HEADER REPLICATION, TRANSFERASE/DNA 11-SEP-07 2R8K
TITLE STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE ETA IN COMPLEX WITH 1,2-
TITLE 2 D(GPG)-CISPLATIN CONTAINING DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*DGP*DTP*DGP*DGP*DTP*DGP*DAP*DGP*DC)-3';
COMPND 3 CHAIN: Q, P;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-D(P*DGP*DGP*DCP*DTP*DCP*DAP*DCP*DCP*DAP*DC)-3';
COMPND 7 CHAIN: U, T;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: DNA POLYMERASE ETA;
COMPND 11 CHAIN: A, B;
COMPND 12 FRAGMENT: CATALYTIC DOMAIN;
COMPND 13 SYNONYM: RADIATION SENSITIVE PROTEIN 30;
COMPND 14 EC: 2.7.7.7;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 4932;
SOURCE 9 STRAIN: YPH499 (ATCC 76625);
SOURCE 10 GENE: RAD30, DBH1;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 ROSETTA;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PEXP007
KEYWDS PROTEIN-CISPLATIN-DNA-DNTP COMPLEX, REPLICATION, TRANSFERASE-DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.CARELL,A.ALT,K.LAMMENS
REVDAT 6 30-AUG-23 2R8K 1 REMARK SEQADV LINK
REVDAT 5 13-JUL-11 2R8K 1 VERSN
REVDAT 4 23-JUN-10 2R8K 1 FORMUL
REVDAT 3 26-MAY-09 2R8K 1 HET
REVDAT 2 24-FEB-09 2R8K 1 VERSN
REVDAT 1 11-DEC-07 2R8K 0
JRNL AUTH A.ALT,K.LAMMENS,C.CHIOCCHINI,A.LAMMENS,J.C.PIECK,D.KUCH,
JRNL AUTH 2 K.P.HOPFNER,T.CARELL
JRNL TITL BYPASS OF DNA LESIONS GENERATED DURING ANTICANCER TREATMENT
JRNL TITL 2 WITH CISPLATIN BY DNA POLYMERASE ETA
JRNL REF SCIENCE V. 318 967 2007
JRNL REFN ISSN 0036-8075
JRNL PMID 17991862
JRNL DOI 10.1126/SCIENCE.1148242
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 24626
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 SET) : 0.230
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1945
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8118
REMARK 3 NUCLEIC ACID ATOMS : 774
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.334
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.224 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.185 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.513 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.483 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R8K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044559.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0719
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24858
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1JIH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 170 MM CALCIUM CHLORIDE, 16% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 146.40500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.87000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.87000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.20250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.87000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.87000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 219.60750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.87000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.87000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 73.20250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.87000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.87000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 219.60750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 146.40500
