HEADER TRANSFERASE/DNA 08-JUN-10 3NE6
TITLE RB69 DNA POLYMERASE (S565G/Y567A) TERNARY COMPLEX WITH DCTP OPPOSITE
TITLE 2 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 (5'-
COMPND 10 D(*TP*CP*AP*GP*GP*TP*AP*AP*GP*CP*AP*GP*TP*CP*CP*GP*CP*G)-3');
COMPND 11 CHAIN: T;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: TEMPLATE DNA STRAND;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA (5'-D(*GP*CP*GP*GP*AP*CP*TP*GP*CP*TP*TP*AP*(DOC))-3');
COMPND 16 CHAIN: P;
COMPND 17 ENGINEERED: YES;
COMPND 18 OTHER_DETAILS: PRIMER DNA STRAND
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE RB69;
SOURCE 3 ORGANISM_COMMON: BACTERIOPHAGE RB69;
SOURCE 4 ORGANISM_TAXID: 12353;
SOURCE 5 GENE: 43, GP43;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES
KEYWDS RB69 DNA POLYMERASE, FIDELITY, MUTATION FREQUENCIES, KINETICS,
KEYWDS 2 TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WANG,J.WANG,W.H.KONIGSBERG
REVDAT 3 06-SEP-23 3NE6 1 REMARK SEQADV LINK
REVDAT 2 02-MAR-11 3NE6 1 JRNL
REVDAT 1 26-JAN-11 3NE6 0
JRNL AUTH S.XIA,M.WANG,H.R.LEE,A.SINHA,G.BLAHA,T.CHRISTIAN,J.WANG,
JRNL AUTH 2 W.KONIGSBERG
JRNL TITL VARIATION IN MUTATION RATES CAUSED BY RB69POL FIDELITY
JRNL TITL 2 MUTANTS CAN BE RATIONALIZED ON THE BASIS OF THEIR KINETIC
JRNL TITL 3 BEHAVIOR AND CRYSTAL STRUCTURES.
JRNL REF J.MOL.BIOL. V. 406 558 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21216248
JRNL DOI 10.1016/J.JMB.2010.12.033
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 75880
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4009
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5393
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 253
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7365
REMARK 3 NUCLEIC ACID ATOMS : 630
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 757
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.42000
REMARK 3 B22 (A**2) : 2.45000
REMARK 3 B33 (A**2) : -0.03000
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): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.158
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.253
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8528 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11722 ; 1.055 ; 2.059
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 981 ; 5.011 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 395 ;35.212 ;24.253
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1411 ;14.207 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;14.859 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1246 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6368 ; 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): 4631 ; 1.226 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7555 ; 2.097 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3897 ; 2.407 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4129 ; 3.591 ; 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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 1 T 18
REMARK 3 RESIDUE RANGE : P 103 P 115
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8990 56.9600 29.5500
REMARK 3 T TENSOR
REMARK 3 T11: 0.1217 T22: 0.0731
REMARK 3 T33: 0.1258 T12: 0.0114
REMARK 3 T13: -0.0358 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.0881 L22: 0.1567
REMARK 3 L33: 0.1324 L12: -0.0509
