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PDBsum entry 2pis

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DNA PDB id
2pis
Jmol
Contents
DNA/RNA
Metals
_MG ×6
HEADER    DNA                                     13-APR-07   2PIS
TITLE     EFFORTS TOWARD EXPANSION OF THE GENETIC ALPHABET: STRUCTURE
TITLE    2 AND REPLICATION OF UNNATURAL BASE PAIRS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-D(*CP*GP*(CBR)P*GP*AP*AP*(FFD)
COMPND   3 P*TP*TP*CP*GP*CP*G)-3');
COMPND   4 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: SYNTHESIZED DNA
KEYWDS    NUCLEIC ACID, DUPLEX, REPLICATION, UNNATURAL BASE, DNA
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.MATSUDA,J.D.FILLO,A.A.HENRY,S.J.WILKINS,P.RAI,T.J.DWYER,
AUTHOR   2 B.H.GEIERSTANGER,D.E.WEMMER,P.G.SCHULTZ,G.SPRAGGON,
AUTHOR   3 F.E.ROMESBERG
REVDAT   2   24-FEB-09 2PIS    1       VERSN
REVDAT   1   30-OCT-07 2PIS    0
JRNL        AUTH   S.MATSUDA,J.D.FILLO,A.A.HENRY,P.RAI,S.J.WILKENS,
JRNL        AUTH 2 T.J.DWYER,B.H.GEIERSTANGER,D.E.WEMMER,P.G.SCHULTZ,
JRNL        AUTH 3 G.SPRAGGON,F.E.ROMESBERG
JRNL        TITL   EFFORTS TOWARD EXPANSION OF THE GENETIC ALPHABET:
JRNL        TITL 2 STRUCTURE AND REPLICATION OF UNNATURAL BASE PAIRS.
JRNL        REF    J.AM.CHEM.SOC.                V. 129 10466 2007
JRNL        REFN                   ISSN 0002-7863
JRNL        PMID   17685517
JRNL        DOI    10.1021/JA072276D
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.8
REMARK   3   NUMBER OF REFLECTIONS             : 11034
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 + TEST SET) : 0.228
REMARK   3   R VALUE            (WORKING SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.303
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 599
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.88
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 620
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.10
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3640
REMARK   3   BIN FREE R VALUE SET COUNT          : 39
REMARK   3   BIN FREE R VALUE                    : 0.4800
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 0
REMARK   3   NUCLEIC ACID ATOMS       : 3144
REMARK   3   HETEROGEN ATOMS          : 6
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.35
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.53000
REMARK   3    B22 (A**2) : -2.53000
REMARK   3    B33 (A**2) : 5.05000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.475
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.317
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.642
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3552 ; 0.014 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5468 ; 1.131 ; 2.997
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   600 ; 0.053 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1608 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1740 ; 0.338 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1974 ; 0.342 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   119 ; 0.300 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   120 ; 0.345 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.178 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):    24 ; 2.970 ; 2.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):    48 ;12.619 ; 5.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5040 ;13.620 ; 8.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5340 ;16.424 ;11.000
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS. ELECTRON DENSITY FOR THE CHAINS I,J AND K,L
REMARK   3  WAS EXTREMELY WEAK. THE AUTHOR STATES THAT THESE CHAINS WERE
REMARK   3  MODELED TENTATIVELY INTO THE DENSITY.
REMARK   4
REMARK   4 2PIS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-07.