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 APPLY THE FOLLOWING TO CHAINS: Q, U, A
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 APPLY THE FOLLOWING TO CHAINS: P, T, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -22
REMARK 465 ALA A -21
REMARK 465 SER A -20
REMARK 465 TRP A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 PRO A -16
REMARK 465 GLN A -15
REMARK 465 PHE A -14
REMARK 465 GLU A -13
REMARK 465 LYS A -12
REMARK 465 GLY A -11
REMARK 465 ALA A -10
REMARK 465 SER A -9
REMARK 465 THR A -8
REMARK 465 SER A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 LYS A -4
REMARK 465 LYS A -3
REMARK 465 ALA A -2
REMARK 465 ASP A 510
REMARK 465 LEU A 511
REMARK 465 GLN A 512
REMARK 465 LYS A 513
REMARK 465 THR A 514
REMARK 465 VAL A 515
REMARK 465 VAL A 516
REMARK 465 ASP A 517
REMARK 465 MET A 518
REMARK 465 PHE A 519
REMARK 465 GLY A 520
REMARK 465 ASN A 521
REMARK 465 GLN A 522
REMARK 465 VAL A 523
REMARK 465 HIS A 524
REMARK 465 THR A 525
REMARK 465 PHE A 526
REMARK 465 LYS A 527
REMARK 465 SER A 528
REMARK 465 SER A 529
REMARK 465 ALA A 530
REMARK 465 GLY A 531
REMARK 465 MET B -22
REMARK 465 ALA B -21
REMARK 465 SER B -20
REMARK 465 TRP B -19
REMARK 465 SER B -18
REMARK 465 HIS B -17
REMARK 465 PRO B -16
REMARK 465 GLN B -15
REMARK 465 PHE B -14
REMARK 465 GLU B -13
REMARK 465 LYS B -12
REMARK 465 GLY B -11
REMARK 465 ALA B -10
REMARK 465 SER B -9
REMARK 465 THR B -8
REMARK 465 SER B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 LYS B -4
REMARK 465 LYS B -3
REMARK 465 ALA B -2
REMARK 465 ASP B 510
REMARK 465 LEU B 511
REMARK 465 GLN B 512
REMARK 465 LYS B 513
REMARK 465 THR B 514
REMARK 465 VAL B 515
REMARK 465 VAL B 516
REMARK 465 ASP B 517
REMARK 465 MET B 518
REMARK 465 PHE B 519
REMARK 465 GLY B 520
REMARK 465 ASN B 521
REMARK 465 GLN B 522
REMARK 465 VAL B 523
REMARK 465 HIS B 524
REMARK 465 THR B 525
REMARK 465 PHE B 526
REMARK 465 LYS B 527
REMARK 465 SER B 528
REMARK 465 SER B 529
REMARK 465 ALA B 530
REMARK 465 GLY B 531
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 DC Q 13 O3'
REMARK 470 DC P 13 O3'
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 0 CB CG CD NE CZ NH1 NH2
REMARK 480 MET A 74 CG SD CE
REMARK 480 ASP A 180 CG OD1 OD2
REMARK 480 LYS A 182 CG CD CE NZ
REMARK 480 ASP A 200 CG OD1 OD2
REMARK 480 GLU A 315 CG CD OE1 OE2
REMARK 480 ASP A 318 CG OD1 OD2
REMARK 480 GLU A 333 CG CD OE1 OE2
REMARK 480 LYS A 343 CD CE NZ
REMARK 480 LYS A 349 CG CD CE NZ
REMARK 480 ASP A 354 CB CG OD1 OD2
REMARK 480 ARG A 357 CD NE CZ NH1 NH2
REMARK 480 THR A 359 CB OG1 CG2
REMARK 480 GLU A 372 CB CG CD OE1 OE2
REMARK 480 LYS A 436 CG CD CE NZ
REMARK 480 LYS A 464 CB CG CD CE NZ
REMARK 480 ILE A 466 CB CG1 CG2
REMARK 480 GLN A 469 CD OE1 NE2
REMARK 480 SER A 470 CB OG
REMARK 480 ARG B 0 CG CD NE CZ NH1 NH2
REMARK 480 GLU B 122 CG CD OE1 OE2
REMARK 480 ARG B 133 CG CD NE CZ NH1 NH2
REMARK 480 GLU B 174 CD OE1 OE2
REMARK 480 ASP B 180 CG OD1 OD2
REMARK 480 LYS B 182 CG CD CE NZ
REMARK 480 GLU B 192 CD OE1 OE2
REMARK 480 LYS B 211 CD CE NZ
REMARK 480 SER B 261 OG
REMARK 480 ASP B 318 CG OD1 OD2
REMARK 480 LYS B 343 CD CE NZ
REMARK 480 GLU B 344 CG CD OE1 OE2
REMARK 480 LYS B 349 CG CD CE NZ
REMARK 480 THR B 359 CB OG1 CG2
REMARK 480 ASP B 363 CB CG OD1 OD2
REMARK 480 LYS B 366 CG CD CE NZ
REMARK 480 GLU B 372 CB CG CD OE1 OE2
