HEADER TRANSFERASE/DNA 12-JUN-12 4FK0
TITLE RB69 DNA POLYMERASE TERNARY COMPLEX WITH DCTP/DG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GP43;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA TEMPLATE;
COMPND 10 CHAIN: T;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA PRIMER;
COMPND 14 CHAIN: P;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE RB69;
SOURCE 3 ORGANISM_TAXID: 12353;
SOURCE 4 GENE: 43;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 MOL_ID: 3;
SOURCE 10 SYNTHETIC: YES
KEYWDS DCTP/DG, RB69, RB69 POL, QUADRUPLE, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XIA,J.WANG,W.H.KONIGSBERG
REVDAT 3 28-FEB-24 4FK0 1 REMARK SEQADV LINK
REVDAT 2 30-JAN-13 4FK0 1 JRNL
REVDAT 1 19-DEC-12 4FK0 0
JRNL AUTH S.XIA,J.WANG,W.H.KONIGSBERG
JRNL TITL DNA MISMATCH SYNTHESIS COMPLEXES PROVIDE INSIGHTS INTO BASE
JRNL TITL 2 SELECTIVITY OF A B FAMILY DNA POLYMERASE.
JRNL REF J.AM.CHEM.SOC. V. 135 193 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 23214497
JRNL DOI 10.1021/JA3079048
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 58032
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3105
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) : 2.18
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3793
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 198
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7329
REMARK 3 NUCLEIC ACID ATOMS : 614
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 364
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.65000
REMARK 3 B33 (A**2) : -0.66000
REMARK 3 B12 (A**2) : 0.00000
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): 0.256
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.213
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.271
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
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): 8224 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11247 ; 1.255 ; 1.905
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 899 ; 5.650 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 371 ;35.404 ;24.178
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1339 ;15.117 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;14.655 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1162 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6071 ; 0.006 ; 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): 4490 ; 1.719 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7275 ; 2.837 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3733 ; 3.359 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3968 ; 4.799 ; 9.000
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 : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 2 T 18
REMARK 3 RESIDUE RANGE : P 103 P 114
REMARK 3 RESIDUE RANGE : A 1001 A 1001
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3670 -2.7460 -35.7090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1290 T22: 0.1893
REMARK 3 T33: 0.2926 T12: 0.0415
