HEADER TRANSFERASE/DNA 11-AUG-09 3IN5
TITLE STRUCTURE OF HUMAN DNA POLYMERASE KAPPA INSERTING DATP OPPOSITE AN 8-
TITLE 2 OXOG DNA LESION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE KAPPA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 19-526;
COMPND 5 SYNONYM: DINB PROTEIN, DINP;
COMPND 6 EC: 2.7.7.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(*GP*G*GP*GP*GP*AP*AP*GP*GP*AP*CP*TP*(DOC))-3');
COMPND 10 CHAIN: P, Q;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: DNA PRIMER STRAND;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA (5'-D(*C*CP*TP*AP*(8OG)
COMPND 15 P*GP*AP*GP*TP*CP*CP*TP*TP*CP*CP*CP*CP*C)-3');
COMPND 16 CHAIN: T, U;
COMPND 17 ENGINEERED: YES;
COMPND 18 OTHER_DETAILS: DNA TEMPLATE STRAND
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DINB1, POLK;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BJ5464;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES
KEYWDS ALTERNATIVE SPLICING, DNA DAMAGE, DNA REPAIR, DNA REPLICATION, DNA
KEYWDS 2 SYNTHESIS, DNA-BINDING, DNA-DIRECTED DNA POLYMERASE, MAGNESIUM,
KEYWDS 3 METAL-BINDING, MUTATOR PROTEIN, NUCLEOTIDYLTRANSFERASE, NUCLEUS,
KEYWDS 4 PHOSPHOPROTEIN, POLYMORPHISM, SCHIFF BASE, TRANSFERASE, ZINC, ZINC-
KEYWDS 5 FINGER, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.D.SILVERSTEIN,R.VASQUEZ-DEL CARPIO,A.K.AGGARWAL
REVDAT 2 06-SEP-23 3IN5 1 REMARK LINK
REVDAT 1 08-SEP-09 3IN5 0
SPRSDE 08-SEP-09 3IN5 3HED
JRNL AUTH R.VASQUEZ-DEL CARPIO,T.D.SILVERSTEIN,S.LONE,M.K.SWAN,
JRNL AUTH 2 J.R.CHOUDHURY,R.E.JOHNSON,S.PRAKASH,L.PRAKASH,A.K.AGGARWAL
JRNL TITL STRUCTURE OF HUMAN DNA POLYMERASE KAPPA INSERTING DATP
JRNL TITL 2 OPPOSITE AN 8-OXOG DNA LESION
JRNL REF PLOS ONE V. 4 E5766 2009
JRNL REFN ESSN 1932-6203
JRNL PMID 19492058
JRNL DOI 10.1371/JOURNAL.PONE.0005766
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 31139
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1640
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2264
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6750
REMARK 3 NUCLEIC ACID ATOMS : 1056
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 18
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.18000
REMARK 3 B22 (A**2) : 1.33000
REMARK 3 B33 (A**2) : -4.51000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.449
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.326
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.790
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.907
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.858
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8111 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5150 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11192 ; 1.567 ; 2.144
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12639 ; 0.964 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 873 ; 5.589 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 300 ;37.408 ;24.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1241 ;19.639 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;21.503 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1278 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8203 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1447 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4369 ; 0.514 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1755 ; 0.059 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7006 ; 0.979 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3742 ; 1.196 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4185 ; 2.131 ; 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 : NULL
