HEADER TRANSFERASE/DNA 11-APR-11 3RH4
TITLE DNA POLYMERASE BETA WITH A DIDEOXY-TERMINATED PRIMER WITH AN INCOMING
TITLE 2 RIBONUCLEOTIDE (RCTP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*CP*GP*AP*CP*GP*CP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3';
COMPND 3 CHAIN: T;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*(DDG))-3';
COMPND 7 CHAIN: P;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: 5'-D(P*GP*TP*CP*GP*G)-3';
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: DNA POLYMERASE BETA;
COMPND 15 CHAIN: A;
COMPND 16 EC: 2.7.7.7, 4.2.99.-;
COMPND 17 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 SYNTHETIC: YES;
SOURCE 7 MOL_ID: 4;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: POLB;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: TAP56;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PWL11
KEYWDS DNA POLYMERASE, RIBONUCLEOTIDE INSERTION, RCTP, TRANSFERASE-DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.CAVANAUGH,W.A.BEARD,V.K.BATRA,L.PERERA,L.G.PEDERSEN,S.H.WILSON
REVDAT 4 13-SEP-23 3RH4 1 REMARK LINK
REVDAT 3 21-SEP-11 3RH4 1 JRNL
REVDAT 2 20-JUL-11 3RH4 1 JRNL
REVDAT 1 06-JUL-11 3RH4 0
JRNL AUTH N.A.CAVANAUGH,W.A.BEARD,V.K.BATRA,L.PERERA,L.G.PEDERSEN,
JRNL AUTH 2 S.H.WILSON
JRNL TITL MOLECULAR INSIGHTS INTO DNA POLYMERASE DETERRENTS FOR
JRNL TITL 2 RIBONUCLEOTIDE INSERTION.
JRNL REF J.BIOL.CHEM. V. 286 31650 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21733843
JRNL DOI 10.1074/JBC.M111.253401
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.0
REMARK 3 NUMBER OF REFLECTIONS : 27776
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2779
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 22.5954 - 4.1243 0.97 2867 334 0.1439 0.1764
REMARK 3 2 4.1243 - 3.2768 0.99 2868 339 0.1421 0.2025
REMARK 3 3 3.2768 - 2.8635 0.90 2619 278 0.1906 0.2623
REMARK 3 4 2.8635 - 2.6021 0.85 2438 293 0.1860 0.2584
REMARK 3 5 2.6021 - 2.4159 0.87 2507 282 0.1862 0.2787
REMARK 3 6 2.4159 - 2.2736 0.87 2563 266 0.1902 0.2885
REMARK 3 7 2.2736 - 2.1598 0.91 2619 294 0.1847 0.2825
REMARK 3 8 2.1598 - 2.0658 0.94 2708 291 0.1727 0.2554
REMARK 3 9 2.0658 - 1.9864 0.78 2265 250 0.1783 0.2878
REMARK 3 10 1.9864 - 1.9179 0.53 1543 152 0.2129 0.3253
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 : 0.40
REMARK 3 B_SOL : 61.86
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.18810
REMARK 3 B22 (A**2) : -1.67910
REMARK 3 B33 (A**2) : -2.50890
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.73030
REMARK 3 B23 (A**2) : 0.00000
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 : 0.006 3537
REMARK 3 ANGLE : 1.150 4917
REMARK 3 CHIRALITY : 0.061 531
REMARK 3 PLANARITY : 0.004 525
REMARK 3 DIHEDRAL : 20.740 1400
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 3RH4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064924.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VIRAMAX