REMARK 3 T13: -0.0357 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.2207 L22: 0.1048
REMARK 3 L33: 0.0278 L12: 0.1287
REMARK 3 L13: 0.0221 L23: 0.0255
REMARK 3 S TENSOR
REMARK 3 S11: -0.1290 S12: -0.0267 S13: 0.1966
REMARK 3 S21: -0.0621 S22: 0.0581 S23: 0.1232
REMARK 3 S31: 0.0240 S32: 0.0251 S33: 0.0709
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 105
REMARK 3 RESIDUE RANGE : A 340 A 389
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8240 2.1840 -33.6490
REMARK 3 T TENSOR
REMARK 3 T11: 0.0402 T22: 0.0407
REMARK 3 T33: 0.1148 T12: -0.0133
REMARK 3 T13: -0.0173 T23: 0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 0.1055 L22: 1.2146
REMARK 3 L33: 0.2476 L12: 0.1077
REMARK 3 L13: -0.1315 L23: -0.4184
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: -0.0008 S13: 0.0136
REMARK 3 S21: 0.0454 S22: -0.0355 S23: -0.1036
REMARK 3 S31: -0.0234 S32: 0.0283 S33: 0.0336
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 106 A 339
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3560 -22.0170 -14.9650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0283 T22: 0.0388
REMARK 3 T33: 0.0638 T12: -0.0093
REMARK 3 T13: -0.0109 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.2533 L22: 0.6372
REMARK 3 L33: 0.9535 L12: 0.2285
REMARK 3 L13: 0.1302 L23: 0.1465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: -0.0232 S13: 0.0435
REMARK 3 S21: 0.0771 S22: -0.0511 S23: -0.0363
REMARK 3 S31: 0.0442 S32: -0.0832 S33: 0.0336
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 390 A 468
REMARK 3 RESIDUE RANGE : A 576 A 706
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5890 -6.6780 -60.2830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0568 T22: 0.1083
REMARK 3 T33: 0.0274 T12: -0.0350
REMARK 3 T13: -0.0131 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 0.6647 L22: 0.6481
REMARK 3 L33: 0.1866 L12: 0.4053
REMARK 3 L13: -0.2202 L23: 0.0383
REMARK 3 S TENSOR
REMARK 3 S11: -0.0490 S12: 0.2245 S13: 0.0349
REMARK 3 S21: -0.0815 S22: 0.0973 S23: -0.0034
REMARK 3 S31: -0.0015 S32: -0.1030 S33: -0.0483
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 469 A 575
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4330 -26.3640 -47.2050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0449 T22: 0.0581
REMARK 3 T33: 0.0872 T12: 0.0006
REMARK 3 T13: 0.0179 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.4072 L22: 2.2997
REMARK 3 L33: 0.2841 L12: 0.0572
REMARK 3 L13: -0.0286 L23: 0.4831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0245 S12: 0.0854 S13: -0.1037
REMARK 3 S21: 0.1330 S22: -0.0563 S23: -0.0389
REMARK 3 S31: 0.0497 S32: 0.0443 S33: 0.0809
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 707 A 737
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4660 -22.7760 -47.9540
REMARK 3 T TENSOR
REMARK 3 T11: 0.0396 T22: 0.1081
REMARK 3 T33: 0.0974 T12: -0.0379
REMARK 3 T13: -0.0003 T23: -0.0413
REMARK 3 L TENSOR
REMARK 3 L11: 0.7520 L22: 0.7092
REMARK 3 L33: 1.1519 L12: -0.5068
REMARK 3 L13: -0.8785 L23: 0.3916
REMARK 3 S TENSOR
REMARK 3 S11: -0.0445 S12: -0.0368 S13: -0.0178
