HEADER TRANSFERASE/DNA 18-DEC-13 4O3O
TITLE CRYSTAL STRUCTURE OF HUMAN POLYMERASE ETA INSERTING DATP OPPOSITE AN
TITLE 2 8-OXOG CONTAINING DNA TEMPLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE ETA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RAD30 HOMOLOG A, XERODERMA PIGMENTOSUM VARIANT TYPE PROTEIN;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*CP*AP*TP*(8OG)P*AP*TP*GP*AP*CP*GP*CP*T)-3');
COMPND 9 CHAIN: T;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: NUCLEIC ACIDS TEMPLATE: CAT (8OG)AT GAC GCT;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-D(*AP*GP*CP*GP*TP*CP*AP*T)-3');
COMPND 14 CHAIN: P;
COMPND 15 ENGINEERED: YES;
COMPND 16 OTHER_DETAILS: NUCLEIC ACIDS PRIMAR: AGCGTCAT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POLH, RAD30, RAD30A, XPV;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: CHEMICALLY SYNTHESIZED;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS CATALYTIC DOMAIN, DNA, DNA DAMAGE, DNA-DIRECTED DNA POLYMERASE,
KEYWDS 2 CYTOSINE TRIPHOSPHATE, Y-FAMILY POLYMERASE, TRANS-LESION SYNTHESIS
KEYWDS 3 (TLS), DNA BINDING, 8-OXOG LESION BYPASS, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PATRA,M.EGLI
REVDAT 3 20-SEP-23 4O3O 1 REMARK SEQADV LINK
REVDAT 2 02-JUL-14 4O3O 1 JRNL
REVDAT 1 30-APR-14 4O3O 0
JRNL AUTH A.PATRA,L.D.NAGY,Q.ZHANG,Y.SU,L.MULLER,F.P.GUENGERICH,M.EGLI
JRNL TITL KINETICS, STRUCTURE, AND MECHANISM OF
JRNL TITL 2 8-OXO-7,8-DIHYDRO-2'-DEOXYGUANOSINE BYPASS BY HUMAN DNA
JRNL TITL 3 POLYMERASE ETA
JRNL REF J.BIOL.CHEM. V. 289 16867 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24759104
JRNL DOI 10.1074/JBC.M114.551820
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1551)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 49366
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2497
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 42.6942 - 4.4494 0.99 2649 152 0.1740 0.2090
REMARK 3 2 4.4494 - 3.5322 1.00 2660 115 0.1476 0.1912
REMARK 3 3 3.5322 - 3.0858 1.00 2652 136 0.1592 0.1943
REMARK 3 4 3.0858 - 2.8037 1.00 2614 142 0.1788 0.2120
REMARK 3 5 2.8037 - 2.6028 1.00 2627 131 0.1748 0.1932
REMARK 3 6 2.6028 - 2.4494 1.00 2640 132 0.1820 0.2474
REMARK 3 7 2.4494 - 2.3267 1.00 2602 140 0.1734 0.2324
REMARK 3 8 2.3267 - 2.2254 1.00 2611 134 0.1678 0.2646
REMARK 3 9 2.2254 - 2.1398 1.00 2601 131 0.1621 0.2185
REMARK 3 10 2.1398 - 2.0659 1.00 2601 147 0.1645 0.2311
REMARK 3 11 2.0659 - 2.0013 1.00 2594 143 0.1733 0.2285
REMARK 3 12 2.0013 - 1.9441 0.99 2593 139 0.1764 0.2316
REMARK 3 13 1.9441 - 1.8930 0.99 2572 151 0.1850 0.2259
