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PDBsum entry 1pvi

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Hydrolase/DNA PDB id
1pvi
Jmol
Contents
Protein chains
156 a.a.
DNA/RNA
HEADER    HYDROLASE/DNA                           16-NOV-94   1PVI
TITLE     STRUCTURE OF PVUII ENDONUCLEASE WITH COGNATE DNA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-
COMPND   3 D(*TP*GP*AP*CP*CP*AP*GP*CP*TP*GP*GP*TP*C)-3');
COMPND   4 CHAIN: C, D;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: PROTEIN (PVUII (E.C.3.1.21.4));
COMPND   8 CHAIN: A, B
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 ORGANISM_SCIENTIFIC: PROTEUS VULGARIS;
SOURCE   5 ORGANISM_TAXID: 585
KEYWDS    PROTEIN-DNA COMPLEX, HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.CHENG,K.BALENDIRAN,I.SCHILDKRAUT,J.E.ANDERSON
REVDAT   3   24-FEB-09 1PVI    1       VERSN
REVDAT   2   15-MAY-95 1PVI    1       REMARK
REVDAT   1   14-FEB-95 1PVI    0
JRNL        AUTH   X.CHENG,K.BALENDIRAN,I.SCHILDKRAUT,J.E.ANDERSON
JRNL        TITL   STRUCTURE OF PVUII ENDONUCLEASE WITH COGNATE DNA.
JRNL        REF    EMBO J.                       V.  13  3927 1994
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   8076590
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.BALENDIRAN,J.BONVENTRE,R.KNOTT,W.JACK,J.BENNER,
REMARK   1  AUTH 2 I.SCHILDKRAUT,J.E.ANDERSON
REMARK   1  TITL   EXPRESSION, PURIFICATION, AND CRYSTALLIZATION OF
REMARK   1  TITL 2 RESTRICTION ENDONUCLEASE PVUII WITH DNA CONTAINING
REMARK   1  TITL 3 ITS RECOGNITION SITE
REMARK   1  REF    PROTEINS                      V.  19    77 1994
REMARK   1  REFN                   ISSN 0887-3585
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.7
REMARK   3   NUMBER OF REFLECTIONS             : 9799
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.189
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2670
REMARK   3   NUCLEIC ACID ATOMS       : 526
REMARK   3   HETEROGEN ATOMS          : 0
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) : NULL
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.012
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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  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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1PVI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : 4.400
REMARK 200  R MERGE                    (I) : 0.07000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       47.90000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       24.25000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.15000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       24.25000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.90000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.15000
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: C, D, 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     MET A     1
REMARK 465     MET B     1
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     TYR A  94    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     TYR B  94    CG   CD1  CD2  CE1  CE2  CZ   OH
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     DT C   2   C5'    DT C   2   C4'     0.082
REMARK 500     DT C   2   C2'    DT C   2   C1'     0.065
REMARK 500     DT C   2   N1     DT C   2   C2      0.075
REMARK 500     DT C   2   C2     DT C   2   N3      0.060
REMARK 500     DT C   2   C4     DT C   2   C5      0.059
REMARK 500     DT C   2   C5     DT C   2   C7      0.046
REMARK 500     DG C   3   P      DG C   3   O5'     0.081
REMARK 500     DG C   3   C4'    DG C   3   C3'    -0.068
REMARK 500     DA C   4   O3'    DA C   4   C3'    -0.042