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27776
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.918
REMARK 200 RESOLUTION RANGE LOW (A) : 22.594
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.42100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.070
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2FMS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG3350, 350 MM SODIUM ACETATE, 50
REMARK 280 MM IMIDAZOLE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 39.89500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -148.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, P, D, 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 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 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 ARG A 4
REMARK 465 LYS A 5
REMARK 465 ALA A 6
REMARK 465 PRO A 7
REMARK 465 GLN A 8
REMARK 465 GLU A 9
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 D 1 P DG D 1 OP3 -0.130
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 DC T 2 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC T 5 O4' - C1' - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DG T 6 O4' - C1' - N9 ANGL. DEV. = -7.2 DEGREES
REMARK 500 DC T 7 C3' - O3' - P ANGL. DEV. = 7.6 DEGREES
REMARK 500 DA T 11 O4' - C1' - N9 ANGL. DEV. = -5.0 DEGREES
REMARK 500 DC P 8 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG D 1 O4' - C1' - N9 ANGL. DEV. = -5.1 DEGREES
REMARK 500 DT D 2 O4' - C1' - N1 ANGL. DEV. = -4.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 29 -60.84 -101.04
REMARK 500 LYS A 120 9.19 -150.61
REMARK 500 ASP A 170 117.24 -162.04
REMARK 500 CYS A 178 -135.86 -116.02
REMARK 500 SER A 204 150.00 178.72
REMARK 500 SER A 275 -178.87 -67.48
REMARK 500 ASN A 294 -168.45 -126.56
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 MN P 345 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG P 9 N7
REMARK 620 2 HOH P 128 O 92.0
REMARK 620 3 HOH P 213 O 97.8 76.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 351 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG P 9 OP1
REMARK 620 2 HOH P 130 O 92.0
REMARK 620 3 THR A 101 O 162.9 74.2
REMARK 620 4 VAL A 103 O 100.1 167.7 93.5
REMARK 620 5 ILE A 106 O 101.1 92.9 89.8 86.5
REMARK 620 6 HOH A 572 O 90.2 92.3 80.5 85.9 167.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 340 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH P 11 O
REMARK 620 2 ASP A 190 OD2 91.6
REMARK 620 3 ASP A 192 OD1 153.1 115.2
REMARK 620 4 ASP A 256 OD2 83.9 96.8 94.6
REMARK 620 5 CTP A 338 O1A 76.2 101.1 95.4 153.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 352 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC D 3 OP1
REMARK 620 2 HOH D 93 O 83.5
REMARK 620 3 LYS A 60 O 176.6 95.8
REMARK 620 4 LEU A 62 O 89.3 172.5 91.3
REMARK 620 5 VAL A 65 O 92.4 88.2 90.8 94.3
