HEADER TRANSFERASE/ELECTRON TRANSPORT/DNA 10-JUN-05 1ZYQ
TITLE T7 DNA POLYMERASE IN COMPLEX WITH 8OG AND INCOMING DDATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*GP*AP*AP*AP*AP*CP*GP*AP*CP*GP*GP*CP*CP*AP*GP*TP*GP
COMPND 3 *CP*CP*AP*(DDG))-3';
COMPND 4 CHAIN: P;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: PRIMER STRAND;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 5'-D(*CP*CP*CP*(8OG)
COMPND 9 P*CP*TP*GP*GP*CP*AP*CP*TP*GP*GP*CP*CP*GP*TP*CP*GP*TP*TP*TP*TP*CP*G)-
COMPND 10 3';
COMPND 11 CHAIN: T;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: TEMPLATE STRAND;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA POLYMERASE;
COMPND 16 CHAIN: A;
COMPND 17 SYNONYM: T7 DNA POLYMERASE;
COMPND 18 EC: 2.7.7.7;
COMPND 19 ENGINEERED: YES;
COMPND 20 MUTATION: YES;
COMPND 21 MOL_ID: 4;
COMPND 22 MOLECULE: THIOREDOXIN 1;
COMPND 23 CHAIN: B;
COMPND 24 SYNONYM: TRX1, TRX;
COMPND 25 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: ENTEROBACTERIA PHAGE T7;
SOURCE 7 ORGANISM_TAXID: 10760;
SOURCE 8 GENE: 5;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 15 ORGANISM_TAXID: 562;
SOURCE 16 GENE: TRXA, FIPA, TSNC;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS 8OG, FIDELITY, TRANSFERASE-ELECTRON TRANSPORT-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.G.BRIEBA,R.J.KOKOSKA,K.BEBENEK,T.A.KUNKEL,T.ELLENBERGER
REVDAT 4 14-FEB-24 1ZYQ 1 REMARK
REVDAT 3 20-OCT-21 1ZYQ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1ZYQ 1 VERSN
REVDAT 1 22-NOV-05 1ZYQ 0
JRNL AUTH L.G.BRIEBA,R.J.KOKOSKA,K.BEBENEK,T.A.KUNKEL,T.ELLENBERGER
JRNL TITL A LYSINE RESIDUE IN THE FINGERS SUBDOMAIN OF T7 DNA
JRNL TITL 2 POLYMERASE MODULATES THE MISCODING POTENTIAL OF
JRNL TITL 3 8-OXO-7,8-DIHYDROGUANOSINE.
JRNL REF STRUCTURE V. 13 1653 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 16271888
JRNL DOI 10.1016/J.STR.2005.07.020
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1895166.730
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 32113
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1578
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4635
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 243
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6216
REMARK 3 NUCLEIC ACID ATOMS : 574
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 219
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.65000
REMARK 3 B22 (A**2) : -0.82000
REMARK 3 B33 (A**2) : -4.83000
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) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.31
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 31.05
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-TT5.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : WATER.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
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
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE AUTHORS STATE THAT THE UNUSUAL PEPTIDE BOND LENGTHS FOR K293-
REMARK 3 V294 (IN
REMARK 3 THIOREDOXIN BINDING LOOP) AND V541-G542 (IN THE FINGERS SUBDOMAIN)
REMARK 3 MAY
REMARK 3 REFLECT INHERENT PROBLEMS WITH MODEL REFINEMENT RESULTING FROM
REMARK 3 LOCAL
REMARK 3 DISORDER IN THESE REGIONS OF THE STRUCTURE, WHICH ARE KNOWN TO BE
REMARK 3 MOBILE IN
REMARK 3 DIFFERENT STRUCTURES OF T7 DNA POLYMERASE.
