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PDBsum entry 2od8

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Top Page protein Protein-protein interface(s) links
Protein binding PDB id
2od8
Jmol
Contents
Protein chains
255 a.a.
11 a.a.
Waters ×18
HEADER    PROTEIN BINDING                         21-DEC-06   2OD8
TITLE     STRUCTURE OF A PEPTIDE DERIVED FROM CDC9 BOUND TO PCNA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PCNA;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: DNA LIGASE I, MITOCHONDRIAL PRECURSOR;
COMPND   8 CHAIN: B;
COMPND   9 FRAGMENT: RESIDUES 32-53;
COMPND  10 SYNONYM: CDC9, POLYDEOXYRIBONUCLEOTIDE SYNTHASE;
COMPND  11 EC: 6.5.1.1;
COMPND  12 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   4 ORGANISM_TAXID: 4932;
SOURCE   5 GENE: POL30;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7-PCNA;
SOURCE  11 MOL_ID: 2;
SOURCE  12 SYNTHETIC: YES;
SOURCE  13 OTHER_DETAILS: PEPTIDE SYNTHESIZED BASED ON CDC9 SEQUENCE (UNP
SOURCE  14 P04819), RESIDUES 32-53.
KEYWDS    HOMOTRIMER, PCNA-PEPTIDE COMPLEX, PCNA, PROTEIN BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.R.CHAPADOS,J.A.TAINER
REVDAT   3   13-JUL-11 2OD8    1       VERSN
REVDAT   2   24-FEB-09 2OD8    1       VERSN
REVDAT   1   01-MAY-07 2OD8    0
JRNL        AUTH   S.VIJAYAKUMAR,B.R.CHAPADOS,K.H.SCHMIDT,R.D.KOLODNER,
JRNL        AUTH 2 J.A.TAINER,A.E.TOMKINSON
JRNL        TITL   THE C-TERMINAL DOMAIN OF YEAST PCNA IS REQUIRED FOR PHYSICAL
JRNL        TITL 2 AND FUNCTIONAL INTERACTIONS WITH CDC9 DNA LIGASE.
JRNL        REF    NUCLEIC ACIDS RES.            V.  35  1624 2007
JRNL        REFN                   ISSN 0305-1048
JRNL        PMID   17308348
JRNL        DOI    10.1093/NAR/GKM006
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 29.70
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 10682
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) : 0.249
REMARK   3   R VALUE            (WORKING SET) : 0.247
REMARK   3   FREE R VALUE                     : 0.285
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 537
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) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 786
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.16
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3930
REMARK   3   BIN FREE R VALUE SET COUNT          : 39
REMARK   3   BIN FREE R VALUE                    : 0.3000
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2095
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 18
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : 94.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.32
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.684
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.361
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.371
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.060
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2127 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2866 ; 1.081 ; 1.991
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   264 ; 6.097 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    93 ;35.102 ;25.376
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   404 ;16.997 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;19.664 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   337 ; 0.071 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1550 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   877 ; 0.160 ; 0.300
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1423 ; 0.313 ; 0.500
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   111 ; 0.172 ; 0.500
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):    31 ; 0.125 ; 0.300
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.168 ; 0.500
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):  1362 ; 0.338 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2148 ; 0.607 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   837 ; 0.525 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   718 ; 0.879 ; 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  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    35        B    45
REMARK   3    ORIGIN FOR THE GROUP (A): 140.5880  18.2650  47.4900
REMARK   3    T TENSOR
REMARK   3      T11:   1.1783 T22:   1.0623
REMARK   3      T33:   1.1730 T12:   0.3405
REMARK   3      T13:   0.0515 T23:   0.0162
REMARK   3    L TENSOR
REMARK   3      L11:  11.4663 L22:  14.7756
REMARK   3      L33:  20.0460 L12:  -4.1276
REMARK   3      L13:  13.9890 L23:   1.2566
REMARK   3    S TENSOR
REMARK   3      S11:   1.2736 S12:  -0.5391 S13:  -1.3595
REMARK   3      S21:   0.9956 S22:  -0.8022 S23:  -2.6504
REMARK   3      S31:  -1.1780 S32:   2.0207 S33:  -0.4714
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A   255
REMARK   3    ORIGIN FOR THE GROUP (A): 119.4550  21.1500  51.0470
REMARK   3    T TENSOR
REMARK   3      T11:   0.9884 T22:   0.5305
REMARK   3      T33:   0.4796 T12:   0.1721
REMARK   3      T13:  -0.2015 T23:   0.0537
REMARK   3    L TENSOR
REMARK   3      L11:   4.1147 L22:   7.7453
REMARK   3      L33:   1.6087 L12:   4.8737
REMARK   3      L13:  -0.8938 L23:   0.6118
REMARK   3    S TENSOR
REMARK   3      S11:   0.1806 S12:  -0.2079 S13:  -0.0507
REMARK   3      S21:   1.0719 S22:   0.1373 S23:  -0.1509
REMARK   3      S31:   0.7841 S32:   0.1530 S33:  -0.3179
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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2OD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-06.
