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PDBsum entry 1fok

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Hydrolase/DNA PDB id
1fok
Jmol
Contents
Protein chain
568 a.a.
DNA/RNA
Waters ×172
HEADER    HYDROLASE/DNA                           18-APR-97   1FOK
TITLE     STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI BOUND TO DNA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-
COMPND   3 D(*TP*CP*GP*GP*AP*TP*GP*AP*TP*AP*AP*CP*GP*CP*TP*AP*G
COMPND   4 P*TP*CP*A)-3');
COMPND   5 CHAIN: B;
COMPND   6 SYNONYM: R.FOKI;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: DNA (5'-
COMPND  10 D(*AP*TP*GP*AP*CP*TP*AP*GP*CP*GP*TP*TP*AP*TP*CP*AP*T
COMPND  11 P*CP*CP*G)-3');
COMPND  12 CHAIN: C;
COMPND  13 ENGINEERED: YES;
COMPND  14 MOL_ID: 3;
COMPND  15 MOLECULE: PROTEIN (FOKI RESTRICTION ENDONUCLEAS);
COMPND  16 CHAIN: A;
COMPND  17 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PLANOMICROBIUM OKEANOKOITES;
SOURCE   3 ORGANISM_TAXID: 244;
SOURCE   4 STRAIN: IFO12536;
SOURCE   5 ATCC: 33414;
SOURCE   6 GENE: FOKI;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 MOL_ID: 2;
SOURCE  10 MOL_ID: 3;
SOURCE  11 ORGANISM_SCIENTIFIC: PLANOMICROBIUM OKEANOKOITES;
SOURCE  12 ORGANISM_TAXID: 244
KEYWDS    COMPLEX (ENDONUCLEASE/DNA), TYPE IIS, RESTRICTION
KEYWDS   2 ENDONUCLEASE, DEOXYRIBONUCLEASE, DNA HYDROLYSIS, DNA
KEYWDS   3 CLEAVAGE, HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.A.AGGARWAL,J.A.WAH,L.F.HIRSCH,I.DORNER,A.K.SCHILDKRAUT
REVDAT   2   24-FEB-09 1FOK    1       VERSN
REVDAT   1   03-DEC-97 1FOK    0
JRNL        AUTH   D.A.WAH,J.A.HIRSCH,L.F.DORNER,I.SCHILDKRAUT,
JRNL        AUTH 2 A.K.AGGARWAL
JRNL        TITL   STRUCTURE OF THE MULTIMODULAR ENDONUCLEASE FOKI
JRNL        TITL 2 BOUND TO DNA.
JRNL        REF    NATURE                        V. 388    97 1997
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   9214510
JRNL        DOI    10.1038/40446
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.A.HIRSCH,D.A.WAH,L.F.DORNER,I.SCHILDKRAUT,
REMARK   1  AUTH 2 A.K.AGGARWAL
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK   1  TITL 2 RESTRICTION ENDONUCLEASE FOKI BOUND TO DNA
REMARK   1  REF    FEBS LETT.                    V. 403   136 1997
REMARK   1  REFN                   ISSN 0014-5793
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.9
REMARK   3   NUMBER OF REFLECTIONS             : 24931
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 SET) : 0.214
REMARK   3   FREE R VALUE                     : 0.296
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 710
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.92
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2900
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3540
REMARK   3   BIN FREE R VALUE                    : 0.4070
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 90
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4541
REMARK   3   NUCLEIC ACID ATOMS       : 814
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 172
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 57.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.76000
REMARK   3    B22 (A**2) : -1.09000
REMARK   3    B33 (A**2) : -0.67000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 2.07000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33
REMARK   3   ESD FROM SIGMAA              (A) : 0.49
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.48
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.69