REMARK 4
REMARK 4 1ZYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033276.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-05; 15-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 200; 200
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : NSLS; ROTATING ANODE
REMARK 200 BEAMLINE : X26C; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1; 1.4
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : NULL
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
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; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, AMONIUM SULFATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 53.07400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 106.50350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.07400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 106.50350
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, T, A, B
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 DC P 1001
REMARK 465 DG P 1002
REMARK 465 DA P 1003
REMARK 465 DA P 1004
REMARK 465 DA P 1005
REMARK 465 DA P 1006
REMARK 465 DC P 1007
REMARK 465 DG P 1008
REMARK 465 DA P 1009
REMARK 465 DC T 2001
REMARK 465 DC T 2002
REMARK 465 DT T 2018
REMARK 465 DC T 2019
REMARK 465 DG T 2020
REMARK 465 DT T 2021
REMARK 465 DT T 2022
REMARK 465 DT T 2023
REMARK 465 DT T 2024
REMARK 465 DC T 2025
REMARK 465 DG T 2026
REMARK 465 ILE A 297
REMARK 465 PHE A 298
REMARK 465 LYS A 299
REMARK 465 LYS A 300
REMARK 465 PRO A 301
REMARK 465 LYS A 302
REMARK 465 ASN A 303
REMARK 465 LYS A 304
REMARK 465 ALA A 305
REMARK 465 GLN A 306
REMARK 465 ARG A 307
REMARK 465 GLU A 308
REMARK 465 GLY A 309
REMARK 465 ARG A 310
REMARK 465 GLU A 311
REMARK 465 PRO A 312
REMARK 465 CYS A 313
REMARK 465 GLU A 314
REMARK 465 SER B 1
REMARK 465 ASP B 2
REMARK 465 ALA B 108
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 LYS A 545 CD CE NZ
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 ASN A 60 32.49 81.39
REMARK 500 TYR A 64 -76.82 -115.67
REMARK 500 GLU A 152 -179.62 -66.49
REMARK 500 ASP A 156 -88.31 26.42
REMARK 500 ILE A 289 -166.00 -117.16
REMARK 500 GLU A 319 43.17 -101.63
REMARK 500 VAL A 321 -92.31 -116.71
REMARK 500 ALA A 322 -67.25 -167.78
REMARK 500 ASN A 423 48.53 -140.89
REMARK 500 LEU A 437 4.29 -68.51
REMARK 500 GLN A 439 25.70 -140.80
REMARK 500 ARG A 444 36.67 -94.90
REMARK 500 ILE A 464 -68.58 -93.78
REMARK 500 LEU A 501 45.46 -83.98
REMARK 500 PRO A 516 -78.13 -68.42
REMARK 500 PHE A 524 -71.45 -56.91
REMARK 500 ALA A 543 -155.82 -80.69
REMARK 500 LYS A 549 -48.21 -179.49
REMARK 500 THR A 559 87.37 -170.18
REMARK 500 SER A 576 161.92 173.54
REMARK 500 GLN A 578 -143.12 -101.01
