HEADER TRANSFERASE/DNA 05-JAN-04 1S10
TITLE SNAPSHOTS OF REPLICATION THROUGH AN ABASIC LESION: STRUCTURAL BASIS
TITLE 2 FOR BASE SUBSTITUTION AND FRAMESHIFT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*GP*GP*GP*GP*GP*AP*AP*GP*GP*AP*CP*TP*A)-3';
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-D(*TP*CP*AP*GP*TP*AP*GP*TP*CP*CP*TP*TP*CP*CP*CP*CP*C)-
COMPND 7 3';
COMPND 8 CHAIN: C;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: DNA POLYMERASE IV;
COMPND 12 CHAIN: A;
COMPND 13 SYNONYM: POL IV;
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: SULFOLOBUS SOLFATARICUS;
SOURCE 7 ORGANISM_TAXID: 273057;
SOURCE 8 STRAIN: P2;
SOURCE 9 GENE: DPO4;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ABAIC LESION, LESION BYPASS, POLYMERASE, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LING,F.BOUDSOCQ,R.WOODGATE,W.YANG
REVDAT 5 23-AUG-23 1S10 1 REMARK LINK
REVDAT 4 04-APR-18 1S10 1 REMARK
REVDAT 3 13-JUL-11 1S10 1 VERSN
REVDAT 2 24-FEB-09 1S10 1 VERSN
REVDAT 1 30-MAR-04 1S10 0
JRNL AUTH H.LING,F.BOUDSOCQ,R.WOODGATE,W.YANG
JRNL TITL SNAPSHOTS OF REPLICATION THROUGH AN ABASIC LESION;
JRNL TITL 2 STRUCTURAL BASIS FOR BASE SUBSTITUTIONS AND FRAMESHIFTS.
JRNL REF MOL.CELL V. 13 751 2004
JRNL REFN ISSN 1097-2765
JRNL PMID 15023344
JRNL DOI 10.1016/S1097-2765(04)00101-7
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 30778
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 915
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 : 2743
REMARK 3 NUCLEIC ACID ATOMS : 600
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 333
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) : -4.62200
REMARK 3 B22 (A**2) : 1.76900
REMARK 3 B33 (A**2) : 2.85300
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 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) : 1.660
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.447 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.254 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.260 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.438 ; 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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : DCP_COMB.PARAM
REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021230.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30778
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1JX4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, CA(AC)2, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 49.19750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.33200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.19750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.33200
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 APPLY THE FOLLOWING TO CHAINS: B, C, 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 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 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 DT C1906 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT C1906 C7 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 OE2 GLU A 63 O HOH A 894 2.09
REMARK 500 OD2 ASP A 105 O HOH A 970 2.13
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 B1805 O3' DG B1805 C3' -0.049
REMARK 500 DC C1915 O3' DC C1915 C3' -0.044
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 B1803 O5' - P - OP1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 DG B1808 O3' - P - OP2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 DG B1809 O3' - P - OP2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 DA B1810 O3' - P - OP2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 DA B1813 O3' - P - OP2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 DA B1813 C3' - C2' - C1' ANGL. DEV. = -6.5 DEGREES
