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PDBsum entry 2qs6

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DNA PDB id
2qs6
Jmol
Contents
DNA/RNA
Waters ×40
HEADER    DNA                                     30-JUL-07   2QS6
TITLE     STRUCTURE OF A HOOGSTEEN ANTIPARALLEL DUPLEX WITH EXTRA-HELICAL
TITLE    2 THYMINES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-D(*DAP*DTP*DAP*DTP*DAP*DTP*DCP*DT)-3');
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: PHOSPHORAMIDITE METHOD
KEYWDS    HOOGSTEEN, OLIGONUCLEOTIDE, DNA, THYMINES
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.POUS,L.URPI,J.A.SUBIRANA,C.GOUYETTE,J.NAVAZA,J.L.CAMPOS
REVDAT   4   13-JUL-11 2QS6    1       VERSN
REVDAT   3   24-FEB-09 2QS6    1       VERSN
REVDAT   2   03-JUN-08 2QS6    1       JRNL
REVDAT   1   25-MAR-08 2QS6    0
JRNL        AUTH   J.POUS,L.URPI,J.A.SUBIRANA,C.GOUYETTE,J.NAVAZA,J.L.CAMPOS
JRNL        TITL   STABILIZATION BY EXTRA-HELICAL THYMINES OF A DNA DUPLEX WITH
JRNL        TITL 2 HOOGSTEEN BASE PAIRS.
JRNL        REF    J.AM.CHEM.SOC.                V. 130  6755 2008
JRNL        REFN                   ISSN 0002-7863
JRNL        PMID   18447354
JRNL        DOI    10.1021/JA078022+
REMARK   2
REMARK   2 RESOLUTION.    3.08 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0051
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) : 3.08
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.43
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.9
REMARK   3   NUMBER OF REFLECTIONS             : 5188
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) : 0.214
REMARK   3   R VALUE            (WORKING SET) : 0.207
REMARK   3   FREE R VALUE                     : 0.289
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.700
REMARK   3   FREE R VALUE TEST SET COUNT      : 555
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) : 3.08
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.17
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 251
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.02
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650
REMARK   3   BIN FREE R VALUE SET COUNT          : 31
REMARK   3   BIN FREE R VALUE                    : 0.4950
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 0
REMARK   3   NUCLEIC ACID ATOMS       : 2181
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 40
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.78
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.96000
REMARK   3    B22 (A**2) : -1.18000
REMARK   3    B33 (A**2) : -0.59000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -4.62000
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): 0.629
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.506
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.211
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2613 ; 0.085 ; 0.055
REMARK   3   BOND LENGTHS OTHERS               (A):  1164 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3716 ; 1.070 ; 3.000
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2863 ; 0.939 ; 3.000
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):   425 ; 0.061 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1119 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   218 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   908 ; 0.250 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    64 ; 0.404 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):    10 ; 0.112 ; 0.200
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):    50 ; 0.234 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    24 ; 0.290 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.190 ; 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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2613 ; 1.184 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3716 ; 1.668 ; 4.500
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  : 1
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 14
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A     6
REMARK   3    RESIDUE RANGE :   B     1        B     6
REMARK   3    RESIDUE RANGE :   C     1        C     6
REMARK   3    RESIDUE RANGE :   D     1        D     6
REMARK   3    RESIDUE RANGE :   E     1        E     6
REMARK   3    RESIDUE RANGE :   F     1        F     6
REMARK   3    RESIDUE RANGE :   G     1        G     6
REMARK   3    RESIDUE RANGE :   H     1        H     6
REMARK   3    RESIDUE RANGE :   I     1        I     6
REMARK   3    RESIDUE RANGE :   J     1        J     6
REMARK   3    RESIDUE RANGE :   K     1        K     6
REMARK   3    RESIDUE RANGE :   L     1        L     6
REMARK   3    RESIDUE RANGE :   M     1        M     6
REMARK   3    RESIDUE RANGE :   N     1        N     6
REMARK   3    ORIGIN FOR THE GROUP (A):  77.6220   6.4140  42.4490
REMARK   3    T TENSOR
REMARK   3      T11:   -.1341 T22:    .0274
REMARK   3      T33:   -.1792 T12:    .1767
REMARK   3      T13:    .1262 T23:    .2242
REMARK   3    L TENSOR
REMARK   3      L11:   2.0275 L22:   5.8677
REMARK   3      L33:   3.3643 L12:  -2.5723
REMARK   3      L13:   2.1497 L23:  -4.1624
REMARK   3    S TENSOR
REMARK   3      S11:   -.0876 S12:   -.1444 S13:   -.0793
REMARK   3      S21:    .0177 S22:    .3001 S23:    .3277
REMARK   3      S31:    .0091 S32:   -.2120 S33:   -.2125
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2QS6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-07.