REMARK 3 L13: -0.1297 L23: 0.1139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0578 S12: 0.0440 S13: -0.0233
REMARK 3 S21: -0.0477 S22: -0.0177 S23: -0.1009
REMARK 3 S31: 0.0061 S32: -0.0457 S33: -0.0401
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): 24.9280 62.1180 31.3590
REMARK 3 T TENSOR
REMARK 3 T11: 0.1469 T22: 0.0676
REMARK 3 T33: 0.2140 T12: -0.0364
REMARK 3 T13: 0.0825 T23: -0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 0.0602 L22: 0.8259
REMARK 3 L33: 0.0894 L12: 0.2035
REMARK 3 L13: 0.0522 L23: 0.2074
REMARK 3 S TENSOR
REMARK 3 S11: -0.0750 S12: 0.0579 S13: -0.1067
REMARK 3 S21: -0.2485 S22: 0.1649 S23: -0.2813
REMARK 3 S31: -0.0064 S32: 0.0648 S33: -0.0899
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): 10.4390 38.1000 49.7040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0516 T22: 0.0554
REMARK 3 T33: 0.0865 T12: -0.0141
REMARK 3 T13: 0.0249 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 0.0545 L22: 0.6653
REMARK 3 L33: 0.3754 L12: 0.0708
REMARK 3 L13: 0.0817 L23: 0.3692
REMARK 3 S TENSOR
REMARK 3 S11: -0.0294 S12: -0.0041 S13: -0.0188
REMARK 3 S21: -0.1290 S22: 0.0845 S23: -0.1242
REMARK 3 S31: -0.0511 S32: 0.0986 S33: -0.0552
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): -3.6540 53.1250 4.8020
REMARK 3 T TENSOR
REMARK 3 T11: 0.1127 T22: 0.1042
REMARK 3 T33: 0.1242 T12: -0.0032
REMARK 3 T13: -0.0470 T23: 0.0575
REMARK 3 L TENSOR
REMARK 3 L11: 0.2524 L22: 0.6048
REMARK 3 L33: 0.1758 L12: -0.0261
REMARK 3 L13: -0.0291 L23: -0.2284
REMARK 3 S TENSOR
REMARK 3 S11: 0.0385 S12: 0.1398 S13: 0.1164
REMARK 3 S21: -0.1177 S22: 0.0067 S23: 0.0876
REMARK 3 S31: 0.0796 S32: 0.0062 S33: -0.0453
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): 9.2850 33.0660 17.8670
REMARK 3 T TENSOR
REMARK 3 T11: 0.1065 T22: 0.1077
REMARK 3 T33: 0.2014 T12: -0.0359
REMARK 3 T13: -0.0617 T23: 0.0976
REMARK 3 L TENSOR
REMARK 3 L11: 0.5617 L22: 1.3087
REMARK 3 L33: 0.4526 L12: 0.3930
REMARK 3 L13: -0.1952 L23: -0.6462
REMARK 3 S TENSOR
REMARK 3 S11: -0.0504 S12: 0.1787 S13: 0.2709
REMARK 3 S21: -0.0153 S22: 0.0554 S23: 0.0745
REMARK 3 S31: 0.0469 S32: 0.0244 S33: -0.0050
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): -9.5450 37.2910 17.8000
REMARK 3 T TENSOR
REMARK 3 T11: 0.1835 T22: 0.0347
REMARK 3 T33: 0.2587 T12: -0.0195
REMARK 3 T13: -0.1290 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.2543 L22: 1.4017
REMARK 3 L33: 0.2677 L12: -0.1822
REMARK 3 L13: 0.0876 L23: -0.4325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0618 S12: -0.0012 S13: 0.0918
REMARK 3 S21: -0.2124 S22: 0.1320 S23: 0.2794
REMARK 3 S31: 0.0630 S32: -0.0744 S33: -0.0701
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 901
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1110 39.3530 37.5180
REMARK 3 T TENSOR
REMARK 3 T11: 0.1923 T22: 0.2152
REMARK 3 T33: 1.3387 T12: 0.0130
REMARK 3 T13: 0.2927 T23: 0.1255
REMARK 3 L TENSOR
REMARK 3 L11: 1.2979 L22: 0.6097
REMARK 3 L33: 0.1699 L12: -0.0713
REMARK 3 L13: -0.2221 L23: 0.0110
REMARK 3 S TENSOR
REMARK 3 S11: 0.1949 S12: 0.1006 S13: 1.1362
REMARK 3 S21: 0.0538 S22: 0.0654 S23: 0.2570
REMARK 3 S31: -0.0454 S32: -0.1309 S33: -0.2603
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3NE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059716.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-10