REMARK 500     DA C   4   N3     DA C   4   C4      0.041
REMARK 500     DC C   5   N1     DC C   5   C2     -0.063
REMARK 500     DC C   6   N1     DC C   6   C2     -0.072
REMARK 500     DC C   6   N1     DC C   6   C6     -0.074
REMARK 500     DA C   7   C4     DA C   7   C5     -0.049
REMARK 500     DA C   7   C5     DA C   7   N7      0.043
REMARK 500     DC C   6   O3'    DA C   7   P      -0.074
REMARK 500     DG C   8   P      DG C   8   O5'     0.082
REMARK 500     DG C   8   C2     DG C   8   N3     -0.057
REMARK 500     DG C   8   C2     DG C   8   N2     -0.070
REMARK 500     DC C   9   P      DC C   9   O5'     0.072
REMARK 500     DC C   9   C5'    DC C   9   C4'    -0.068
REMARK 500     DT C  10   C4     DT C  10   C5     -0.059
REMARK 500     DG C  11   O4'    DG C  11   C4'     0.069
REMARK 500     DG C  12   C2'    DG C  12   C1'    -0.061
REMARK 500     DT C  13   C2'    DT C  13   C1'    -0.065
REMARK 500     DC C  14   C5'    DC C  14   C4'     0.083
REMARK 500     DC C  14   C4'    DC C  14   C3'     0.065
REMARK 500     DT D   2   C5'    DT D   2   C4'     0.109
REMARK 500     DT D   2   N1     DT D   2   C2      0.079
REMARK 500     DT D   2   C4     DT D   2   C5      0.056
REMARK 500     DT D   2   C5     DT D   2   C7      0.112
REMARK 500     DG D   3   C5'    DG D   3   C4'    -0.092
REMARK 500     DG D   3   N7     DG D   3   C8      0.040
REMARK 500     DA D   7   P      DA D   7   O5'     0.073
REMARK 500     DA D   7   C6     DA D   7   N1     -0.051
REMARK 500     DG D   8   C6     DG D   8   N1     -0.045
REMARK 500     DT D  10   O4'    DT D  10   C4'    -0.063
REMARK 500     DT D  10   N1     DT D  10   C2      0.074
REMARK 500     DT D  10   C2     DT D  10   N3      0.098
REMARK 500     DT D  10   C2     DT D  10   O2      0.065
REMARK 500     DT D  10   C5     DT D  10   C7     -0.049
REMARK 500     DG D  11   C5'    DG D  11   C4'     0.047
REMARK 500     DG D  11   N9     DG D  11   C4     -0.051
REMARK 500     DG D  12   C5'    DG D  12   C4'     0.120
REMARK 500     DG D  12   C5     DG D  12   N7      0.037
REMARK 500     DG D  12   C8     DG D  12   N9      0.043
REMARK 500     DT D  13   C2     DT D  13   N3      0.059
REMARK 500     DC D  14   C3'    DC D  14   C2'     0.077
REMARK 500     DC D  14   C1'    DC D  14   N1      0.081
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 C   2   C4' -  C3' -  C2' ANGL. DEV. =  -4.6 DEGREES
REMARK 500     DT C   2   O4' -  C1' -  C2' ANGL. DEV. = -10.1 DEGREES
REMARK 500     DT C   2   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES
REMARK 500     DT C   2   C4  -  C5  -  C7  ANGL. DEV. =   6.3 DEGREES
REMARK 500     DT C   2   C6  -  C5  -  C7  ANGL. DEV. =  -9.8 DEGREES
REMARK 500     DG C   3   O4' -  C4' -  C3' ANGL. DEV. =  -2.7 DEGREES
REMARK 500     DG C   3   C5' -  C4' -  O4' ANGL. DEV. =   7.1 DEGREES
REMARK 500     DG C   3   N9  -  C4  -  C5  ANGL. DEV. =   2.8 DEGREES
REMARK 500     DT C   2   C3' -  O3' -  P   ANGL. DEV. =  11.3 DEGREES
REMARK 500     DA C   4   C3' -  C2' -  C1' ANGL. DEV. = -10.7 DEGREES
REMARK 500     DA C   4   O4' -  C1' -  C2' ANGL. DEV. =  -6.6 DEGREES
REMARK 500     DA C   4   O4' -  C1' -  N9  ANGL. DEV. =   7.0 DEGREES
REMARK 500     DA C   4   N1  -  C6  -  N6  ANGL. DEV. =   4.4 DEGREES
REMARK 500     DA C   4   C5  -  C6  -  N6  ANGL. DEV. =  -5.0 DEGREES
REMARK 500     DC C   5   O4' -  C4' -  C3' ANGL. DEV. =  -4.7 DEGREES
REMARK 500     DC C   5   C4' -  C3' -  C2' ANGL. DEV. =  -4.8 DEGREES
REMARK 500     DC C   5   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES
REMARK 500     DC C   5   C2  -  N3  -  C4  ANGL. DEV. =   4.1 DEGREES