REMARK 620 6 HOH A 585 O 82.5 96.4 94.3 80.5 172.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 341 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 145 OD2
REMARK 620 2 HIS A 252 ND1 88.4
REMARK 620 3 HOH A 552 O 86.7 91.6
REMARK 620 4 HOH A 553 O 90.1 173.6 82.1
REMARK 620 5 HOH A 555 O 101.5 101.3 164.8 85.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 339 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 190 OD1
REMARK 620 2 ASP A 192 OD2 96.4
REMARK 620 3 CTP A 338 O2B 173.3 89.2
REMARK 620 4 CTP A 338 O1G 88.0 174.0 86.1
REMARK 620 5 CTP A 338 O1A 91.1 92.6 92.4 91.3
REMARK 620 6 HOH A 403 O 88.2 84.8 88.6 91.4 177.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 342 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 285 ND1
REMARK 620 2 HOH A 413 O 99.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 346 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CTP A 338 O2G
REMARK 620 2 HOH A 644 O 85.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 343 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CTP A 350 O3G
REMARK 620 2 CTP A 350 O1B 64.7
REMARK 620 3 CTP A 350 O1A 103.3 67.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN P 345
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP A 338
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP A 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RH5 RELATED DB: PDB
REMARK 900 RELATED ID: 3RH6 RELATED DB: PDB
DBREF 3RH4 A 1 335 UNP P06746 DPOLB_HUMAN 1 335
DBREF 3RH4 T 1 16 PDB 3RH4 3RH4 1 16
DBREF 3RH4 P 1 10 PDB 3RH4 3RH4 1 10
DBREF 3RH4 D 1 5 PDB 3RH4 3RH4 1 5
SEQRES 1 T 16 DC DC DG DA DC DG DC DC DG DC DA DT DC
SEQRES 2 T 16 DA DG DC
SEQRES 1 P 10 DG DC DT DG DA DT DG DC DG DDG
SEQRES 1 D 5 DG DT DC DG DG
SEQRES 1 A 335 MET SER LYS ARG LYS ALA PRO GLN GLU THR LEU ASN GLY
SEQRES 2 A 335 GLY ILE THR ASP MET LEU THR GLU LEU ALA ASN PHE GLU
SEQRES 3 A 335 LYS ASN VAL SER GLN ALA ILE HIS LYS TYR ASN ALA TYR
SEQRES 4 A 335 ARG LYS ALA ALA SER VAL ILE ALA LYS TYR PRO HIS LYS
SEQRES 5 A 335 ILE LYS SER GLY ALA GLU ALA LYS LYS LEU PRO GLY VAL
SEQRES 6 A 335 GLY THR LYS ILE ALA GLU LYS ILE ASP GLU PHE LEU ALA
SEQRES 7 A 335 THR GLY LYS LEU ARG LYS LEU GLU LYS ILE ARG GLN ASP
SEQRES 8 A 335 ASP THR SER SER SER ILE ASN PHE LEU THR ARG VAL SER
SEQRES 9 A 335 GLY ILE GLY PRO SER ALA ALA ARG LYS PHE VAL ASP GLU
SEQRES 10 A 335 GLY ILE LYS THR LEU GLU ASP LEU ARG LYS ASN GLU ASP
SEQRES 11 A 335 LYS LEU ASN HIS HIS GLN ARG ILE GLY LEU LYS TYR PHE
SEQRES 12 A 335 GLY ASP PHE GLU LYS ARG ILE PRO ARG GLU GLU MET LEU
SEQRES 13 A 335 GLN MET GLN ASP ILE VAL LEU ASN GLU VAL LYS LYS VAL
SEQRES 14 A 335 ASP SER GLU TYR ILE ALA THR VAL CYS GLY SER PHE ARG
SEQRES 15 A 335 ARG GLY ALA GLU SER SER GLY ASP MET ASP VAL LEU LEU
SEQRES 16 A 335 THR HIS PRO SER PHE THR SER GLU SER THR LYS GLN PRO
SEQRES 17 A 335 LYS LEU LEU HIS GLN VAL VAL GLU GLN LEU GLN LYS VAL