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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79966
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.78100
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3NCI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% (W/V) PEG 350 MONOMETHYL ETHER
REMARK 280 (MME), 175 MM CACL2, 100 MM NACACODYLATE (PH 6.5), MICRO-BATCH
REMARK 280 VAPOR-DIFFUSION, TEMPERATURE 293K
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 37.56750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.32600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.89150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.32600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.56750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.89150
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: 6930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DA P 114 O3' DOC P 115 P -0.116
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DA T 3 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DG T 4 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT T 6 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA T 8 O4' - C1' - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DC T 15 O4' - C1' - N1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DC T 17 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG P 103 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DC P 104 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG P 105 C3' - O3' - P ANGL. DEV. = 7.8 DEGREES
REMARK 500 DC P 108 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DC P 111 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DT P 113 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DOC P 115 O3' - P - OP2 ANGL. DEV. = 8.6 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 GLU A 43 -152.45 -152.74
REMARK 500 PHE A 221 -68.52 -120.93
REMARK 500 SER A 414 66.76 31.20
REMARK 500 SER A 414 67.99 29.79
REMARK 500 ASN A 424 51.26 74.47
REMARK 500 PRO A 458 4.75 -66.02
REMARK 500 ASP A 579 109.80 -162.54
REMARK 500 THR A 622 -63.41 69.02
REMARK 500 ASP A 623 12.20 -148.78
REMARK 500 GLU A 686 -75.62 -102.92
REMARK 500 PHE A 901 -124.32 -125.17
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 A 908 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 116 OE1
REMARK 620 2 GLU A 116 OE2 47.9
REMARK 620 3 HOH A1039 O 78.8 67.4
REMARK 620 4 HOH A1238 O 153.2 148.8 91.5
REMARK 620 5 HOH A1568 O 116.8 69.0 73.7 83.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 904 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 411 OD2
REMARK 620 2 ASP A 411 OD1 50.0
REMARK 620 3 LEU A 412 O 101.8 74.6
REMARK 620 4 ASP A 623 OD1 81.7 121.3 87.6
REMARK 620 5 DCP A 909 O1G 108.6 73.5 100.8 164.8
REMARK 620 6 DCP A 909 O2B 162.6 146.9 90.4 86.5 80.8
REMARK 620 7 DCP A 909 O2A 85.1 120.4 163.4 78.3 91.1 79.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 905 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 411 OD2
REMARK 620 2 ASP A 623 OD2 81.2
REMARK 620 3 DCP A 909 O2A 86.6 79.3
REMARK 620 4 HOH A1217 O 127.5 68.0 125.2
REMARK 620 5 HOH A1218 O 93.4 141.9 138.3 86.9
REMARK 620 6 HOH A1219 O 126.1 141.0 75.7 103.4 70.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 906 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 505 O
REMARK 620 2 ASN A 507 OD1 107.7
