES 3 E 287 LEU SER LEU GLY LYS SER PRO LEU PRO SER LEU GLU TYR
SEQRES 4 E 287 GLY ALA ASN TYR PHE LEU GLN ILE SER ARG VAL ASN ASP
SEQRES 5 E 287 LEU ASN ARG MET PRO THR ASP MET LEU LYS LEU PHE THR
SEQRES 6 E 287 HIS ASP ILE MET LEU PRO GLU SER ASP LEU ASP LYS VAL
SEQRES 7 E 287 TYR GLU ILE LEU LYS ILE ASN SER VAL LYS TYR TYR GLY
SEQRES 8 E 287 ARG SER THR LYS ALA ASP ALA VAL VAL ALA ASP LEU SER
SEQRES 9 E 287 ALA ARG ASN LYS LEU PHE LYS ARG GLU ARG ASP ALA ILE
SEQRES 10 E 287 LYS SER ASN ASN HIS LEU THR GLU ASN ASN LEU TYR ILE
SEQRES 11 E 287 SER ASP TYR LYS MET LEU THR PHE ASP VAL PHE ARG PRO
SEQRES 12 E 287 LEU PHE ASP PHE VAL ASN GLU LYS TYR CYS ILE ILE LYS
SEQRES 13 E 287 LEU PRO THR LEU PHE GLY ARG GLY VAL ILE ASP THR MET
SEQRES 14 E 287 ARG ILE TYR CYS SER LEU PHE LYS ASN VAL ARG LEU LEU
SEQRES 15 E 287 LYS CYS VAL SER ASP SER TRP LEU LYS ASP SER ALA ILE
SEQRES 16 E 287 MET VAL ALA SER ASP VAL CYS LYS LYS ASN LEU ASP LEU
SEQRES 17 E 287 PHE MET SER HIS VAL LYS SER VAL THR LYS SER SER SER
SEQRES 18 E 287 TRP LYS ASP VAL ASN SER VAL GLN PHE SER ILE LEU ASN
SEQRES 19 E 287 ASN PRO VAL ASP THR GLU PHE ILE ASN LYS PHE LEU GLU
SEQRES 20 E 287 PHE SER ASN ARG VAL TYR GLU ALA LEU TYR TYR VAL HIS
SEQRES 21 E 287 SER LEU LEU TYR SER SER MET THR SER ASP SER LYS SER
SEQRES 22 E 287 ILE GLU ASN LYS HIS GLN ARG ARG LEU VAL LYS LEU LEU
SEQRES 23 E 287 LEU
HET SAH A1845 26
HET SAH D1845 26
HET GTP D1846 32
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
FORMUL 5 SAH 2(C14 H20 N6 O5 S)
FORMUL 7 GTP C10 H16 N5 O14 P3
FORMUL 8 HOH *25(H2 O)
HELIX 1 1 ASP A 2 VAL A 6 5 5
HELIX 2 2 THR A 10 LEU A 25 1 16
HELIX 3 3 LEU A 47 ASN A 55 1 9
HELIX 4 4 LEU A 82 VAL A 85 5 4
HELIX 5 5 LYS A 91 ALA A 98 1 8
HELIX 6 6 ASP A 133 SER A 140 5 8
HELIX 7 7 SER A 174 HIS A 182 1 9
HELIX 8 8 PRO A 204 MET A 221 1 18
HELIX 9 9 PRO A 243 VAL A 248 5 6
HELIX 10 10 ASP A 326 LEU A 338 1 13
HELIX 11 11 THR A 358 LEU A 370 1 13
HELIX 12 12 GLY A 384 SER A 387 5 4
HELIX 13 13 ASN A 466 GLY A 469 5 4
HELIX 14 14 ARG A 493 SER A 503 1 11
HELIX 15 15 GLN A 510 ILE A 523 1 14
HELIX 16 16 LYS A 524 ILE A 528 5 5
HELIX 17 17 GLY A 563 SER A 582 1 20
HELIX 18 18 ASP A 604 GLY A 611 1 8
HELIX 19 19 ASP A 622 ASN A 637 1 16
HELIX 20 20 THR A 658 ARG A 664 1 7
HELIX 21 21 ALA A 680 SER A 684 5 5
HELIX 22 22 HIS A 686 ARG A 688 5 3
HELIX 23 23 HIS A 689 LEU A 700 1 12
HELIX 24 24 ASP A 713 LYS A 719 1 7
HELIX 25 25 LYS A 767 TYR A 778 1 12
HELIX 26 26 PHE A 788 ARG A 794 1 7
HELIX 27 27 SER A 795 GLY A 801 1 7
HELIX 28 28 ALA A 802 GLU A 806 5 5
HELIX 29 29 ARG A 808 LYS A 823 1 16