REMARK 500 DA B1813 N9 - C1' - C2' ANGL. DEV. = 10.3 DEGREES
REMARK 500 DA B1813 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DA C1904 O3' - P - OP2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 DG C1905 O3' - P - OP1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 DA C1907 O3' - P - OP2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 DG C1908 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT C1909 O3' - P - OP2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 DC C1910 O3' - P - OP2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 DT C1912 O3' - P - OP2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 DC C1914 O3' - P - OP2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 DC C1914 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC C1915 O3' - P - OP2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 DC C1915 O4' - C1' - N1 ANGL. DEV. = 2.2 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 TYR A 10 54.71 19.69
REMARK 500 ARG A 77 71.03 -119.50
REMARK 500 SER A 96 132.13 -175.11
REMARK 500 SER A 145 -168.49 -163.31
REMARK 500 ASN A 161 57.75 38.31
REMARK 500 ASP A 277 83.56 36.47
REMARK 500 LYS A 278 -24.48 85.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DA B1813 0.06 SIDE CHAIN
REMARK 500 DG C1905 0.05 SIDE CHAIN
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 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 7 OD1
REMARK 620 2 ASP A 7 OD2 44.0
REMARK 620 3 ASP A 105 OD1 90.3 131.2
REMARK 620 4 ASP A 105 OD2 55.4 99.3 41.4
REMARK 620 5 GLU A 106 OE1 120.6 95.8 95.6 130.4
REMARK 620 6 DCP A 804 O1A 76.5 94.1 89.1 62.1 162.1
REMARK 620 7 HOH A 829 O 153.9 161.8 66.4 98.5 75.3 90.9
REMARK 620 8 HOH A 831 O 101.0 62.1 166.3 142.9 85.3 86.1 100.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 7 OD1
REMARK 620 2 PHE A 8 O 96.1
REMARK 620 3 ASP A 105 OD2 82.9 85.4
REMARK 620 4 DCP A 804 O1A 98.3 162.5 86.6
REMARK 620 5 DCP A 804 O1G 107.9 104.4 164.2 80.5
REMARK 620 6 DCP A 804 O2B 172.5 89.0 92.1 75.7 75.9
REMARK 620 7 HOH A 970 O 123.8 78.2 41.1 85.5 127.9 52.0
REMARK 620 8 HOH A 971 O 65.3 68.9 135.5 126.5 60.3 121.8 146.9
REMARK 620 N 1 2 3 4 5 6 7
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 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCP A 804
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JX4 RELATED DB: PDB
REMARK 900 RELATED ID: 1RYR RELATED DB: PDB
REMARK 900 RELATED ID: 1RYS RELATED DB: PDB
REMARK 900 RELATED ID: 1S0M RELATED DB: PDB
REMARK 900 RELATED ID: 1S0N RELATED DB: PDB
REMARK 900 RELATED ID: 1S0O RELATED DB: PDB
DBREF 1S10 A 1 352 UNP Q97W02 DPO42_SULSO 1 352
DBREF 1S10 B 1801 1813 PDB 1S10 1S10 1801 1813
DBREF 1S10 C 1902 1918 PDB 1S10 1S10 1902 1918
SEQRES 1 B 13 DG DG DG DG DG DA DA DG DG DA DC DT DA
SEQRES 1 C 17 DT DC DA DG DT DA DG DT DC DC DT DT DC
SEQRES 2 C 17 DC DC DC DC
SEQRES 1 A 352 MET ILE VAL LEU PHE VAL ASP PHE ASP TYR PHE TYR ALA
SEQRES 2 A 352 GLN VAL GLU GLU VAL LEU ASN PRO SER LEU LYS GLY LYS
SEQRES 3 A 352 PRO VAL VAL VAL CYS VAL PHE SER GLY ARG PHE GLU ASP
SEQRES 4 A 352 SER GLY ALA VAL ALA THR ALA ASN TYR GLU ALA ARG LYS
SEQRES 5 A 352 PHE GLY VAL LYS ALA GLY ILE PRO ILE VAL GLU ALA LYS
SEQRES 6 A 352 LYS ILE LEU PRO ASN ALA VAL TYR LEU PRO MET ARG LYS
SEQRES 7 A 352 GLU VAL TYR GLN GLN VAL SER SER ARG ILE MET ASN LEU
SEQRES 8 A 352 LEU ARG GLU TYR SER GLU LYS ILE GLU ILE ALA SER ILE