REMARK 3 S21: 0.0311 S22: 0.0760 S23: 0.0555
REMARK 3 S31: 0.0488 S32: 0.0526 S33: -0.0315
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 : A 738 A 900
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1990 -20.7170 -27.6800
REMARK 3 T TENSOR
REMARK 3 T11: 0.0079 T22: 0.1243
REMARK 3 T33: 0.0740 T12: 0.0231
REMARK 3 T13: 0.0145 T23: 0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 1.5794 L22: 0.3985
REMARK 3 L33: 1.5662 L12: 0.0403
REMARK 3 L13: 0.3174 L23: 0.5792
REMARK 3 S TENSOR
REMARK 3 S11: -0.1034 S12: -0.2877 S13: -0.1311
REMARK 3 S21: 0.0080 S22: 0.0852 S23: 0.0651
REMARK 3 S31: -0.0104 S32: -0.1198 S33: 0.0183
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4FK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072994.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : APEX II CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58032
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM CACL2, 10% (W/V) PEG 350
REMARK 280 MONOMETHYL ETHER (MME), AND 100 MM SODIUM CACODYLATE PH 6.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 37.42300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.30950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.07450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.30950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.42300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.07450
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: 6670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T, P
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 PHE A 901
REMARK 465 ASP A 902
REMARK 465 PHE A 903
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 871 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 DG P 110 C3' - O3' - P ANGL. DEV. = 7.3 DEGREES
REMARK 500 DT P 113 C3' - O3' - P ANGL. DEV. = -8.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 44 46.21 -77.05
REMARK 500 ASP A 121 40.64 -100.78
REMARK 500 PHE A 221 -70.02 -126.49
REMARK 500 ASN A 316 69.06 -154.07
REMARK 500 ASN A 402 164.70 178.59
REMARK 500 PRO A 458 1.03 -63.97
REMARK 500 ASP A 579 113.36 -161.55
REMARK 500 THR A 622 -70.27 70.57
REMARK 500 ASP A 623 16.84 -143.25
REMARK 500 GLU A 686 -70.36 -95.99
REMARK 500 LYS A 800 19.49 59.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 116 OE2
REMARK 620 2 GLU A 116 OE1 46.6
REMARK 620 3 HOH A1114 O 64.2 79.6
REMARK 620 4 HOH A1347 O 71.3 117.8 69.9
REMARK 620 5 HOH A1368 O 141.3 158.3 88.5 73.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 411 OD1
REMARK 620 2 ASP A 411 OD2 49.4
REMARK 620 3 LEU A 412 O 83.3 109.2
REMARK 620 4 ASP A 623 OD1 116.4 75.3 89.0
REMARK 620 5 DCP A1001 O1G 79.9 117.6 95.6 163.5
REMARK 620 6 DCP A1001 O2B 154.6 154.0 89.7 87.7 76.5
REMARK 620 7 DCP A1001 O2A 111.4 82.6 165.3 85.5 86.1 76.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 411 OD2
REMARK 620 2 ASP A 623 OD2 76.3
REMARK 620 3 DCP A1001 O2A 86.4 81.6
REMARK 620 4 HOH P 211 O 97.2 138.8 139.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 505 O
