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PDBsum entry 1qri

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Hydrolase/DNA PDB id
1qri
Jmol
Contents
Protein chain
261 a.a.
DNA/RNA
Waters ×52
HEADER    HYDROLASE/DNA                           14-JUN-99   1QRI
TITLE     X-RAY STRUCTURE OF THE DNA-ECO RI ENDONUCLEASE COMPLEXES
TITLE    2 WITH AN E144D MUTATION AT 2.7 A
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*TP*CP*GP*CP*GP*AP*AP*TP*TP*CP*GP*CP*G)-3';
COMPND   3 CHAIN: M;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: ECO RI ENDONCULEASE;
COMPND   7 CHAIN: A;
COMPND   8 FRAGMENT: RESIDUES 17-277;
COMPND   9 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   5 ORGANISM_TAXID: 562
KEYWDS    RESTRICTION ENDONUCLEASE, DNA-PROTEIN COMPLEX, SITE-
KEYWDS   2 DIRECTED MUTATION, SEQUENCE-SPECIFIC, X-RAY CRYSTALLOGRAPHY,
KEYWDS   3 PROTEIN STRUCTURE, HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.CHOI,Y.KIM,P.GREENE,P.HAGER,J.M.ROSENBERG
REVDAT   4   24-FEB-09 1QRI    1       VERSN
REVDAT   3   26-SEP-01 1QRI    3       ATOM
REVDAT   2   27-MAR-00 1QRI    1       DBREF  SEQADV REMARK
REVDAT   1   23-JUN-99 1QRI    0
JRNL        AUTH   J.CHOI,Y.KIM,P.GREENE,P.HAGER,J.M.ROSENBERG
JRNL        TITL   X-RAY STRUCTURE OF THE DNA-ECO RI ENDONUCLEASE
JRNL        TITL 2 COMPLEXES WITH THE ED144 AND RK145 MUTATIONS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
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) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 7040
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) : 0.164
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            : 2530
REMARK   3   NUCLEIC ACID ATOMS       : 292
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 52
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.04
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) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
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: 52 WATER MOLECULES FIT INTO
REMARK   3  DIFFERENCE MAPS
REMARK   4
REMARK   4 1QRI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-99.
REMARK 100 THE RCSB ID CODE IS RCSB009180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS-NICOLET X100
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200  DATA SCALING SOFTWARE          : XENGEN
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7508
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.620
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.600
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 61.0
REMARK 200  DATA REDUNDANCY                : 7.000
REMARK 200  R MERGE                    (I) : 0.07200
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) : 2.62
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.78
REMARK 200  COMPLETENESS FOR SHELL     (%) : 10.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.13300
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITANT: 40% PEG 400; 40 MM
REMARK 280  BTP; PH 8.0; RESERVOIR: 16% PEG 400; 40 MM BTP; PH 6.5; DROP:
REMARK 280  5 UL PROTEIN, 2 UL DNA, 1 UL PPT, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z
REMARK 290       6555   -X,-X+Y,-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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  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: M, A