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 3IN5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.100
REMARK 200 MONOCHROMATOR : SI (111)
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 : 34388
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 8.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2OH2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 5000 MONOMETHYL ETHER, 0.2M
REMARK 280 POTASSIUM ACETATE, 0.1M SODIUM CHLORIDE, 0.1M SODIUM CACODYLATE,
REMARK 280 PH 6.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 108.64650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 108.64650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.42300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.24000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.42300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.24000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 108.64650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.42300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.24000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 108.64650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 58.42300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.24000
REMARK 290 SMTRY3 8 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: 6200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, T
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: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Q, U
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 MET A 19
REMARK 465 GLY A 20
REMARK 465 LEU A 21
REMARK 465 ASN A 22
REMARK 465 ASP A 23
REMARK 465 ASN A 24
REMARK 465 MET A 225
REMARK 465 GLY A 226
REMARK 465 SER A 227
REMARK 465 SER A 228
REMARK 465 VAL A 229
REMARK 465 GLU A 230
REMARK 465 ASN A 231
REMARK 465 ASP A 232
REMARK 465 ASN A 233
REMARK 465 PRO A 234
REMARK 465 GLY A 235
REMARK 465 LYS A 236
REMARK 465 GLU A 237
REMARK 465 VAL A 238
REMARK 465 ASN A 239
REMARK 465 LYS A 240
REMARK 465 LEU A 241
REMARK 465 SER A 242
REMARK 465 GLU A 243
REMARK 465 HIS A 244
REMARK 465 GLU A 245
REMARK 465 ARG A 246
REMARK 465 SER A 247
REMARK 465 ILE A 248
REMARK 465 SER A 249
REMARK 465 PRO A 250
REMARK 465 LEU A 251
REMARK 465 LEU A 252
REMARK 465 PHE A 253
REMARK 465 GLU A 254
REMARK 465 GLU A 255
REMARK 465 SER A 256
REMARK 465 PRO A 257
REMARK 465 SER A 258
REMARK 465 ASP A 259
REMARK 465 VAL A 260
REMARK 465 GLN A 261
REMARK 465 PRO A 262
REMARK 465 PRO A 263
REMARK 465 GLY A 264
REMARK 465 ASP A 265
REMARK 465 PRO A 266
REMARK 465 PHE A 267
REMARK 465 GLN A 268
REMARK 465 VAL A 269
REMARK 465 ASN A 270
REMARK 465 PHE A 271
REMARK 465 GLU A 272
REMARK 465 GLU A 273
REMARK 465 GLN A 274
REMARK 465 ASN A 275
REMARK 465 ASN A 276
REMARK 465 PRO A 277
REMARK 465 GLN A 278
REMARK 465 ILE A 279
REMARK 465 LEU A 280
REMARK 465 GLU A 519
REMARK 465 GLU A 520
REMARK 465 ASP A 521
REMARK 465 ARG A 522
REMARK 465 LYS A 523
REMARK 465 HIS A 524
REMARK 465 GLN A 525
REMARK 465 GLN A 526
REMARK 465 MET B 19
REMARK 465 GLY B 20
REMARK 465 LEU B 21
REMARK 465 LYS B 224
REMARK 465 MET B 225
REMARK 465 GLY B 226
REMARK 465 SER B 227
REMARK 465 SER B 228
REMARK 465 VAL B 229
REMARK 465 GLU B 230
REMARK 465 ASN B 231
REMARK 465 ASP B 232
REMARK 465 ASN B 233