REMARK 3 14 1.8930 - 1.8468 0.99 2585 134 0.1916 0.2748
REMARK 3 15 1.8468 - 1.8048 0.99 2580 132 0.2029 0.2917
REMARK 3 16 1.8048 - 1.7664 0.99 2584 152 0.2202 0.2711
REMARK 3 17 1.7664 - 1.7310 0.99 2567 149 0.2320 0.2754
REMARK 3 18 1.7310 - 1.6984 0.98 2537 137 0.2574 0.3188
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 4003
REMARK 3 ANGLE : 1.409 5501
REMARK 3 CHIRALITY : 0.058 611
REMARK 3 PLANARITY : 0.006 635
REMARK 3 DIHEDRAL : 20.293 1573
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4O3O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07810
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49366
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.698
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.4740
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.95900
REMARK 200 R SYM FOR SHELL (I) : 0.95900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER (MR)
REMARK 200 STARTING MODEL: PDB ENTRY 4ECQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 5.5, 5MM MAGNESIUM
REMARK 280 CHLORIDE, 15% PEG 2000 MME , VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.18500
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 54.37000
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 40.77750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 67.96250
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 13.59250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 156
REMARK 465 ALA A 157
REMARK 465 GLU A 158
REMARK 465 GLU A 159
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 T 1 O5' C5' C4' O4' C3' C2' C1'
REMARK 470 DC T 1 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC T 1 C6
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 O HOH A 712 O HOH A 866 1.96
REMARK 500 O HOH T 113 O HOH T 129 1.97
REMARK 500 O HOH A 801 O HOH T 129 2.01
REMARK 500 O HOH A 638 O HOH A 865 2.02
REMARK 500 O HOH A 746 O HOH A 877 2.02
REMARK 500 O HOH A 906 O HOH A 925 2.05
REMARK 500 O HOH A 862 O HOH A 920 2.07
REMARK 500 O HOH A 674 O HOH A 930 2.08
REMARK 500 O HOH T 117 O HOH T 127 2.11
REMARK 500 NZ LYS A 163 O HOH A 711 2.13
REMARK 500 O HOH A 901 O HOH A 902 2.14
REMARK 500 O HOH A 824 O HOH A 880 2.14
REMARK 500 OP1 DC T 11 O HOH T 116 2.14
REMARK 500 O HOH A 605 O HOH A 782 2.15
REMARK 500 O HOH A 861 O HOH A 920 2.17
REMARK 500 NZ LYS A 354 OD2 ASP A 358 2.19
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 DG P 2 O3' DG P 2 C3' -0.050
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 DG T 7 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC T 9 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DA P 7 O4' - C4' - C3' 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 CYS A 16 64.08 22.10