HELIX 30 30 ASP A 828 LEU A 833 1 6
HELIX 31 31 MET B 1 GLY B 11 1 11
HELIX 32 32 SER B 36 GLY B 40 5 5
HELIX 33 33 ASN B 42 ILE B 47 1 6
HELIX 34 34 ILE B 47 ARG B 55 1 9
HELIX 35 35 PRO B 57 ASP B 67 1 11
HELIX 36 36 SER B 73 LEU B 82 1 10
HELIX 37 37 ASP B 132 LEU B 136 5 5
HELIX 38 38 THR B 137 VAL B 140 5 4
HELIX 39 39 PHE B 141 ASP B 146 1 6
HELIX 40 40 GLY B 162 LEU B 175 1 14
HELIX 41 41 CYS B 202 LYS B 218 1 17
HELIX 42 42 LYS B 223 SER B 227 5 5
HELIX 43 43 ASP B 238 SER B 269 1 32
HELIX 44 44 ASN B 276 LEU B 287 1 12
HELIX 45 45 ASP D 2 VAL D 6 5 5
HELIX 46 46 THR D 10 LEU D 25 1 16
HELIX 47 47 LEU D 47 ASN D 55 1 9
HELIX 48 48 LEU D 82 VAL D 85 5 4
HELIX 49 49 LYS D 91 ALA D 98 1 8
HELIX 50 50 ASP D 133 SER D 140 5 8
HELIX 51 51 SER D 174 HIS D 182 1 9
HELIX 52 52 PRO D 204 MET D 221 1 18
HELIX 53 53 PRO D 243 VAL D 248 5 6
HELIX 54 54 ASP D 326 LEU D 338 1 13
HELIX 55 55 THR D 358 LEU D 370 1 13
HELIX 56 56 GLY D 384 SER D 387 5 4
HELIX 57 57 ASN D 466 GLY D 469 5 4
HELIX 58 58 ARG D 493 SER D 503 1 11
HELIX 59 59 GLN D 510 ILE D 523 1 14
HELIX 60 60 LYS D 524 ILE D 528 5 5
HELIX 61 61 GLY D 563 SER D 582 1 20
HELIX 62 62 ASP D 604 GLY D 611 1 8
HELIX 63 63 ASP D 622 ASN D 637 1 16
HELIX 64 64 THR D 658 GLU D 665 1 8
HELIX 65 65 ALA D 680 SER D 684 5 5
HELIX 66 66 HIS D 686 ARG D 688 5 3
HELIX 67 67 HIS D 689 LEU D 700 1 12
HELIX 68 68 ASP D 713 LYS D 719 1 7
HELIX 69 69 LYS D 767 GLU D 777 1 11
HELIX 70 70 PHE D 788 ARG D 794 1 7
HELIX 71 71 SER D 795 GLY D 801 1 7
HELIX 72 72 ALA D 802 GLU D 806 5 5
HELIX 73 73 ARG D 808 LYS D 823 1 16
HELIX 74 74 ASP D 828 LEU D 833 1 6
HELIX 75 75 MET E 1 GLY E 11 1 11
HELIX 76 76 SER E 36 GLY E 40 5 5
HELIX 77 77 ASN E 42 ILE E 47 1 6
HELIX 78 78 ILE E 47 ARG E 55 1 9
HELIX 79 79 PRO E 57 ASP E 67 1 11
HELIX 80 80 SER E 73 LEU E 82 1 10
HELIX 81 81 ASP E 132 LEU E 136 5 5
HELIX 82 82 THR E 137 VAL E 140 5 4
HELIX 83 83 PHE E 141 ASP E 146 1 6
HELIX 84 84 GLY E 162 LEU E 175 1 14
HELIX 85 85 CYS E 202 LYS E 218 1 17
HELIX 86 86 LYS E 223 SER E 227 5 5
HELIX 87 87 ASP E 238 SER E 269 1 32
HELIX 88 88 ASN E 276 LEU E 287 1 12
SHEET 1 AA 9 ASN A 36 PHE A 42 0
SHEET 2 AA 9 CYS A 119 ILE A 130 -1 O LEU A 120 N VAL A 41
SHEET 3 AA 9 VAL A 103 HIS A 116 -1 O TRP A 104 N HIS A 129
SHEET 4 AA 9 VAL A 74 THR A 78 -1 O LYS A 75 N LYS A 107
SHEET 5 AA 9 ILE A 59 THR A 69 -1 O PHE A 66 N THR A 78
SHEET 6 AA 9 ARG A 142 LYS A 152 -1 O ARG A 142 N THR A 67
SHEET 7 AA 9 PHE A 156 SER A 168 -1 O ILE A 158 N ALA A 151
SHEET 8 AA 9 ASN A 188 PHE A 195 -1 O ASN A 188 N LYS A 163