REMARK 465 PRO B 234
REMARK 465 GLY B 235
REMARK 465 LYS B 236
REMARK 465 GLU B 237
REMARK 465 VAL B 238
REMARK 465 ASN B 239
REMARK 465 LYS B 240
REMARK 465 LEU B 241
REMARK 465 SER B 242
REMARK 465 GLU B 243
REMARK 465 HIS B 244
REMARK 465 GLU B 245
REMARK 465 ARG B 246
REMARK 465 SER B 247
REMARK 465 ILE B 248
REMARK 465 SER B 249
REMARK 465 PRO B 250
REMARK 465 LEU B 251
REMARK 465 LEU B 252
REMARK 465 PHE B 253
REMARK 465 GLU B 254
REMARK 465 GLU B 255
REMARK 465 SER B 256
REMARK 465 PRO B 257
REMARK 465 SER B 258
REMARK 465 ASP B 259
REMARK 465 VAL B 260
REMARK 465 GLN B 261
REMARK 465 PRO B 262
REMARK 465 PRO B 263
REMARK 465 GLY B 264
REMARK 465 ASP B 265
REMARK 465 PRO B 266
REMARK 465 PHE B 267
REMARK 465 GLN B 268
REMARK 465 VAL B 269
REMARK 465 ASN B 270
REMARK 465 PHE B 271
REMARK 465 GLU B 272
REMARK 465 GLU B 273
REMARK 465 GLN B 274
REMARK 465 ASN B 275
REMARK 465 ASN B 276
REMARK 465 PRO B 277
REMARK 465 GLN B 278
REMARK 465 ILE B 279
REMARK 465 LEU B 280
REMARK 465 GLN B 281
REMARK 465 ASN B 282
REMARK 465 SER B 283
REMARK 465 GLU B 519
REMARK 465 GLU B 520
REMARK 465 ASP B 521
REMARK 465 ARG B 522
REMARK 465 LYS B 523
REMARK 465 HIS B 524
REMARK 465 GLN B 525
REMARK 465 GLN B 526
REMARK 465 DG P 1
REMARK 465 DG P 2
REMARK 465 DC T 1
REMARK 465 DC T 17
REMARK 465 DC T 18
REMARK 465 DG Q 1
REMARK 465 DC U 1
REMARK 465 DC U 2
REMARK 465 DT U 3
REMARK 465 DC U 18
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 LYS A 25 CG CD CE NZ
REMARK 470 MET A 28 CG SD CE
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 LYS A 33 CG CD CE NZ
REMARK 470 LYS A 35 CG CD CE NZ
REMARK 470 LYS A 38 CG CD CE NZ
REMARK 470 GLU A 42 CG CD OE1 OE2
REMARK 470 LYS A 45 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 58 CG CD CE NZ
REMARK 470 GLN A 59 CG CD OE1 NE2
REMARK 470 ARG A 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 92 CG CD OE1 OE2
REMARK 470 LYS A 124 CG CD CE NZ
REMARK 470 ARG A 145 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 149 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 PHE A 222 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 224 CG CD CE NZ
REMARK 470 LYS A 359 CG CD CE NZ
REMARK 470 SER A 388 OG
REMARK 470 ARG A 409 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 412 CG CD OE1 OE2
REMARK 470 LYS A 414 CG CD CE NZ
REMARK 470 ASP B 23 CG OD1 OD2
REMARK 470 ASN B 24 CG OD1 ND2
REMARK 470 GLU B 34 CG CD OE1 OE2
REMARK 470 LYS B 35 CG CD CE NZ
REMARK 470 LYS B 38 CG CD CE NZ
REMARK 470 GLU B 42 CG CD OE1 OE2
REMARK 470 LYS B 45 CG CD CE NZ
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 GLN B 59 CG CD OE1 NE2
REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 115 CG1 CG2
REMARK 470 GLU B 122 CG CD OE1 OE2
REMARK 470 LYS B 124 CG CD CE NZ
REMARK 470 ASP B 125 CG OD1 OD2
REMARK 470 LYS B 126 CG CD CE NZ
REMARK 470 ARG B 145 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 158 CG CD CE NZ
REMARK 470 GLN B 163 CG CD OE1 NE2
REMARK 470 ARG B 175 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 179 CG CD CE NZ
REMARK 470 LYS B 182 CG CD CE NZ
REMARK 470 LYS B 206 CG CD CE NZ
REMARK 470 ASP B 217 CG OD1 OD2
REMARK 470 ARG B 220 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 222 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE B 223 CG1 CG2 CD1
REMARK 470 VAL B 284 CG1 CG2
REMARK 470 VAL B 285 CG1 CG2
REMARK 470 LYS B 359 CG CD CE NZ
REMARK 470 ARG B 409 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 410 CG OD1 OD2