REMARK 480 ARG B 389 CG CD NE CZ NH1 NH2
REMARK 480 ILE B 466 N CA C O CB CG1 CG2
REMARK 480 GLN B 469 CD OE1 NE2
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 DG U 4 C5' DG U 4 C4' 0.044
REMARK 500 DG U 4 N3 DG U 4 C4 0.042
REMARK 500 DG U 4 N7 DG U 4 C8 -0.040
REMARK 500 DG U 5 C5' DG U 5 C4' 0.043
REMARK 500 DG U 5 O3' DG U 5 C3' 0.146
REMARK 500 DG U 5 N3 DG U 5 C4 0.049
REMARK 500 DG U 5 O3' DC U 6 P 0.073
REMARK 500 DG T 4 P DG T 4 O5' -0.080
REMARK 500 DG T 4 C5' DG T 4 C4' 0.073
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 Q 9 N1 - C1' - C2' ANGL. DEV. = 13.0 DEGREES
REMARK 500 DG Q 12 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG U 4 C4' - C3' - C2' ANGL. DEV. = -6.0 DEGREES
REMARK 500 DG U 4 O4' - C1' - N9 ANGL. DEV. = 7.6 DEGREES
REMARK 500 DG U 5 O4' - C1' - N9 ANGL. DEV. = 5.3 DEGREES
REMARK 500 DG U 5 N3 - C2 - N2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 DA P 11 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG T 4 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DG T 5 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 MET A 1 136.89 -179.91
REMARK 500 SER A 2 157.48 -49.92
REMARK 500 PRO A 15 22.80 -64.99
REMARK 500 SER A 16 -42.57 -133.04
REMARK 500 TYR A 19 0.46 -63.28
REMARK 500 GLU A 20 -63.57 -91.03
REMARK 500 SER A 21 -38.58 -15.89
REMARK 500 SER A 22 -22.52 84.01
REMARK 500 CYS A 25 67.73 -153.29
REMARK 500 ALA A 33 51.99 28.30
REMARK 500 PHE A 34 -76.00 -37.63
REMARK 500 PRO A 50 76.69 -61.90
REMARK 500 TRP A 56 -93.26 63.21
REMARK 500 MET A 74 33.55 -83.34
REMARK 500 CYS A 84 94.23 -168.18
REMARK 500 LYS A 117 30.68 -92.38
REMARK 500 LEU A 161 21.05 -72.61
REMARK 500 GLU A 174 -58.38 -124.81
REMARK 500 TYR A 175 132.04 -37.26
REMARK 500 THR A 178 -152.05 -164.45
REMARK 500 ASP A 180 76.06 49.49
REMARK 500 LEU A 181 86.18 -179.53
REMARK 500 ASN A 198 78.92 -66.23
REMARK 500 ILE A 201 6.85 -56.79
REMARK 500 ASN A 223 69.77 -150.51
REMARK 500 TRP A 306 137.82 -36.49
REMARK 500 LEU A 308 15.37 -164.59
REMARK 500 VAL A 311 -40.08 -145.73
REMARK 500 ASP A 321 -44.38 69.53
REMARK 500 LEU A 322 103.02 22.57
REMARK 500 ASP A 337 -82.36 -80.71
REMARK 500 ASN A 338 -175.78 -172.07
REMARK 500 GLN A 341 -70.14 -60.01
REMARK 500 ALA A 348 40.42 -78.05
REMARK 500 LYS A 349 1.26 -152.41
REMARK 500 GLN A 352 -122.70 -177.39
REMARK 500 ARG A 357 40.89 -70.54
REMARK 500 THR A 359 51.52 -143.29
REMARK 500 ALA A 371 -79.21 -70.02
REMARK 500 LYS A 399 101.50 -168.44
REMARK 500 SER A 405 -81.34 -42.22
REMARK 500 CYS A 406 92.11 -62.34
REMARK 500 THR A 449 -166.12 -79.40
REMARK 500 ILE A 466 -18.35 168.25
REMARK 500 ASN A 467 45.67 -153.63
REMARK 500 GLN A 469 -66.14 -173.30
REMARK 500 SER A 470 -17.93 -34.93
REMARK 500 TYR A 493 -80.47 -125.45
REMARK 500 LYS A 498 115.92 -172.18
REMARK 500 THR A 504 -159.19 -142.36
REMARK 500
REMARK 500 THIS ENTRY HAS 113 RAMACHANDRAN OUTLIERS.
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 CPT U 45 PT1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG U 4 N7
REMARK 620 2 CPT U 45 N1 90.2
REMARK 620 3 CPT U 45 N2 179.3 90.3
REMARK 620 4 DG U 5 N7 89.1 178.3 90.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CPT T 45 PT1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG T 4 N7
REMARK 620 2 CPT T 45 N1 89.9
REMARK 620 3 CPT T 45 N2 176.0 89.1