REMARK 100 THE RCSB ID CODE IS RCSB040988.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-02
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL9-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97900
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(311) BENT
REMARK 200                                   (HORIZONTAL FOCUSING)
REMARK 200  OPTICS                         : VERTICAL FOCUSING MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11287
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 4.400
REMARK 200  R MERGE                    (I) : 0.03900
REMARK 200  R SYM                      (I) : 0.03900
REMARK 200   FOR THE DATA SET  : 5.0000
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     (%) : 99.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.41800
REMARK 200  R SYM FOR SHELL            (I) : 0.41800
REMARK 200   FOR SHELL         : 2.000
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: PDB ENTRY 1PLQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 65.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M (NH4)2SO4, SODIUM CITRATE, PH
REMARK 280  5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   Z,X,Y
REMARK 290       6555   Z,-X,-Y
REMARK 290       7555   -Z,-X,Y
REMARK 290       8555   -Z,X,-Y
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z,-X
REMARK 290      11555   Y,-Z,-X
REMARK 290      12555   -Y,-Z,X
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2
REMARK 290      24555   -Y+1/2,-Z+1/2,X+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        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        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       69.64000
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       69.64000
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       69.64000
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       69.64000
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       69.64000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       69.64000
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       69.64000
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       69.64000
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       69.64000
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       69.64000
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       69.64000
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       69.64000
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       69.64000
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       69.64000
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       69.64000
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       69.64000
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       69.64000
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       69.64000
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       69.64000
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       69.64000
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       69.64000
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       69.64000
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       69.64000
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       69.64000
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       69.64000
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       69.64000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: -Y, Z, -X AND -Z,
REMARK 300 -X, Y
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: HEXAMERIC
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   BIOMT1   2  0.000000  0.000000 -1.000000      139.28000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      139.28000
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      139.28000
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000      139.28000
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     ASP A   256
REMARK 465     GLU A   257
REMARK 465     GLU A   258
REMARK 465     ALA B    32
REMARK 465     GLY B    33
REMARK 465     LYS B    34
REMARK 465     THR B    46
REMARK 465     SER B    47
REMARK 465     MET B    48
REMARK 465     LYS B    49
REMARK 465     ASN B    50
REMARK 465     LYS B    51
REMARK 465     PRO B    52
REMARK 465     THR B    53
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    GLN A  24      -61.74   -101.61
REMARK 500    LYS A  31     -152.65   -116.39
REMARK 500    ASN A  83       87.73    -68.94
REMARK 500    ARG A 110       54.41   -146.43
REMARK 500    ASP A 122       47.35     75.15
REMARK 500    ALA A 123     -161.13   -122.20
REMARK 500    THR A 163     -164.41   -112.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAIN B IS THE PEPTIDE SYNTHESIZED BASED ON SEQUENCE OF
REMARK 999 RESIDUES 32-53 OF CDC9 (UNP P04819) SHOWN IN DBREF.