REMARK 470 GLU B 412 CG CD OE1 OE2
REMARK 470 GLU B 429 CG CD OE1 OE2
REMARK 470 LYS B 448 CG CD CE NZ
REMARK 470 ARG B 450 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 489 CG CD CE NZ
REMARK 470 PHE B 500 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 DG P 3 P OP1 OP2
REMARK 470 DC T 2 P OP1 OP2
REMARK 470 DG Q 2 P OP1 OP2
REMARK 470 DA U 4 P OP1 OP2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR B 141 O3G ATP B 2 2.09
REMARK 500 O TRP B 214 NH2 ARG B 219 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 GLU B 389 CD GLU B 389 OE2 0.086
REMARK 500 DT P 12 O3' DT P 12 C3' -0.061
REMARK 500 DG T 6 O3' DG T 6 C3' -0.038
REMARK 500 DA Q 6 O3' DA Q 6 C3' -0.043
REMARK 500 DC Q 11 O3' DC Q 11 C3' -0.049
REMARK 500 DT Q 12 O3' DT Q 12 C3' -0.057
REMARK 500 DA U 4 C5' DA U 4 C4' 0.052
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 ARG B 211 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG P 3 C3' - O3' - P ANGL. DEV. = 8.8 DEGREES
REMARK 500 DG P 4 O4' - C1' - N9 ANGL. DEV. = 5.6 DEGREES
REMARK 500 DG P 5 O4' - C1' - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DA P 6 O4' - C1' - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DG P 8 O4' - C1' - N9 ANGL. DEV. = -4.4 DEGREES
REMARK 500 DC P 11 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT P 12 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DC T 2 C4' - C3' - C2' ANGL. DEV. = -4.3 DEGREES
REMARK 500 DC T 2 C3' - C2' - C1' ANGL. DEV. = -5.5 DEGREES
REMARK 500 DC T 2 O4' - C1' - C2' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DC T 2 O4' - C1' - N1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 DC T 2 C3' - O3' - P ANGL. DEV. = 9.1 DEGREES
REMARK 500 DT T 3 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DA T 4 C3' - O3' - P ANGL. DEV. = 9.6 DEGREES
REMARK 500 DG T 6 O4' - C4' - C3' ANGL. DEV. = -3.4 DEGREES
REMARK 500 DG T 6 O4' - C1' - N9 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DA T 7 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DT T 9 N3 - C4 - O4 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DC T 10 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT T 12 O4' - C1' - N1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 DT T 12 N3 - C4 - O4 ANGL. DEV. = 4.4 DEGREES
REMARK 500 DC T 14 O4' - C1' - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DC T 15 O4' - C1' - N1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 DC T 16 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG Q 2 C3' - O3' - P ANGL. DEV. = 10.8 DEGREES
REMARK 500 DA Q 6 O4' - C4' - C3' ANGL. DEV. = -2.9 DEGREES
REMARK 500 DA Q 6 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DT Q 12 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DA U 4 O4' - C4' - C3' ANGL. DEV. = -6.9 DEGREES
REMARK 500 DA U 4 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DA U 7 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG U 8 O4' - C1' - N9 ANGL. DEV. = 7.0 DEGREES
REMARK 500 DT U 12 O4' - C1' - N1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 DT U 13 N3 - C4 - O4 ANGL. DEV. = 3.8 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 29 -165.89 -108.80
REMARK 500 LYS A 45 -72.52 -33.15
REMARK 500 GLN A 73 47.13 -108.73
REMARK 500 ALA A 110 58.04 32.66
REMARK 500 MET A 135 134.05 177.16
REMARK 500 ALA A 151 -2.27 59.40
REMARK 500 PRO A 190 -17.73 -46.70
REMARK 500 SER A 196 -175.97 -171.75