SEQRES 18 A 335 HIS PHE ILE THR ASP THR LEU SER LYS GLY GLU THR LYS
SEQRES 19 A 335 PHE MET GLY VAL CYS GLN LEU PRO SER LYS ASN ASP GLU
SEQRES 20 A 335 LYS GLU TYR PRO HIS ARG ARG ILE ASP ILE ARG LEU ILE
SEQRES 21 A 335 PRO LYS ASP GLN TYR TYR CYS GLY VAL LEU TYR PHE THR
SEQRES 22 A 335 GLY SER ASP ILE PHE ASN LYS ASN MET ARG ALA HIS ALA
SEQRES 23 A 335 LEU GLU LYS GLY PHE THR ILE ASN GLU TYR THR ILE ARG
SEQRES 24 A 335 PRO LEU GLY VAL THR GLY VAL ALA GLY GLU PRO LEU PRO
SEQRES 25 A 335 VAL ASP SER GLU LYS ASP ILE PHE ASP TYR ILE GLN TRP
SEQRES 26 A 335 LYS TYR ARG GLU PRO LYS ASP ARG SER GLU
MODRES 3RH4 DDG P 10 DG
HET DDG P 10 21
HET MN P 345 1
HET MN D 344 1
HET MN A 339 1
HET MN A 340 1
HET MN A 341 1
HET MN A 342 1
HET MN A 343 1
HET MN A 346 1
HET NA A 351 1
HET NA A 352 1
HET CL A 353 1
HET CL A 354 1
HET CL A 355 1
HET CL A 356 1
HET CL A 357 1
HET CL A 358 1
HET CTP A 338 29
HET CTP A 350 29
HETNAM DDG 2',3'-DIDEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETNAM MN MANGANESE (II) ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM CTP CYTIDINE-5'-TRIPHOSPHATE
FORMUL 2 DDG C10 H14 N5 O6 P
FORMUL 5 MN 8(MN 2+)
FORMUL 13 NA 2(NA 1+)
FORMUL 15 CL 6(CL 1-)
FORMUL 21 CTP 2(C9 H16 N3 O14 P3)
FORMUL 23 HOH *450(H2 O)
HELIX 1 1 ASN A 12 VAL A 29 1 18
HELIX 2 2 ALA A 32 TYR A 49 1 18
HELIX 3 3 SER A 55 LYS A 61 1 7
HELIX 4 4 GLY A 66 GLY A 80 1 15
HELIX 5 5 LEU A 82 ASP A 91 1 10
HELIX 6 6 ASP A 91 THR A 101 1 11
HELIX 7 7 GLY A 107 GLU A 117 1 11
HELIX 8 8 THR A 121 LYS A 127 1 7
HELIX 9 9 ASN A 128 LEU A 132 5 5
HELIX 10 10 ASN A 133 TYR A 142 1 10
HELIX 11 11 TYR A 142 GLU A 147 1 6
HELIX 12 12 ARG A 152 ASP A 170 1 19
HELIX 13 13 CYS A 178 ARG A 183 1 6
HELIX 14 14 LYS A 209 VAL A 221 1 13
HELIX 15 15 PRO A 261 ASP A 263 5 3
HELIX 16 16 GLN A 264 GLY A 274 1 11
HELIX 17 17 SER A 275 LYS A 289 1 15
HELIX 18 18 SER A 315 ILE A 323 1 9
HELIX 19 19 GLU A 329 ARG A 333 5 5
SHEET 1 A 2 ILE A 150 PRO A 151 0
SHEET 2 A 2 SER A 187 SER A 188 -1 O SER A 188 N ILE A 150
SHEET 1 B 5 ILE A 174 VAL A 177 0
SHEET 2 B 5 MET A 191 THR A 196 -1 O LEU A 194 N THR A 176
SHEET 3 B 5 ARG A 253 LEU A 259 1 O ASP A 256 N VAL A 193
SHEET 4 B 5 LYS A 234 CYS A 239 -1 N CYS A 239 O ARG A 253
SHEET 5 B 5 ILE A 224 LYS A 230 -1 N LEU A 228 O MET A 236
SHEET 1 C 2 PHE A 291 ILE A 293 0
SHEET 2 C 2 ILE A 298 PRO A 300 -1 O ARG A 299 N THR A 292
LINK O3' DG P 9 P DDG P 10 1555 1555 1.60
LINK N7 DG P 9 MN MN P 345 1555 1555 2.37
LINK OP1 DG P 9 NA NA A 351 1555 1555 2.49
LINK O HOH P 11 MN MN A 340 1555 1555 2.37
LINK O HOH P 128 MN MN P 345 1555 1555 2.65
LINK O HOH P 130 NA NA A 351 1555 1555 2.72
LINK O HOH P 213 MN MN P 345 1555 1555 2.47
LINK OP1 DC D 3 NA NA A 352 1555 1555 2.71
LINK N7 DG D 4 MN MN D 344 1555 1555 2.58
LINK O HOH D 93 NA NA A 352 1555 1555 2.88
LINK O LYS A 60 NA NA A 352 1555 1555 2.50
