HEADER TRANSFERASE/DNA 04-MAR-11 3QZ8
TITLE TT-4 TERNARY COMPLEX OF DPO4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE IV;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DPO4, Y-FAMILY DNA POLYMERASE, POL IV;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 5'-D(*GP*GP*CP*AP*CP*TP*GP*AP*TP*CP*AP*GP*G)-3';
COMPND 9 CHAIN: P;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: PRIMER DNA STRAND;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: 5'-D(*TP*TP*AP*CP*GP*CP*CP*TP*TP*GP*AP*TP*CP*AP*GP*TP*GP*CP
COMPND 14 *C)-3';
COMPND 15 CHAIN: T;
COMPND 16 ENGINEERED: YES;
COMPND 17 OTHER_DETAILS: TEMPLATE DNA STRAND
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 STRAIN: P2;
SOURCE 5 GENE: DBH, DPO4, SSO2448;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BLR(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKKT7;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES
KEYWDS LESION BYPASS, SINGLE-BASE DELETION, -1 FRAMESHIFT, REPLICATION-DNA
KEYWDS 2 COMPLEX, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.PATA,Y.WU,R.C.WILSON
REVDAT 3 13-SEP-23 3QZ8 1 REMARK SEQADV LINK
REVDAT 2 11-MAY-11 3QZ8 1 JRNL
REVDAT 1 06-APR-11 3QZ8 0
JRNL AUTH Y.WU,R.C.WILSON,J.D.PATA
JRNL TITL THE Y-FAMILY DNA POLYMERASE DPO4 USES A TEMPLATE SLIPPAGE
JRNL TITL 2 MECHANISM TO CREATE SINGLE-BASE DELETIONS.
JRNL REF J.BACTERIOL. V. 193 2630 2011
JRNL REFN ISSN 0021-9193
JRNL PMID 21421759
JRNL DOI 10.1128/JB.00012-11
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 33611
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1670
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 24.6812 - 4.5684 0.99 3101 154 0.1854 0.1893
REMARK 3 2 4.5684 - 3.6298 1.00 2986 153 0.1609 0.2144
REMARK 3 3 3.6298 - 3.1721 1.00 2953 144 0.2058 0.2539
REMARK 3 4 3.1721 - 2.8825 0.99 2903 156 0.2178 0.2837
REMARK 3 5 2.8825 - 2.6762 0.98 2820 193 0.2332 0.2837
REMARK 3 6 2.6762 - 2.5186 0.98 2852 143 0.2285 0.2662
REMARK 3 7 2.5186 - 2.3925 0.96 2769 143 0.2293 0.2710
REMARK 3 8 2.3925 - 2.2885 0.95 2753 152 0.2213 0.2475
REMARK 3 9 2.2885 - 2.2004 0.92 2647 145 0.2218 0.2781
REMARK 3 10 2.2004 - 2.1245 0.86 2502 113 0.2362 0.2399
REMARK 3 11 2.1245 - 2.0581 0.73 2123 95 0.2547 0.3087
REMARK 3 12 2.0581 - 1.9993 0.53 1532 79 0.2745 0.3983
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.65
REMARK 3 K_SOL : 0.41
REMARK 3 B_SOL : 40.11
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.720
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) : 8.68730
REMARK 3 B22 (A**2) : -3.75250
REMARK 3 B33 (A**2) : -4.93470
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 3461
REMARK 3 ANGLE : 1.577 4782
REMARK 3 CHIRALITY : 0.190 544
REMARK 3 PLANARITY : 0.005 501
REMARK 3 DIHEDRAL : 18.763 1373
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 3QZ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064289.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.04
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35093
