HEADER TRANSFERASE/DNA 13-MAR-15 4YQW
TITLE MUTANT HUMAN DNA POLYMERASE ETA Q38A/R61A INSERTING DCTP OPPOSITE
TITLE 2 TEMPLATE G
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 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(*AP*TP*GP*AP*TP*GP*AP*CP*GP*CP*T)-3');
COMPND 10 CHAIN: T;
COMPND 11 ENGINEERED: YES;
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
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 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 15 ORGANISM_TAXID: 32630
KEYWDS DCTP TEMPLATE G, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SU,A.PATRA,J.M.HARP,M.EGLI,F.P.GUENGERICH
REVDAT 6 27-SEP-23 4YQW 1 LINK
REVDAT 5 04-DEC-19 4YQW 1 REMARK
REVDAT 4 20-SEP-17 4YQW 1 SOURCE JRNL REMARK
REVDAT 3 08-JUL-15 4YQW 1 JRNL
REVDAT 2 20-MAY-15 4YQW 1 JRNL
REVDAT 1 13-MAY-15 4YQW 0
JRNL AUTH Y.SU,A.PATRA,J.M.HARP,M.EGLI,F.P.GUENGERICH
JRNL TITL ROLES OF RESIDUES ARG-61 AND GLN-38 OF HUMAN DNA POLYMERASE
JRNL TITL 2 ETA IN BYPASS OF DEOXYGUANOSINE AND
JRNL TITL 3 7,8-DIHYDRO-8-OXO-2'-DEOXYGUANOSINE.
JRNL REF J.BIOL.CHEM. V. 290 15921 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 25947374
JRNL DOI 10.1074/JBC.M115.653691
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1839)
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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 28355
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 1461
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 42.9806 - 4.4451 1.00 2738 157 0.1708 0.1918
REMARK 3 2 4.4451 - 3.5287 1.00 2701 149 0.1413 0.1792
REMARK 3 3 3.5287 - 3.0828 1.00 2709 134 0.1625 0.2115
REMARK 3 4 3.0828 - 2.8010 1.00 2682 160 0.1828 0.2494
REMARK 3 5 2.8010 - 2.6003 1.00 2696 137 0.1808 0.2629
REMARK 3 6 2.6003 - 2.4470 1.00 2697 144 0.1900 0.2738
REMARK 3 7 2.4470 - 2.3244 1.00 2692 131 0.1831 0.2949
REMARK 3 8 2.3244 - 2.2232 1.00 2674 143 0.1890 0.2453
REMARK 3 9 2.2232 - 2.1377 1.00 2688 153 0.2113 0.2878
REMARK 3 10 2.1377 - 2.0639 0.98 2617 153 0.2525 0.3282
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.450
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 : 0.008 3865
REMARK 3 ANGLE : 1.108 5325
REMARK 3 CHIRALITY : 0.045 601
REMARK 3 PLANARITY : 0.004 609
REMARK 3 DIHEDRAL : 19.910 1465
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 4YQW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
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 : 28389
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.96400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.290
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 4O3N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAMES (PH 6.0), POLYETHYLENE GLYCOL
REMARK 280 MONOMETHYL ETHER 2000, AND CALCIUM CHLORIDE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
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 27.45933
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 54.91867
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 41.18900
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 68.64833
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 13.72967
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: 4950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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 155
REMARK 465 THR A 156
REMARK 465 ALA A 157
REMARK 465 GLU A 158
REMARK 465 GLU A 159