REMARK 620 3 LYS A 531 O 164.8 81.3
REMARK 620 4 HOH A1092 O 89.3 78.6 80.4
REMARK 620 5 HOH A1093 O 75.5 141.7 89.8 63.2
REMARK 620 6 HOH A1094 O 96.0 140.8 83.4 133.6 73.7
REMARK 620 7 HOH A1095 O 65.9 80.5 128.7 140.5 131.1 81.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 907 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 716 OE1
REMARK 620 2 HOH A1103 O 106.5
REMARK 620 3 HOH A1104 O 77.2 148.3
REMARK 620 4 HOH A1311 O 72.9 122.4 89.1
REMARK 620 5 HOH A1355 O 98.4 58.4 153.3 64.7
REMARK 620 6 HOH A1550 O 168.3 65.5 114.1 103.5 70.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCP A 909
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IG9 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE REPLICATING COMPLEX OF A POL ALPHA FAMILY DNA
REMARK 900 POLYMERASE
REMARK 900 RELATED ID: 3NCI RELATED DB: PDB
REMARK 900 RB69 DNA POLYMERASE TERNARY COMPLEX WITH DCTP OPPOSITE DG AT 1.8
REMARK 900 ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 3LZJ RELATED DB: PDB
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DCTP OPPOSITE 7,8-
REMARK 900 DIHYDRO-8-OXOGUANINE
REMARK 900 RELATED ID: 3LZI RELATED DB: PDB
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DATP OPPOSITE 7,8-
REMARK 900 DIHYDRO-8-OXOGUANINE
REMARK 900 RELATED ID: 3NAE RELATED DB: PDB
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DATP OPPOSITE
REMARK 900 GUANIDINOHYDANTOIN
REMARK 900 RELATED ID: 3NDK RELATED DB: PDB
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DCTP OPPOSITE DG
DBREF 3NE6 A 1 903 UNP Q38087 DPOL_BPR69 1 903
DBREF 3NE6 T 1 18 PDB 3NE6 3NE6 1 18
DBREF 3NE6 P 103 115 PDB 3NE6 3NE6 103 115
SEQADV 3NE6 ALA A 222 UNP Q38087 ASP 222 ENGINEERED MUTATION
SEQADV 3NE6 ALA A 327 UNP Q38087 ASP 327 ENGINEERED MUTATION
SEQADV 3NE6 GLY A 565 UNP Q38087 SER 565 ENGINEERED MUTATION
SEQADV 3NE6 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 LEU 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 LEU 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 18 DT DC DA DG DG DT DA DA DG DC DA DG DT
SEQRES 2 T 18 DC DC DG DC DG
SEQRES 1 P 13 DG DC DG DG DA DC DT DG DC DT DT DA DOC
MODRES 3NE6 DOC P 115 DC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HET DOC P 115 18
HET CA A 904 1
HET CA A 905 1
HET CA A 906 1
HET CA A 907 1
HET CA A 908 1
HET DCP A 909 28
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HETNAM CA CALCIUM ION
HETNAM DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE
FORMUL 3 DOC C9 H14 N3 O6 P
FORMUL 4 CA 5(CA 2+)
FORMUL 9 DCP C9 H16 N3 O13 P3
FORMUL 10 HOH *757(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 SER A 310 5 3
HELIX 14 14 LYS A 311 GLN A 339 1 29
HELIX 15 15 GLN A 339 LYS A 352 1 14
HELIX 16 16 GLN A 354 PHE A 359 5 6
HELIX 17 17 SER A 360 GLU A 375 1 16
HELIX 18 18 SER A 414 ASN A 424 1 11
HELIX 19 19 SER A 426 GLU A 428 5 3
HELIX 20 20 PRO A 438 ASN A 444 1 7
HELIX 21 21 GLY A 469 LEU A 503 1 35
HELIX 22 22 SER A 523 LYS A 531 1 9
HELIX 23 23 SER A 534 LEU A 570 1 37
HELIX 24 24 ASP A 579 GLY A 610 1 32
HELIX 25 25 ALA A 629 GLY A 637 1 9
HELIX 26 26 GLU A 638 PHE A 641 5 4
HELIX 27 27 ASP A 643 ARG A 658 1 16
HELIX 28 28 ARG A 658 MET A 674 1 17
HELIX 29 29 LEU A 730 LYS A 734 5 5
HELIX 30 30 PRO A 738 GLU A 755 1 18
HELIX 31 31 GLY A 756 PHE A 771 1 16
HELIX 32 32 ARG A 772 LEU A 774 5 3
HELIX 33 33 ASN A 775 ALA A 780 5 6