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.999
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 (%) : 94.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.46900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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 1JX4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 100 MM MES-TRIS, 100 MM
REMARK 280 CALCIUM ACETATE, 2.5% GLYCEROL, PH 6.04, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 49.45300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.34700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.45300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.34700
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLU A 342
REMARK 465 ALA A 343
REMARK 465 ILE A 344
REMARK 465 GLY A 345
REMARK 465 LEU A 346
REMARK 465 ASP A 347
REMARK 465 LYS A 348
REMARK 465 PHE A 349
REMARK 465 PHE A 350
REMARK 465 ASP A 351
REMARK 465 THR A 352
REMARK 465 GLY A 353
REMARK 465 GLY A 354
REMARK 465 HIS A 355
REMARK 465 HIS A 356
REMARK 465 HIS A 357
REMARK 465 HIS A 358
REMARK 465 HIS A 359
REMARK 465 HIS A 360
REMARK 465 DT T 1
REMARK 465 DT T 2
REMARK 465 DA T 3
REMARK 465 DC T 4
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 432 O HOH A 455 1.85
REMARK 500 O HOH A 482 O HOH P 162 1.93
REMARK 500 O HOH T 103 O HOH T 136 1.94
REMARK 500 O HOH T 131 O HOH T 136 2.15
REMARK 500 O HOH A 446 O HOH A 447 2.17
REMARK 500 O HOH A 473 O HOH P 156 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 481 O HOH P 72 3546 2.10
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 P 1 O4' - C1' - N9 ANGL. DEV. = -4.3 DEGREES
REMARK 500 DC P 5 C1' - O4' - C4' ANGL. DEV. = -6.4 DEGREES
REMARK 500 DT P 9 O4' - C1' - N1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 DG P 12 O4' - C1' - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DG T 5 O4' - C1' - N9 ANGL. DEV. = -4.2 DEGREES
REMARK 500 DT T 9 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DG T 10 O5' - C5' - C4' ANGL. DEV. = -11.0 DEGREES
REMARK 500 DG T 10 O4' - C4' - C3' ANGL. DEV. = 3.8 DEGREES
REMARK 500 DT T 16 O4' - C4' - C3' ANGL. DEV. = -3.5 DEGREES
REMARK 500 DT T 16 O4' - C1' - N1 ANGL. DEV. = 5.9 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 TYR A 10 55.14 25.75
REMARK 500 ARG A 77 74.88 -119.97
REMARK 500 SER A 96 137.01 -175.59
REMARK 500 SER A 103 -171.21 -174.11
REMARK 500 SER A 145 -163.71 -166.26
REMARK 500 ASP A 277 -108.53 59.45
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 361 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 7 OD1
REMARK 620 2 PHE A 8 O 91.5
REMARK 620 3 ASP A 105 OD2 86.9 82.4
REMARK 620 4 DCP A 364 O1B 174.1 93.1 90.1
REMARK 620 5 DCP A 364 O2A 101.0 161.1 84.1 73.7
REMARK 620 6 DCP A 364 O1G 103.6 107.6 165.0 78.5 83.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 362 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 7 OD1
REMARK 620 2 ASP A 105 OD1 93.5
REMARK 620 3 DCP A 364 O2A 80.5 95.2