REMARK 500     DA C   4   C3' -  O3' -  P   ANGL. DEV. = -11.2 DEGREES
REMARK 500     DC C   6   O4' -  C4' -  C3' ANGL. DEV. =  -4.1 DEGREES
REMARK 500     DC C   6   C4' -  C3' -  C2' ANGL. DEV. =  -8.1 DEGREES
REMARK 500     DC C   6   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES
REMARK 500     DC C   6   C2  -  N3  -  C4  ANGL. DEV. =   3.9 DEGREES
REMARK 500     DC C   6   N3  -  C4  -  C5  ANGL. DEV. =  -5.9 DEGREES
REMARK 500     DA C   7   C3' -  C2' -  C1' ANGL. DEV. =  -7.0 DEGREES
REMARK 500     DA C   7   O4' -  C1' -  C2' ANGL. DEV. =   3.5 DEGREES
REMARK 500     DA C   7   N7  -  C8  -  N9  ANGL. DEV. =  -3.5 DEGREES
REMARK 500     DC C   6   C3' -  O3' -  P   ANGL. DEV. =   7.6 DEGREES
REMARK 500     DG C   8   O4' -  C4' -  C3' ANGL. DEV. =   3.7 DEGREES
REMARK 500     DG C   8   O4' -  C1' -  N9  ANGL. DEV. =   6.6 DEGREES
REMARK 500     DG C   8   C2  -  N3  -  C4  ANGL. DEV. =  -3.1 DEGREES
REMARK 500     DG C   8   N3  -  C2  -  N2  ANGL. DEV. =  -5.8 DEGREES
REMARK 500     DA C   7   C3' -  O3' -  P   ANGL. DEV. =   7.5 DEGREES
REMARK 500     DC C   9   C5' -  C4' -  C3' ANGL. DEV. = -12.0 DEGREES
REMARK 500     DC C   9   C3' -  C2' -  C1' ANGL. DEV. =  -5.4 DEGREES
REMARK 500     DC C   9   O4' -  C1' -  N1  ANGL. DEV. =  10.1 DEGREES
REMARK 500     DC C   9   C2  -  N1  -  C1' ANGL. DEV. =  -7.1 DEGREES
REMARK 500     DT C  10   C1' -  O4' -  C4' ANGL. DEV. = -17.7 DEGREES
REMARK 500     DT C  10   C4' -  C3' -  C2' ANGL. DEV. = -13.8 DEGREES
REMARK 500     DT C  10   C4  -  C5  -  C6  ANGL. DEV. =   5.2 DEGREES
REMARK 500     DT C  10   C6  -  C5  -  C7  ANGL. DEV. =  -5.1 DEGREES
REMARK 500     DC C   9   C3' -  O3' -  P   ANGL. DEV. =   7.4 DEGREES
REMARK 500     DG C  11   O4' -  C4' -  C3' ANGL. DEV. =  10.0 DEGREES
REMARK 500     DG C  11   C5' -  C4' -  C3' ANGL. DEV. = -14.5 DEGREES
REMARK 500     DG C  11   C5' -  C4' -  O4' ANGL. DEV. =  10.1 DEGREES
REMARK 500     DG C  11   C1' -  O4' -  C4' ANGL. DEV. =  -9.4 DEGREES
REMARK 500     DG C  11   C4' -  C3' -  C2' ANGL. DEV. = -10.1 DEGREES
REMARK 500     DG C  11   O4' -  C1' -  N9  ANGL. DEV. =   9.3 DEGREES
REMARK 500     DG C  11   C2  -  N3  -  C4  ANGL. DEV. =   3.6 DEGREES
REMARK 500     DG C  11   N3  -  C4  -  C5  ANGL. DEV. =  -4.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     150 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    LEU A  40      -32.48    -38.62
REMARK 500    ALA A  63       15.43   -143.05
REMARK 500    THR A  82      -84.19   -129.28
REMARK 500    HIS A  85       79.47   -150.60
REMARK 500    ARG A  95      -53.74    -28.54
REMARK 500    SER A 133       52.34    -69.92
REMARK 500    ASP A 134       -9.60   -168.52
REMARK 500    PRO B  52      151.47    -44.47
REMARK 500    ASN B  62        6.63    -58.53
REMARK 500    ILE B  74      -15.58    -48.22
REMARK 500    LEU B  76       -8.32   -152.55
REMARK 500    THR B  82      -76.74   -123.97
REMARK 500    ARG B  95      -11.44    -47.85
REMARK 500    ILE B 107       68.47   -117.33
REMARK 500    ASN B 141       60.14     60.27
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     DT C   2         0.10    SIDE_CHAIN
REMARK 500     DA C   7         0.06    SIDE_CHAIN
REMARK 500     DG C   8         0.06    SIDE_CHAIN
REMARK 500     DG C  11         0.07    SIDE_CHAIN
REMARK 500     DT C  13         0.11    SIDE_CHAIN
REMARK 500     DT D   2         0.11    SIDE_CHAIN
REMARK 500     DG D   3         0.06    SIDE_CHAIN
REMARK 500     DC D   6         0.12    SIDE_CHAIN
REMARK 500     DC D   9         0.06    SIDE_CHAIN
REMARK 500     DG D  12         0.06    SIDE_CHAIN