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 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
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     DG M   3   O4' -  C1' -  C2' ANGL. DEV. =  -8.4 DEGREES
REMARK 500     DG M   3   O3' -  P   -  O5' ANGL. DEV. = -25.9 DEGREES
REMARK 500     DG M   3   O3' -  P   -  OP1 ANGL. DEV. =  22.0 DEGREES
REMARK 500     DC M   4   C3' -  C2' -  C1' ANGL. DEV. =   7.7 DEGREES
REMARK 500     DC M   4   O3' -  P   -  OP2 ANGL. DEV. =  10.0 DEGREES
REMARK 500     DG M   5   O4' -  C4' -  C3' ANGL. DEV. =  -7.6 DEGREES
REMARK 500     DA M   6   C4' -  C3' -  C2' ANGL. DEV. =  -5.5 DEGREES
REMARK 500     DA M   7   O4' -  C1' -  C2' ANGL. DEV. =  -5.3 DEGREES
REMARK 500     DA M   7   O3' -  P   -  O5' ANGL. DEV. = -14.8 DEGREES
REMARK 500     DA M   7   O3' -  P   -  OP2 ANGL. DEV. = -30.4 DEGREES
REMARK 500     DA M   7   O3' -  P   -  OP1 ANGL. DEV. =  38.6 DEGREES
REMARK 500     DT M   8   C6  -  C5  -  C7  ANGL. DEV. =  -5.1 DEGREES
REMARK 500     DT M   8   O3' -  P   -  OP1 ANGL. DEV. =   7.0 DEGREES
REMARK 500     DT M   9   C6  -  C5  -  C7  ANGL. DEV. =  -5.4 DEGREES
REMARK 500     DT M   9   O3' -  P   -  OP2 ANGL. DEV. =  12.8 DEGREES
REMARK 500     DC M  10   O4' -  C1' -  C2' ANGL. DEV. =  -6.5 DEGREES
REMARK 500     DC M  10   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES
REMARK 500     DG M  11   O4' -  C1' -  N9  ANGL. DEV. =  -4.5 DEGREES
REMARK 500     DG M  11   O3' -  P   -  O5' ANGL. DEV. = -21.3 DEGREES
REMARK 500     DG M  11   O3' -  P   -  OP1 ANGL. DEV. =  26.4 DEGREES
REMARK 500     DC M  12   O4' -  C1' -  C2' ANGL. DEV. =  -7.6 DEGREES
REMARK 500     DC M  12   O4' -  C1' -  N1  ANGL. DEV. =   3.8 DEGREES
REMARK 500     DG M  13   O4' -  C1' -  C2' ANGL. DEV. =  -6.5 DEGREES
REMARK 500     DG M  13   O4' -  C1' -  N9  ANGL. DEV. =   5.1 DEGREES
REMARK 500     DG M  13   O3' -  P   -  O5' ANGL. DEV. = -19.0 DEGREES
REMARK 500     DG M  13   O3' -  P   -  OP2 ANGL. DEV. = -32.4 DEGREES
REMARK 500     DG M  13   O3' -  P   -  OP1 ANGL. DEV. =  45.3 DEGREES
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    ASN A  85       48.45   -100.67
REMARK 500    ASP A  91        1.78    -66.70
REMARK 500    ASN A 124     -153.86    -91.68
REMARK 500    VAL A 128     -160.00    -92.40
REMARK 500    PRO A 184       11.60    -62.76
REMARK 500    HIS A 225      -65.85   -159.28
REMARK 500    LYS A 226     -126.87    -96.61
REMARK 500    LYS A 228       92.63    -49.28
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     DG M   5         0.05    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CKQ   RELATED DB: PDB
REMARK 900 1.85 A COGNATE PRE-TRANSITION STATE ECORI-DNA CRYSTAL
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1QPS   RELATED DB: PDB
REMARK 900 2.5 A COGNATE POST-REACTIVE ECO-RI DNA CRYSTAL STRUCTURE IN
REMARK 900 THE PRESENCE OF MN2+
REMARK 900 RELATED ID: 1QC9   RELATED DB: PDB
REMARK 900 3.3 A CRYSTAL STRUCTURE OF ECO RI DIMER IN THE ABSENCE OF
REMARK 900 DNA
REMARK 900 RELATED ID: 1CL8   RELATED DB: PDB
REMARK 900 1.80 A CRYSTAL STRUCTURE OF A COGNATE ECO RI-DNA COMPLEX
REMARK 900 WITH A BASE ANALOG SUBSTITUTION IN THE DNA RECOGNITION
REMARK 900 REGION
DBREF  1QRI A   17   277  UNP    P00642   T2E1_ECOLI      16    276
DBREF  1QRI M    1    13  PDB    1QRI     1QRI             1     13