SHEET 9 AA 9 ASN A 36 PHE A 42 -1 O LEU A 38 N PHE A 195
SHEET 1 AB 7 VAL A 227 LEU A 229 0
SHEET 2 AB 7 TYR A 284 TYR A 288 -1 O ILE A 285 N ILE A 228
SHEET 3 AB 7 GLY A 274 PHE A 279 -1 O LEU A 275 N TYR A 288
SHEET 4 AB 7 ILE A 264 THR A 271 -1 O THR A 267 N TYR A 278
SHEET 5 AB 7 VAL A 298 LYS A 306 -1 O VAL A 298 N VAL A 270
SHEET 6 AB 7 TRP A 310 ILE A 318 -1 O THR A 311 N VAL A 305
SHEET 7 AB 7 ILE A 345 SER A 349 1 O VAL A 346 N VAL A 312
SHEET 1 AC 5 LYS A 238 MET A 241 0
SHEET 2 AC 5 ILE A 389 ILE A 393 1 O ASP A 390 N PHE A 240
SHEET 3 AC 5 VAL A 377 TYR A 381 -1 O VAL A 377 N ILE A 393
SHEET 4 AC 5 LEU A 255 THR A 259 -1 O TYR A 256 N PHE A 380
SHEET 5 AC 5 TYR A 352 GLU A 353 -1 O GLU A 353 N ALA A 257
SHEET 1 AD 2 ILE A 416 PHE A 417 0
SHEET 2 AD 2 ILE A 422 ASP A 432 -1 O PHE A 423 N ILE A 416
SHEET 1 AE 2 PHE A 435 VAL A 445 0
SHEET 2 AE 2 ILE A 422 ASP A 432 -1 O VAL A 424 N ILE A 444
SHEET 1 AF 5 ILE A 489 PRO A 492 0
SHEET 2 AF 5 LYS A 478 LEU A 484 -1 O GLU A 482 N LEU A 490
SHEET 3 AF 5 THR A 398 VAL A 405 -1 O ILE A 399 N PHE A 483
SHEET 4 AF 5 ILE A 422 ASP A 432 -1 O LYS A 427 N ASN A 404
SHEET 5 AF 5 PHE A 435 VAL A 445 -1 O PHE A 435 N ASP A 432
SHEET 1 AG 5 ILE A 489 PRO A 492 0
SHEET 2 AG 5 LYS A 478 LEU A 484 -1 O GLU A 482 N LEU A 490
SHEET 3 AG 5 THR A 398 VAL A 405 -1 O ILE A 399 N PHE A 483
SHEET 4 AG 5 ILE A 422 ASP A 432 -1 O LYS A 427 N ASN A 404
SHEET 5 AG 5 ILE A 416 PHE A 417 -1 O ILE A 416 N PHE A 423
SHEET 1 AH 3 VAL A 450 LEU A 453 0
SHEET 2 AH 3 CYS A 458 HIS A 465 -1 O CYS A 458 N LEU A 453
SHEET 3 AH 3 ILE A 470 PRO A 476 -1 O ILE A 470 N HIS A 465
SHEET 1 AI 7 LYS A 646 GLN A 651 0
SHEET 2 AI 7 LEU A 615 ASP A 620 1 O LEU A 616 N ASP A 648
SHEET 3 AI 7 LYS A 593 ALA A 596 1 O VAL A 594 N VAL A 617
SHEET 4 AI 7 PHE A 672 GLN A 678 1 N ASN A 673 O LYS A 593
SHEET 5 AI 7 THR A 701 MET A 712 1 N ALA A 702 O PHE A 672
SHEET 6 AI 7 TYR A 836 LYS A 843 -1 O VAL A 837 N THR A 711
SHEET 7 AI 7 PHE A 780 ASP A 787 -1 O VAL A 781 N SER A 842
SHEET 1 AJ 4 LYS A 724 ILE A 727 0
SHEET 2 AJ 4 TYR A 738 LYS A 743 -1 O MET A 739 N PHE A 726
SHEET 3 AJ 4 ARG A 748 TYR A 752 -1 O VAL A 750 N GLU A 742
SHEET 4 AJ 4 MET A 761 TYR A 764 -1 O MET A 761 N VAL A 751
SHEET 1 BA 6 THR B 12 LEU B 16 0
SHEET 2 BA 6 PHE B 176 LYS B 183 -1 O VAL B 179 N LEU B 16
SHEET 3 BA 6 ALA B 194 VAL B 201 -1 O ILE B 195 N LEU B 182
SHEET 4 BA 6 TYR B 152 LEU B 157 -1 O CYS B 153 N ALA B 198
SHEET 5 BA 6 ALA B 98 ASP B 102 1 O VAL B 99 N ILE B 154
SHEET 6 BA 6 VAL B 87 LYS B 88 1 O LYS B 88 N VAL B 100
SHEET 1 BB 2 LEU B 25 LEU B 29 0
