HEADER TRANSFERASE/DNA 30-OCT-09 3KHR
TITLE DPO4 POST-EXTENSION TERNARY COMPLEX WITH THE CORRECT C OPPOSITE THE 2-
TITLE 2 AMINOFLUORENE-GUANINE [AF]G LESION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE IV;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: POL IV;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 5'-D(*TP*TP*GP*GP*AP*TP*GP*GP*TP*AP*GP*CP*(DDG))-3';
COMPND 9 CHAIN: D, H;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: DNA PRIMER STRAND (DIDEOXY-TERMINATED AT THE 3'-END);
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: 5'-D(*CP*C*TP*AP*AP*CP*GP*CP*TP*AP*CP*CP*AP*TP*CP*CP*AP*AP*
COMPND 14 CP*C)-3';
COMPND 15 CHAIN: E, J;
COMPND 16 ENGINEERED: YES;
COMPND 17 OTHER_DETAILS: DNA [AF]G-MODIFIED TEMPLATE STRAND
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS P2;
SOURCE 3 ORGANISM_TAXID: 273057;
SOURCE 4 STRAIN: P2 / DSM 1617 / JCM 11322;
SOURCE 5 GENE: DBH, DPO4, SSO2448;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL(STRATAGENE);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: DNA PRIMER STRAND (DIDEOXY-TERMINATED AT THE 3'-END);
SOURCE 14 MOL_ID: 3;
SOURCE 15 SYNTHETIC: YES;
SOURCE 16 OTHER_DETAILS: DNA [AF]G-MODIFIED TEMPLATE STRAND
KEYWDS LESION BYPASS, DNA POLYMERASE, Y-FAMILY POLYMERASE, 2-AMINOFLUORENE,
KEYWDS 2 SEMI-TARGETED MUTAGENESIS, DNA DAMAGE, DNA REPAIR, DNA REPLICATION,
KEYWDS 3 DNA-BINDING, DNA-DIRECTED DNA POLYMERASE, MAGNESIUM, METAL-BINDING,
KEYWDS 4 MUTATOR PROTEIN, NUCLEOTIDYLTRANSFERASE, TRANSFERASE, TRANSFERASE-
KEYWDS 5 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR O.RECHKOBLIT,L.MALININA,D.J.PATEL
REVDAT 5 06-SEP-23 3KHR 1 REMARK
REVDAT 4 13-OCT-21 3KHR 1 REMARK DBREF SEQADV LINK
REVDAT 3 13-JUL-11 3KHR 1 VERSN
REVDAT 2 16-MAR-10 3KHR 1 JRNL
REVDAT 1 16-FEB-10 3KHR 0
JRNL AUTH O.RECHKOBLIT,A.KOLBANOVSKIY,L.MALININA,N.E.GEACINTOV,
JRNL AUTH 2 S.BROYDE,D.J.PATEL
JRNL TITL MECHANISM OF ERROR-FREE AND SEMITARGETED MUTAGENIC BYPASS OF
JRNL TITL 2 AN AROMATIC AMINE LESION BY Y-FAMILY POLYMERASE DPO4.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 379 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20154704
JRNL DOI 10.1038/NSMB.1771
REMARK 2
REMARK 2 RESOLUTION. 2.01 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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 59976
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3185
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3880
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 207
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5480
REMARK 3 NUCLEIC ACID ATOMS : 1233
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 402
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.40000
REMARK 3 B22 (A**2) : -1.31000
REMARK 3 B33 (A**2) : 0.25000
REMARK 3 B12 (A**2) : 0.81000
REMARK 3 B13 (A**2) : -0.54000
REMARK 3 B23 (A**2) : 1.28000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.206
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.177
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.052
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7083 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9783 ; 1.444 ; 2.225
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 686 ; 4.913 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 244 ;33.852 ;23.566
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1128 ;15.979 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;17.692 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1103 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4760 ; 0.005 ; 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): 3432 ; 0.802 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5555 ; 1.296 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3651 ; 1.743 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4228 ; 2.821 ; 4.500
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 : 4
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 : E 902 E 918