REMARK 500 TYR A 39 88.31 67.02
REMARK 500 SER A 62 -18.85 79.16
REMARK 500 GLN A 133 76.78 -63.70
REMARK 500 SER A 217 -158.31 -155.15
REMARK 500 SER A 257 -9.35 92.77
REMARK 500 ASN A 407 83.51 -68.96
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 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD2
REMARK 620 2 MET A 14 O 84.5
REMARK 620 3 ASP A 115 OD2 97.7 87.5
REMARK 620 4 DZ4 A 501 O3G 83.9 94.4 177.6
REMARK 620 5 DZ4 A 501 O1B 168.4 89.3 91.8 86.8
REMARK 620 6 DZ4 A 501 O1A 99.4 173.0 86.1 91.9 87.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 ASP A 115 OD1 94.9
REMARK 620 3 GLU A 116 OE2 87.0 93.0
REMARK 620 4 DZ4 A 501 O1A 101.8 89.7 170.6
REMARK 620 5 HOH A 603 O 86.8 171.9 95.0 82.2
REMARK 620 6 DT P 8 O3' 168.7 92.3 84.0 86.8 87.2
REMARK 620 7 DT P 8 O3' 165.2 90.2 78.8 92.1 90.1 5.7
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 DZ4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O3N RELATED DB: PDB
REMARK 900 RELATED ID: 4O3P RELATED DB: PDB
REMARK 900 RELATED ID: 4O3Q RELATED DB: PDB
REMARK 900 RELATED ID: 4O3R RELATED DB: PDB
REMARK 900 RELATED ID: 4O3S RELATED DB: PDB
DBREF 4O3O A 1 432 UNP Q9Y253 POLH_HUMAN 1 432
DBREF 4O3O T 1 12 PDB 4O3O 4O3O 1 12
DBREF 4O3O P 1 8 PDB 4O3O 4O3O 1 8
SEQADV 4O3O GLY A -2 UNP Q9Y253 EXPRESSION TAG
SEQADV 4O3O PRO A -1 UNP Q9Y253 EXPRESSION TAG
SEQADV 4O3O HIS A 0 UNP Q9Y253 EXPRESSION TAG
SEQRES 1 A 435 GLY PRO HIS MET ALA THR GLY GLN ASP ARG VAL VAL ALA
SEQRES 2 A 435 LEU VAL ASP MET ASP CYS PHE PHE VAL GLN VAL GLU GLN
SEQRES 3 A 435 ARG GLN ASN PRO HIS LEU ARG ASN LYS PRO CYS ALA VAL
SEQRES 4 A 435 VAL GLN TYR LYS SER TRP LYS GLY GLY GLY ILE ILE ALA
SEQRES 5 A 435 VAL SER TYR GLU ALA ARG ALA PHE GLY VAL THR ARG SER
SEQRES 6 A 435 MET TRP ALA ASP ASP ALA LYS LYS LEU CYS PRO ASP LEU
SEQRES 7 A 435 LEU LEU ALA GLN VAL ARG GLU SER ARG GLY LYS ALA ASN
SEQRES 8 A 435 LEU THR LYS TYR ARG GLU ALA SER VAL GLU VAL MET GLU
SEQRES 9 A 435 ILE MET SER ARG PHE ALA VAL ILE GLU ARG ALA SER ILE
SEQRES 10 A 435 ASP GLU ALA TYR VAL ASP LEU THR SER ALA VAL GLN GLU
SEQRES 11 A 435 ARG LEU GLN LYS LEU GLN GLY GLN PRO ILE SER ALA ASP
SEQRES 12 A 435 LEU LEU PRO SER THR TYR ILE GLU GLY LEU PRO GLN GLY
SEQRES 13 A 435 PRO THR THR ALA GLU GLU THR VAL GLN LYS GLU GLY MET
SEQRES 14 A 435 ARG LYS GLN GLY LEU PHE GLN TRP LEU ASP SER LEU GLN
SEQRES 15 A 435 ILE ASP ASN LEU THR SER PRO ASP LEU GLN LEU THR VAL
SEQRES 16 A 435 GLY ALA VAL ILE VAL GLU GLU MET ARG ALA ALA ILE GLU