REMARK 100 THE RCSB ID CODE IS RCSB043987.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-04
REMARK 200  TEMPERATURE           (KELVIN) : 113.15
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : BM16
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790
REMARK 200  MONOCHROMATOR                  : MIRRORS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6262
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.080
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.430
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 5.350
REMARK 200  R MERGE                    (I) : 0.07700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.08
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.22200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: D(ATATAT)2 MODEL WITH HOOGSTEEN BASE PAIRS (FROM
REMARK 200  NDB ENTRY UD0049)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DROP: 1.0MM OCTAMER, 10% MPD, 22MM
REMARK 280  SODIUM CACODYLATE, 10MM MAGNESIUM CHLORIDE, 1.5MM SPERMINE
REMARK 280  TETRACHLORIDE. RESERVOIR: FROM 25% TO 45% MPD, PH 6.5, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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       60.41800
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.77000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       60.41800
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       19.77000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.4 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.4 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.6 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.9 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.5 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.9 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N
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      DT F     8
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 I   8    O5'  C5'  C4'  O4'  C3'  O3'  C2'
REMARK 470      DT I   8    C1'  N1   C2   O2   N3   C4   O4
REMARK 470      DT I   8    C5   C7   C6
REMARK 470      DC M   7    N1   C2   O2   N3   C4   N4   C5
REMARK 470      DC M   7    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   OP2   DA A     5     O    HOH A    10              2.01
REMARK 500   O3'   DT N     4     O    HOH N    25              2.04
REMARK 500   O5'   DA F     5     O    HOH F    11              2.15
REMARK 500   O5'   DA D     3     O    HOH D    50              2.19
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 D   7   C1'    DC D   7   N1      0.078
REMARK 500     DA H   5   O3'    DA H   5   C3'    -0.050
REMARK 500     DT J   6   O3'    DT J   6   C3'    -0.045
REMARK 500     DA L   5   O3'    DA L   5   C3'    -0.049
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     DT A   4   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES
REMARK 500     DT B   4   O4' -  C1' -  N1  ANGL. DEV. =   4.6 DEGREES
REMARK 500     DT C   4   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES
REMARK 500     DA C   5   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES
REMARK 500     DC C   7   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES
REMARK 500     DA D   3   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES
REMARK 500     DC D   7   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES
REMARK 500     DT E   6   O4' -  C1' -  N1  ANGL. DEV. =   4.3 DEGREES
REMARK 500     DT F   4   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES
REMARK 500     DA F   5   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DT F   6   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DT G   6   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES
REMARK 500     DT G   8   C1' -  O4' -  C4' ANGL. DEV. =  -6.5 DEGREES
REMARK 500     DT G   8   O4' -  C1' -  N1  ANGL. DEV. =   5.4 DEGREES
REMARK 500     DA H   5   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES
REMARK 500     DT H   8   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES
REMARK 500     DA I   5   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES
REMARK 500     DT J   4   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES
REMARK 500     DA J   5   O4' -  C1' -  N9  ANGL. DEV. =   2.8 DEGREES
REMARK 500     DC J   7   O4' -  C1' -  N1  ANGL. DEV. =   3.9 DEGREES
REMARK 500     DT J   8   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DA K   5   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES
REMARK 500     DA L   3   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES
REMARK 500     DT L   4   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES
REMARK 500     DT L   6   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES
REMARK 500     DT N   4   O4' -  C1' -  N1  ANGL. DEV. =   3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF  2QS6 A    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 B    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 C    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 D    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 E    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 F    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 G    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 H    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 I    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 J    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 K    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 L    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 M    1     8  PDB    2QS6     2QS6             1      8
DBREF  2QS6 N    1     8  PDB    2QS6     2QS6             1      8
SEQRES   1 A    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 B    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 C    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 D    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 E    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 F    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 G    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 H    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 I    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 J    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 K    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 L    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 M    8   DA  DT  DA  DT  DA  DT  DC  DT
SEQRES   1 N    8   DA  DT  DA  DT  DA  DT  DC  DT
FORMUL  15  HOH   *40(H2 O)
CRYST1  120.836   39.540   71.753  90.00  95.08  90.00 C 1 2 1      56
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      0.008276  0.000000  0.000736        0.00000
SCALE2      0.000000  0.025291  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013992        0.00000
      
 References