REMARK 500 TRP A 579 34.75 -176.10
REMARK 500 VAL A 580 89.74 -64.35
REMARK 500 ALA A 581 -176.45 77.89
REMARK 500 GLU A 583 -132.60 -174.70
REMARK 500 GLN A 584 130.19 177.23
REMARK 500 HIS A 653 -82.37 62.27
REMARK 500 LEU B 53 145.39 -170.76
REMARK 500 LYS B 69 -9.58 -59.79
REMARK 500 THR B 89 136.45 178.18
REMARK 500 LYS B 100 -39.85 -37.15
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 DC P1020 0.12 SIDE CHAIN
REMARK 500 DA P1021 0.06 SIDE CHAIN
REMARK 500 DG T2007 0.07 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 MG A4003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 5 OD2
REMARK 620 2 ASP A 5 OD1 45.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A4001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 475 OD1
REMARK 620 2 ASP A 475 OD2 51.9
REMARK 620 3 ALA A 476 O 89.7 125.8
REMARK 620 4 ASP A 654 OD2 136.3 93.0 93.6
REMARK 620 5 DAD A1024 O1G 77.4 89.2 121.6 133.9
REMARK 620 6 DAD A1024 O1A 126.4 84.1 143.9 61.9 72.5
REMARK 620 7 DAD A1024 O2B 150.8 148.5 83.9 72.7 81.8 64.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A4002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 475 OD2
REMARK 620 2 ASP A 654 OD1 81.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAD A 1024
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T7P RELATED DB: PDB
DBREF 1ZYQ A 1 698 UNP P00581 DPOL_BPT7 1 704
DBREF 1ZYQ B 1 108 UNP P0AA25 THIO_ECOLI 1 108
DBREF 1ZYQ P 1001 1022 PDB 1ZYQ 1ZYQ 1001 1022
DBREF 1ZYQ T 2001 2026 PDB 1ZYQ 1ZYQ 2001 2026
SEQADV 1ZYQ A UNP P00581 LYS 118 DELETION
SEQADV 1ZYQ A UNP P00581 ARG 119 DELETION
SEQADV 1ZYQ A UNP P00581 PHE 120 DELETION
SEQADV 1ZYQ A UNP P00581 GLY 121 DELETION
SEQADV 1ZYQ A UNP P00581 SER 122 DELETION
SEQADV 1ZYQ A UNP P00581 HIS 123 DELETION
SEQADV 1ZYQ ALA A 536 UNP P00581 LYS 536 ENGINEERED MUTATION
SEQRES 1 P 22 DC DG DA DA DA DA DC DG DA DC DG DG DC
SEQRES 2 P 22 DC DA DG DT DG DC DC DA DDG
SEQRES 1 T 26 DC DC DC 8OG DC DT DG DG DC DA DC DT DG
SEQRES 2 T 26 DG DC DC DG DT DC DG DT DT DT DT DC DG
SEQRES 1 A 698 MET ILE VAL SER ASP ILE GLU ALA ASN ALA LEU LEU GLU
SEQRES 2 A 698 SER VAL THR LYS PHE HIS CYS GLY VAL ILE TYR ASP TYR
SEQRES 3 A 698 SER THR ALA GLU TYR VAL SER TYR ARG PRO SER ASP PHE
SEQRES 4 A 698 GLY ALA TYR LEU ASP ALA LEU GLU ALA GLU VAL ALA ARG
SEQRES 5 A 698 GLY GLY LEU ILE VAL PHE HIS ASN GLY HIS LYS TYR ASP
SEQRES 6 A 698 VAL PRO ALA LEU THR LYS LEU ALA LYS LEU GLN LEU ASN
SEQRES 7 A 698 ARG GLU PHE HIS LEU PRO ARG GLU ASN CYS ILE ASP THR
SEQRES 8 A 698 LEU VAL LEU SER ARG LEU ILE HIS SER ASN LEU LYS ASP
SEQRES 9 A 698 THR ASP MET GLY LEU LEU ARG SER GLY LYS LEU PRO GLY