REMARK 620 2 ASN A 507 OD1 94.3
REMARK 620 3 LYS A 531 O 166.6 84.0
REMARK 620 4 HOH A1193 O 76.3 141.6 96.8
REMARK 620 5 HOH A1273 O 89.0 74.5 77.8 68.2
REMARK 620 6 HOH A1281 O 103.6 140.5 85.7 77.5 139.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1102 O
REMARK 620 2 HOH A1144 O 107.1
REMARK 620 3 HOH A1150 O 136.6 91.1
REMARK 620 4 HOH A1267 O 80.1 76.1 66.2
REMARK 620 5 HOH A1353 O 157.3 63.5 65.9 114.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FJ5 RELATED DB: PDB
REMARK 900 RELATED ID: 4FJ7 RELATED DB: PDB
REMARK 900 RELATED ID: 4FJ8 RELATED DB: PDB
REMARK 900 RELATED ID: 4FJ9 RELATED DB: PDB
REMARK 900 RELATED ID: 4FJG RELATED DB: PDB
REMARK 900 RELATED ID: 4FJH RELATED DB: PDB
REMARK 900 RELATED ID: 4FJI RELATED DB: PDB
REMARK 900 RELATED ID: 4FJJ RELATED DB: PDB
REMARK 900 RELATED ID: 4FJK RELATED DB: PDB
REMARK 900 RELATED ID: 4FJL RELATED DB: PDB
REMARK 900 RELATED ID: 4FJM RELATED DB: PDB
REMARK 900 RELATED ID: 4FJN RELATED DB: PDB
REMARK 900 RELATED ID: 4FJX RELATED DB: PDB
REMARK 900 RELATED ID: 4FK2 RELATED DB: PDB
REMARK 900 RELATED ID: 4FK4 RELATED DB: PDB
DBREF 4FK0 A 1 903 UNP Q38087 DPOL_BPR69 1 903
DBREF 4FK0 T 2 18 PDB 4FK0 4FK0 2 18
DBREF 4FK0 P 103 115 PDB 4FK0 4FK0 103 115
SEQADV 4FK0 ALA A 222 UNP Q38087 ASP 222 ENGINEERED MUTATION
SEQADV 4FK0 ALA A 327 UNP Q38087 ASP 327 ENGINEERED MUTATION
SEQADV 4FK0 ALA A 415 UNP Q38087 LEU 415 ENGINEERED MUTATION
SEQADV 4FK0 ALA A 561 UNP Q38087 LEU 561 ENGINEERED MUTATION
SEQADV 4FK0 GLY A 565 UNP Q38087 SER 565 ENGINEERED MUTATION
SEQADV 4FK0 ALA A 567 UNP Q38087 TYR 567 ENGINEERED MUTATION
SEQRES 1 A 903 MET LYS GLU PHE TYR LEU THR VAL GLU GLN ILE GLY ASP
SEQRES 2 A 903 SER ILE PHE GLU ARG TYR ILE ASP SER ASN GLY ARG GLU
SEQRES 3 A 903 ARG THR ARG GLU VAL GLU TYR LYS PRO SER LEU PHE ALA
SEQRES 4 A 903 HIS CYS PRO GLU SER GLN ALA THR LYS TYR PHE ASP ILE
SEQRES 5 A 903 TYR GLY LYS PRO CYS THR ARG LYS LEU PHE ALA ASN MET
SEQRES 6 A 903 ARG ASP ALA SER GLN TRP ILE LYS ARG MET GLU ASP ILE
SEQRES 7 A 903 GLY LEU GLU ALA LEU GLY MET ASP ASP PHE LYS LEU ALA
SEQRES 8 A 903 TYR LEU SER ASP THR TYR ASN TYR GLU ILE LYS TYR ASP
SEQRES 9 A 903 HIS THR LYS ILE ARG VAL ALA ASN PHE ASP ILE GLU VAL
SEQRES 10 A 903 THR SER PRO ASP GLY PHE PRO GLU PRO SER GLN ALA LYS
SEQRES 11 A 903 HIS PRO ILE ASP ALA ILE THR HIS TYR ASP SER ILE ASP
SEQRES 12 A 903 ASP ARG PHE TYR VAL PHE ASP LEU LEU ASN SER PRO TYR
SEQRES 13 A 903 GLY ASN VAL GLU GLU TRP SER ILE GLU ILE ALA ALA LYS
SEQRES 14 A 903 LEU GLN GLU GLN GLY GLY ASP GLU VAL PRO SER GLU ILE
SEQRES 15 A 903 ILE ASP LYS ILE ILE TYR MET PRO PHE ASP ASN GLU LYS
SEQRES 16 A 903 GLU LEU LEU MET GLU TYR LEU ASN PHE TRP GLN GLN LYS
SEQRES 17 A 903 THR PRO VAL ILE LEU THR GLY TRP ASN VAL GLU SER PHE
SEQRES 18 A 903 ALA ILE PRO TYR VAL TYR ASN ARG ILE LYS ASN ILE PHE
SEQRES 19 A 903 GLY GLU SER THR ALA LYS ARG LEU SER PRO HIS ARG LYS
SEQRES 20 A 903 THR ARG VAL LYS VAL ILE GLU ASN MET TYR GLY SER ARG
SEQRES 21 A 903 GLU ILE ILE THR LEU PHE GLY ILE SER VAL LEU ASP TYR