SEQRES 17 A 435 ARG GLU THR GLY PHE GLN CYS SER ALA GLY ILE SER HIS
SEQRES 18 A 435 ASN LYS VAL LEU ALA LYS LEU ALA CYS GLY LEU ASN LYS
SEQRES 19 A 435 PRO ASN ARG GLN THR LEU VAL SER HIS GLY SER VAL PRO
SEQRES 20 A 435 GLN LEU PHE SER GLN MET PRO ILE ARG LYS ILE ARG SER
SEQRES 21 A 435 LEU GLY GLY LYS LEU GLY ALA SER VAL ILE GLU ILE LEU
SEQRES 22 A 435 GLY ILE GLU TYR MET GLY GLU LEU THR GLN PHE THR GLU
SEQRES 23 A 435 SER GLN LEU GLN SER HIS PHE GLY GLU LYS ASN GLY SER
SEQRES 24 A 435 TRP LEU TYR ALA MET CYS ARG GLY ILE GLU HIS ASP PRO
SEQRES 25 A 435 VAL LYS PRO ARG GLN LEU PRO LYS THR ILE GLY CYS SER
SEQRES 26 A 435 LYS ASN PHE PRO GLY LYS THR ALA LEU ALA THR ARG GLU
SEQRES 27 A 435 GLN VAL GLN TRP TRP LEU LEU GLN LEU ALA GLN GLU LEU
SEQRES 28 A 435 GLU GLU ARG LEU THR LYS ASP ARG ASN ASP ASN ASP ARG
SEQRES 29 A 435 VAL ALA THR GLN LEU VAL VAL SER ILE ARG VAL GLN GLY
SEQRES 30 A 435 ASP LYS ARG LEU SER SER LEU ARG ARG CYS CYS ALA LEU
SEQRES 31 A 435 THR ARG TYR ASP ALA HIS LYS MET SER HIS ASP ALA PHE
SEQRES 32 A 435 THR VAL ILE LYS ASN CYS ASN THR SER GLY ILE GLN THR
SEQRES 33 A 435 GLU TRP SER PRO PRO LEU THR MET LEU PHE LEU CYS ALA
SEQRES 34 A 435 THR LYS PHE SER ALA SER
SEQRES 1 T 12 DC DA DT 8OG DA DT DG DA DC DG DC DT
SEQRES 1 P 8 DA DG DC DG DT DC DA DT
MODRES 4O3O 8OG T 4 DG
HET 8OG T 4 23
HET DZ4 A 501 30
HET MG A 502 1
HET MG A 503 1
HET GOL A 504 6
HETNAM 8OG 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETNAM DZ4 2'-DEOXY-5'-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOOXY)
HETNAM 2 DZ4 PHOSPHORYL]AMINO}PHOSPHORYL]ADENOSINE
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN 8OG 8-OXO-7,8-DIHYDRO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 8OG C10 H14 N5 O8 P
FORMUL 4 DZ4 C10 H17 N6 O11 P3
FORMUL 5 MG 2(MG 2+)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *421(H2 O)
HELIX 1 1 CYS A 16 ASN A 26 1 11
HELIX 2 2 PRO A 27 ARG A 30 5 4
HELIX 3 3 SER A 51 ALA A 56 1 6
HELIX 4 4 TRP A 64 CYS A 72 1 9
HELIX 5 5 LEU A 89 SER A 104 1 16
HELIX 6 6 LEU A 121 LEU A 132 1 12
HELIX 7 7 SER A 138 LEU A 142 5 5
HELIX 8 8 GLN A 162 SER A 177 1 16
HELIX 9 9 SER A 185 GLY A 209 1 25
HELIX 10 10 ASN A 219 ASN A 230 1 12
HELIX 11 11 SER A 242 GLN A 249 1 8
HELIX 12 12 MET A 250 ILE A 255 5 6
HELIX 13 13 GLY A 260 GLY A 271 1 12
HELIX 14 14 TYR A 274 PHE A 281 5 8
HELIX 15 15 THR A 282 GLY A 291 1 10
HELIX 16 16 GLY A 291 CYS A 302 1 12
HELIX 17 17 PRO A 326 ALA A 330 5 5
HELIX 18 18 ARG A 334 ASP A 360 1 27
HELIX 19 19 ASP A 391 LYS A 404 1 14
HELIX 20 20 ASN A 405 ASN A 407 5 3
SHEET 1 A 6 ILE A 109 SER A 113 0