DBREF  2OD8 A    1   258  UNP    P15873   PCNA_YEAST       1    258
DBREF  2OD8 B   32    53  UNP    P04819   DNLI_YEAST      32     53
SEQRES   1 A  258  MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE LYS
SEQRES   2 A  258  ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU VAL
SEQRES   3 A  258  ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN ALA
SEQRES   4 A  258  VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU ILE
SEQRES   5 A  258  GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS PRO
SEQRES   6 A  258  VAL THR LEU GLY MET ASP LEU THR SER LEU SER LYS ILE
SEQRES   7 A  258  LEU ARG CYS GLY ASN ASN THR ASP THR LEU THR LEU ILE
SEQRES   8 A  258  ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE GLU
SEQRES   9 A  258  ASP THR LYS LYS ASP ARG ILE ALA GLU TYR SER LEU LYS
SEQRES  10 A  258  LEU MET ASP ILE ASP ALA ASP PHE LEU LYS ILE GLU GLU
SEQRES  11 A  258  LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER GLU
SEQRES  12 A  258  PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER ASP
SEQRES  13 A  258  SER ILE ASN ILE MET ILE THR LYS GLU THR ILE LYS PHE
SEQRES  14 A  258  VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE ILE
SEQRES  15 A  258  LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER ILE
SEQRES  16 A  258  LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE GLY
SEQRES  17 A  258  ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER LEU
SEQRES  18 A  258  SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA PRO
SEQRES  19 A  258  ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU GLN
SEQRES  20 A  258  PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU
SEQRES   1 B   22  ALA GLY LYS LYS PRO LYS GLN ALA THR LEU ALA ARG PHE
SEQRES   2 B   22  PHE THR SER MET LYS ASN LYS PRO THR
FORMUL   3  HOH   *18(H2 O)
HELIX    1   1 GLU A    8  GLY A   18  1                                  11
HELIX    2   2 LEU A   72  ARG A   80  1                                   9
HELIX    3   3 SER A  141  SER A  152  1                                  12
HELIX    4   4 HIS A  190  SER A  194  5                                   5
HELIX    5   5 ALA A  209  ILE A  216  1                                   8
HELIX    6   6 LYS A  217  LEU A  221  5                                   5
HELIX    7   7 THR B   40  PHE B   45  5                                   6
SHEET    1   A 5 PHE A  57  CYS A  62  0
SHEET    2   A 5 LEU A   2  PHE A   6 -1  N  GLU A   3   O  ARG A  61
SHEET    3   A 5 THR A  87  ALA A  92 -1  O  LEU A  88   N  PHE A   6
SHEET    4   A 5 SER A  98  GLU A 104 -1  O  ILE A 100   N  ILE A  91
SHEET    5   A 5 ALA A 112  LYS A 117 -1  O  ALA A 112   N  PHE A 103
SHEET    1   B 9 VAL A  66  ASP A  71  0
SHEET    2   B 9 LEU A  25  CYS A  30 -1  N  CYS A  30   O  VAL A  66
SHEET    3   B 9 ILE A  35  VAL A  40 -1  O  ILE A  36   N  GLN A  29
SHEET    4   B 9 LEU A  46  ILE A  52 -1  O  VAL A  48   N  ALA A  39
SHEET    5   B 9 GLY A 244  LEU A 250 -1  O  GLN A 247   N  SER A  49
SHEET    6   B 9 ALA A 235  LEU A 241 -1  N  PHE A 237   O  PHE A 248
SHEET    7   B 9 ARG A 224  LEU A 229 -1  N  GLY A 226   O  GLN A 238
SHEET    8   B 9 SER A 135  PRO A 140 -1  N  LEU A 137   O  ILE A 227
SHEET    9   B 9 LYS A 196  MET A 199 -1  O  LYS A 196   N  SER A 138
SHEET    1   C 4 SER A 177  ILE A 182  0
SHEET    2   C 4 THR A 166  ASP A 172 -1  N  PHE A 169   O  VAL A 180
SHEET    3   C 4 SER A 157  THR A 163 -1  N  ASN A 159   O  VAL A 170
SHEET    4   C 4 VAL A 203  GLY A 208 -1  O  PHE A 207   N  ILE A 158
SHEET    1   D 2 LYS A 253  PHE A 254  0
SHEET    2   D 2 LYS B  37  GLN B  38 -1  O  LYS B  37   N  PHE A 254
CISPEP   1 ILE A   52    GLY A   53          0         9.56
CISPEP   2 ASN A   84    THR A   85          0         3.31
CISPEP   3 LYS A  108    ASP A  109          0         5.36
CISPEP   4 ILE A  121    ASP A  122          0        22.80
CISPEP   5 GLU A  129    GLU A  130          0       -19.59
CISPEP   6 LYS A  242    SER A  243          0         3.64
CRYST1  139.280  139.280  139.280  90.00  90.00  90.00 I 2 3        24
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      0.007180  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007180  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007180        0.00000
      
PROCHECK
Go to PROCHECK summary
 References