SEQRES 22 A 903 ILE ASP LEU TYR LYS LYS PHE SER PHE THR ASN GLN PRO
SEQRES 23 A 903 SER TYR SER LEU ASP TYR ILE SER GLU PHE GLU LEU ASN
SEQRES 24 A 903 VAL GLY LYS LEU LYS TYR ASP GLY PRO ILE SER LYS LEU
SEQRES 25 A 903 ARG GLU SER ASN HIS GLN ARG TYR ILE SER TYR ASN ILE
SEQRES 26 A 903 ILE ALA VAL TYR ARG VAL LEU GLN ILE ASP ALA LYS ARG
SEQRES 27 A 903 GLN PHE ILE ASN LEU SER LEU ASP MET GLY TYR TYR ALA
SEQRES 28 A 903 LYS ILE GLN ILE GLN SER VAL PHE SER PRO ILE LYS THR
SEQRES 29 A 903 TRP ASP ALA ILE ILE PHE ASN SER LEU LYS GLU GLN ASN
SEQRES 30 A 903 LYS VAL ILE PRO GLN GLY ARG SER HIS PRO VAL GLN PRO
SEQRES 31 A 903 TYR PRO GLY ALA PHE VAL LYS GLU PRO ILE PRO ASN ARG
SEQRES 32 A 903 TYR LYS TYR VAL MET SER PHE ASP LEU THR SER ALA TYR
SEQRES 33 A 903 PRO SER ILE ILE ARG GLN VAL ASN ILE SER PRO GLU THR
SEQRES 34 A 903 ILE ALA GLY THR PHE LYS VAL ALA PRO LEU HIS ASP TYR
SEQRES 35 A 903 ILE ASN ALA VAL ALA GLU ARG PRO SER ASP VAL TYR SER
SEQRES 36 A 903 CYS SER PRO ASN GLY MET MET TYR TYR LYS ASP ARG ASP
SEQRES 37 A 903 GLY VAL VAL PRO THR GLU ILE THR LYS VAL PHE ASN GLN
SEQRES 38 A 903 ARG LYS GLU HIS LYS GLY TYR MET LEU ALA ALA GLN ARG
SEQRES 39 A 903 ASN GLY GLU ILE ILE LYS GLU ALA LEU HIS ASN PRO ASN
SEQRES 40 A 903 LEU SER VAL ASP GLU PRO LEU ASP VAL ASP TYR ARG PHE
SEQRES 41 A 903 ASP PHE SER ASP GLU ILE LYS GLU LYS ILE LYS LYS LEU
SEQRES 42 A 903 SER ALA LYS SER LEU ASN GLU MET LEU PHE ARG ALA GLN
SEQRES 43 A 903 ARG THR GLU VAL ALA GLY MET THR ALA GLN ILE ASN ARG
SEQRES 44 A 903 LYS ALA LEU ILE ASN GLY LEU ALA GLY ALA LEU GLY ASN
SEQRES 45 A 903 VAL TRP PHE ARG TYR TYR ASP LEU ARG ASN ALA THR ALA
SEQRES 46 A 903 ILE THR THR PHE GLY GLN MET ALA LEU GLN TRP ILE GLU
SEQRES 47 A 903 ARG LYS VAL ASN GLU TYR LEU ASN GLU VAL CYS GLY THR
SEQRES 48 A 903 GLU GLY GLU ALA PHE VAL LEU TYR GLY ASP THR ASP SER
SEQRES 49 A 903 ILE TYR VAL SER ALA ASP LYS ILE ILE ASP LYS VAL GLY
SEQRES 50 A 903 GLU SER LYS PHE ARG ASP THR ASN HIS TRP VAL ASP PHE
SEQRES 51 A 903 LEU ASP LYS PHE ALA ARG GLU ARG MET GLU PRO ALA ILE
SEQRES 52 A 903 ASP ARG GLY PHE ARG GLU MET CYS GLU TYR MET ASN ASN
SEQRES 53 A 903 LYS GLN HIS LEU MET PHE MET ASP ARG GLU ALA ILE ALA
SEQRES 54 A 903 GLY PRO PRO LEU GLY SER LYS GLY ILE GLY GLY PHE TRP
SEQRES 55 A 903 THR GLY LYS LYS ARG TYR ALA LEU ASN VAL TRP ASP MET
SEQRES 56 A 903 GLU GLY THR ARG TYR ALA GLU PRO LYS LEU LYS ILE MET
SEQRES 57 A 903 GLY LEU GLU THR GLN LYS SER SER THR PRO LYS ALA VAL
SEQRES 58 A 903 GLN LYS ALA LEU LYS GLU CYS ILE ARG ARG MET LEU GLN
SEQRES 59 A 903 GLU GLY GLU GLU SER LEU GLN GLU TYR PHE LYS GLU PHE
SEQRES 60 A 903 GLU LYS GLU PHE ARG GLN LEU ASN TYR ILE SER ILE ALA
SEQRES 61 A 903 SER VAL SER SER ALA ASN ASN ILE ALA LYS TYR ASP VAL
SEQRES 62 A 903 GLY GLY PHE PRO GLY PRO LYS CYS PRO PHE HIS ILE ARG
SEQRES 63 A 903 GLY ILE LEU THR TYR ASN ARG ALA ILE LYS GLY ASN ILE
SEQRES 64 A 903 ASP ALA PRO GLN VAL VAL GLU GLY GLU LYS VAL TYR VAL
SEQRES 65 A 903 LEU PRO LEU ARG GLU GLY ASN PRO PHE GLY ASP LYS CYS
SEQRES 66 A 903 ILE ALA TRP PRO SER GLY THR GLU ILE THR ASP LEU ILE