SEQRES 10 A 698 ALA LEU GLU ALA TRP GLY TYR ARG LEU GLY GLU MET LYS
SEQRES 11 A 698 GLY GLU TYR LYS ASP ASP PHE LYS ARG MET LEU GLU GLU
SEQRES 12 A 698 GLN GLY GLU GLU TYR VAL ASP GLY MET GLU TRP TRP ASN
SEQRES 13 A 698 PHE ASN GLU GLU MET MET ASP TYR ASN VAL GLN ASP VAL
SEQRES 14 A 698 VAL VAL THR LYS ALA LEU LEU GLU LYS LEU LEU SER ASP
SEQRES 15 A 698 LYS HIS TYR PHE PRO PRO GLU ILE ASP PHE THR ASP VAL
SEQRES 16 A 698 GLY TYR THR THR PHE TRP SER GLU SER LEU GLU ALA VAL
SEQRES 17 A 698 ASP ILE GLU HIS ARG ALA ALA TRP LEU LEU ALA LYS GLN
SEQRES 18 A 698 GLU ARG ASN GLY PHE PRO PHE ASP THR LYS ALA ILE GLU
SEQRES 19 A 698 GLU LEU TYR VAL GLU LEU ALA ALA ARG ARG SER GLU LEU
SEQRES 20 A 698 LEU ARG LYS LEU THR GLU THR PHE GLY SER TRP TYR GLN
SEQRES 21 A 698 PRO LYS GLY GLY THR GLU MET PHE CYS HIS PRO ARG THR
SEQRES 22 A 698 GLY LYS PRO LEU PRO LYS TYR PRO ARG ILE LYS THR PRO
SEQRES 23 A 698 LYS VAL GLY GLY ILE PHE LYS LYS PRO LYS ASN LYS ALA
SEQRES 24 A 698 GLN ARG GLU GLY ARG GLU PRO CYS GLU LEU ASP THR ARG
SEQRES 25 A 698 GLU TYR VAL ALA GLY ALA PRO TYR THR PRO VAL GLU HIS
SEQRES 26 A 698 VAL VAL PHE ASN PRO SER SER ARG ASP HIS ILE GLN LYS
SEQRES 27 A 698 LYS LEU GLN GLU ALA GLY TRP VAL PRO THR LYS TYR THR
SEQRES 28 A 698 ASP LYS GLY ALA PRO VAL VAL ASP ASP GLU VAL LEU GLU
SEQRES 29 A 698 GLY VAL ARG VAL ASP ASP PRO GLU LYS GLN ALA ALA ILE
SEQRES 30 A 698 ASP LEU ILE LYS GLU TYR LEU MET ILE GLN LYS ARG ILE
SEQRES 31 A 698 GLY GLN SER ALA GLU GLY ASP LYS ALA TRP LEU ARG TYR
SEQRES 32 A 698 VAL ALA GLU ASP GLY LYS ILE HIS GLY SER VAL ASN PRO
SEQRES 33 A 698 ASN GLY ALA VAL THR GLY ARG ALA THR HIS ALA PHE PRO
SEQRES 34 A 698 ASN LEU ALA GLN ILE PRO GLY VAL ARG SER PRO TYR GLY
SEQRES 35 A 698 GLU GLN CYS ARG ALA ALA PHE GLY ALA GLU HIS HIS LEU
SEQRES 36 A 698 ASP GLY ILE THR GLY LYS PRO TRP VAL GLN ALA GLY ILE
SEQRES 37 A 698 ASP ALA SER GLY LEU GLU LEU ARG CYS LEU ALA HIS PHE
SEQRES 38 A 698 MET ALA ARG PHE ASP ASN GLY GLU TYR ALA HIS GLU ILE
SEQRES 39 A 698 LEU ASN GLY ASP ILE HIS THR LYS ASN GLN ILE ALA ALA
SEQRES 40 A 698 GLU LEU PRO THR ARG ASP ASN ALA LYS THR PHE ILE TYR
SEQRES 41 A 698 GLY PHE LEU TYR GLY ALA GLY ASP GLU ALA ILE GLY GLN
SEQRES 42 A 698 ILE VAL GLY ALA GLY LYS GLU ARG GLY LYS GLU LEU LYS
SEQRES 43 A 698 LYS LYS PHE LEU GLU ASN THR PRO ALA ILE ALA ALA LEU
SEQRES 44 A 698 ARG GLU SER ILE GLN GLN THR LEU VAL GLU SER SER GLN
SEQRES 45 A 698 TRP VAL ALA GLY GLU GLN GLN VAL LYS TRP LYS ARG ARG
SEQRES 46 A 698 TRP ILE LYS GLY LEU ASP GLY ARG LYS VAL HIS VAL ARG
SEQRES 47 A 698 SER PRO HIS ALA ALA LEU ASN THR LEU LEU GLN SER ALA
SEQRES 48 A 698 GLY ALA LEU ILE CYS LYS LEU TRP ILE ILE LYS THR GLU