REMARK 620 4 DG T 5 N7 91.9 177.9 89.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 30 OD2
REMARK 620 2 ASP A 155 OD2 74.2
REMARK 620 3 GLU A 156 OE1 71.5 100.1
REMARK 620 4 DTP A2001 O1A 95.1 96.4 154.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 30 OD1
REMARK 620 2 ASP A 30 OD2 47.9
REMARK 620 3 MET A 31 O 71.4 114.2
REMARK 620 4 ASP A 155 OD1 101.7 79.6 92.2
REMARK 620 5 DTP A2001 O1G 88.7 98.6 103.4 163.5
REMARK 620 6 DTP A2001 O1B 148.8 162.1 83.5 97.3 79.2
REMARK 620 7 DTP A2001 O3A 142.4 111.1 133.9 103.8 61.2 52.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B3001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 30 OD2
REMARK 620 2 ASP B 155 OD2 81.2
REMARK 620 3 GLU B 156 OE1 75.9 106.0
REMARK 620 4 DTP B4001 O1A 107.8 109.2 144.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B3002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 30 OD1
REMARK 620 2 ASP B 30 OD2 45.9
REMARK 620 3 MET B 31 O 62.6 103.2
REMARK 620 4 ASP B 155 OD1 90.6 70.6 88.3
REMARK 620 5 DTP B4001 O3A 153.3 116.1 140.6 101.4
REMARK 620 6 DTP B4001 O3G 77.2 100.7 85.3 167.8 90.1
REMARK 620 7 DTP B4001 O3B 126.8 148.5 92.7 137.7 54.8 53.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT U 45
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT T 45
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTP A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTP B 4001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JIH RELATED DB: PDB
REMARK 900 APOENZYME STRUCTURE
REMARK 900 RELATED ID: 2R8J RELATED DB: PDB
REMARK 900 DNA POLYMERASE ETA IN COMPLEX WITH 1,2-D(GPG)-CISPLATIN
DBREF 2R8K A 1 531 UNP Q04049 POLH_YEAST 1 531
DBREF 2R8K B 1 531 UNP Q04049 POLH_YEAST 1 531
DBREF 2R8K P 5 13 PDB 2R8K 2R8K 5 13
DBREF 2R8K Q 5 13 PDB 2R8K 2R8K 5 13
DBREF 2R8K U 4 13 PDB 2R8K 2R8K 4 13
DBREF 2R8K T 4 13 PDB 2R8K 2R8K 4 13
SEQADV 2R8K MET A -22 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K ALA A -21 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K SER A -20 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K TRP A -19 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K SER A -18 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K HIS A -17 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K PRO A -16 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K GLN A -15 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K PHE A -14 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K GLU A -13 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K LYS A -12 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K GLY A -11 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K ALA A -10 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K SER A -9 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K THR A -8 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K SER A -7 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K LEU A -6 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K TYR A -5 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K LYS A -4 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K LYS A -3 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K ALA A -2 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K GLY A -1 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K ARG A 0 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K MET B -22 