REMARK 500     DT D  13         0.07    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1PVI A    1   157  UNP    P23657   T2P2_PROVU       1    157
DBREF  1PVI B    1   157  UNP    P23657   T2P2_PROVU       1    157
DBREF  1PVI C    2    14  PDB    1PVI     1PVI             2     14
DBREF  1PVI D    2    14  PDB    1PVI     1PVI             2     14
SEQRES   1 C   13   DT  DG  DA  DC  DC  DA  DG  DC  DT  DG  DG  DT  DC
SEQRES   1 D   13   DT  DG  DA  DC  DC  DA  DG  DC  DT  DG  DG  DT  DC
SEQRES   1 A  157  MET SER HIS PRO ASP LEU ASN LYS LEU LEU GLU LEU TRP
SEQRES   2 A  157  PRO HIS ILE GLN GLU TYR GLN ASP LEU ALA LEU LYS HIS
SEQRES   3 A  157  GLY ILE ASN ASP ILE PHE GLN ASP ASN GLY GLY LYS LEU
SEQRES   4 A  157  LEU GLN VAL LEU LEU ILE THR GLY LEU THR VAL LEU PRO
SEQRES   5 A  157  GLY ARG GLU GLY ASN ASP ALA VAL ASP ASN ALA GLY GLN
SEQRES   6 A  157  GLU TYR GLU LEU LYS SER ILE ASN ILE ASP LEU THR LYS
SEQRES   7 A  157  GLY PHE SER THR HIS HIS HIS MET ASN PRO VAL ILE ILE
SEQRES   8 A  157  ALA LYS TYR ARG GLN VAL PRO TRP ILE PHE ALA ILE TYR
SEQRES   9 A  157  ARG GLY ILE ALA ILE GLU ALA ILE TYR ARG LEU GLU PRO
SEQRES  10 A  157  LYS ASP LEU GLU PHE TYR TYR ASP LYS TRP GLU ARG LYS
SEQRES  11 A  157  TRP TYR SER ASP GLY HIS LYS ASP ILE ASN ASN PRO LYS
SEQRES  12 A  157  ILE PRO VAL LYS TYR VAL MET GLU HIS GLY THR LYS ILE
SEQRES  13 A  157  TYR
SEQRES   1 B  157  MET SER HIS PRO ASP LEU ASN LYS LEU LEU GLU LEU TRP
SEQRES   2 B  157  PRO HIS ILE GLN GLU TYR GLN ASP LEU ALA LEU LYS HIS
SEQRES   3 B  157  GLY ILE ASN ASP ILE PHE GLN ASP ASN GLY GLY LYS LEU
SEQRES   4 B  157  LEU GLN VAL LEU LEU ILE THR GLY LEU THR VAL LEU PRO
SEQRES   5 B  157  GLY ARG GLU GLY ASN ASP ALA VAL ASP ASN ALA GLY GLN
SEQRES   6 B  157  GLU TYR GLU LEU LYS SER ILE ASN ILE ASP LEU THR LYS
SEQRES   7 B  157  GLY PHE SER THR HIS HIS HIS MET ASN PRO VAL ILE ILE
SEQRES   8 B  157  ALA LYS TYR ARG GLN VAL PRO TRP ILE PHE ALA ILE TYR
SEQRES   9 B  157  ARG GLY ILE ALA ILE GLU ALA ILE TYR ARG LEU GLU PRO
SEQRES  10 B  157  LYS ASP LEU GLU PHE TYR TYR ASP LYS TRP GLU ARG LYS
SEQRES  11 B  157  TRP TYR SER ASP GLY HIS LYS ASP ILE ASN ASN PRO LYS
SEQRES  12 B  157  ILE PRO VAL LYS TYR VAL MET GLU HIS GLY THR LYS ILE
SEQRES  13 B  157  TYR
HELIX    1   1 PRO A    4  HIS A   26  5                                  23
HELIX    2   2 GLY A   36  THR A   46  1                                  11
HELIX    3   3 PRO A   88  ARG A   95  1                                   8
HELIX    4   4 PRO A  117  TYR A  132  1                                  16
HELIX    5   5 VAL A  146  HIS A  152  1                                   7
HELIX    6   6 PRO B    4  HIS B   26  5                                  23
HELIX    7   7 GLY B   36  THR B   46  1                                  11
HELIX    8   8 PRO B   88  LYS B   93  1                                   6
HELIX    9   9 PRO B  117  ASP B  134  1                                  18
HELIX   10  10 VAL B  146  MET B  150  1                                   5
SHEET    1   A 4 ASP A  58  VAL A  60  0
SHEET    2   A 4 GLU A  66  ASN A  73 -1  N  TYR A  67   O  ALA A  59
SHEET    3   A 4 PRO A  98  ARG A 105  1  N  PRO A  98   O  GLU A  68
SHEET    4   A 4 ALA A 108  LEU A 115 -1  N  LEU A 115   O  TRP A  99
SHEET    1   B 3 TYR B  67  ASN B  73  0
SHEET    2   B 3 PRO B  98  TYR B 104  1  N  PRO B  98   O  GLU B  68
SHEET    3   B 3 ILE B 109  LEU B 115 -1  N  LEU B 115   O  TRP B  99
CRYST1   95.800   86.300   48.500  90.00  90.00  90.00 P 21 21 21    8
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      0.010438  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.020619        0.00000
      
PROCHECK
Go to PROCHECK summary
 References