SEQRES 49 A 698 GLU MET LEU VAL GLU LYS GLY LEU LYS HIS GLY TRP ASP
SEQRES 50 A 698 GLY ASP PHE ALA TYR MET ALA TRP VAL HIS ASP GLU ILE
SEQRES 51 A 698 GLN VAL GLY CYS ARG THR GLU GLU ILE ALA GLN VAL VAL
SEQRES 52 A 698 ILE GLU THR ALA GLN GLU ALA MET ARG TRP VAL GLY ASP
SEQRES 53 A 698 HIS TRP ASN PHE ARG CYS LEU LEU ASP THR GLU GLY LYS
SEQRES 54 A 698 MET GLY PRO ASN TRP ALA ILE CYS HIS
SEQRES 1 B 108 SER ASP LYS ILE ILE HIS LEU THR ASP ASP SER PHE ASP
SEQRES 2 B 108 THR ASP VAL LEU LYS ALA ASP GLY ALA ILE LEU VAL ASP
SEQRES 3 B 108 PHE TRP ALA GLU TRP CYS GLY PRO CYS LYS MET ILE ALA
SEQRES 4 B 108 PRO ILE LEU ASP GLU ILE ALA ASP GLU TYR GLN GLY LYS
SEQRES 5 B 108 LEU THR VAL ALA LYS LEU ASN ILE ASP GLN ASN PRO GLY
SEQRES 6 B 108 THR ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU
SEQRES 7 B 108 LEU LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL
SEQRES 8 B 108 GLY ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP
SEQRES 9 B 108 ALA ASN LEU ALA
MODRES 1ZYQ DDG P 1022 DG
MODRES 1ZYQ 8OG T 2004 DG
HET DDG P1022 21
HET 8OG T2004 23
HET MG A4001 1
HET MG A4002 1
HET MG A4003 1
HET DAD A1024 29
HETNAM DDG 2',3'-DIDEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETNAM 8OG 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM DAD 2',3'-DIDEOXYADENOSINE-5'-TRIPHOSPHATE
HETSYN 8OG 8-OXO-7,8-DIHYDRO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
FORMUL 1 DDG C10 H14 N5 O6 P
FORMUL 2 8OG C10 H14 N5 O8 P
FORMUL 5 MG 3(MG 2+)
FORMUL 8 DAD C10 H16 N5 O11 P3
FORMUL 9 HOH *219(H2 O)
HELIX 1 1 LEU A 11 VAL A 15 5 5
HELIX 2 2 ARG A 35 SER A 37 5 3
HELIX 3 3 ASP A 38 ARG A 52 1 15
HELIX 4 4 TYR A 64 ASN A 78 1 15
HELIX 5 5 PRO A 84 GLU A 86 5 3
HELIX 6 6 THR A 91 HIS A 99 1 9
HELIX 7 7 ARG A 111 LEU A 115 5 5
HELIX 8 8 GLU A 126 GLU A 134 1 9
HELIX 9 9 GLU A 134 GLU A 149 1 16
HELIX 10 10 GLY A 157 TRP A 161 5 5
HELIX 11 11 ASN A 164 SER A 187 1 24
HELIX 12 12 GLY A 202 SER A 210 1 9
HELIX 13 13 LEU A 211 GLY A 231 1 21
HELIX 14 14 ASP A 235 PHE A 261 1 27
HELIX 15 15 SER A 338 ALA A 349 1 12
HELIX 16 16 ASP A 365 GLU A 370 1 6
HELIX 17 17 ASP A 376 ALA A 400 1 25
HELIX 18 18 ALA A 405 VAL A 410 1 6
HELIX 19 19 TYR A 447 ALA A 454 1 8
HELIX 20 20 PHE A 455 HIS A 460 5 6
HELIX 21 21 GLY A 478 ASN A 493 1 16
HELIX 22 22 GLY A 494 LEU A 501 1 8
HELIX 23 23 ASP A 504 ALA A 513 1 10
HELIX 24 24 THR A 517 TYR A 530 1 14
HELIX 25 25 GLY A 533 VAL A 541 1 9
HELIX 26 26 GLU A 546 ASN A 558 1 13
HELIX 27 27 PRO A 560 LEU A 573 1 14
HELIX 28 28 SER A 605 HIS A 607 5 3
HELIX 29 29 ALA A 608 LYS A 636 1 29
HELIX 30 30 THR A 662 TRP A 684 1 23
HELIX 31 31 SER B 11 VAL B 16 1 6
HELIX 32 32 CYS B 32 TYR B 49 1 18