REMARK 465 GLY A 410
REMARK 465 ILE A 411
REMARK 465 GLN A 412
REMARK 465 DC T 1
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 GLY A -2 N
REMARK 470 MET A 1 CG SD CE
REMARK 470 GLU A 127 OE1 OE2
REMARK 470 GLN A 130 CG CD OE1 NE2
REMARK 470 LYS A 131 CG CD CE NZ
REMARK 470 LEU A 132 CG CD1 CD2
REMARK 470 GLN A 133 CG CD OE1 NE2
REMARK 470 GLN A 162 CG CD OE1 NE2
REMARK 470 MET A 166 CG SD CE
REMARK 470 GLN A 179 CG CD OE1 NE2
REMARK 470 THR A 184 OG1 CG2
REMARK 470 ARG A 256 CZ NH1 NH2
REMARK 470 GLU A 268 CG CD OE1 OE2
REMARK 470 LYS A 293 CG CD CE NZ
REMARK 470 LYS A 317 NZ
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 ARG A 334 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 371 CZ NH1 NH2
REMARK 470 VAL A 372 CG1
REMARK 470 ASP A 375 OD1
REMARK 470 LYS A 376 CG CD CE NZ
REMARK 470 ARG A 377 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 378 N CA CB CG CD1 CD2
REMARK 470 ASN A 405 CG OD1 ND2
REMARK 470 CYS A 406 SG
REMARK 470 SER A 409 OG
REMARK 470 THR A 413 OG1 CG2
REMARK 470 ALA A 431 CB
REMARK 470 DA T 2 P OP1 OP2 O5' C5' N9 C8
REMARK 470 DA T 2 N7 C5 C6 N6 N1 C2 N3
REMARK 470 DA T 2 C4
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 T 12 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DA P 7 O4' - C1' - N9 ANGL. DEV. = 1.9 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 66.90 22.14
REMARK 500 TYR A 39 172.50 66.96
REMARK 500 LYS A 40 -32.29 -139.00
REMARK 500 GLN A 133 90.09 -58.70
REMARK 500 SER A 217 -159.36 -159.09
REMARK 500 SER A 257 -3.52 88.78
REMARK 500 THR A 408 42.34 -95.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 ASP A 13 OD2 52.0
REMARK 620 3 MET A 14 O 75.0 107.5
REMARK 620 4 ASP A 115 OD2 120.1 84.3 84.2
REMARK 620 5 DCP A 501 O1A 123.7 87.6 161.3 86.4
REMARK 620 6 DCP A 501 O1B 150.2 157.8 87.1 80.5 75.4
REMARK 620 7 DCP A 501 O1G 80.9 112.5 101.5 159.0 82.0 79.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD2
REMARK 620 2 ASP A 115 OD1 92.0
REMARK 620 3 GLU A 116 OE2 78.9 133.2
REMARK 620 4 DCP A 501 O1A 84.5 93.3 130.5
REMARK 620 5 HOH A 858 O 84.0 161.9 63.3 68.8
REMARK 620 6 DT P 8 O3' 163.5 72.4 107.7 101.2 112.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DCP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA 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 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YR0 RELATED DB: PDB
REMARK 900 RELATED ID: 4YR3 RELATED DB: PDB
REMARK 900 RELATED ID: 4YR2 RELATED DB: PDB
DBREF 4YQW A 1 432 UNP Q9Y253 POLH_HUMAN 1 432
DBREF 4YQW T 1 12 PDB 4YQW 4YQW 1 12
DBREF 4YQW P 1 8 PDB 4YQW 4YQW 1 8
SEQADV 4YQW GLY A -2 UNP Q9Y253 EXPRESSION TAG
SEQADV 4YQW PRO A -1 UNP Q9Y253 EXPRESSION TAG
SEQADV 4YQW HIS A 0 UNP Q9Y253 EXPRESSION TAG
SEQADV 4YQW ALA A 38 UNP Q9Y253 GLN 38 ENGINEERED MUTATION
SEQADV 4YQW ALA A 61 UNP Q9Y253 ARG 61 ENGINEERED MUTATION
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 ALA 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 ALA 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 DG DA DT DG DA DC DG DC DT
SEQRES 1 P 8 DA DG DC DG DT DC DA DT
HET DCP A 501 28
HET CA A 502 1
HET CA A 503 1
HET GOL A 504 6
HET GOL A 505 6
HETNAM DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 DCP C9 H16 N3 O13 P3
FORMUL 5 CA 2(CA 2+)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 9 HOH *297(H2 O)
HELIX 1 AA1 CYS A 16 ASN A 26 1 11