HELIX 34 34 PRO A 802 ILE A 815 1 14
HELIX 35 35 ILE A 858 MET A 866 1 9
HELIX 36 36 ASP A 867 PHE A 876 1 10
HELIX 37 37 PHE A 876 ALA A 887 1 12
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 ARG A 27 N TYR A 19
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 PHE A 146 O ILE A 187
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 THR A 214 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 ASN A 255 0
SHEET 2 E 2 GLY A 258 LEU A 265 -1 O THR A 264 N ARG A 249
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 ARG A 707 N THR A 703
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 VAL A 407 O ALA A 689
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 ASP A 621 -1 N TYR A 619 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 ARG A 707 N THR A 703
SHEET 4 G 4 THR A 718 MET A 728 -1 O LYS A 726 N LEU A 710
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 1.49
LINK OE1 GLU A 116 CA CA A 908 1555 1555 2.66
LINK OE2 GLU A 116 CA CA A 908 1555 1555 2.74
LINK OD2 ASP A 411 CA CA A 904 1555 1555 2.46
LINK OD1 ASP A 411 CA CA A 904 1555 1555 2.69
LINK OD2 ASP A 411 CA CA A 905 1555 1555 2.53
LINK O LEU A 412 CA CA A 904 1555 1555 2.30
LINK O ASN A 505 CA CA A 906 1555 1555 2.29
LINK OD1 ASN A 507 CA CA A 906 1555 1555 2.35
LINK O LYS A 531 CA CA A 906 1555 1555 2.20
LINK OD1 ASP A 623 CA CA A 904 1555 1555 2.19
LINK OD2 ASP A 623 CA CA A 905 1555 1555 2.77
LINK OE1 GLU A 716 CA CA A 907 1555 1555 2.90
LINK CA CA A 904 O1G DCP A 909 1555 1555 2.26
LINK CA CA A 904 O2B DCP A 909 1555 1555 2.29
LINK CA CA A 904 O2A DCP A 909 1555 1555 2.61
LINK CA CA A 905 O2A DCP A 909 1555 1555 2.48
LINK CA CA A 905 O HOH A1217 1555 1555 2.28
LINK CA CA A 905 O HOH A1218 1555 1555 2.49
LINK CA CA A 905 O HOH A1219 1555 1555 2.60
LINK CA CA A 906 O HOH A1092 1555 1555 2.59
LINK CA CA A 906 O HOH A1093 1555 1555 2.61
LINK CA CA A 906 O HOH A1094 1555 1555 2.26
LINK CA CA A 906 O HOH A1095 1555 1555 2.62
LINK CA CA A 907 O HOH A1103 1555 1555 2.33
LINK CA CA A 907 O HOH A1104 1555 1555 2.20
LINK CA CA A 907 O HOH A1311 1555 1555 2.88
LINK CA CA A 907 O HOH A1355 1555 1555 3.00
LINK CA CA A 907 O HOH A1550 1555 1555 2.72
LINK CA CA A 908 O HOH A1039 1555 1555 2.57
LINK CA CA A 908 O HOH A1238 1555 1555 2.32
LINK CA CA A 908 O HOH A1568 1555 1555 2.33
CISPEP 1 PRO A 42 GLU A 43 0 -5.03
CISPEP 2 ASP A 899 MET A 900 0 1.24
SITE 1 AC1 5 ASP A 411 LEU A 412 ASP A 623 CA A 905
SITE 2 AC1 5 DCP A 909
SITE 1 AC2 7 ASP A 411 ASP A 623 CA A 904 DCP A 909
SITE 2 AC2 7 HOH A1217 HOH A1218 HOH A1219
SITE 1 AC3 7 ASN A 505 ASN A 507 LYS A 531 HOH A1092
SITE 2 AC3 7 HOH A1093 HOH A1094 HOH A1095
SITE 1 AC4 6 GLU A 716 HOH A1103 HOH A1104 HOH A1311
SITE 2 AC4 6 HOH A1355 HOH A1550
SITE 1 AC5 4 GLU A 116 HOH A1039 HOH A1238 HOH A1568
SITE 1 AC6 23 ASP A 411 LEU A 412 SER A 414 LEU A 415
SITE 2 AC6 23 TYR A 416 ARG A 482 LYS A 486 LYS A 560
SITE 3 AC6 23 ASN A 564 THR A 622 ASP A 623 CA A 904
SITE 4 AC6 23 CA A 905 HOH A1035 HOH A1087 HOH A1102
SITE 5 AC6 23 HOH A1105 HOH A1219 HOH A1425 HOH A1464
SITE 6 AC6 23 DOC P 115 DG T 4 DG T 5
CRYST1 75.135 119.783 130.652 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 0.013309 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008348 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007654 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