REMARK 3 RESIDUE RANGE : D 803 D 814
REMARK 3 RESIDUE RANGE : A 414 A 414
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4088 -11.4801 -8.3164
REMARK 3 T TENSOR
REMARK 3 T11: 0.2496 T22: 0.1377
REMARK 3 T33: 0.2228 T12: -0.0095
REMARK 3 T13: 0.0243 T23: -0.0692
REMARK 3 L TENSOR
REMARK 3 L11: 1.3519 L22: 3.1387
REMARK 3 L33: 1.2809 L12: -1.4595
REMARK 3 L13: -0.6466 L23: 0.2135
REMARK 3 S TENSOR
REMARK 3 S11: 0.1651 S12: 0.3635 S13: -0.2675
REMARK 3 S21: -0.4558 S22: -0.3869 S23: -0.1812
REMARK 3 S31: 0.1940 S32: -0.1527 S33: 0.2219
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1901 J 1918
REMARK 3 RESIDUE RANGE : H 1803 H 1814
REMARK 3 RESIDUE RANGE : B 1414 B 1414
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8296 32.5105 -47.1225
REMARK 3 T TENSOR
REMARK 3 T11: 0.1926 T22: 0.2713
REMARK 3 T33: 0.2051 T12: 0.0740
REMARK 3 T13: 0.0476 T23: -0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 1.1820 L22: 2.7618
REMARK 3 L33: 3.6132 L12: -0.7539
REMARK 3 L13: -0.5842 L23: 0.5074
REMARK 3 S TENSOR
REMARK 3 S11: -0.1162 S12: -0.2314 S13: 0.3164
REMARK 3 S21: 0.6428 S22: 0.1559 S23: 0.2172
REMARK 3 S31: -0.2345 S32: -0.4583 S33: -0.0398
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 1 A 341
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0217 2.3216 1.6495
REMARK 3 T TENSOR
REMARK 3 T11: 0.0667 T22: 0.0698
REMARK 3 T33: 0.0557 T12: -0.0529
REMARK 3 T13: -0.0024 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 0.4390 L22: 1.6814
REMARK 3 L33: 0.4127 L12: -0.0398
REMARK 3 L13: -0.1963 L23: 0.0063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0718 S12: 0.0355 S13: -0.0690
REMARK 3 S21: 0.0363 S22: -0.0578 S23: 0.0092
REMARK 3 S31: -0.0152 S32: -0.0352 S33: -0.0140
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1001 B 1341
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0735 21.5894 -56.3325
REMARK 3 T TENSOR
REMARK 3 T11: 0.0160 T22: 0.0964
REMARK 3 T33: 0.0715 T12: 0.0011
REMARK 3 T13: -0.0141 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 1.1812 L22: 1.4045
REMARK 3 L33: 2.0056 L12: -0.1835
REMARK 3 L13: -0.5354 L23: -0.5806
REMARK 3 S TENSOR
REMARK 3 S11: -0.0023 S12: -0.0550 S13: 0.0867
REMARK 3 S21: 0.1037 S22: 0.0055 S23: -0.1005
REMARK 3 S31: 0.0546 S32: 0.0534 S33: -0.0032
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 3KHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000056008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97914
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 63173
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
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) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.46900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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 2ASD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.0, 100 MM CALCIUM
REMARK 280 ACETATE, 10% PEG 4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, J
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 DC E 901
REMARK 465 DC E 919
REMARK 465 DC J 1919
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 DT E 902 P OP1 OP2
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 J1903 O3' DA J1903 C3' -0.047
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 DT D 803 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT D 808 O4' - C1' - N1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DG D 809 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DT D 811 C4 - C5 - C7 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DG D 813 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DC D 814 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DA E 903 O3' - P - O5' ANGL. DEV. = -22.1 DEGREES
REMARK 500 DA E 903 O3' - P - OP2 ANGL. DEV. = -15.0 DEGREES
REMARK 500 DA E 903 O3' - P - OP1 ANGL. DEV. = -15.1 DEGREES