SHEET 2 BB 2 PHE B 230 LEU B 233 -1 O SER B 231 N SER B 28
SHEET 1 DA 9 ASN D 36 PHE D 42 0
SHEET 2 DA 9 CYS D 119 ILE D 130 -1 O LEU D 120 N VAL D 41
SHEET 3 DA 9 VAL D 103 HIS D 116 -1 O TRP D 104 N HIS D 129
SHEET 4 DA 9 VAL D 74 THR D 78 -1 O LYS D 75 N LYS D 107
SHEET 5 DA 9 ILE D 59 THR D 69 -1 O PHE D 66 N THR D 78
SHEET 6 DA 9 ARG D 142 LYS D 152 -1 O ARG D 142 N THR D 67
SHEET 7 DA 9 PHE D 156 SER D 168 -1 O ILE D 158 N ALA D 151
SHEET 8 DA 9 ASN D 188 PHE D 195 -1 O ASN D 188 N LYS D 163
SHEET 9 DA 9 ASN D 36 PHE D 42 -1 O LEU D 38 N PHE D 195
SHEET 1 DB 7 VAL D 227 LEU D 229 0
SHEET 2 DB 7 TYR D 284 TYR D 288 -1 O ILE D 285 N ILE D 228
SHEET 3 DB 7 GLY D 274 PHE D 279 -1 O LEU D 275 N TYR D 288
SHEET 4 DB 7 ILE D 264 THR D 271 -1 O THR D 267 N TYR D 278
SHEET 5 DB 7 VAL D 298 LYS D 306 -1 O VAL D 298 N VAL D 270
SHEET 6 DB 7 TRP D 310 ILE D 318 -1 O THR D 311 N VAL D 305
SHEET 7 DB 7 ILE D 345 SER D 349 1 O VAL D 346 N VAL D 312
SHEET 1 DC 5 LYS D 238 MET D 241 0
SHEET 2 DC 5 ILE D 389 ILE D 393 1 O ASP D 390 N PHE D 240
SHEET 3 DC 5 VAL D 377 TYR D 381 -1 O VAL D 377 N ILE D 393
SHEET 4 DC 5 LEU D 255 THR D 259 -1 O TYR D 256 N PHE D 380
SHEET 5 DC 5 TYR D 352 GLU D 353 -1 O GLU D 353 N ALA D 257
SHEET 1 DD 2 ILE D 416 PHE D 417 0
SHEET 2 DD 2 ILE D 422 ASP D 432 -1 O PHE D 423 N ILE D 416
SHEET 1 DE 2 PHE D 435 VAL D 445 0
SHEET 2 DE 2 ILE D 422 ASP D 432 -1 O VAL D 424 N ILE D 444
SHEET 1 DF 5 ILE D 489 PRO D 492 0
SHEET 2 DF 5 LYS D 478 LEU D 484 -1 O GLU D 482 N LEU D 490
SHEET 3 DF 5 THR D 398 VAL D 405 -1 O ILE D 399 N PHE D 483
SHEET 4 DF 5 ILE D 422 ASP D 432 -1 O LYS D 427 N ASN D 404
SHEET 5 DF 5 PHE D 435 VAL D 445 -1 O PHE D 435 N ASP D 432
SHEET 1 DG 5 ILE D 489 PRO D 492 0
SHEET 2 DG 5 LYS D 478 LEU D 484 -1 O GLU D 482 N LEU D 490
SHEET 3 DG 5 THR D 398 VAL D 405 -1 O ILE D 399 N PHE D 483
SHEET 4 DG 5 ILE D 422 ASP D 432 -1 O LYS D 427 N ASN D 404
SHEET 5 DG 5 ILE D 416 PHE D 417 -1 O ILE D 416 N PHE D 423
SHEET 1 DH 3 VAL D 450 LEU D 453 0
SHEET 2 DH 3 CYS D 458 HIS D 465 -1 O CYS D 458 N LEU D 453
SHEET 3 DH 3 ILE D 470 PRO D 476 -1 O ILE D 470 N HIS D 465
SHEET 1 DI 7 LYS D 646 GLN D 651 0
SHEET 2 DI 7 LEU D 615 ASP D 620 1 O LEU D 616 N ASP D 648
SHEET 3 DI 7 LYS D 593 ALA D 596 1 O VAL D 594 N VAL D 617
SHEET 4 DI 7 PHE D 672 GLN D 678 1 N ASN D 673 O LYS D 593
SHEET 5 DI 7 THR D 701 MET D 712 1 N ALA D 702 O PHE D 672
SHEET 6 DI 7 TYR D 836 LYS D 843 -1 O VAL D 837 N THR D 711
SHEET 7 DI 7 PHE D 780 ASP D 787 -1 O VAL D 781 N SER D 842
SHEET 1 DJ 4 LYS D 724 ILE D 727 0
SHEET 2 DJ 4 TYR D 738 LYS D 743 -1 O MET D 739 N PHE D 726