SEQRES 67 A 903 LYS ASP ASP VAL LEU HIS TRP MET ASP TYR THR VAL LEU
SEQRES 68 A 903 LEU GLU LYS THR PHE ILE LYS PRO LEU GLU GLY PHE THR
SEQRES 69 A 903 SER ALA ALA LYS LEU ASP TYR GLU LYS LYS ALA SER LEU
SEQRES 70 A 903 PHE ASP MET PHE ASP PHE
SEQRES 1 T 17 DC DG DG DG DT DA DA DG DC DA DG DT DC
SEQRES 2 T 17 DC DG DC DG
SEQRES 1 P 13 DG DC DG DG DA DC DT DG DC DT DT DA DOC
MODRES 4FK0 DOC P 115 DC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HET DOC P 115 18
HET DCP A1001 28
HET CA A1002 1
HET CA A1003 1
HET CA A1004 1
HET CA A1005 1
HET CA A1006 1
HET CA T 101 1
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HETNAM DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE
HETNAM CA CALCIUM ION
FORMUL 3 DOC C9 H14 N3 O6 P
FORMUL 4 DCP C9 H16 N3 O13 P3
FORMUL 5 CA 6(CA 2+)
FORMUL 11 HOH *364(H2 O)
HELIX 1 1 ASN A 64 GLY A 79 1 16
HELIX 2 2 ASP A 87 TYR A 97 1 11
HELIX 3 3 ASP A 104 ILE A 108 5 5
HELIX 4 4 SER A 163 LYS A 169 1 7
HELIX 5 5 LEU A 170 GLY A 174 5 5
HELIX 6 6 PRO A 179 ASP A 184 1 6
HELIX 7 7 ASN A 193 LYS A 208 1 16
HELIX 8 8 PHE A 221 GLY A 235 1 15
HELIX 9 9 GLY A 235 LYS A 240 1 6
HELIX 10 10 ARG A 241 SER A 243 5 3
HELIX 11 11 ASP A 272 SER A 281 1 10
HELIX 12 12 SER A 289 ASN A 299 1 11
HELIX 13 13 PRO A 308 GLN A 339 1 32
HELIX 14 14 GLN A 339 LYS A 352 1 14
HELIX 15 15 GLN A 354 PHE A 359 5 6
HELIX 16 16 SER A 360 GLU A 375 1 16
HELIX 17 17 SER A 414 ASN A 424 1 11
HELIX 18 18 PRO A 438 ASN A 444 1 7
HELIX 19 19 GLY A 469 LEU A 503 1 35
HELIX 20 20 SER A 523 LYS A 531 1 9
HELIX 21 21 SER A 534 LEU A 570 1 37
HELIX 22 22 ASP A 579 CYS A 609 1 31
HELIX 23 23 ALA A 629 GLY A 637 1 9
HELIX 24 24 GLU A 638 PHE A 641 5 4
HELIX 25 25 ASP A 643 ARG A 658 1 16
HELIX 26 26 ARG A 658 ASN A 675 1 18
HELIX 27 27 LEU A 730 LYS A 734 5 5
HELIX 28 28 PRO A 738 GLU A 755 1 18
HELIX 29 29 GLY A 756 PHE A 771 1 16
HELIX 30 30 ARG A 772 LEU A 774 5 3
HELIX 31 31 ASN A 775 ALA A 780 1 6
HELIX 32 32 PRO A 802 LYS A 816 1 15
HELIX 33 33 THR A 855 MET A 866 1 12
HELIX 34 34 ASP A 867 PHE A 876 1 10
HELIX 35 35 PHE A 876 ALA A 887 1 12
HELIX 36 36 SER A 896 MET A 900 5 5
SHEET 1 A 3 PHE A 4 ILE A 11 0
SHEET 2 A 3 SER A 14 ILE A 20 -1 O ARG A 18 N LEU A 6
SHEET 3 A 3 GLU A 26 VAL A 31 -1 O VAL A 31 N ILE A 15
SHEET 1 B 4 SER A 36 HIS A 40 0
SHEET 2 B 4 PRO A 56 LEU A 61 -1 O LYS A 60 N LEU A 37
SHEET 3 B 4 TYR A 49 ASP A 51 -1 N TYR A 49 O CYS A 57
SHEET 4 B 4 LYS A 378 VAL A 379 1 O VAL A 379 N PHE A 50
SHEET 1 C 6 ILE A 186 PHE A 191 0
SHEET 2 C 6 ARG A 145 LEU A 151 1 N ASP A 150 O PHE A 191
SHEET 3 C 6 ILE A 133 ASP A 140 -1 N ILE A 136 O PHE A 149
SHEET 4 C 6 VAL A 110 VAL A 117 -1 N ASN A 112 O TYR A 139
SHEET 5 C 6 ILE A 212 THR A 214 1 O ILE A 212 N ALA A 111
SHEET 6 C 6 SER A 269 VAL A 270 1 O SER A 269 N LEU A 213
SHEET 1 D 2 ASN A 153 SER A 154 0
SHEET 2 D 2 GLY A 157 ASN A 158 -1 O GLY A 157 N SER A 154
SHEET 1 E 2 THR A 248 GLU A 254 0
SHEET 2 E 2 SER A 259 LEU A 265 -1 O ILE A 262 N LYS A 251
SHEET 1 F 7 ASN A 402 ARG A 403 0
SHEET 2 F 7 GLY A 700 GLY A 704 -1 O TRP A 702 N ASN A 402