SEQADV 1QRI ASP A  144  UNP  P00642    GLU   143 ENGINEERED
SEQRES   1 M   13   DT  DC  DG  DC  DG  DA  DA  DT  DT  DC  DG  DC  DG
SEQRES   1 A  261  SER GLN GLY VAL ILE GLY ILE PHE GLY ASP TYR ALA LYS
SEQRES   2 A  261  ALA HIS ASP LEU ALA VAL GLY GLU VAL SER LYS LEU VAL
SEQRES   3 A  261  LYS LYS ALA LEU SER ASN GLU TYR PRO GLN LEU SER PHE
SEQRES   4 A  261  ARG TYR ARG ASP SER ILE LYS LYS THR GLU ILE ASN GLU
SEQRES   5 A  261  ALA LEU LYS LYS ILE ASP PRO ASP LEU GLY GLY THR LEU
SEQRES   6 A  261  PHE VAL SER ASN SER SER ILE LYS PRO ASP GLY GLY ILE
SEQRES   7 A  261  VAL GLU VAL LYS ASP ASP TYR GLY GLU TRP ARG VAL VAL
SEQRES   8 A  261  LEU VAL ALA GLU ALA LYS HIS GLN GLY LYS ASP ILE ILE
SEQRES   9 A  261  ASN ILE ARG ASN GLY LEU LEU VAL GLY LYS ARG GLY ASP
SEQRES  10 A  261  GLN ASP LEU MET ALA ALA GLY ASN ALA ILE ASP ARG SER
SEQRES  11 A  261  HIS LYS ASN ILE SER GLU ILE ALA ASN PHE MET LEU SER
SEQRES  12 A  261  GLU SER HIS PHE PRO TYR VAL LEU PHE LEU GLU GLY SER
SEQRES  13 A  261  ASN PHE LEU THR GLU ASN ILE SER ILE THR ARG PRO ASP
SEQRES  14 A  261  GLY ARG VAL VAL ASN LEU GLU TYR ASN SER GLY ILE LEU
SEQRES  15 A  261  ASN ARG LEU ASP ARG LEU THR ALA ALA ASN TYR GLY MET
SEQRES  16 A  261  PRO ILE ASN SER ASN LEU CYS ILE ASN LYS PHE VAL ASN
SEQRES  17 A  261  HIS LYS ASP LYS SER ILE MET LEU GLN ALA ALA SER ILE
SEQRES  18 A  261  TYR THR GLN GLY ASP GLY ARG GLU TRP ASP SER LYS ILE
SEQRES  19 A  261  MET PHE GLU ILE MET PHE ASP ILE SER THR THR SER LEU
SEQRES  20 A  261  ARG VAL LEU GLY ARG ASP LEU PHE GLU GLN LEU THR SER
SEQRES  21 A  261  LYS
FORMUL   3  HOH   *52(H2 O)
HELIX    1   1 GLY A   19  ALA A   30  1                                  12
HELIX    2   2 ALA A   34  TYR A   50  1                                  17
HELIX    3   3 LYS A   63  LYS A   72  1                                  10
HELIX    4   4 LYS A  117  ASN A  124  1                                   8
HELIX    5   5 ASN A  141  ASP A  144  5                                   4
HELIX    6   6 ARG A  145  MET A  157  1                                  13
HELIX    7   7 ARG A  187  LEU A  191  5                                   5
HELIX    8   8 ASP A  247  LEU A  266  1                                  20
HELIX    9   9 GLY A  267  ASP A  269  5                                   3
HELIX   10  10 LEU A  270  SER A  276  1                                   7
SHEET    1   A 5 SER A  54  ARG A  58  0
SHEET    2   A 5 ILE A  94  LYS A  98 -1  O  ILE A  94   N  ARG A  58
SHEET    3   A 5 TRP A 104  HIS A 114 -1  N  ARG A 105   O  VAL A  97
SHEET    4   A 5 TYR A 165  GLU A 170  1  N  VAL A 166   O  VAL A 109
SHEET    5   A 5 SER A 236  THR A 239  1  O  SER A 236   N  LEU A 167
SHEET    1   B 2 ILE A  61  LYS A  62  0
SHEET    2   B 2 SER A  87  ILE A  88 -1  N  ILE A  88   O  ILE A  61
SHEET    1   C 2 ILE A 179  THR A 182  0
SHEET    2   C 2 VAL A 188  LEU A 191 -1  N  VAL A 189   O  ILE A 181
SHEET    1   D 2 LYS A 221  VAL A 223  0
SHEET    2   D 2 ILE A 230  LEU A 232 -1  N  ILE A 230   O  VAL A 223
CRYST1  118.400  118.400   49.700  90.00  90.00 120.00 P 3 2 1       6
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      0.008446  0.004876  0.000000        0.00000
SCALE2      0.000000  0.009753  0.000000        0.00000
SCALE3      0.000000  0.000000  0.020121        0.00000
      
PROCHECK
Go to PROCHECK summary
 References