REMARK 500 SER A 283 148.70 -177.53
REMARK 500 THR A 306 -13.53 91.41
REMARK 500 PHE A 345 -72.18 -71.20
REMARK 500 ILE A 346 -45.39 -29.30
REMARK 500 ALA A 381 -73.07 -53.62
REMARK 500 ASP A 410 -149.62 -71.23
REMARK 500 GLU A 412 124.90 73.56
REMARK 500 GLU A 424 140.50 -37.83
REMARK 500 LEU A 438 -70.21 -68.30
REMARK 500 ARG A 450 56.65 39.29
REMARK 500 ASN A 462 173.63 -53.32
REMARK 500 VAL A 474 -88.17 -85.05
REMARK 500 SER A 475 -10.72 158.72
REMARK 500 SER A 476 -106.72 -83.89
REMARK 500 VAL A 477 -89.82 -155.23
REMARK 500 VAL A 478 135.98 100.70
REMARK 500 SER A 479 -53.55 -147.27
REMARK 500 ALA B 26 -49.05 84.76
REMARK 500 GLU B 29 -102.97 -35.26
REMARK 500 LYS B 45 -105.08 14.50
REMARK 500 PHE B 111 -92.39 -35.98
REMARK 500 MET B 135 146.67 -171.61
REMARK 500 CYS B 161 77.58 -168.44
REMARK 500 GLN B 163 40.82 -77.56
REMARK 500 ILE B 204 30.62 -88.06
REMARK 500 ARG B 211 -32.93 -38.95
REMARK 500 TRP B 214 126.58 -38.43
REMARK 500 LYS B 218 5.24 -67.11
REMARK 500 PHE B 222 -100.62 -84.38
REMARK 500 THR B 305 -9.30 -146.60
REMARK 500 THR B 306 -19.46 76.20
REMARK 500 PRO B 315 -18.56 -47.04
REMARK 500 ASN B 330 57.54 70.22
REMARK 500 ARG B 409 82.57 -61.10
REMARK 500 ASP B 410 113.84 -179.16
REMARK 500 ASN B 462 167.19 -48.67
REMARK 500 SER B 476 -86.47 -87.78
REMARK 500 VAL B 477 153.31 158.91
REMARK 500 SER B 479 -11.09 -153.26
REMARK 500 PHE B 500 136.93 -37.03
REMARK 500 SER B 515 78.97 57.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 ATP A 1
REMARK 610 ATP B 2
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 MG A 2 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A 1 O1B
REMARK 620 2 ATP A 1 O1A 76.7
REMARK 620 3 ASP A 107 OD1 160.3 103.7
REMARK 620 4 MET A 108 O 83.4 158.8 92.6
REMARK 620 5 ASP A 198 OD2 96.6 93.0 103.1 96.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP B 2 O1G
REMARK 620 2 ATP B 2 O2B 90.7
REMARK 620 3 ATP B 2 O1A 110.2 96.7
REMARK 620 4 ASP B 107 OD1 88.5 159.9 102.5
REMARK 620 5 MET B 108 O 82.1 83.9 167.7 76.1
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 ATP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T94 RELATED DB: PDB
REMARK 900 HUMAN POLYMERASE KAPPA APO-ENZYME
REMARK 900 RELATED ID: 2OH2 RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF HUMAN POLYMERASE KAPPA
DBREF 3IN5 A 19 526 UNP Q9UBT6 POLK_HUMAN 19 526
DBREF 3IN5 B 19 526 UNP Q9UBT6 POLK_HUMAN 19 526
DBREF 3IN5 P 1 13 PDB 3IN5 3IN5 1 13
DBREF 3IN5 Q 1 13 PDB 3IN5 3IN5 1 13
DBREF 3IN5 T 1 18 PDB 3IN5 3IN5 1 18
DBREF 3IN5 U 1 18 PDB 3IN5 3IN5 1 18
SEQRES 1 A 508 MET GLY LEU ASN ASP ASN LYS ALA GLY MET GLU GLY LEU
SEQRES 2 A 508 ASP LYS GLU LYS ILE ASN LYS ILE ILE MET GLU ALA THR
SEQRES 3 A 508 LYS GLY SER ARG PHE TYR GLY ASN GLU LEU LYS LYS GLU
SEQRES 4 A 508 LYS GLN VAL ASN GLN ARG ILE GLU ASN MET MET GLN GLN
SEQRES 5 A 508 LYS ALA GLN ILE THR SER GLN GLN LEU ARG LYS ALA GLN
SEQRES 6 A 508 LEU GLN VAL ASP ARG PHE ALA MET GLU LEU GLU GLN SER
SEQRES 7 A 508 ARG ASN LEU SER ASN THR ILE VAL HIS ILE ASP MET ASP
SEQRES 8 A 508 ALA PHE TYR ALA ALA VAL GLU MET ARG ASP ASN PRO GLU
SEQRES 9 A 508 LEU LYS ASP LYS PRO ILE ALA VAL GLY SER MET SER MET
SEQRES 10 A 508 LEU SER THR SER ASN TYR HIS ALA ARG ARG PHE GLY VAL
SEQRES 11 A 508 ARG ALA ALA MET PRO GLY PHE ILE ALA LYS ARG LEU CYS
SEQRES 12 A 508 PRO GLN LEU ILE ILE VAL PRO PRO ASN PHE ASP LYS TYR
SEQRES 13 A 508 ARG ALA VAL SER LYS GLU VAL LYS GLU ILE LEU ALA ASP