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.011
REMARK   3   BOND ANGLES            (DEGREES) : 1.70
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.80
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.57
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.490 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.630 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.650 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.360 ; 2.500
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  : PARAMCSDX_MOD.PRO
REMARK   3  PARAMETER FILE  2  : PARAM_NDBX96.DNA
REMARK   3  PARAMETER FILE  3  : PARAM19.SOL
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOP_NDBX96.DNA
REMARK   3  TOPOLOGY FILE  3   : TOPH11.WAT
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1FOK 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        : 03-MAY-94
REMARK 200  TEMPERATURE           (KELVIN) : 130.00
REMARK 200  PH                             : 6.00
REMARK 200  NUMBER OF CRYSTALS USED        : 7
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F1
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                  : BENT, TRIANGULAR SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD, IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : SOL GRUNER, FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26253
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5
REMARK 200  DATA REDUNDANCY                : 7.700
REMARK 200  R MERGE                    (I) : 0.07500
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) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.32500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: PHASES, CCP4, SOLOMON, X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: CRYSTALS WERE FLASH FROZEN IN NITROGEN STREAM.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       59.67000
REMARK 290   SMTRY3   2  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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 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     LEU A   252
REMARK 465     GLY A   253
REMARK 465     LYS A   254
REMARK 465     THR A   282
REMARK 465     LYS A   283
REMARK 465     PHE A   284
REMARK 465     THR A   285
REMARK 465     ARG A   286
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     PRO A 255    CG   CD
REMARK 470     HIS A 523    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS A 525    CG   CD   CE   NZ
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 934   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES
REMARK 500    LYS A  99   N   -  CA  -  C   ANGL. DEV. = -17.2 DEGREES
REMARK 500    GLY A 213   N   -  CA  -  C   ANGL. DEV. = -15.3 DEGREES
REMARK 500    PRO A 255   N   -  CA  -  CB  ANGL. DEV. =   7.4 DEGREES
REMARK 500    ILE A 499   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES
REMARK 500    LEU A 518   CA  -  CB  -  CG  ANGL. DEV. =  16.9 DEGREES
REMARK 500    GLY A 526   N   -  CA  -  C   ANGL. DEV. =  16.5 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    GLN A  12      -73.11    -81.75
REMARK 500    PRO A  14      127.34    -39.19
REMARK 500    ILE A  40      -72.68   -118.11
REMARK 500    ASN A 124      -71.86    -43.81
REMARK 500    LYS A 125      -59.19    -25.16
REMARK 500    ASP A 171       -4.08    -57.71
REMARK 500    PHE A 186       68.86    -68.47
REMARK 500    ALA A 205      -79.89    -68.93
REMARK 500    PRO A 209      -26.99    -39.80
REMARK 500    ILE A 215       25.52    -75.28