REMARK 620 4 HOH A 432 O 90.6 163.6 101.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 363 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 181 O
REMARK 620 2 ILE A 186 O 92.8
REMARK 620 3 HOH A 399 O 85.5 71.7
REMARK 620 4 HOH A 456 O 94.7 138.0 67.8
REMARK 620 5 HOH A 462 O 95.4 73.9 145.7 145.7
REMARK 620 6 HOH P 133 O 175.8 87.6 90.7 82.1 88.8
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 CA A 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 363
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCP A 364
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QZ7 RELATED DB: PDB
REMARK 900 T-3 TERNARY COMPLEX OF DPO4
DBREF 3QZ8 A 1 352 UNP Q97W02 DPO42_SULSO 1 352
DBREF 3QZ8 P 1 13 PDB 3QZ8 3QZ8 1 13
DBREF 3QZ8 T 1 19 PDB 3QZ8 3QZ8 1 19
SEQADV 3QZ8 GLY A 353 UNP Q97W02 EXPRESSION TAG
SEQADV 3QZ8 GLY A 354 UNP Q97W02 EXPRESSION TAG
SEQADV 3QZ8 HIS A 355 UNP Q97W02 EXPRESSION TAG
SEQADV 3QZ8 HIS A 356 UNP Q97W02 EXPRESSION TAG
SEQADV 3QZ8 HIS A 357 UNP Q97W02 EXPRESSION TAG
SEQADV 3QZ8 HIS A 358 UNP Q97W02 EXPRESSION TAG
SEQADV 3QZ8 HIS A 359 UNP Q97W02 EXPRESSION TAG
SEQADV 3QZ8 HIS A 360 UNP Q97W02 EXPRESSION TAG
SEQRES 1 A 360 MET ILE VAL LEU PHE VAL ASP PHE ASP TYR PHE TYR ALA
SEQRES 2 A 360 GLN VAL GLU GLU VAL LEU ASN PRO SER LEU LYS GLY LYS
SEQRES 3 A 360 PRO VAL VAL VAL CYS VAL PHE SER GLY ARG PHE GLU ASP
SEQRES 4 A 360 SER GLY ALA VAL ALA THR ALA ASN TYR GLU ALA ARG LYS
SEQRES 5 A 360 PHE GLY VAL LYS ALA GLY ILE PRO ILE VAL GLU ALA LYS
SEQRES 6 A 360 LYS ILE LEU PRO ASN ALA VAL TYR LEU PRO MET ARG LYS
SEQRES 7 A 360 GLU VAL TYR GLN GLN VAL SER SER ARG ILE MET ASN LEU
SEQRES 8 A 360 LEU ARG GLU TYR SER GLU LYS ILE GLU ILE ALA SER ILE
SEQRES 9 A 360 ASP GLU ALA TYR LEU ASP ILE SER ASP LYS VAL ARG ASP
SEQRES 10 A 360 TYR ARG GLU ALA TYR ASN LEU GLY LEU GLU ILE LYS ASN
SEQRES 11 A 360 LYS ILE LEU GLU LYS GLU LYS ILE THR VAL THR VAL GLY
SEQRES 12 A 360 ILE SER LYS ASN LYS VAL PHE ALA LYS ILE ALA ALA ASP
SEQRES 13 A 360 MET ALA LYS PRO ASN GLY ILE LYS VAL ILE ASP ASP GLU
SEQRES 14 A 360 GLU VAL LYS ARG LEU ILE ARG GLU LEU ASP ILE ALA ASP
SEQRES 15 A 360 VAL PRO GLY ILE GLY ASN ILE THR ALA GLU LYS LEU LYS
SEQRES 16 A 360 LYS LEU GLY ILE ASN LYS LEU VAL ASP THR LEU SER ILE
SEQRES 17 A 360 GLU PHE ASP LYS LEU LYS GLY MET ILE GLY GLU ALA LYS
SEQRES 18 A 360 ALA LYS TYR LEU ILE SER LEU ALA ARG ASP GLU TYR ASN
SEQRES 19 A 360 GLU PRO ILE ARG THR ARG VAL ARG LYS SER ILE GLY ARG
SEQRES 20 A 360 ILE VAL THR MET LYS ARG ASN SER ARG ASN LEU GLU GLU
SEQRES 21 A 360 ILE LYS PRO TYR LEU PHE ARG ALA ILE GLU GLU SER TYR
SEQRES 22 A 360 TYR LYS LEU ASP LYS ARG ILE PRO LYS ALA ILE HIS VAL
SEQRES 23 A 360 VAL ALA VAL THR GLU ASP LEU ASP ILE VAL SER ARG GLY
SEQRES 24 A 360 ARG THR PHE PRO HIS GLY ILE SER LYS GLU THR ALA TYR
SEQRES 25 A 360 SER GLU SER VAL LYS LEU LEU GLN LYS ILE LEU GLU GLU
SEQRES 26 A 360 ASP GLU ARG LYS ILE ARG ARG ILE GLY VAL ARG PHE SER
SEQRES 27 A 360 LYS PHE ILE GLU ALA ILE GLY LEU ASP LYS PHE PHE ASP
SEQRES 28 A 360 THR GLY GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 P 13 DG DG DC DA DC DT DG DA DT DC DA DG DG