HELIX 33 33 THR B 66 GLY B 71 5 6
HELIX 34 34 SER B 95 ALA B 105 1 11
SHEET 1 A 5 TYR A 31 TYR A 34 0
SHEET 2 A 5 PHE A 18 ASP A 25 -1 N ILE A 23 O VAL A 32
SHEET 3 A 5 ILE A 2 ALA A 8 -1 N VAL A 3 O TYR A 24
SHEET 4 A 5 ILE A 56 PHE A 58 1 O VAL A 57 N SER A 4
SHEET 5 A 5 CYS A 88 ASP A 90 1 O ILE A 89 N PHE A 58
SHEET 1 B 2 PHE A 232 PRO A 233 0
SHEET 2 B 2 LYS A 415 ILE A 416 -1 O ILE A 416 N PHE A 232
SHEET 1 C 3 TRP A 264 PRO A 267 0
SHEET 2 C 3 THR A 327 VAL A 332 -1 O VAL A 332 N TRP A 264
SHEET 3 C 3 GLY B 74 ILE B 75 -1 O ILE B 75 N THR A 327
SHEET 1 D 2 SER A 419 ASN A 421 0
SHEET 2 D 2 THR A 431 ALA A 433 -1 O THR A 431 N ASN A 421
SHEET 1 E 4 PHE A 646 TRP A 651 0
SHEET 2 E 4 GLU A 655 CYS A 660 -1 O GLN A 657 N MET A 649
SHEET 3 E 4 VAL A 470 ALA A 476 -1 N VAL A 470 O CYS A 660
SHEET 4 E 4 THR A 692 GLY A 697 -1 O GLY A 697 N GLN A 471
SHEET 1 F 2 VAL A 574 SER A 577 0
SHEET 2 F 2 VAL A 586 TRP A 588 -1 O LYS A 587 N SER A 576
SHEET 1 G 2 TRP A 592 LYS A 594 0
SHEET 2 G 2 LYS A 600 HIS A 602 -1 O VAL A 601 N ILE A 593
SHEET 1 H 5 ILE B 5 HIS B 6 0
SHEET 2 H 5 THR B 54 ASN B 59 1 O LYS B 57 N ILE B 5
SHEET 3 H 5 ALA B 22 TRP B 28 1 N LEU B 24 O THR B 54
SHEET 4 H 5 THR B 77 LYS B 82 -1 O LEU B 79 N VAL B 25
SHEET 5 H 5 GLU B 85 VAL B 91 -1 O ALA B 87 N LEU B 80
LINK O3' DA P1021 P DDG P1022 1555 1555 1.61
LINK O3' DC T2003 P 8OG T2004 1555 1555 1.61
LINK O3' 8OG T2004 P DC T2005 1555 1555 1.62
LINK OD2 ASP A 5 MG MG A4003 1555 1555 3.06
LINK OD1 ASP A 5 MG MG A4003 1555 1555 2.51
LINK OD1 ASP A 475 MG MG A4001 1555 1555 2.57
LINK OD2 ASP A 475 MG MG A4001 1555 1555 2.51
LINK OD2 ASP A 475 MG MG A4002 1555 1555 2.92
LINK O ALA A 476 MG MG A4001 1555 1555 2.18
LINK OD2 ASP A 654 MG MG A4001 1555 1555 2.34
LINK OD1 ASP A 654 MG MG A4002 1555 1555 2.87
LINK O1G DAD A1024 MG MG A4001 1555 1555 2.43
LINK O1A DAD A1024 MG MG A4001 1555 1555 2.56
LINK O2B DAD A1024 MG MG A4001 1555 1555 2.63
CISPEP 1 PHE A 434 PRO A 435 0 -0.79
CISPEP 2 ILE B 75 PRO B 76 0 0.24
SITE 1 AC1 4 ASP A 475 ALA A 476 ASP A 654 DAD A1024
SITE 1 AC2 5 ASP A 475 ASP A 654 GLU A 655 HIS A 704
SITE 2 AC2 5 DAD A1024
SITE 1 AC3 2 ASP A 5 ASP A 174
SITE 1 AC4 17 ARG A 429 ASP A 475 ALA A 476 SER A 477
SITE 2 AC4 17 GLY A 478 LEU A 479 GLU A 480 HIS A 506
SITE 3 AC4 17 ARG A 518 LYS A 522 TYR A 526 ASP A 654
SITE 4 AC4 17 MG A4001 MG A4002 DDG P1022 8OG T2004
SITE 5 AC4 17 DC T2005
CRYST1 106.148 213.007 52.990 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 0.009421 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004695 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018871 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