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K ALA B -21 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K SER B -20 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K TRP B -19 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K SER B -18 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K HIS B -17 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K PRO B -16 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K GLN B -15 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K PHE B -14 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K GLU B -13 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K LYS B -12 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K GLY B -11 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K ALA B -10 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K SER B -9 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K THR B -8 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K SER B -7 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K LEU B -6 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K TYR B -5 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K LYS B -4 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K LYS B -3 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K ALA B -2 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K GLY B -1 UNP Q04049 EXPRESSION TAG
SEQADV 2R8K ARG B 0 UNP Q04049 EXPRESSION TAG
SEQRES 1 Q 9 DG DT DG DG DT DG DA DG DC
SEQRES 1 U 10 DG DG DC DT DC DA DC DC DA DC
SEQRES 1 P 9 DG DT DG DG DT DG DA DG DC
SEQRES 1 T 10 DG DG DC DT DC DA DC DC DA DC
SEQRES 1 A 554 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 554 SER THR SER LEU TYR LYS LYS ALA GLY ARG MET SER LYS
SEQRES 3 A 554 PHE THR TRP LYS GLU LEU ILE GLN LEU GLY SER PRO SER
SEQRES 4 A 554 LYS ALA TYR GLU SER SER LEU ALA CYS ILE ALA HIS ILE
SEQRES 5 A 554 ASP MET ASN ALA PHE PHE ALA GLN VAL GLU GLN MET ARG
SEQRES 6 A 554 CYS GLY LEU SER LYS GLU ASP PRO VAL VAL CYS VAL GLN
SEQRES 7 A 554 TRP ASN SER ILE ILE ALA VAL SER TYR ALA ALA ARG LYS
SEQRES 8 A 554 TYR GLY ILE SER ARG MET ASP THR ILE GLN GLU ALA LEU
SEQRES 9 A 554 LYS LYS CYS SER ASN LEU ILE PRO ILE HIS THR ALA VAL
SEQRES 10 A 554 PHE LYS LYS GLY GLU ASP PHE TRP GLN TYR HIS ASP GLY
SEQRES 11 A 554 CYS GLY SER TRP VAL GLN ASP PRO ALA LYS GLN ILE SER
SEQRES 12 A 554 VAL GLU ASP HIS LYS VAL SER LEU GLU PRO TYR ARG ARG
SEQRES 13 A 554 GLU SER ARG LYS ALA LEU LYS ILE PHE LYS SER ALA CYS
SEQRES 14 A 554 ASP LEU VAL GLU ARG ALA SER ILE ASP GLU VAL PHE LEU
SEQRES 15 A 554 ASP LEU GLY ARG ILE CYS PHE ASN MET LEU MET PHE ASP
SEQRES 16 A 554 ASN GLU TYR GLU LEU THR GLY ASP LEU LYS LEU LYS ASP
SEQRES 17 A 554 ALA LEU SER ASN ILE ARG GLU ALA PHE ILE GLY GLY ASN
SEQRES 18 A 554 TYR ASP ILE ASN SER HIS LEU PRO LEU ILE PRO GLU LYS
SEQRES 19 A 554 ILE LYS SER LEU LYS PHE GLU GLY ASP VAL PHE ASN PRO
SEQRES 20 A 554 GLU GLY ARG ASP LEU ILE THR ASP TRP ASP ASP VAL ILE
SEQRES 21 A 554 LEU ALA LEU GLY SER GLN VAL CYS LYS GLY ILE ARG ASP
SEQRES 22 A 554 SER ILE LYS ASP ILE LEU GLY TYR THR THR SER CYS GLY
SEQRES 23 A 554 LEU SER SER THR LYS ASN VAL CYS LYS LEU ALA SER ASN
SEQRES 24 A 554 TYR LYS LYS PRO ASP ALA GLN THR ILE VAL LYS ASN ASP
SEQRES 25 A 554 CYS LEU LEU ASP PHE LEU ASP CYS GLY LYS PHE GLU ILE
SEQRES 26 A 554 THR SER PHE TRP THR LEU GLY GLY VAL LEU GLY LYS GLU