REMARK 500 DA E 903 O5' - P - OP1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 DA E 903 O5' - P - OP2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 DC E 905 C3' - C2' - C1' ANGL. DEV. = -5.2 DEGREES
REMARK 500 DC E 905 O4' - C1' - N1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 DC E 907 O4' - C4' - C3' ANGL. DEV. = -2.4 DEGREES
REMARK 500 DC E 907 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC E 911 O4' - C1' - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT E 913 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC E 914 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DA E 917 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT H1804 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG H1805 C3' - O3' - P ANGL. DEV. = 7.6 DEGREES
REMARK 500 DA H1812 O4' - C1' - N9 ANGL. DEV. = -4.5 DEGREES
REMARK 500 DC H1814 O4' - C1' - N1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 DC J1901 O4' - C1' - N1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 DT J1902 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC J1905 C1' - O4' - C4' ANGL. DEV. = -6.7 DEGREES
REMARK 500 DC J1907 C1' - O4' - C4' ANGL. DEV. = -6.1 DEGREES
REMARK 500 DC J1907 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC J1914 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC J1915 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DC J1918 O4' - C1' - N1 ANGL. DEV. = 2.7 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 TYR A 10 54.92 29.83
REMARK 500 ARG A 77 73.46 -107.35
REMARK 500 ASN A 234 44.14 -153.00
REMARK 500 ASP A 277 86.64 36.72
REMARK 500 LYS A 278 -24.84 80.60
REMARK 500 TYR B1010 53.73 30.83
REMARK 500 ASN B1234 35.07 -145.60
REMARK 500 LYS B1278 -24.23 82.57
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 416 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 7 OD1
REMARK 620 2 PHE A 8 O 90.9
REMARK 620 3 ASP A 105 OD2 101.7 80.0
REMARK 620 4 TTP A 414 O1A 103.8 160.4 84.4
REMARK 620 5 TTP A 414 O1B 171.0 84.0 84.7 82.9
REMARK 620 6 TTP A 414 O3G 92.7 106.7 164.1 85.7 81.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 415 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 105 OD1
REMARK 620 2 TTP A 414 O1A 91.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 417 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 181 O
REMARK 620 2 ILE A 186 O 90.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1415 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B1007 OD2
REMARK 620 2 GLU B1106 OE2 119.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1416 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B1007 OD1
REMARK 620 2 PHE B1008 O 84.9
REMARK 620 3 ASP B1105 OD2 105.0 81.8
REMARK 620 4 TTP B1414 O1A 111.6 162.6 88.3
REMARK 620 5 TTP B1414 O1B 161.4 84.3 88.4 81.1
REMARK 620 6 TTP B1414 O3G 85.9 102.6 168.7 84.8 81.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1417 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B1181 O
REMARK 620 2 ILE B1186 O 91.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF E 926
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B 1414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF J 1926
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KHG RELATED DB: PDB
REMARK 900 DPO4 EXTENSION TERNARY COMPLEX WITH MISINSERTED A OPPOSITE THE 2-
REMARK 900 AMINOFLUORENE-GUANINE [AF]G LESION.
REMARK 900 RELATED ID: 3KHH RELATED DB: PDB
REMARK 900 DPO4 EXTENSION TERNARY COMPLEX WITH A C BASE OPPOSITE THE 2-
REMARK 900 AMINOFLUORENE-GUANINE [AF]G LESION.
REMARK 900 RELATED ID: 3KHL RELATED DB: PDB
REMARK 900 DPO4 POST-EXTENSION TERNARY COMPLEX WITH MISINSERTED A OPPOSITE THE
REMARK 900 2-AMINOFLUORENE-GUANINE [AF]G LESION.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FOR CHAINS E AND J, THE 19-MER SEQUENCE OF THE DNA OLIGO
REMARK 999 IS 5'-C T A A C [AF]G C T A C C A T C C A A C C-3', WHERE
REMARK 999 [AF]G DENOTES A COVALENT MODIFICATION BY AF ON THE G BASE
REMARK 999 906 IN CHAIN E AND THE G BASE 1906 IN CHAIN J.