HELIX 2 AA2 PRO A 27 ARG A 30 5 4
HELIX 3 AA3 SER A 51 ALA A 56 1 6
HELIX 4 AA4 TRP A 64 CYS A 72 1 9
HELIX 5 AA5 LEU A 89 ALA A 107 1 19
HELIX 6 AA6 LEU A 121 LYS A 131 1 11
HELIX 7 AA7 SER A 138 LEU A 142 5 5
HELIX 8 AA8 GLN A 162 LEU A 178 1 17
HELIX 9 AA9 SER A 185 GLY A 209 1 25
HELIX 10 AB1 ASN A 219 GLY A 228 1 10
HELIX 11 AB2 SER A 239 GLY A 241 5 3
HELIX 12 AB3 SER A 242 GLN A 249 1 8
HELIX 13 AB4 MET A 250 ILE A 255 5 6
HELIX 14 AB5 GLY A 260 GLY A 271 1 12
HELIX 15 AB6 TYR A 274 PHE A 281 5 8
HELIX 16 AB7 THR A 282 GLY A 291 1 10
HELIX 17 AB8 GLY A 291 CYS A 302 1 12
HELIX 18 AB9 PRO A 326 ALA A 330 5 5
HELIX 19 AC1 ARG A 334 ASP A 360 1 27
HELIX 20 AC2 ASP A 391 LYS A 404 1 14
HELIX 21 AC3 ASN A 405 ASN A 407 5 3
SHEET 1 AA1 6 ILE A 109 SER A 113 0
SHEET 2 AA1 6 GLU A 116 ASP A 120 -1 O TYR A 118 N GLU A 110
SHEET 3 AA1 6 VAL A 9 MET A 14 -1 N VAL A 12 O ALA A 117
SHEET 4 AA1 6 CYS A 212 SER A 217 -1 O SER A 217 N VAL A 9
SHEET 5 AA1 6 GLN A 235 LEU A 237 1 O THR A 236 N ILE A 216
SHEET 6 AA1 6 THR A 145 ILE A 147 1 N TYR A 146 O LEU A 237
SHEET 1 AA2 3 GLY A 46 VAL A 50 0
SHEET 2 AA2 3 CYS A 34 ALA A 38 -1 N VAL A 36 O ILE A 48
SHEET 3 AA2 3 LEU A 76 GLN A 79 1 O ALA A 78 N VAL A 37
SHEET 1 AA3 2 GLU A 82 SER A 83 0
SHEET 2 AA3 2 LYS A 86 ALA A 87 -1 O LYS A 86 N SER A 83
SHEET 1 AA4 3 ILE A 319 ASN A 324 0
SHEET 2 AA4 3 GLU A 414 SER A 430 -1 O ALA A 426 N ILE A 319
SHEET 3 AA4 3 LEU A 331 THR A 333 -1 N ALA A 332 O TRP A 415
SHEET 1 AA5 4 ILE A 319 ASN A 324 0
SHEET 2 AA5 4 GLU A 414 SER A 430 -1 O ALA A 426 N ILE A 319
SHEET 3 AA5 4 VAL A 362 VAL A 372 -1 N VAL A 367 O CYS A 425
SHEET 4 AA5 4 LEU A 381 ALA A 386 -1 O ARG A 383 N VAL A 368
LINK OD1 ASP A 13 CA CA A 502 1555 1555 2.50
LINK OD2 ASP A 13 CA CA A 502 1555 1555 2.46
LINK OD2 ASP A 13 CA CA A 503 1555 1555 2.32
LINK O MET A 14 CA CA A 502 1555 1555 2.33
LINK OD2 ASP A 115 CA CA A 502 1555 1555 2.38
LINK OD1 ASP A 115 CA CA A 503 1555 1555 2.36
LINK OE2 GLU A 116 CA CA A 503 1555 1555 2.24
LINK O1A DCP A 501 CA CA A 502 1555 1555 2.22
LINK O1B DCP A 501 CA CA A 502 1555 1555 2.28
LINK O1G DCP A 501 CA CA A 502 1555 1555 2.23
LINK O1A DCP A 501 CA CA A 503 1555 1555 2.50
LINK CA CA A 503 O HOH A 858 1555 1555 2.46
LINK CA CA A 503 O3' DT P 8 1555 1555 2.41
CISPEP 1 LEU A 150 PRO A 151 0 2.71
CISPEP 2 LYS A 231 PRO A 232 0 -1.98
CISPEP 3 SER A 416 PRO A 417 0 -3.30
CISPEP 4 ALA A 431 SER A 432 0 -0.35
SITE 1 AC1 25 ASP A 13 MET A 14 ASP A 15 CYS A 16
SITE 2 AC1 25 PHE A 17 PHE A 18 ILE A 48 ALA A 49
SITE 3 AC1 25 TYR A 52 ARG A 55 ASP A 115 LYS A 231
SITE 4 AC1 25 CA A 502 CA A 503 HOH A 746 HOH A 752
SITE 5 AC1 25 HOH A 753 HOH A 796 HOH A 797 HOH A 801
SITE 6 AC1 25 HOH A 858 DT P 8 DT T 3 DG T 4
SITE 7 AC1 25 DA T 5
SITE 1 AC2 5 ASP A 13 MET A 14 ASP A 115 DCP A 501
SITE 2 AC2 5 CA A 503
SITE 1 AC3 7 ASP A 13 ASP A 115 GLU A 116 DCP A 501
SITE 2 AC3 7 CA A 502 HOH A 858 DT P 8
SITE 1 AC4 8 PRO A 244 SER A 248 GLY A 276 GLU A 277
SITE 2 AC4 8 HOH A 612 HOH A 627 HOH A 637 HOH A 652
SITE 1 AC5 7 GLU A 94 ALA A 95 GLU A 98 HOH A 633
SITE 2 AC5 7 HOH A 642 HOH A 666 HOH A 756
CRYST1 99.238 99.238 82.378 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 0.010077 0.005818 0.000000 0.00000
SCALE2 0.000000 0.011636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012139 0.00000
(ATOM LINES ARE NOT SHOWN.)
END