SEQRES 1 T 19 DT DT DA DC DG DC DC DT DT DG DA DT DC
SEQRES 2 T 19 DA DG DT DG DC DC
HET CA A 361 1
HET CA A 362 1
HET CA A 363 1
HET DCP A 364 40
HETNAM CA CALCIUM ION
HETNAM DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE
FORMUL 4 CA 3(CA 2+)
FORMUL 7 DCP C9 H16 N3 O13 P3
FORMUL 8 HOH *167(H2 O)
HELIX 1 1 TYR A 10 ASN A 20 1 11
HELIX 2 2 PRO A 21 LYS A 24 5 4
HELIX 3 3 ASN A 47 LYS A 52 1 6
HELIX 4 4 PRO A 60 LEU A 68 1 9
HELIX 5 5 ARG A 77 ARG A 93 1 17
HELIX 6 6 ASP A 117 LYS A 137 1 21
HELIX 7 7 ASN A 147 LYS A 159 1 13
HELIX 8 8 ASP A 167 LEU A 178 1 12
HELIX 9 9 ASP A 179 VAL A 183 5 5
HELIX 10 10 GLY A 187 LYS A 196 1 10
HELIX 11 11 VAL A 203 ILE A 208 1 6
HELIX 12 12 GLU A 209 GLY A 218 1 10
HELIX 13 13 GLY A 218 ARG A 230 1 13
HELIX 14 14 ASN A 257 ASP A 277 1 21
HELIX 15 15 SER A 307 ASP A 326 1 20
SHEET 1 A 5 ILE A 99 SER A 103 0
SHEET 2 A 5 GLU A 106 ASP A 110 -1 O TYR A 108 N GLU A 100
SHEET 3 A 5 VAL A 3 PHE A 8 -1 N LEU A 4 O LEU A 109
SHEET 4 A 5 VAL A 140 SER A 145 -1 O GLY A 143 N PHE A 5
SHEET 5 A 5 ILE A 163 VAL A 165 1 O LYS A 164 N ILE A 144
SHEET 1 B 3 GLY A 41 ALA A 46 0
SHEET 2 B 3 VAL A 28 PHE A 33 -1 N VAL A 30 O ALA A 44
SHEET 3 B 3 VAL A 72 PRO A 75 1 O LEU A 74 N CYS A 31
SHEET 1 C 4 SER A 244 SER A 255 0
SHEET 2 C 4 ILE A 330 PHE A 340 -1 O PHE A 337 N ILE A 245
SHEET 3 C 4 PRO A 281 THR A 290 -1 N VAL A 289 O ARG A 331
SHEET 4 C 4 ILE A 295 THR A 301 -1 O VAL A 296 N ALA A 288
LINK OD1 ASP A 7 CA CA A 361 1555 1555 2.27
LINK OD1 ASP A 7 CA CA A 362 1555 1555 3.02
LINK O PHE A 8 CA CA A 361 1555 1555 2.25
LINK OD2 ASP A 105 CA CA A 361 1555 1555 2.26
LINK OD1 ASP A 105 CA CA A 362 1555 1555 2.57
LINK O ALA A 181 CA CA A 363 1555 1555 2.26
LINK O ILE A 186 CA CA A 363 1555 1555 2.51
LINK CA CA A 361 O1B DCP A 364 1555 1555 2.22
LINK CA CA A 361 O2A DCP A 364 1555 1555 2.31
LINK CA CA A 361 O1G DCP A 364 1555 1555 2.35
LINK CA CA A 362 O2A DCP A 364 1555 1555 2.39
LINK CA CA A 362 O HOH A 432 1555 1555 2.47
LINK CA CA A 363 O HOH A 399 1555 1555 2.58
LINK CA CA A 363 O HOH A 456 1555 1555 2.82
LINK CA CA A 363 O HOH A 462 1555 1555 2.58
LINK CA CA A 363 O HOH P 133 1555 1555 2.55
CISPEP 1 LYS A 159 PRO A 160 0 -0.65
SITE 1 AC1 5 ASP A 7 PHE A 8 ASP A 105 CA A 362
SITE 2 AC1 5 DCP A 364
SITE 1 AC2 7 ASP A 7 ASP A 105 GLU A 106 CA A 361
SITE 2 AC2 7 DCP A 364 HOH A 432 DG P 13
SITE 1 AC3 6 ALA A 181 ILE A 186 HOH A 399 HOH A 456
SITE 2 AC3 6 HOH A 462 HOH P 133
SITE 1 AC4 18 ASP A 7 PHE A 8 ASP A 9 TYR A 10
SITE 2 AC4 18 PHE A 11 TYR A 12 ALA A 44 THR A 45
SITE 3 AC4 18 TYR A 48 ARG A 51 ASP A 105 LYS A 159
SITE 4 AC4 18 CA A 361 CA A 362 HOH A 378 HOH A 442
SITE 5 AC4 18 DG P 13 DG T 5
CRYST1 98.906 102.694 52.617 90.00 90.00 90.00 P 21 21 2 4
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 0.010111 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009738 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019005 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