DBREF 3KHR A 2 341 UNP Q97W02 DPO42_SULSO 2 341
DBREF 3KHR D 803 815 PDB 3KHR 3KHR 803 815
DBREF 3KHR E 901 919 PDB 3KHR 3KHR 901 919
DBREF 3KHR B 1002 1341 UNP Q97W02 DPO42_SULSO 2 341
DBREF 3KHR H 1803 1815 PDB 3KHR 3KHR 1803 1815
DBREF 3KHR J 1901 1919 PDB 3KHR 3KHR 1901 1919
SEQADV 3KHR GLY A 1 UNP Q97W02 EXPRESSION TAG
SEQADV 3KHR DDG D 815 PDB 3KHR G 14 ENGINEERED MUTATION
SEQADV 3KHR GLY B 1001 UNP Q97W02 EXPRESSION TAG
SEQADV 3KHR DDG H 1815 PDB 3KHR G 14 ENGINEERED MUTATION
SEQRES 1 A 341 GLY ILE VAL LEU PHE VAL ASP PHE ASP TYR PHE TYR ALA
SEQRES 2 A 341 GLN VAL GLU GLU VAL LEU ASN PRO SER LEU LYS GLY LYS
SEQRES 3 A 341 PRO VAL VAL VAL CYS VAL PHE SER GLY ARG PHE GLU ASP
SEQRES 4 A 341 SER GLY ALA VAL ALA THR ALA ASN TYR GLU ALA ARG LYS
SEQRES 5 A 341 PHE GLY VAL LYS ALA GLY ILE PRO ILE VAL GLU ALA LYS
SEQRES 6 A 341 LYS ILE LEU PRO ASN ALA VAL TYR LEU PRO MET ARG LYS
SEQRES 7 A 341 GLU VAL TYR GLN GLN VAL SER SER ARG ILE MET ASN LEU
SEQRES 8 A 341 LEU ARG GLU TYR SER GLU LYS ILE GLU ILE ALA SER ILE
SEQRES 9 A 341 ASP GLU ALA TYR LEU ASP ILE SER ASP LYS VAL ARG ASP
SEQRES 10 A 341 TYR ARG GLU ALA TYR ASN LEU GLY LEU GLU ILE LYS ASN
SEQRES 11 A 341 LYS ILE LEU GLU LYS GLU LYS ILE THR VAL THR VAL GLY
SEQRES 12 A 341 ILE SER LYS ASN LYS VAL PHE ALA LYS ILE ALA ALA ASP
SEQRES 13 A 341 MET ALA LYS PRO ASN GLY ILE LYS VAL ILE ASP ASP GLU
SEQRES 14 A 341 GLU VAL LYS ARG LEU ILE ARG GLU LEU ASP ILE ALA ASP
SEQRES 15 A 341 VAL PRO GLY ILE GLY ASN ILE THR ALA GLU LYS LEU LYS
SEQRES 16 A 341 LYS LEU GLY ILE ASN LYS LEU VAL ASP THR LEU SER ILE
SEQRES 17 A 341 GLU PHE ASP LYS LEU LYS GLY MET ILE GLY GLU ALA LYS
SEQRES 18 A 341 ALA LYS TYR LEU ILE SER LEU ALA ARG ASP GLU TYR ASN
SEQRES 19 A 341 GLU PRO ILE ARG THR ARG VAL ARG LYS SER ILE GLY ARG
SEQRES 20 A 341 ILE VAL THR MET LYS ARG ASN SER ARG ASN LEU GLU GLU
SEQRES 21 A 341 ILE LYS PRO TYR LEU PHE ARG ALA ILE GLU GLU SER TYR
SEQRES 22 A 341 TYR LYS LEU ASP LYS ARG ILE PRO LYS ALA ILE HIS VAL
SEQRES 23 A 341 VAL ALA VAL THR GLU ASP LEU ASP ILE VAL SER ARG GLY
SEQRES 24 A 341 ARG THR PHE PRO HIS GLY ILE SER LYS GLU THR ALA TYR
SEQRES 25 A 341 SER GLU SER VAL LYS LEU LEU GLN LYS ILE LEU GLU GLU
SEQRES 26 A 341 ASP GLU ARG LYS ILE ARG ARG ILE GLY VAL ARG PHE SER
SEQRES 27 A 341 LYS PHE ILE
SEQRES 1 D 13 DT DT DG DG DA DT DG DG DT DA DG DC DDG
SEQRES 1 E 19 DC DT DA DA DC DG DC DT DA DC DC DA DT
SEQRES 2 E 19 DC DC DA DA DC DC
SEQRES 1 B 341 GLY ILE VAL LEU PHE VAL ASP PHE ASP TYR PHE TYR ALA