LINK O LEU A 62 NA NA A 352 1555 1555 2.60
LINK O VAL A 65 NA NA A 352 1555 1555 2.54
LINK O THR A 101 NA NA A 351 1555 1555 2.52
LINK O VAL A 103 NA NA A 351 1555 1555 2.63
LINK O ILE A 106 NA NA A 351 1555 1555 2.63
LINK OD2 ASP A 145 MN MN A 341 1555 1555 2.26
LINK OD1 ASP A 190 MN MN A 339 1555 1555 2.13
LINK OD2 ASP A 190 MN MN A 340 1555 1555 2.18
LINK OD2 ASP A 192 MN MN A 339 1555 1555 2.14
LINK OD1 ASP A 192 MN MN A 340 1555 1555 2.17
LINK ND1 HIS A 252 MN MN A 341 1555 1555 2.45
LINK OD2 ASP A 256 MN MN A 340 1555 1555 2.21
LINK ND1 HIS A 285 MN MN A 342 1555 1555 2.49
LINK O2B CTP A 338 MN MN A 339 1555 1555 2.09
LINK O1G CTP A 338 MN MN A 339 1555 1555 2.17
LINK O1A CTP A 338 MN MN A 339 1555 1555 2.29
LINK O1A CTP A 338 MN MN A 340 1555 1555 2.27
LINK O2G CTP A 338 MN MN A 346 1555 1555 2.37
LINK MN MN A 339 O HOH A 403 1555 1555 2.27
LINK MN MN A 341 O HOH A 552 1555 1555 2.43
LINK MN MN A 341 O HOH A 553 1555 1555 2.61
LINK MN MN A 341 O HOH A 555 1555 1555 2.31
LINK MN MN A 342 O HOH A 413 1555 1555 2.44
LINK MN MN A 343 O3G CTP A 350 1555 1555 2.31
LINK MN MN A 343 O1B CTP A 350 1555 1555 2.40
LINK MN MN A 343 O1A CTP A 350 1555 1555 2.42
LINK MN MN A 346 O HOH A 644 1555 1555 2.25
LINK NA NA A 351 O HOH A 572 1555 1555 2.90
LINK NA NA A 352 O HOH A 585 1555 1555 2.87
CISPEP 1 GLY A 274 SER A 275 0 6.16
SITE 1 AC1 4 HOH A 602 DG P 9 HOH P 128 HOH P 213
SITE 1 AC2 2 DG D 4 DG D 5
SITE 1 AC3 5 ASP A 190 ASP A 192 CTP A 338 MN A 340
SITE 2 AC3 5 HOH A 403
SITE 1 AC4 6 ASP A 190 ASP A 192 ASP A 256 CTP A 338
SITE 2 AC4 6 MN A 339 HOH P 11
SITE 1 AC5 6 ASP A 145 HIS A 252 HOH A 552 HOH A 553
SITE 2 AC5 6 HOH A 555 HOH D 155
SITE 1 AC6 3 HIS A 285 GLU A 288 HOH A 413
SITE 1 AC7 1 CTP A 350
SITE 1 AC8 3 CTP A 338 HOH A 442 HOH A 644
SITE 1 AC9 6 THR A 101 VAL A 103 ILE A 106 HOH A 572
SITE 2 AC9 6 DG P 9 HOH P 130
SITE 1 BC1 6 LYS A 60 LEU A 62 VAL A 65 HOH A 585
SITE 2 BC1 6 DC D 3 HOH D 93
SITE 1 BC2 2 ASN A 294 THR A 297
SITE 1 BC3 4 ALA A 32 ILE A 33 HIS A 34 LYS A 35
SITE 1 BC4 3 LEU A 82 GLU A 86 ARG A 89
SITE 1 BC5 2 PRO A 330 LYS A 331
SITE 1 BC6 2 GLN A 159 VAL A 177
SITE 1 BC7 2 LYS A 84 HOH A 633
SITE 1 BC8 24 GLY A 179 SER A 180 ARG A 183 GLY A 189
SITE 2 BC8 24 ASP A 190 ASP A 192 TYR A 271 PHE A 272
SITE 3 BC8 24 THR A 273 GLY A 274 ASP A 276 ASN A 279
SITE 4 BC8 24 MN A 339 MN A 340 MN A 346 HOH A 379
SITE 5 BC8 24 HOH A 383 HOH A 403 HOH A 442 HOH A 644
SITE 6 BC8 24 DDG P 10 HOH P 11 HOH P 66 DG T 6
SITE 1 BC9 11 ILE A 174 THR A 176 THR A 196 LYS A 262
SITE 2 BC9 11 TYR A 265 TYR A 266 MN A 343 HOH A 409
SITE 3 BC9 11 HOH A 423 HOH A 581 HOH A 591
CRYST1 51.170 79.790 55.000 90.00 107.95 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019543 0.000000 0.006331 0.00000
SCALE2 0.000000 0.012533 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019112 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