SEQRES 14 A 508 TYR ASP PRO ASN PHE MET ALA MET SER LEU ASP GLU ALA
SEQRES 15 A 508 TYR LEU ASN ILE THR LYS HIS LEU GLU GLU ARG GLN ASN
SEQRES 16 A 508 TRP PRO GLU ASP LYS ARG ARG TYR PHE ILE LYS MET GLY
SEQRES 17 A 508 SER SER VAL GLU ASN ASP ASN PRO GLY LYS GLU VAL ASN
SEQRES 18 A 508 LYS LEU SER GLU HIS GLU ARG SER ILE SER PRO LEU LEU
SEQRES 19 A 508 PHE GLU GLU SER PRO SER ASP VAL GLN PRO PRO GLY ASP
SEQRES 20 A 508 PRO PHE GLN VAL ASN PHE GLU GLU GLN ASN ASN PRO GLN
SEQRES 21 A 508 ILE LEU GLN ASN SER VAL VAL PHE GLY THR SER ALA GLN
SEQRES 22 A 508 GLU VAL VAL LYS GLU ILE ARG PHE ARG ILE GLU GLN LYS
SEQRES 23 A 508 THR THR LEU THR ALA SER ALA GLY ILE ALA PRO ASN THR
SEQRES 24 A 508 MET LEU ALA LYS VAL CYS SER ASP LYS ASN LYS PRO ASN
SEQRES 25 A 508 GLY GLN TYR GLN ILE LEU PRO ASN ARG GLN ALA VAL MET
SEQRES 26 A 508 ASP PHE ILE LYS ASP LEU PRO ILE ARG LYS VAL SER GLY
SEQRES 27 A 508 ILE GLY LYS VAL THR GLU LYS MET LEU LYS ALA LEU GLY
SEQRES 28 A 508 ILE ILE THR CYS THR GLU LEU TYR GLN GLN ARG ALA LEU
SEQRES 29 A 508 LEU SER LEU LEU PHE SER GLU THR SER TRP HIS TYR PHE
SEQRES 30 A 508 LEU HIS ILE SER LEU GLY LEU GLY SER THR HIS LEU THR
SEQRES 31 A 508 ARG ASP GLY GLU ARG LYS SER MET SER VAL GLU ARG THR
SEQRES 32 A 508 PHE SER GLU ILE ASN LYS ALA GLU GLU GLN TYR SER LEU
SEQRES 33 A 508 CYS GLN GLU LEU CYS SER GLU LEU ALA GLN ASP LEU GLN
SEQRES 34 A 508 LYS GLU ARG LEU LYS GLY ARG THR VAL THR ILE LYS LEU
SEQRES 35 A 508 LYS ASN VAL ASN PHE GLU VAL LYS THR ARG ALA SER THR
SEQRES 36 A 508 VAL SER SER VAL VAL SER THR ALA GLU GLU ILE PHE ALA
SEQRES 37 A 508 ILE ALA LYS GLU LEU LEU LYS THR GLU ILE ASP ALA ASP
SEQRES 38 A 508 PHE PRO HIS PRO LEU ARG LEU ARG LEU MET GLY VAL ARG
SEQRES 39 A 508 ILE SER SER PHE PRO ASN GLU GLU ASP ARG LYS HIS GLN
SEQRES 40 A 508 GLN
SEQRES 1 B 508 MET GLY LEU ASN ASP ASN LYS ALA GLY MET GLU GLY LEU
SEQRES 2 B 508 ASP LYS GLU LYS ILE ASN LYS ILE ILE MET GLU ALA THR
SEQRES 3 B 508 LYS GLY SER ARG PHE TYR GLY ASN GLU LEU LYS LYS GLU
SEQRES 4 B 508 LYS GLN VAL ASN GLN ARG ILE GLU ASN MET MET GLN GLN
SEQRES 5 B 508 LYS ALA GLN ILE THR SER GLN GLN LEU ARG LYS ALA GLN
SEQRES 6 B 508 LEU GLN VAL ASP ARG PHE ALA MET GLU LEU GLU GLN SER
SEQRES 7 B 508 ARG ASN LEU SER ASN THR ILE VAL HIS ILE ASP MET ASP
SEQRES 8 B 508 ALA PHE TYR ALA ALA VAL GLU MET ARG ASP ASN PRO GLU
SEQRES 9 B 508 LEU LYS ASP LYS PRO ILE ALA VAL GLY SER MET SER MET
SEQRES 10 B 508 LEU SER THR SER ASN TYR HIS ALA ARG ARG PHE GLY VAL
SEQRES 11 B 508 ARG ALA ALA MET PRO GLY PHE ILE ALA LYS ARG LEU CYS
SEQRES 12 B 508 PRO GLN LEU ILE ILE VAL PRO PRO ASN PHE ASP LYS TYR
SEQRES 13 B 508 ARG ALA VAL SER LYS GLU VAL LYS GLU ILE LEU ALA ASP
SEQRES 14 B 508 TYR ASP PRO ASN PHE MET ALA MET SER LEU ASP GLU ALA
SEQRES 15 B 508 TYR LEU ASN ILE THR LYS HIS LEU GLU GLU ARG GLN ASN
SEQRES 16 B 508 TRP PRO GLU ASP LYS ARG ARG TYR PHE ILE LYS MET GLY
SEQRES 17 B 508 SER SER VAL GLU ASN ASP ASN PRO GLY LYS GLU VAL ASN
SEQRES 18 B 508 LYS LEU SER GLU HIS GLU ARG SER ILE SER PRO LEU LEU
SEQRES 19 B 508 PHE GLU GLU SER PRO SER ASP VAL GLN PRO PRO GLY ASP
SEQRES 20 B 508 PRO PHE GLN VAL ASN PHE GLU GLU GLN ASN ASN PRO GLN
SEQRES 21 B 508 ILE LEU GLN ASN SER VAL VAL PHE GLY THR SER ALA GLN
SEQRES 22 B 508 GLU VAL VAL LYS GLU ILE ARG PHE ARG ILE GLU GLN LYS
SEQRES 23 B 508 THR THR LEU THR ALA SER ALA GLY ILE ALA PRO ASN THR
SEQRES 24 B 508 MET LEU ALA LYS VAL CYS SER ASP LYS ASN LYS PRO ASN
SEQRES 25 B 508 GLY GLN TYR GLN ILE LEU PRO ASN ARG GLN ALA VAL MET