REMARK 100 THE RCSB ID CODE IS RCSB042419.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 8.2.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92017, 0.9203, 0.9050
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12382
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8
REMARK 200  DATA REDUNDANCY                : 15.300
REMARK 200  R MERGE                    (I) : 0.05400
REMARK 200  R SYM                      (I) : 0.05400
REMARK 200   FOR THE DATA SET  : 40.5800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.59700
REMARK 200  R SYM FOR SHELL            (I) : 0.38800
REMARK 200   FOR SHELL         : 3.730
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% (V/V) MPD IN 0.1M SODIUM
REMARK 280  CACODYLATE , PH 6.0, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       3555   -Y,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X,Z+3/4
REMARK 290       5555   -X+1/2,Y,-Z+3/4
REMARK 290       6555   X,-Y+1/2,-Z+1/4
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X,-Y,Z
REMARK 290      11555   -Y+1/2,X,Z+3/4
REMARK 290      12555   Y,-X+1/2,Z+1/4
REMARK 290      13555   -X,Y+1/2,-Z+1/4
REMARK 290      14555   X+1/2,-Y,-Z+3/4
REMARK 290      15555   Y,X,-Z
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
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       73.01250
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       73.01250
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.57000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       73.01250
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.28500
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       73.01250
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       69.85500
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       73.01250
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       69.85500
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       73.01250
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       23.28500
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       73.01250
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       73.01250
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       46.57000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       73.01250
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       73.01250
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       46.57000
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       73.01250
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       69.85500
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       73.01250
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       23.28500
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       73.01250
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       23.28500
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       73.01250
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       69.85500
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       73.01250
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       73.01250
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       46.57000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
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 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   N4   DC  G    12     O6   DG  H    15              1.97
REMARK 500   O2   DC  I    12     N2   DG  J    15              2.06
REMARK 500   C5   DC  B    14     O6   DG  C     2              2.13
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   O6   DG  A     4     C5   DC  G     1     8657     2.09
REMARK 500   C5   DC  F    14     O6   DG  F    17    16556     2.14
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     DC A   1   O3'    DC A   1   C3'    -0.051
REMARK 500     DG A   4   O3'    DG A   4   C3'    -0.072
REMARK 500     DG B  17   O3'    DG B  17   C3'    -0.039
REMARK 500     DG B  24   O3'    DG B  24   C3'    -0.057
REMARK 500     DG C   4   C2     DG C   4   N3      0.052
REMARK 500     DT C   8   O3'    DT C   8   C3'    -0.066
REMARK 500     DG C  11   O3'    DG C  11   C3'    -0.079
REMARK 500     DG E  11   O3'    DG E  11   C3'    -0.043
REMARK 500     DC F  14   O3'    DC F  14   C3'    -0.040
REMARK 500     DG F  15   O3'    DG F  15   C3'    -0.096
REMARK 500     DG F  24   C2     DG F  24   N3      0.050
REMARK 500     DC G   1   O3'    DC G   1   C3'    -0.054
REMARK 500     DG G   2   O3'    DG G   2   C3'    -0.046
REMARK 500     DG G   4   O3'    DG G   4   C3'    -0.064
REMARK 500     DA G   6   O3'    DA G   6   C3'    -0.043
REMARK 500     DA H  18   O3'    DA H  18   C3'    -0.049
REMARK 500     DT J  22   O3'    DT J  22   C3'    -0.039