SHEET 3 DJ 4 ARG D 748 TYR D 752 -1 O VAL D 750 N GLU D 742
SHEET 4 DJ 4 MET D 761 TYR D 764 -1 O MET D 761 N VAL D 751
SHEET 1 EA 6 THR E 12 LEU E 16 0
SHEET 2 EA 6 PHE E 176 LYS E 183 -1 O VAL E 179 N LEU E 16
SHEET 3 EA 6 ALA E 194 VAL E 201 -1 O ILE E 195 N LEU E 182
SHEET 4 EA 6 TYR E 152 LEU E 157 -1 O CYS E 153 N ALA E 198
SHEET 5 EA 6 ALA E 98 ASP E 102 1 O VAL E 99 N ILE E 154
SHEET 6 EA 6 VAL E 87 LYS E 88 1 O LYS E 88 N VAL E 100
SHEET 1 EB 2 LEU E 25 LEU E 29 0
SHEET 2 EB 2 PHE E 230 LEU E 233 -1 O SER E 231 N SER E 28
CISPEP 1 GLU D 319 PRO D 320 0 -13.09
SITE 1 AC1 14 ARG A 548 LEU A 549 ASN A 550 LYS A 573
SITE 2 AC1 14 ASP A 598 PHE A 599 GLY A 600 ASP A 620
SITE 3 AC1 14 PRO A 621 ARG A 655 GLN A 678 PHE A 679
SITE 4 AC1 14 ALA A 680 TYR A 683
SITE 1 AC2 16 ARG D 548 LEU D 549 ASN D 550 LYS D 573
SITE 2 AC2 16 ASP D 598 PHE D 599 GLY D 600 ALA D 603
SITE 3 AC2 16 ASP D 604 ASP D 620 PRO D 621 ASP D 622
SITE 4 AC2 16 ARG D 655 GLN D 678 PHE D 679 TYR D 683
SITE 1 AC3 14 THR D 239 VAL D 258 LYS D 260 PRO D 265
SITE 2 AC3 14 GLU D 303 ILE D 315 LYS D 350 ILE D 378
SITE 3 AC3 14 ASP D 390 LYS D 392 ASP D 400 ARG D 493
SITE 4 AC3 14 LYS D 496 HOH D2007
CRYST1 60.340 197.730 61.110 90.13 109.27 94.05 P 1 2
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 0.016573 0.001173 0.005828 0.00000
SCALE2 0.000000 0.005070 0.000138 0.00000
SCALE3 0.000000 0.000000 0.017342 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.986259 -0.164926 0.009643 -60.19046 1
MTRIX2 2 -0.164909 0.986306 0.002518 89.11481 1
MTRIX3 2 -0.009926 0.000893 -0.999950 18.42090 1
MTRIX1 3 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 3 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 3 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 4 -0.986536 -0.163521 0.002881 -60.11407 1
MTRIX2 4 -0.163523 0.986539 -0.000399 89.28198 1
MTRIX3 4 -0.002777 -0.000864 -0.999996 18.62575 1
MTRIX1 5 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 5 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 5 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 6 -0.992491 -0.122202 -0.005247 -57.46082 1
MTRIX2 6 -0.122230 0.992488 0.005220 91.51631 1
MTRIX3 6 0.004569 0.005822 -0.999973 19.42024 1
MTRIX1 7 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 7 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 7 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 8 -0.991299 -0.131421 0.007444 -58.36908 1
MTRIX2 8 -0.131426 0.991326 -0.000160 90.97787 1
MTRIX3 8 -0.007358 -0.001137 -0.999972 18.37049 1
(ATOM LINES ARE NOT SHOWN.)
END