SEQRES 26 B 508 ASP PHE ILE LYS ASP LEU PRO ILE ARG LYS VAL SER GLY
SEQRES 27 B 508 ILE GLY LYS VAL THR GLU LYS MET LEU LYS ALA LEU GLY
SEQRES 28 B 508 ILE ILE THR CYS THR GLU LEU TYR GLN GLN ARG ALA LEU
SEQRES 29 B 508 LEU SER LEU LEU PHE SER GLU THR SER TRP HIS TYR PHE
SEQRES 30 B 508 LEU HIS ILE SER LEU GLY LEU GLY SER THR HIS LEU THR
SEQRES 31 B 508 ARG ASP GLY GLU ARG LYS SER MET SER VAL GLU ARG THR
SEQRES 32 B 508 PHE SER GLU ILE ASN LYS ALA GLU GLU GLN TYR SER LEU
SEQRES 33 B 508 CYS GLN GLU LEU CYS SER GLU LEU ALA GLN ASP LEU GLN
SEQRES 34 B 508 LYS GLU ARG LEU LYS GLY ARG THR VAL THR ILE LYS LEU
SEQRES 35 B 508 LYS ASN VAL ASN PHE GLU VAL LYS THR ARG ALA SER THR
SEQRES 36 B 508 VAL SER SER VAL VAL SER THR ALA GLU GLU ILE PHE ALA
SEQRES 37 B 508 ILE ALA LYS GLU LEU LEU LYS THR GLU ILE ASP ALA ASP
SEQRES 38 B 508 PHE PRO HIS PRO LEU ARG LEU ARG LEU MET GLY VAL ARG
SEQRES 39 B 508 ILE SER SER PHE PRO ASN GLU GLU ASP ARG LYS HIS GLN
SEQRES 40 B 508 GLN
SEQRES 1 P 13 DG DG DG DG DG DA DA DG DG DA DC DT DOC
SEQRES 1 T 18 DC DC DT DA 8OG DG DA DG DT DC DC DT DT
SEQRES 2 T 18 DC DC DC DC DC
SEQRES 1 Q 13 DG DG DG DG DG DA DA DG DG DA DC DT DOC
SEQRES 1 U 18 DC DC DT DA 8OG DG DA DG DT DC DC DT DT
SEQRES 2 U 18 DC DC DC DC DC
MODRES 3IN5 DOC P 13 DC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
MODRES 3IN5 8OG T 5 DG
MODRES 3IN5 DOC Q 13 DC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
MODRES 3IN5 8OG U 5 DG
HET DOC P 13 18
HET 8OG T 5 23
HET DOC Q 13 18
HET 8OG U 5 23
HET ATP A 1 30
HET MG A 2 1
HET MG A 3 1
HET ATP B 2 30
HET MG B 1 1
HET MG B 4 1
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HETNAM 8OG 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN 8OG 8-OXO-7,8-DIHYDRO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
FORMUL 3 DOC 2(C9 H14 N3 O6 P)
FORMUL 4 8OG 2(C10 H14 N5 O8 P)
FORMUL 7 ATP 2(C10 H16 N5 O13 P3)
FORMUL 8 MG 4(MG 2+)
FORMUL 13 HOH *18(H2 O)
HELIX 1 1 ASP A 32 ALA A 43 1 12
HELIX 2 2 SER A 47 GLN A 73 1 27
HELIX 3 3 THR A 75 SER A 96 1 22
HELIX 4 4 ALA A 110 ASN A 120 1 11
HELIX 5 5 PRO A 121 LYS A 126 5 6
HELIX 6 6 ASN A 140 PHE A 146 1 7
HELIX 7 7 PRO A 153 CYS A 161 1 9
HELIX 8 8 ASN A 170 ASP A 189 1 20
HELIX 9 9 ILE A 204 ARG A 211 1 8
HELIX 10 10 GLN A 212 TRP A 214 5 3
HELIX 11 11 PRO A 215 LYS A 218 5 4
HELIX 12 12 SER A 289 THR A 306 1 18
HELIX 13 13 ASN A 316 ASN A 327 1 12
HELIX 14 14 ASN A 338 LYS A 347 1 10
HELIX 15 15 ASP A 348 LEU A 349 5 2
HELIX 16 16 PRO A 350 VAL A 354 5 5
HELIX 17 17 GLY A 358 LEU A 368 1 11
HELIX 18 18 THR A 372 GLN A 379 1 8
HELIX 19 19 GLN A 379 PHE A 387 1 9
HELIX 20 20 SER A 388 LEU A 400 1 13
HELIX 21 21 LYS A 427 GLU A 449 1 23
HELIX 22 22 THR A 480 ASP A 499 1 20
HELIX 23 23 ASP B 32 LYS B 45 1 14
HELIX 24 24 SER B 47 ALA B 72 1 26
HELIX 25 25 THR B 75 SER B 96 1 22
HELIX 26 26 ALA B 110 ASN B 120 1 11
HELIX 27 27 PRO B 121 LYS B 124 5 4
HELIX 28 28 ASN B 140 ARG B 145 1 6
HELIX 29 29 PRO B 153 LEU B 160 1 8
HELIX 30 30 ASN B 170 ASP B 189 1 20
HELIX 31 31 ILE B 204 GLN B 212 1 9
HELIX 32 32 GLU B 216 ARG B 220 5 5
HELIX 33 33 SER B 289 THR B 306 1 18
HELIX 34 34 ASN B 316 ASN B 327 1 12
HELIX 35 35 ASN B 338 LYS B 347 1 10
HELIX 36 36 PRO B 350 VAL B 354 5 5
HELIX 37 37 GLY B 358 ALA B 367 1 10
HELIX 38 38 THR B 372 GLN B 379 1 8
HELIX 39 39 GLN B 379 PHE B 387 1 9
HELIX 40 40 SER B 388 GLY B 401 1 14
HELIX 41 41 LYS B 427 LYS B 448 1 22