SHEET 2 A 6 GLU A 116 ASP A 120 -1 O GLU A 116 N ALA A 112
SHEET 3 A 6 VAL A 9 MET A 14 -1 N ALA A 10 O VAL A 119
SHEET 4 A 6 CYS A 212 SER A 217 -1 O SER A 217 N VAL A 9
SHEET 5 A 6 GLN A 235 LEU A 237 1 O THR A 236 N ILE A 216
SHEET 6 A 6 THR A 145 ILE A 147 1 N TYR A 146 O LEU A 237
SHEET 1 B 3 GLY A 46 VAL A 50 0
SHEET 2 B 3 CYS A 34 GLN A 38 -1 N VAL A 36 O ILE A 48
SHEET 3 B 3 LEU A 76 GLN A 79 1 O ALA A 78 N VAL A 37
SHEET 1 C 2 GLU A 82 SER A 83 0
SHEET 2 C 2 LYS A 86 ALA A 87 -1 O LYS A 86 N SER A 83
SHEET 1 D 3 ILE A 319 ASN A 324 0
SHEET 2 D 3 GLU A 414 ALA A 431 -1 O ALA A 426 N ILE A 319
SHEET 3 D 3 LEU A 331 THR A 333 -1 N ALA A 332 O TRP A 415
SHEET 1 E 4 ILE A 319 ASN A 324 0
SHEET 2 E 4 GLU A 414 ALA A 431 -1 O ALA A 426 N ILE A 319
SHEET 3 E 4 ARG A 361 VAL A 372 -1 N VAL A 367 O CYS A 425
SHEET 4 E 4 LEU A 381 ALA A 386 -1 O ARG A 383 N VAL A 368
LINK O3' DT T 3 P 8OG T 4 1555 1555 1.61
LINK O3' 8OG T 4 P DA T 5 1555 1555 1.60
LINK OD2 ASP A 13 MG MG A 502 1555 1555 2.03
LINK OD1 ASP A 13 MG MG A 503 1555 1555 2.06
LINK O MET A 14 MG MG A 502 1555 1555 2.11
LINK OD2 ASP A 115 MG MG A 502 1555 1555 2.07
LINK OD1 ASP A 115 MG MG A 503 1555 1555 2.02
LINK OE2 GLU A 116 MG MG A 503 1555 1555 2.13
LINK O3G DZ4 A 501 MG MG A 502 1555 1555 2.05
LINK O1B DZ4 A 501 MG MG A 502 1555 1555 2.06
LINK O1A DZ4 A 501 MG MG A 502 1555 1555 2.22
LINK O1A DZ4 A 501 MG MG A 503 1555 1555 2.16
LINK MG MG A 503 O HOH A 603 1555 1555 2.19
LINK MG MG A 503 O3'B DT P 8 1555 1555 2.28
LINK MG MG A 503 O3'A DT P 8 1555 1555 2.28
CISPEP 1 LEU A 150 PRO A 151 0 4.21
CISPEP 2 LYS A 231 PRO A 232 0 3.78
CISPEP 3 SER A 416 PRO A 417 0 -3.17
SITE 1 AC1 29 ASP A 13 MET A 14 ASP A 15 CYS A 16
SITE 2 AC1 29 PHE A 17 PHE A 18 ILE A 48 ALA A 49
SITE 3 AC1 29 TYR A 52 ARG A 55 ARG A 61 ILE A 114
SITE 4 AC1 29 ASP A 115 LYS A 231 MG A 502 MG A 503
SITE 5 AC1 29 HOH A 603 HOH A 604 HOH A 606 HOH A 609
SITE 6 AC1 29 HOH A 620 HOH A 663 HOH A 803 HOH A 883
SITE 7 AC1 29 DT P 8 HOH P 102 DT T 3 8OG T 4
SITE 8 AC1 29 DA T 5
SITE 1 AC2 6 ASP A 13 MET A 14 ASP A 115 LYS A 231
SITE 2 AC2 6 DZ4 A 501 MG A 503
SITE 1 AC3 7 ASP A 13 ASP A 115 GLU A 116 DZ4 A 501
SITE 2 AC3 7 MG A 502 HOH A 603 DT P 8
SITE 1 AC4 8 PRO A 244 PHE A 247 SER A 248 GLY A 276
SITE 2 AC4 8 GLU A 277 HOH A 956 HOH A 957 HOH A 958
CRYST1 98.567 98.567 81.555 90.00 90.00 120.00 P 61 6
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 0.010145 0.005857 0.000000 0.00000
SCALE2 0.000000 0.011715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012262 0.00000
(ATOM LINES ARE NOT SHOWN.)
END