SEQRES 2 B 341 GLN VAL GLU GLU VAL LEU ASN PRO SER LEU LYS GLY LYS
SEQRES 3 B 341 PRO VAL VAL VAL CYS VAL PHE SER GLY ARG PHE GLU ASP
SEQRES 4 B 341 SER GLY ALA VAL ALA THR ALA ASN TYR GLU ALA ARG LYS
SEQRES 5 B 341 PHE GLY VAL LYS ALA GLY ILE PRO ILE VAL GLU ALA LYS
SEQRES 6 B 341 LYS ILE LEU PRO ASN ALA VAL TYR LEU PRO MET ARG LYS
SEQRES 7 B 341 GLU VAL TYR GLN GLN VAL SER SER ARG ILE MET ASN LEU
SEQRES 8 B 341 LEU ARG GLU TYR SER GLU LYS ILE GLU ILE ALA SER ILE
SEQRES 9 B 341 ASP GLU ALA TYR LEU ASP ILE SER ASP LYS VAL ARG ASP
SEQRES 10 B 341 TYR ARG GLU ALA TYR ASN LEU GLY LEU GLU ILE LYS ASN
SEQRES 11 B 341 LYS ILE LEU GLU LYS GLU LYS ILE THR VAL THR VAL GLY
SEQRES 12 B 341 ILE SER LYS ASN LYS VAL PHE ALA LYS ILE ALA ALA ASP
SEQRES 13 B 341 MET ALA LYS PRO ASN GLY ILE LYS VAL ILE ASP ASP GLU
SEQRES 14 B 341 GLU VAL LYS ARG LEU ILE ARG GLU LEU ASP ILE ALA ASP
SEQRES 15 B 341 VAL PRO GLY ILE GLY ASN ILE THR ALA GLU LYS LEU LYS
SEQRES 16 B 341 LYS LEU GLY ILE ASN LYS LEU VAL ASP THR LEU SER ILE
SEQRES 17 B 341 GLU PHE ASP LYS LEU LYS GLY MET ILE GLY GLU ALA LYS
SEQRES 18 B 341 ALA LYS TYR LEU ILE SER LEU ALA ARG ASP GLU TYR ASN
SEQRES 19 B 341 GLU PRO ILE ARG THR ARG VAL ARG LYS SER ILE GLY ARG
SEQRES 20 B 341 ILE VAL THR MET LYS ARG ASN SER ARG ASN LEU GLU GLU
SEQRES 21 B 341 ILE LYS PRO TYR LEU PHE ARG ALA ILE GLU GLU SER TYR
SEQRES 22 B 341 TYR LYS LEU ASP LYS ARG ILE PRO LYS ALA ILE HIS VAL
SEQRES 23 B 341 VAL ALA VAL THR GLU ASP LEU ASP ILE VAL SER ARG GLY
SEQRES 24 B 341 ARG THR PHE PRO HIS GLY ILE SER LYS GLU THR ALA TYR
SEQRES 25 B 341 SER GLU SER VAL LYS LEU LEU GLN LYS ILE LEU GLU GLU
SEQRES 26 B 341 ASP GLU ARG LYS ILE ARG ARG ILE GLY VAL ARG PHE SER
SEQRES 27 B 341 LYS PHE ILE
SEQRES 1 H 13 DT DT DG DG DA DT DG DG DT DA DG DC DDG
SEQRES 1 J 19 DC DT DA DA DC DG DC DT DA DC DC DA DT
SEQRES 2 J 19 DC DC DA DA DC DC
MODRES 3KHR DDG D 815 DG
MODRES 3KHR DDG H 1815 DG
HET DDG D 815 21
HET DDG H1815 21
HET TTP A 414 29
HET CA A 415 1
HET CA A 416 1
HET CA A 417 1
HET AF E 926 14
HET TTP B1414 29
HET CA B1415 1
HET CA B1416 1
HET CA B1417 1
HET AF J1926 14
HETNAM DDG 2',3'-DIDEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETNAM TTP THYMIDINE-5'-TRIPHOSPHATE
HETNAM CA CALCIUM ION
HETNAM AF 2-AMINOFLUORENE
FORMUL 2 DDG 2(C10 H14 N5 O6 P)
FORMUL 7 TTP 2(C10 H17 N2 O14 P3)
FORMUL 8 CA 6(CA 2+)
FORMUL 11 AF 2(C13 H11 N)
FORMUL 17 HOH *402(H2 O)
HELIX 1 1 TYR A 10 ASN A 20 1 11
HELIX 2 2 PRO A 21 LYS A 24 5 4
HELIX 3 3 ASN A 47 LYS A 52 1 6