SEQRES 9 A 352 ASP GLU ALA TYR LEU ASP ILE SER ASP LYS VAL ARG ASP
SEQRES 10 A 352 TYR ARG GLU ALA TYR ASN LEU GLY LEU GLU ILE LYS ASN
SEQRES 11 A 352 LYS ILE LEU GLU LYS GLU LYS ILE THR VAL THR VAL GLY
SEQRES 12 A 352 ILE SER LYS ASN LYS VAL PHE ALA LYS ILE ALA ALA ASP
SEQRES 13 A 352 MET ALA LYS PRO ASN GLY ILE LYS VAL ILE ASP ASP GLU
SEQRES 14 A 352 GLU VAL LYS ARG LEU ILE ARG GLU LEU ASP ILE ALA ASP
SEQRES 15 A 352 VAL PRO GLY ILE GLY ASN ILE THR ALA GLU LYS LEU LYS
SEQRES 16 A 352 LYS LEU GLY ILE ASN LYS LEU VAL ASP THR LEU SER ILE
SEQRES 17 A 352 GLU PHE ASP LYS LEU LYS GLY MET ILE GLY GLU ALA LYS
SEQRES 18 A 352 ALA LYS TYR LEU ILE SER LEU ALA ARG ASP GLU TYR ASN
SEQRES 19 A 352 GLU PRO ILE ARG THR ARG VAL ARG LYS SER ILE GLY ARG
SEQRES 20 A 352 ILE VAL THR MET LYS ARG ASN SER ARG ASN LEU GLU GLU
SEQRES 21 A 352 ILE LYS PRO TYR LEU PHE ARG ALA ILE GLU GLU SER TYR
SEQRES 22 A 352 TYR LYS LEU ASP LYS ARG ILE PRO LYS ALA ILE HIS VAL
SEQRES 23 A 352 VAL ALA VAL THR GLU ASP LEU ASP ILE VAL SER ARG GLY
SEQRES 24 A 352 ARG THR PHE PRO HIS GLY ILE SER LYS GLU THR ALA TYR
SEQRES 25 A 352 SER GLU SER VAL LYS LEU LEU GLN LYS ILE LEU GLU GLU
SEQRES 26 A 352 ASP GLU ARG LYS ILE ARG ARG ILE GLY VAL ARG PHE SER
SEQRES 27 A 352 LYS PHE ILE GLU ALA ILE GLY LEU ASP LYS PHE PHE ASP
SEQRES 28 A 352 THR
HET CA A 403 1
HET CA A 404 1
HET DCP A 804 28
HETNAM CA CALCIUM ION
HETNAM DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE
FORMUL 4 CA 2(CA 2+)
FORMUL 6 DCP C9 H16 N3 O13 P3
FORMUL 7 HOH *333(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 GLU A 94 SER A 96 5 3
HELIX 7 7 ASP A 117 LYS A 137 1 21
HELIX 8 8 ASN A 147 LYS A 159 1 13
HELIX 9 9 ASP A 167 LEU A 178 1 12
HELIX 10 10 ASP A 179 VAL A 183 5 5
HELIX 11 11 GLY A 187 LYS A 196 1 10
HELIX 12 12 LYS A 201 SER A 207 5 7
HELIX 13 13 GLU A 209 GLY A 218 1 10
HELIX 14 14 GLY A 218 ARG A 230 1 13
HELIX 15 15 ASN A 257 ASP A 277 1 21
HELIX 16 16 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 32 O ALA A 42
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 ARG A 298 N VAL A 286
LINK OD1 ASP A 7 CA CA A 403 1555 1555 2.92
LINK OD2 ASP A 7 CA CA A 403 1555 1555 2.92
LINK OD1 ASP A 7 CA CA A 404 1555 1555 2.21
LINK O PHE A 8 CA CA A 404 1555 1555 2.22
LINK OD1 ASP A 105 CA CA A 403 1555 1555 2.64
LINK OD2 ASP A 105 CA CA A 403 1555 1555 3.31
LINK OD2 ASP A 105 CA CA A 404 1555 1555 2.19
LINK OE1 GLU A 106 CA CA A 403 1555 1555 2.67
LINK CA CA A 403 O1A DCP A 804 1555 1555 2.71
LINK CA CA A 403 O HOH A 829 1555 1555 2.78
LINK CA CA A 403 O HOH A 831 1555 1555 2.32
LINK CA CA A 404 O1A DCP A 804 1555 1555 2.39
LINK CA CA A 404 O1G DCP A 804 1555 1555 2.37
LINK CA CA A 404 O2B DCP A 804 1555 1555 2.33
LINK CA CA A 404 O HOH A 970 1555 1555 3.22
LINK CA CA A 404 O HOH A 971 1555 1555 3.07
CISPEP 1 LYS A 159 PRO A 160 0 1.65
SITE 1 AC1 7 ASP A 7 ASP A 105 GLU A 106 CA A 404
SITE 2 AC1 7 DCP A 804 HOH A 829 HOH A 831
SITE 1 AC2 6 ASP A 7 PHE A 8 ASP A 105 CA A 403
SITE 2 AC2 6 DCP A 804 HOH A 971
SITE 1 AC3 23 ASP A 7 PHE A 8 TYR A 10 PHE A 11
SITE 2 AC3 23 TYR A 12 ALA A 44 THR A 45 TYR A 48
SITE 3 AC3 23 ARG A 51 MET A 76 ASP A 105 LYS A 159
SITE 4 AC3 23 CA A 403 CA A 404 HOH A 836 HOH A 843
SITE 5 AC3 23 HOH A 877 HOH A 904 HOH A 970 HOH A 971
SITE 6 AC3 23 HOH A 989 DA B1813 DG C1905
CRYST1 98.395 102.664 52.340 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 0.010163 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009741 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019106 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