SHEET 3 F 7 ARG A 707 MET A 715 -1 O ALA A 709 N PHE A 701
SHEET 4 F 7 MET A 683 ALA A 689 -1 N ILE A 688 O TRP A 713
SHEET 5 F 7 VAL A 407 LEU A 412 -1 N SER A 409 O GLU A 686
SHEET 6 F 7 SER A 624 SER A 628 -1 O VAL A 627 N MET A 408
SHEET 7 F 7 VAL A 617 TYR A 619 -1 N LEU A 618 O TYR A 626
SHEET 1 G 4 ASN A 402 ARG A 403 0
SHEET 2 G 4 GLY A 700 GLY A 704 -1 O TRP A 702 N ASN A 402
SHEET 3 G 4 ARG A 707 MET A 715 -1 O ALA A 709 N PHE A 701
SHEET 4 G 4 THR A 718 MET A 728 -1 O MET A 728 N TYR A 708
SHEET 1 H 3 ILE A 430 THR A 433 0
SHEET 2 H 3 MET A 461 TYR A 463 -1 O MET A 462 N ALA A 431
SHEET 3 H 3 SER A 455 SER A 457 -1 N SER A 455 O TYR A 463
SHEET 1 I 3 SER A 781 SER A 784 0
SHEET 2 I 3 LYS A 829 PRO A 834 -1 O VAL A 830 N SER A 783
SHEET 3 I 3 CYS A 845 PRO A 849 -1 O TRP A 848 N TYR A 831
SHEET 1 J 2 ASP A 792 VAL A 793 0
SHEET 2 J 2 PHE A 796 PRO A 797 -1 O PHE A 796 N VAL A 793
LINK O3' DA P 114 P DOC P 115 1555 1555 1.59
LINK OE2 GLU A 116 CA CA A1006 1555 1555 2.70
LINK OE1 GLU A 116 CA CA A1006 1555 1555 2.80
LINK OD1 ASP A 411 CA CA A1002 1555 1555 2.32
LINK OD2 ASP A 411 CA CA A1002 1555 1555 2.80
LINK OD2 ASP A 411 CA CA A1003 1555 1555 2.18
LINK O LEU A 412 CA CA A1002 1555 1555 2.24
LINK O ASN A 505 CA CA A1004 1555 1555 2.35
LINK OD1 ASN A 507 CA CA A1004 1555 1555 2.27
LINK O LYS A 531 CA CA A1004 1555 1555 2.17
LINK OD1 ASP A 623 CA CA A1002 1555 1555 2.31
LINK OD2 ASP A 623 CA CA A1003 1555 1555 2.81
LINK O1G DCP A1001 CA CA A1002 1555 1555 2.19
LINK O2B DCP A1001 CA CA A1002 1555 1555 2.26
LINK O2A DCP A1001 CA CA A1002 1555 1555 2.35
LINK O2A DCP A1001 CA CA A1003 1555 1555 2.77
LINK CA CA A1003 O HOH P 211 1555 1555 2.50
LINK CA CA A1004 O HOH A1193 1555 1555 2.48
LINK CA CA A1004 O HOH A1273 1555 1555 2.65
LINK CA CA A1004 O HOH A1281 1555 1555 1.97
LINK CA CA A1005 O HOH A1102 1555 1555 2.84
LINK CA CA A1005 O HOH A1144 1555 1555 2.99
LINK CA CA A1005 O HOH A1150 1555 1555 2.97
LINK CA CA A1005 O HOH A1267 1555 1555 2.62
LINK CA CA A1005 O HOH A1353 1555 1555 2.32
LINK CA CA A1006 O HOH A1114 1555 1555 2.63
LINK CA CA A1006 O HOH A1347 1555 1555 2.31
LINK CA CA A1006 O HOH A1368 1555 1555 2.39
SITE 1 AC1 19 ASP A 411 LEU A 412 THR A 413 SER A 414
SITE 2 AC1 19 ALA A 415 TYR A 416 ARG A 482 LYS A 560
SITE 3 AC1 19 ASN A 564 THR A 622 ASP A 623 CA A1002
SITE 4 AC1 19 CA A1003 HOH A1102 HOH A1115 HOH A1165
SITE 5 AC1 19 DOC P 115 DG T 4 DG T 5
SITE 1 AC2 4 ASP A 411 LEU A 412 ASP A 623 DCP A1001
SITE 1 AC3 4 ASP A 411 ASP A 623 DCP A1001 HOH P 211
SITE 1 AC4 6 ASN A 505 ASN A 507 LYS A 531 HOH A1193
SITE 2 AC4 6 HOH A1273 HOH A1281
SITE 1 AC5 6 GLU A 716 HOH A1102 HOH A1144 HOH A1150
SITE 2 AC5 6 HOH A1267 HOH A1353
SITE 1 AC6 4 GLU A 116 HOH A1114 HOH A1347 HOH A1368
CRYST1 74.846 120.149 130.619 90.00 90.00 90.00 P 21 21 21 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 0.013361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008323 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007656 0.00000
(ATOM LINES ARE NOT SHOWN.)
END