HELIX 4 4 PRO A 60 LEU A 68 1 9
HELIX 5 5 ARG A 77 ARG A 93 1 17
HELIX 6 6 GLU A 94 SER A 96 5 3
HELIX 7 7 ASP A 117 LYS A 137 1 21
HELIX 8 8 ASN A 147 LYS A 159 1 13
HELIX 9 9 ASP A 167 LEU A 178 1 12
HELIX 10 10 ASP A 179 VAL A 183 5 5
HELIX 11 11 GLY A 187 LYS A 196 1 10
HELIX 12 12 LYS A 201 ILE A 208 5 8
HELIX 13 13 GLU A 209 GLY A 218 1 10
HELIX 14 14 GLY A 218 ARG A 230 1 13
HELIX 15 15 ASN A 257 ASP A 277 1 21
HELIX 16 16 SER A 307 ASP A 326 1 20
HELIX 17 17 TYR B 1010 ASN B 1020 1 11
HELIX 18 18 PRO B 1021 LYS B 1024 5 4
HELIX 19 19 ASN B 1047 PHE B 1053 1 7
HELIX 20 20 PRO B 1060 LEU B 1068 1 9
HELIX 21 21 ARG B 1077 GLU B 1094 1 18
HELIX 22 22 ASP B 1117 LYS B 1137 1 21
HELIX 23 23 ASN B 1147 LYS B 1159 1 13
HELIX 24 24 ASP B 1167 LEU B 1178 1 12
HELIX 25 25 ASP B 1179 VAL B 1183 5 5
HELIX 26 26 GLY B 1187 LEU B 1197 1 11
HELIX 27 27 LYS B 1201 ILE B 1208 5 8
HELIX 28 28 GLU B 1209 GLY B 1218 1 10
HELIX 29 29 GLY B 1218 ARG B 1230 1 13
HELIX 30 30 ASN B 1257 LEU B 1276 1 20
HELIX 31 31 SER B 1307 GLU B 1324 1 18
SHEET 1 A 5 ILE A 99 SER A 103 0
SHEET 2 A 5 GLU A 106 ASP A 110 -1 O TYR A 108 N GLU A 100
SHEET 3 A 5 VAL A 3 PHE A 8 -1 N LEU A 4 O LEU A 109
SHEET 4 A 5 VAL A 140 SER A 145 -1 O SER A 145 N VAL A 3
SHEET 5 A 5 ILE A 163 VAL A 165 1 O LYS A 164 N ILE A 144
SHEET 1 B 3 GLY A 41 ALA A 46 0
SHEET 2 B 3 VAL A 28 PHE A 33 -1 N VAL A 32 O ALA A 42
SHEET 3 B 3 VAL A 72 PRO A 75 1 O LEU A 74 N CYS A 31
SHEET 1 C 4 SER A 244 SER A 255 0
SHEET 2 C 4 ILE A 330 PHE A 340 -1 O ILE A 330 N SER A 255
SHEET 3 C 4 PRO A 281 THR A 290 -1 N VAL A 287 O GLY A 334
SHEET 4 C 4 ILE A 295 THR A 301 -1 O VAL A 296 N ALA A 288
SHEET 1 D 5 ILE B1099 SER B1103 0
SHEET 2 D 5 GLU B1106 ASP B1110 -1 O TYR B1108 N GLU B1100
SHEET 3 D 5 VAL B1003 PHE B1008 -1 N LEU B1004 O LEU B1109
SHEET 4 D 5 VAL B1140 SER B1145 -1 O GLY B1143 N PHE B1005
SHEET 5 D 5 ILE B1163 VAL B1165 1 O LYS B1164 N ILE B1144
SHEET 1 E 3 GLY B1041 ALA B1046 0
SHEET 2 E 3 VAL B1028 PHE B1033 -1 N VAL B1032 O ALA B1042
SHEET 3 E 3 VAL B1072 PRO B1075 1 O LEU B1074 N CYS B1031
SHEET 1 F 4 SER B1244 SER B1255 0
SHEET 2 F 4 ILE B1330 PHE B1340 -1 O ILE B1330 N SER B1255
SHEET 3 F 4 PRO B1281 THR B1290 -1 N VAL B1289 O ARG B1331
SHEET 4 F 4 ILE B1295 THR B1301 -1 O VAL B1296 N ALA B1288
LINK O3' DC D 814 P DDG D 815 1555 1555 1.60
LINK C8 DG E 906 N AF E 926 1555 1555 1.45
LINK O3' DC H1814 P DDG H1815 1555 1555 1.60
LINK C8 DG J1906 N AF J1926 1555 1555 1.45
LINK OD1 ASP A 7 CA CA A 416 1555 1555 2.29