SEQRES 27 A 554 LEU ILE ASP VAL LEU ASP LEU PRO HIS GLU ASN SER ILE
SEQRES 28 A 554 LYS HIS ILE ARG GLU THR TRP PRO ASP ASN ALA GLY GLN
SEQRES 29 A 554 LEU LYS GLU PHE LEU ASP ALA LYS VAL LYS GLN SER ASP
SEQRES 30 A 554 TYR ASP ARG SER THR SER ASN ILE ASP PRO LEU LYS THR
SEQRES 31 A 554 ALA ASP LEU ALA GLU LYS LEU PHE LYS LEU SER ARG GLY
SEQRES 32 A 554 ARG TYR GLY LEU PRO LEU SER SER ARG PRO VAL VAL LYS
SEQRES 33 A 554 SER MET MET SER ASN LYS ASN LEU ARG GLY LYS SER CYS
SEQRES 34 A 554 ASN SER ILE VAL ASP CYS ILE SER TRP LEU GLU VAL PHE
SEQRES 35 A 554 CYS ALA GLU LEU THR SER ARG ILE GLN ASP LEU GLU GLN
SEQRES 36 A 554 GLU TYR ASN LYS ILE VAL ILE PRO ARG THR VAL SER ILE
SEQRES 37 A 554 SER LEU LYS THR LYS SER TYR GLU VAL TYR ARG LYS SER
SEQRES 38 A 554 GLY PRO VAL ALA TYR LYS GLY ILE ASN PHE GLN SER HIS
SEQRES 39 A 554 GLU LEU LEU LYS VAL GLY ILE LYS PHE VAL THR ASP LEU
SEQRES 40 A 554 ASP ILE LYS GLY LYS ASN LYS SER TYR TYR PRO LEU THR
SEQRES 41 A 554 LYS LEU SER MET THR ILE THR ASN PHE ASP ILE ILE ASP
SEQRES 42 A 554 LEU GLN LYS THR VAL VAL ASP MET PHE GLY ASN GLN VAL
SEQRES 43 A 554 HIS THR PHE LYS SER SER ALA GLY
SEQRES 1 B 554 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 554 SER THR SER LEU TYR LYS LYS ALA GLY ARG MET SER LYS
SEQRES 3 B 554 PHE THR TRP LYS GLU LEU ILE GLN LEU GLY SER PRO SER
SEQRES 4 B 554 LYS ALA TYR GLU SER SER LEU ALA CYS ILE ALA HIS ILE
SEQRES 5 B 554 ASP MET ASN ALA PHE PHE ALA GLN VAL GLU GLN MET ARG
SEQRES 6 B 554 CYS GLY LEU SER LYS GLU ASP PRO VAL VAL CYS VAL GLN
SEQRES 7 B 554 TRP ASN SER ILE ILE ALA VAL SER TYR ALA ALA ARG LYS
SEQRES 8 B 554 TYR GLY ILE SER ARG MET ASP THR ILE GLN GLU ALA LEU
SEQRES 9 B 554 LYS LYS CYS SER ASN LEU ILE PRO ILE HIS THR ALA VAL
SEQRES 10 B 554 PHE LYS LYS GLY GLU ASP PHE TRP GLN TYR HIS ASP GLY
SEQRES 11 B 554 CYS GLY SER TRP VAL GLN ASP PRO ALA LYS GLN ILE SER
SEQRES 12 B 554 VAL GLU ASP HIS LYS VAL SER LEU GLU PRO TYR ARG ARG
SEQRES 13 B 554 GLU SER ARG LYS ALA LEU LYS ILE PHE LYS SER ALA CYS
SEQRES 14 B 554 ASP LEU VAL GLU ARG ALA SER ILE ASP GLU VAL PHE LEU
SEQRES 15 B 554 ASP LEU GLY ARG ILE CYS PHE ASN MET LEU MET PHE ASP
SEQRES 16 B 554 ASN GLU TYR GLU LEU THR GLY ASP LEU LYS LEU LYS ASP
SEQRES 17 B 554 ALA LEU SER ASN ILE ARG GLU ALA PHE ILE GLY GLY ASN
SEQRES 18 B 554 TYR ASP ILE ASN SER HIS LEU PRO LEU ILE PRO GLU LYS
SEQRES 19 B 554 ILE LYS SER LEU LYS PHE GLU GLY ASP VAL PHE ASN PRO
SEQRES 20 B 554 GLU GLY ARG ASP LEU ILE THR ASP TRP ASP ASP VAL ILE
SEQRES 21 B 554 LEU ALA LEU GLY SER GLN VAL CYS LYS GLY ILE ARG ASP
SEQRES 22 B 554 SER ILE LYS ASP ILE LEU GLY TYR THR THR SER CYS GLY
SEQRES 23 B 554 LEU SER SER THR LYS ASN VAL CYS LYS LEU ALA SER ASN
SEQRES 24 B 554 TYR LYS LYS PRO ASP ALA GLN THR ILE VAL LYS ASN ASP
SEQRES 25 B 554 CYS LEU LEU ASP PHE LEU ASP CYS GLY LYS PHE GLU ILE
SEQRES 26 B 554 THR SER PHE TRP THR LEU GLY GLY VAL LEU GLY LYS GLU
SEQRES 27 B 554 LEU ILE ASP VAL LEU ASP LEU PRO HIS GLU ASN SER ILE
SEQRES 28 B 554 LYS HIS ILE ARG GLU THR TRP PRO ASP ASN ALA GLY GLN
SEQRES 29 B 554 LEU LYS GLU PHE LEU ASP ALA LYS VAL LYS GLN SER ASP
SEQRES 30 B 554 TYR ASP ARG SER THR SER ASN ILE ASP PRO LEU LYS THR
SEQRES 31 B 554 ALA ASP LEU ALA GLU LYS LEU PHE LYS LEU SER ARG GLY
SEQRES 32 B 554 ARG TYR GLY LEU PRO LEU SER SER ARG PRO VAL VAL LYS