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 A   1   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES
REMARK 500     DG A   2   O4' -  C1' -  N9  ANGL. DEV. =  -5.4 DEGREES
REMARK 500     DG A  11   O4' -  C1' -  N9  ANGL. DEV. =   4.5 DEGREES
REMARK 500     DC B  14   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DG B  24   C3' -  C2' -  C1' ANGL. DEV. =  -5.0 DEGREES
REMARK 500     DG C   4   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES
REMARK 500     DG C  11   O4' -  C1' -  N9  ANGL. DEV. =   3.6 DEGREES
REMARK 500     DG D  17   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES
REMARK 500     DA D  19   C1' -  O4' -  C4' ANGL. DEV. =  -9.8 DEGREES
REMARK 500     DA D  19   O4' -  C1' -  N9  ANGL. DEV. =   5.5 DEGREES
REMARK 500     DG D  24   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES
REMARK 500     DG E   4   O4' -  C1' -  N9  ANGL. DEV. =   3.1 DEGREES
REMARK 500     DT E   8   O4' -  C4' -  C3' ANGL. DEV. =  -2.6 DEGREES
REMARK 500     DA F  19   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES
REMARK 500     DG F  24   O4' -  C1' -  N9  ANGL. DEV. =   4.9 DEGREES
REMARK 500     DG G   4   O4' -  C1' -  N9  ANGL. DEV. =   5.3 DEGREES
REMARK 500     DA G   6   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES
REMARK 500     DT G   9   O4' -  C1' -  N1  ANGL. DEV. =   3.9 DEGREES
REMARK 500     DC G  12   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DG H  17   C1' -  O4' -  C4' ANGL. DEV. =  -6.5 DEGREES
REMARK 500     DG H  17   O4' -  C1' -  N9  ANGL. DEV. =   6.3 DEGREES
REMARK 500     DA H  19   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES
REMARK 500     DA I   5   O4' -  C1' -  N9  ANGL. DEV. =   3.7 DEGREES
REMARK 500     DT I   9   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES
REMARK 500     DC I  10   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES
REMARK 500     DG I  11   O4' -  C1' -  N9  ANGL. DEV. =   3.1 DEGREES
REMARK 500     DT J  22   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES
REMARK 500     DG J  24   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES
REMARK 500     DT K   8   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES
REMARK 500     DG L  17   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DA L  18   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES
REMARK 500     DA L  19   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES
REMARK 500     DC L  25   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF  2PIS A    1    13  PDB    2PIS     2PIS             1     13
DBREF  2PIS B   14    26  PDB    2PIS     2PIS             1     13
DBREF  2PIS C    1    13  PDB    2PIS     2PIS             1     13
DBREF  2PIS D   14    26  PDB    2PIS     2PIS             1     13
DBREF  2PIS E    1    13  PDB    2PIS     2PIS             1     13
DBREF  2PIS F   14    26  PDB    2PIS     2PIS             1     13
DBREF  2PIS G    1    13  PDB    2PIS     2PIS             1     13
DBREF  2PIS H   14    26  PDB    2PIS     2PIS             1     13
DBREF  2PIS I    1    13  PDB    2PIS     2PIS             1     13
DBREF  2PIS J   14    26  PDB    2PIS     2PIS             1     13
DBREF  2PIS K    1    13  PDB    2PIS     2PIS             1     13
DBREF  2PIS L   14    26  PDB    2PIS     2PIS             1     13
SEQRES   1 A   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 B   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 C   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 D   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 E   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 F   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 G   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 H   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 I   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 J   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 K   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
SEQRES   1 L   13   DC  DG CBR  DG  DA  DA FFD  DT  DT  DC  DG  DC  DG
MODRES 2PIS CBR A    3   DC
MODRES 2PIS CBR B   16   DC
MODRES 2PIS CBR C    3   DC
MODRES 2PIS CBR D   16   DC
MODRES 2PIS CBR E    3   DC
MODRES 2PIS CBR F   16   DC
MODRES 2PIS CBR G    3   DC
MODRES 2PIS CBR H   16   DC
MODRES 2PIS CBR I    3   DC
MODRES 2PIS CBR J   16   DC
MODRES 2PIS CBR K    3   DC
MODRES 2PIS CBR L   16   DC
HET    CBR  A   3      20
HET    FFD  A   7      18
HET    CBR  B  16      20
HET    FFD  B  20      18
HET    CBR  C   3      20
HET    FFD  C   7      18
HET    CBR  D  16      20
HET    FFD  D  20      18
HET    CBR  E   3      20
HET    FFD  E   7      18
HET    CBR  F  16      20
HET    FFD  F  20      18
HET    CBR  G   3      20
HET    FFD  G   7      18
HET    CBR  H  16      20
HET    FFD  H  20      18