LINK O PHE A 8 CA CA A 416 1555 1555 2.31
LINK OD1 ASP A 105 CA CA A 415 1555 1555 2.54
LINK OD2 ASP A 105 CA CA A 416 1555 1555 2.33
LINK O ALA A 181 CA CA A 417 1555 1555 2.31
LINK O ILE A 186 CA CA A 417 1555 1555 2.33
LINK O1A TTP A 414 CA CA A 415 1555 1555 2.35
LINK O1A TTP A 414 CA CA A 416 1555 1555 2.32
LINK O1B TTP A 414 CA CA A 416 1555 1555 2.31
LINK O3G TTP A 414 CA CA A 416 1555 1555 2.40
LINK OD2 ASP B1007 CA CA B1415 1555 1555 2.75
LINK OD1 ASP B1007 CA CA B1416 1555 1555 2.30
LINK O PHE B1008 CA CA B1416 1555 1555 2.30
LINK OD2 ASP B1105 CA CA B1416 1555 1555 2.34
LINK OE2 GLU B1106 CA CA B1415 1555 1555 2.33
LINK O ALA B1181 CA CA B1417 1555 1555 2.31
LINK O ILE B1186 CA CA B1417 1555 1555 2.57
LINK O1A TTP B1414 CA CA B1416 1555 1555 2.41
LINK O1B TTP B1414 CA CA B1416 1555 1555 2.31
LINK O3G TTP B1414 CA CA B1416 1555 1555 2.42
CISPEP 1 LYS A 159 PRO A 160 0 -8.16
CISPEP 2 LYS B 1159 PRO B 1160 0 -5.00
SITE 1 AC1 21 ASP A 7 PHE A 8 TYR A 10 PHE A 11
SITE 2 AC1 21 TYR A 12 ALA A 44 THR A 45 TYR A 48
SITE 3 AC1 21 ARG A 51 ALA A 57 ASP A 105 LYS A 159
SITE 4 AC1 21 CA A 415 CA A 416 HOH A 524 HOH A 553
SITE 5 AC1 21 HOH A 567 HOH A 587 HOH A 597 DDG D 815
SITE 6 AC1 21 DA E 904
SITE 1 AC2 7 ASP A 7 ASP A 105 GLU A 106 TTP A 414
SITE 2 AC2 7 CA A 416 HOH A 510 DDG D 815
SITE 1 AC3 5 ASP A 7 PHE A 8 ASP A 105 TTP A 414
SITE 2 AC3 5 CA A 415
SITE 1 AC4 5 ALA A 181 ILE A 186 HOH A 513 HOH A 585
SITE 2 AC4 5 HOH D 514
SITE 1 AC5 9 ARG A 247 ILE A 248 HIS A 285 VAL A 287
SITE 2 AC5 9 VAL A 335 ARG A 336 DC E 905 DG E 906
SITE 3 AC5 9 DC E 907
SITE 1 AC6 22 HOH B 21 HOH B 25 HOH B 39 HOH B 65
SITE 2 AC6 22 HOH B 167 HOH B 400 ASP B1007 PHE B1008
SITE 3 AC6 22 ASP B1009 TYR B1010 PHE B1011 TYR B1012
SITE 4 AC6 22 ALA B1044 THR B1045 TYR B1048 ARG B1051
SITE 5 AC6 22 ALA B1057 ASP B1105 LYS B1159 CA B1416
SITE 6 AC6 22 DDG H1815 DA J1904
SITE 1 AC7 5 ASP B1007 GLU B1106 LYS B1152 HOH B1519
SITE 2 AC7 5 DDG H1815
SITE 1 AC8 5 ASP B1007 PHE B1008 ASP B1105 TTP B1414
SITE 2 AC8 5 HOH B1519
SITE 1 AC9 7 HOH B 344 ALA B1181 ILE B1186 HOH B1511
SITE 2 AC9 7 HOH B1512 HOH B1513 HOH H 331
SITE 1 BC1 8 ILE B1248 HIS B1285 VAL B1287 VAL B1335
SITE 2 BC1 8 ARG B1336 DC J1905 DG J1906 DC J1907
CRYST1 52.477 53.019 99.858 81.76 76.76 70.14 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 0.019056 -0.006882 -0.004000 0.00000
SCALE2 0.000000 0.020054 -0.001441 0.00000
SCALE3 0.000000 0.000000 0.010314 0.00000
(ATOM LINES ARE NOT SHOWN.)
END