SEQRES 33 B 554 SER MET MET SER ASN LYS ASN LEU ARG GLY LYS SER CYS
SEQRES 34 B 554 ASN SER ILE VAL ASP CYS ILE SER TRP LEU GLU VAL PHE
SEQRES 35 B 554 CYS ALA GLU LEU THR SER ARG ILE GLN ASP LEU GLU GLN
SEQRES 36 B 554 GLU TYR ASN LYS ILE VAL ILE PRO ARG THR VAL SER ILE
SEQRES 37 B 554 SER LEU LYS THR LYS SER TYR GLU VAL TYR ARG LYS SER
SEQRES 38 B 554 GLY PRO VAL ALA TYR LYS GLY ILE ASN PHE GLN SER HIS
SEQRES 39 B 554 GLU LEU LEU LYS VAL GLY ILE LYS PHE VAL THR ASP LEU
SEQRES 40 B 554 ASP ILE LYS GLY LYS ASN LYS SER TYR TYR PRO LEU THR
SEQRES 41 B 554 LYS LEU SER MET THR ILE THR ASN PHE ASP ILE ILE ASP
SEQRES 42 B 554 LEU GLN LYS THR VAL VAL ASP MET PHE GLY ASN GLN VAL
SEQRES 43 B 554 HIS THR PHE LYS SER SER ALA GLY
HET CPT U 45 3
HET CPT T 45 3
HET CA A1001 1
HET CA A1002 1
HET DTP A2001 30
HET CA B3001 1
HET CA B3002 1
HET DTP B4001 30
HETNAM CPT CISPLATIN
HETNAM CA CALCIUM ION
HETNAM DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
HETSYN CPT DIAMMINE(DICHLORO)PLATINUM
FORMUL 7 CPT 2(CL2 H6 N2 PT)
FORMUL 9 CA 4(CA 2+)
FORMUL 11 DTP 2(C10 H16 N5 O12 P3)
HELIX 1 1 THR A 5 GLN A 11 1 7
HELIX 2 2 LEU A 12 SER A 14 5 3
HELIX 3 3 ALA A 33 CYS A 43 1 11
HELIX 4 4 SER A 63 LYS A 68 1 6
HELIX 5 5 THR A 76 LYS A 82 1 7
HELIX 6 6 LEU A 128 SER A 144 1 17
HELIX 7 7 LEU A 161 ASP A 172 1 12
HELIX 8 8 LEU A 183 LEU A 187 1 5
HELIX 9 9 LEU A 187 GLY A 197 1 11
HELIX 10 10 PRO A 209 LEU A 215 5 7
HELIX 11 11 ASP A 232 LEU A 256 1 25
HELIX 12 12 THR A 267 LYS A 278 1 12
HELIX 13 13 LYS A 287 ASP A 289 5 3
HELIX 14 14 CYS A 290 ASP A 296 1 7
HELIX 15 15 VAL A 311 ASP A 321 1 11
HELIX 16 16 ASN A 326 GLU A 333 1 8
HELIX 17 17 ASN A 338 ALA A 348 1 11
HELIX 18 18 ALA A 368 ARG A 379 1 12
HELIX 19 19 SER A 408 THR A 424 1 17
HELIX 20 20 ILE A 427 ASN A 435 1 9
HELIX 21 21 HIS A 471 LYS A 487 1 17
HELIX 22 22 THR B 5 GLN B 11 1 7
HELIX 23 23 LEU B 12 SER B 14 5 3
HELIX 24 24 ALA B 33 CYS B 43 1 11
HELIX 25 25 SER B 63 LYS B 68 1 6
HELIX 26 26 THR B 76 LYS B 82 1 7
HELIX 27 27 LEU B 128 SER B 144 1 17
HELIX 28 28 LEU B 161 ASP B 172 1 12
HELIX 29 29 LEU B 183 LEU B 187 1 5
HELIX 30 30 LEU B 187 GLY B 197 1 11
HELIX 31 31 PRO B 209 LEU B 215 5 7
HELIX 32 32 ASP B 232 LEU B 256 1 25
HELIX 33 33 THR B 267 LYS B 278 1 12
HELIX 34 34 LYS B 287 ASP B 289 5 3
HELIX 35 35 CYS B 290 ASP B 296 1 7
HELIX 36 36 GLU B 301 PHE B 305 5 5
HELIX 37 37 GLY B 310 LEU B 320 1 11
HELIX 38 38 ASN B 326 TRP B 335 1 10
HELIX 39 39 ALA B 339 VAL B 350 1 12
HELIX 40 40 LYS B 366 SER B 378 1 13
HELIX 41 41 SER B 408 GLN B 432 1 25
HELIX 42 42 SER B 470 GLY B 488 1 19
SHEET 1 A 6 VAL A 149 SER A 153 0
SHEET 2 A 6 GLU A 156 ASP A 160 -1 O PHE A 158 N GLU A 150
SHEET 3 A 6 ILE A 26 MET A 31 -1 N ALA A 27 O LEU A 159
SHEET 4 A 6 THR A 260 SER A 265 -1 O GLY A 263 N HIS A 28
SHEET 5 A 6 ALA A 282 ILE A 285 1 O THR A 284 N CYS A 262
SHEET 6 A 6 ASP A 220 VAL A 221 1 N ASP A 220 O ILE A 285
SHEET 1 B 3 SER A 58 VAL A 62 0
SHEET 2 B 3 VAL A 51 GLN A 55 -1 N CYS A 53 O ILE A 60
SHEET 3 B 3 ILE A 88 HIS A 91 1 O ILE A 90 N VAL A 52
SHEET 1 C 3 TRP A 102 GLN A 103 0
SHEET 2 C 3 VAL A 94 LYS A 96 -1 N VAL A 94 O GLN A 103
SHEET 3 C 3 HIS A 124 VAL A 126 -1 O LYS A 125 N PHE A 95
SHEET 1 D 2 GLU A 176 THR A 178 0
SHEET 2 D 2 LEU A 181 LYS A 182 -1 O LEU A 181 N LEU A 177
SHEET 1 E 4 MET A 395 LYS A 399 0
SHEET 2 E 4 LYS A 498 ILE A 508 -1 O MET A 501 N SER A 397