HET    CBR  I   3      20
HET    FFD  I   7      18
HET    CBR  J  16      20
HET    FFD  J  20      18
HET    CBR  K   3      20
HET    FFD  K   7      18
HET    CBR  L  16      20
HET    FFD  L  20      18
HET     MG  F   1       1
HET     MG  D   2       1
HET     MG  E  14       1
HET     MG  G  14       1
HET     MG  G  15       1
HET     MG  G  16       1
HETNAM     CBR 5-BROMO-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE
HETNAM     FFD (1R)-1,4-ANHYDRO-2-DEOXY-1-(3-FLUOROPHENYL)-5-O-
HETNAM   2 FFD  PHOSPHONO-D-ERYTHRO-PENTITOL
HETNAM      MG MAGNESIUM ION
FORMUL   1  CBR    12(C9 H13 BR N3 O7 P)
FORMUL   1  FFD    12(C11 H14 F O6 P)
FORMUL  13   MG    6(MG 2+)
LINK         O3'  DG A   2                 P   CBR A   3     1555   1555  1.57
LINK         O3' CBR A   3                 P    DG A   4     1555   1555  1.58
LINK         O3'  DA A   6                 P   FFD A   7     1555   1555  1.59
LINK         O3' FFD A   7                 P    DT A   8     1555   1555  1.60
LINK         O3'  DG B  15                 P   CBR B  16     1555   1555  1.63
LINK         O3' CBR B  16                 P    DG B  17     1555   1555  1.58
LINK         O3'  DA B  19                 P   FFD B  20     1555   1555  1.60
LINK         O3' FFD B  20                 P    DT B  21     1555   1555  1.61
LINK         O3'  DG C   2                 P   CBR C   3     1555   1555  1.58
LINK         O3' CBR C   3                 P    DG C   4     1555   1555  1.61
LINK         O3'  DA C   6                 P   FFD C   7     1555   1555  1.59
LINK         O3' FFD C   7                 P    DT C   8     1555   1555  1.59
LINK         O3'  DG D  15                 P   CBR D  16     1555   1555  1.57
LINK         O3' CBR D  16                 P    DG D  17     1555   1555  1.58
LINK         O3'  DA D  19                 P   FFD D  20     1555   1555  1.59
LINK         O3' FFD D  20                 P    DT D  21     1555   1555  1.60
LINK         O3'  DG E   2                 P   CBR E   3     1555   1555  1.61
LINK         O3' CBR E   3                 P    DG E   4     1555   1555  1.62
LINK         O3'  DA E   6                 P   FFD E   7     1555   1555  1.61
LINK         O3' FFD E   7                 P    DT E   8     1555   1555  1.59
LINK         O3'  DG F  15                 P   CBR F  16     1555   1555  1.53
LINK         O3' CBR F  16                 P    DG F  17     1555   1555  1.59
LINK         O3'  DA F  19                 P   FFD F  20     1555   1555  1.59
LINK         O3' FFD F  20                 P    DT F  21     1555   1555  1.59
LINK         O3'  DG G   2                 P   CBR G   3     1555   1555  1.56
LINK         O3' CBR G   3                 P    DG G   4     1555   1555  1.55
LINK         O3'  DA G   6                 P   FFD G   7     1555   1555  1.59
LINK         O3' FFD G   7                 P    DT G   8     1555   1555  1.59
LINK         O3'  DG H  15                 P   CBR H  16     1555   1555  1.60
LINK         O3' CBR H  16                 P    DG H  17     1555   1555  1.59
LINK         O3'  DA H  19                 P   FFD H  20     1555   1555  1.60
LINK         O3' FFD H  20                 P    DT H  21     1555   1555  1.60
LINK         O3'  DG I   2                 P   CBR I   3     1555   1555  1.59
LINK         O3' CBR I   3                 P    DG I   4     1555   1555  1.59
LINK         O3'  DA I   6                 P   FFD I   7     1555   1555  1.60
LINK         O3' FFD I   7                 P    DT I   8     1555   1555  1.60
LINK         O3'  DG J  15                 P   CBR J  16     1555   1555  1.61
LINK         O3' CBR J  16                 P    DG J  17     1555   1555  1.61
LINK         O3'  DA J  19                 P   FFD J  20     1555   1555  1.60
LINK         O3' FFD J  20                 P    DT J  21     1555   1555  1.60
LINK         O3'  DG K   2                 P   CBR K   3     1555   1555  1.62
LINK         O3' CBR K   3                 P    DG K   4     1555   1555  1.61
LINK         O3'  DA K   6                 P   FFD K   7     1555   1555  1.60
LINK         O3' FFD K   7                 P    DT K   8     1555   1555  1.61
LINK         O3'  DG L  15                 P   CBR L  16     1555   1555  1.61
LINK         O3' CBR L  16                 P    DG L  17     1555   1555  1.61
LINK         O3'  DA L  19                 P   FFD L  20     1555   1555  1.60
LINK         O3' FFD L  20                 P    DT L  21     1555   1555  1.59
CRYST1  146.025  146.025   93.140  90.00  90.00  90.00 I 41 2 2    192
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      0.006848  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006848  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010737        0.00000
      
 References