HELIX 42 42 THR B 480 ALA B 498 1 19
SHEET 1 A 5 MET A 193 ALA A 194 0
SHEET 2 A 5 GLU A 199 ASN A 203 -1 O TYR A 201 N MET A 193
SHEET 3 A 5 ILE A 103 MET A 108 -1 N VAL A 104 O LEU A 202
SHEET 4 A 5 ALA A 309 ALA A 314 -1 O SER A 310 N ASP A 107
SHEET 5 A 5 GLN A 332 GLN A 334 1 O TYR A 333 N ILE A 313
SHEET 1 B 3 MET A 135 SER A 139 0
SHEET 2 B 3 ILE A 128 SER A 132 -1 N SER A 132 O MET A 135
SHEET 3 B 3 ILE A 165 VAL A 167 1 O VAL A 167 N ALA A 129
SHEET 1 C 2 ARG A 220 TYR A 221 0
SHEET 2 C 2 VAL A 284 VAL A 285 -1 O VAL A 284 N TYR A 221
SHEET 1 D 4 SER A 415 ILE A 425 0
SHEET 2 D 4 LEU A 506 SER A 514 -1 O MET A 509 N ARG A 420
SHEET 3 D 4 THR A 455 ASN A 462 -1 N THR A 457 O ARG A 512
SHEET 4 D 4 VAL A 467 THR A 473 -1 O LYS A 468 N LEU A 460
SHEET 1 E 5 MET B 193 SER B 196 0
SHEET 2 E 5 GLU B 199 ASN B 203 -1 O GLU B 199 N MET B 195
SHEET 3 E 5 ILE B 103 MET B 108 -1 N VAL B 104 O LEU B 202
SHEET 4 E 5 ALA B 309 ALA B 314 -1 O SER B 310 N ASP B 107
SHEET 5 E 5 GLN B 332 GLN B 334 1 O TYR B 333 N ILE B 313
SHEET 1 F 3 MET B 135 SER B 139 0
SHEET 2 F 3 ILE B 128 SER B 132 -1 N VAL B 130 O SER B 137
SHEET 3 F 3 ILE B 165 VAL B 167 1 O VAL B 167 N GLY B 131
SHEET 1 G 4 SER B 415 ILE B 425 0
SHEET 2 G 4 LEU B 506 SER B 514 -1 O ARG B 507 N PHE B 422
SHEET 3 G 4 GLY B 453 ASN B 462 -1 N LYS B 461 O ARG B 507
SHEET 4 G 4 VAL B 467 LYS B 468 -1 O LYS B 468 N LEU B 460
SHEET 1 H 4 SER B 415 ILE B 425 0
SHEET 2 H 4 LEU B 506 SER B 514 -1 O ARG B 507 N PHE B 422
SHEET 3 H 4 GLY B 453 ASN B 462 -1 N LYS B 461 O ARG B 507
SHEET 4 H 4 ALA B 471 VAL B 478 -1 O VAL B 474 N ARG B 454
LINK O3' DT P 12 P DOC P 13 1555 1555 1.58
LINK O3' DA T 4 P 8OG T 5 1555 1555 1.57
LINK O3' 8OG T 5 P DG T 6 1555 1555 1.58
LINK O3' DT Q 12 P DOC Q 13 1555 1555 1.60
LINK O3' DA U 4 P 8OG U 5 1555 1555 1.59
LINK O3' 8OG U 5 P DG U 6 1555 1555 1.59
LINK O1B ATP A 1 MG MG A 2 1555 1555 2.27
LINK O1A ATP A 1 MG MG A 2 1555 1555 2.12
LINK MG MG A 2 OD1 ASP A 107 1555 1555 2.08
LINK MG MG A 2 O MET A 108 1555 1555 2.32
LINK MG MG A 2 OD2 ASP A 198 1555 1555 1.89
LINK MG MG A 3 O ILE A 357 1555 1555 2.40
LINK MG MG B 1 O1G ATP B 2 1555 1555 2.20
LINK MG MG B 1 O2B ATP B 2 1555 1555 1.75
LINK MG MG B 1 O1A ATP B 2 1555 1555 1.96
LINK MG MG B 1 OD1 ASP B 107 1555 1555 2.22
LINK MG MG B 1 O MET B 108 1555 1555 2.48
LINK MG MG B 4 OP1 DT Q 12 1555 1555 2.49
CISPEP 1 LYS A 328 PRO A 329 0 -7.19
CISPEP 2 PHE A 500 PRO A 501 0 0.33
CISPEP 3 LYS B 328 PRO B 329 0 -0.48
CISPEP 4 PHE B 500 PRO B 501 0 1.85
SITE 1 AC1 18 MG A 2 ALA A 26 ASP A 107 MET A 108
SITE 2 AC1 18 ASP A 109 ALA A 110 PHE A 111 TYR A 112
SITE 3 AC1 18 SER A 137 THR A 138 TYR A 141 ARG A 144
SITE 4 AC1 18 ASP A 198 LYS A 328 HOH A 527 DOC P 13
SITE 5 AC1 18 8OG T 5 DG T 6
SITE 1 AC2 5 ATP A 1 ASP A 107 MET A 108 ASP A 198
SITE 2 AC2 5 LYS A 328
SITE 1 AC3 4 ARG A 352 VAL A 354 ILE A 357 DT P 12
SITE 1 AC4 17 MG B 1 ALA B 26 ASP B 107 MET B 108
SITE 2 AC4 17 ALA B 110 PHE B 111 TYR B 112 SER B 137
SITE 3 AC4 17 THR B 138 TYR B 141 ARG B 144 ASP B 198
SITE 4 AC4 17 GLU B 199 LYS B 328 DOC Q 13 8OG U 5
SITE 5 AC4 17 DG U 6
SITE 1 AC5 4 ATP B 2 ASP B 107 MET B 108 ASP B 198
SITE 1 AC6 4 ARG B 352 VAL B 354 ILE B 357 DT Q 12
CRYST1 116.846 154.480 217.293 90.00 90.00 90.00 C 2 2 21 16
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 0.008558 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006473 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