SHEET 3 E 4 VAL A 438 LYS A 448 -1 N ARG A 441 O ASN A 505
SHEET 4 E 4 VAL A 454 PRO A 460 -1 O GLY A 459 N VAL A 443
SHEET 1 F 6 VAL B 149 GLU B 150 0
SHEET 2 F 6 GLU B 156 ASP B 160 -1 O PHE B 158 N GLU B 150
SHEET 3 F 6 ILE B 26 MET B 31 -1 N ILE B 29 O VAL B 157
SHEET 4 F 6 THR B 260 SER B 265 -1 O GLY B 263 N HIS B 28
SHEET 5 F 6 ALA B 282 ILE B 285 1 O THR B 284 N CYS B 262
SHEET 6 F 6 ASP B 220 VAL B 221 1 N ASP B 220 O ILE B 285
SHEET 1 G 3 SER B 58 VAL B 62 0
SHEET 2 G 3 VAL B 51 GLN B 55 -1 N CYS B 53 O ILE B 60
SHEET 3 G 3 ILE B 88 HIS B 91 1 O ILE B 90 N VAL B 52
SHEET 1 H 3 TRP B 102 GLN B 103 0
SHEET 2 H 3 VAL B 94 LYS B 96 -1 N VAL B 94 O GLN B 103
SHEET 3 H 3 HIS B 124 VAL B 126 -1 O LYS B 125 N PHE B 95
SHEET 1 I 2 GLU B 176 THR B 178 0
SHEET 2 I 2 LEU B 181 LYS B 182 -1 O LEU B 181 N LEU B 177
SHEET 1 J 4 SER B 394 LYS B 399 0
SHEET 2 J 4 LYS B 498 ILE B 509 -1 O MET B 501 N SER B 397
SHEET 3 J 4 ILE B 437 LYS B 448 -1 N ILE B 437 O ILE B 509
SHEET 4 J 4 VAL B 454 PRO B 460 -1 O GLY B 459 N VAL B 443
LINK N7 DG U 4 PT1 CPT U 45 1555 1555 1.95
LINK N7 DG U 5 PT1 CPT U 45 1555 1555 1.98
LINK N7 DG T 4 PT1 CPT T 45 1555 1555 2.00
LINK N7 DG T 5 PT1 CPT T 45 1555 1555 1.99
LINK OD2 ASP A 30 CA CA A1001 1555 1555 2.78
LINK OD1 ASP A 30 CA CA A1002 1555 1555 2.16
LINK OD2 ASP A 30 CA CA A1002 1555 1555 2.95
LINK O MET A 31 CA CA A1002 1555 1555 2.42
LINK OD2 ASP A 155 CA CA A1001 1555 1555 3.09
LINK OD1 ASP A 155 CA CA A1002 1555 1555 2.25
LINK OE1 GLU A 156 CA CA A1001 1555 1555 2.10
LINK CA CA A1001 O1A DTP A2001 1555 1555 2.09
LINK CA CA A1002 O1G DTP A2001 1555 1555 2.17
LINK CA CA A1002 O1B DTP A2001 1555 1555 2.68
LINK CA CA A1002 O3A DTP A2001 1555 1555 3.06
LINK OD2 ASP B 30 CA CA B3001 1555 1555 2.51
LINK OD1 ASP B 30 CA CA B3002 1555 1555 2.31
LINK OD2 ASP B 30 CA CA B3002 1555 1555 3.04
LINK O MET B 31 CA CA B3002 1555 1555 2.47
LINK OD2 ASP B 155 CA CA B3001 1555 1555 2.69
LINK OD1 ASP B 155 CA CA B3002 1555 1555 2.32
LINK OE1 GLU B 156 CA CA B3001 1555 1555 2.23
LINK CA CA B3001 O1A DTP B4001 1555 1555 2.12
LINK CA CA B3002 O3A DTP B4001 1555 1555 2.29
LINK CA CA B3002 O3G DTP B4001 1555 1555 2.88
LINK CA CA B3002 O3B DTP B4001 1555 1555 2.80
CISPEP 1 LYS A 279 PRO A 280 0 0.03
CISPEP 2 TYR A 494 PRO A 495 0 -0.14
CISPEP 3 LYS B 279 PRO B 280 0 0.06
CISPEP 4 TYR B 494 PRO B 495 0 -0.25
SITE 1 AC1 4 DG Q 12 DG U 4 DG U 5 DC U 6
SITE 1 AC2 3 DG T 4 DG T 5 DC T 6
SITE 1 AC3 4 ASP A 30 ASP A 155 GLU A 156 DTP A2001
SITE 1 AC4 4 ASP A 30 MET A 31 ASP A 155 DTP A2001
SITE 1 AC5 4 ASP B 30 ASP B 155 GLU B 156 DTP B4001
SITE 1 AC6 4 ASP B 30 MET B 31 ASP B 155 DTP B4001
SITE 1 AC7 17 ASP A 30 MET A 31 ASN A 32 ALA A 33
SITE 2 AC7 17 PHE A 34 PHE A 35 ILE A 60 TYR A 64
SITE 3 AC7 17 ARG A 67 ARG A 73 ASP A 155 LYS A 279
SITE 4 AC7 17 CA A1001 CA A1002 DC Q 13 DG U 4
SITE 5 AC7 17 DG U 5
SITE 1 AC8 14 ASP B 30 MET B 31 ALA B 33 PHE B 34
SITE 2 AC8 14 PHE B 35 ILE B 60 TYR B 64 ARG B 67
SITE 3 AC8 14 ARG B 73 ASP B 155 CA B3001 CA B3002
SITE 4 AC8 14 DC P 13 DG T 5
CRYST1 103.740 103.740 292.810 90.00 90.00 90.00 P 41 21 2 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 0.009639 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009639 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003415 0.00000
(ATOM LINES ARE NOT SHOWN.)
END