REMARK 500    GLU A 220      136.71   -176.28
REMARK 500    ALA A 278       29.80    -65.69
REMARK 500    ALA A 297      134.74    178.34
REMARK 500    THR A 298      -88.11    -99.37
REMARK 500    ASP A 302       41.04    -99.96
REMARK 500    GLU A 304      -73.19    -49.98
REMARK 500    ALA A 320     -156.30    -72.39
REMARK 500    SER A 322       83.95     49.74
REMARK 500    GLU A 339     -160.21   -105.16
REMARK 500    LYS A 368       47.25   -106.51
REMARK 500    TYR A 408       -3.35    -58.56
REMARK 500    ARG A 422      -72.34    -41.40
REMARK 500    VAL A 435      -62.89   -106.74
REMARK 500    VAL A 456       79.17   -153.66
REMARK 500    ASP A 461      110.92    -11.33
REMARK 500    TYR A 475      110.47   -172.31
REMARK 500    LEU A 477       98.66    -37.58
REMARK 500    GLN A 493      -67.81    -95.98
REMARK 500    ARG A 495       42.04    -73.99
REMARK 500    ASN A 500       60.40     36.69
REMARK 500    PRO A 501        5.86    -53.13
REMARK 500    LYS A 506       -5.24    -53.81
REMARK 500    TYR A 528      -18.39    -39.82
REMARK 500    ILE A 553       39.80    -75.85
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     DA B 905         0.12    SIDE_CHAIN
REMARK 500     DA C 927         0.06    SIDE_CHAIN
REMARK 500     DT C 931         0.06    SIDE_CHAIN
REMARK 500     DA C 933         0.05    SIDE_CHAIN
REMARK 500    TYR A 292         0.10    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1FOK A    4   579  UNP    P14870   T2F1_FLAOK       8    583
DBREF  1FOK B  901   920  PDB    1FOK     1FOK           901    920
DBREF  1FOK C  921   940  PDB    1FOK     1FOK           921    940
SEQRES   1 B   20   DT  DC  DG  DG  DA  DT  DG  DA  DT  DA  DA  DC  DG
SEQRES   2 B   20   DC  DT  DA  DG  DT  DC  DA
SEQRES   1 C   20   DA  DT  DG  DA  DC  DT  DA  DG  DC  DG  DT  DT  DA
SEQRES   2 C   20   DT  DC  DA  DT  DC  DC  DG
SEQRES   1 A  576  LYS ILE ARG THR PHE GLY TRP VAL GLN ASN PRO GLY LYS
SEQRES   2 A  576  PHE GLU ASN LEU LYS ARG VAL VAL GLN VAL PHE ASP ARG
SEQRES   3 A  576  ASN SER LYS VAL HIS ASN GLU VAL LYS ASN ILE LYS ILE
SEQRES   4 A  576  PRO THR LEU VAL LYS GLU SER LYS ILE GLN LYS GLU LEU
SEQRES   5 A  576  VAL ALA ILE MET ASN GLN HIS ASP LEU ILE TYR THR TYR
SEQRES   6 A  576  LYS GLU LEU VAL GLY THR GLY THR SER ILE ARG SER GLU
SEQRES   7 A  576  ALA PRO CYS ASP ALA ILE ILE GLN ALA THR ILE ALA ASP
SEQRES   8 A  576  GLN GLY ASN LYS LYS GLY TYR ILE ASP ASN TRP SER SER
SEQRES   9 A  576  ASP GLY PHE LEU ARG TRP ALA HIS ALA LEU GLY PHE ILE
SEQRES  10 A  576  GLU TYR ILE ASN LYS SER ASP SER PHE VAL ILE THR ASP
SEQRES  11 A  576  VAL GLY LEU ALA TYR SER LYS SER ALA ASP GLY SER ALA
SEQRES  12 A  576  ILE GLU LYS GLU ILE LEU ILE GLU ALA ILE SER SER TYR
SEQRES  13 A  576  PRO PRO ALA ILE ARG ILE LEU THR LEU LEU GLU ASP GLY
SEQRES  14 A  576  GLN HIS LEU THR LYS PHE ASP LEU GLY LYS ASN LEU GLY
SEQRES  15 A  576  PHE SER GLY GLU SER GLY PHE THR SER LEU PRO GLU GLY
SEQRES  16 A  576  ILE LEU LEU ASP THR LEU ALA ASN ALA MET PRO LYS ASP
SEQRES  17 A  576  LYS GLY GLU ILE ARG ASN ASN TRP GLU GLY SER SER ASP
SEQRES  18 A  576  LYS TYR ALA ARG MET ILE GLY GLY TRP LEU ASP LYS LEU
SEQRES  19 A  576  GLY LEU VAL LYS GLN GLY LYS LYS GLU PHE ILE ILE PRO
SEQRES  20 A  576  THR LEU GLY LYS PRO ASP ASN LYS GLU PHE ILE SER HIS
SEQRES  21 A  576  ALA PHE LYS ILE THR GLY GLU GLY LEU LYS VAL LEU ARG
SEQRES  22 A  576  ARG ALA LYS GLY SER THR LYS PHE THR ARG VAL PRO LYS
SEQRES  23 A  576  ARG VAL TYR TRP GLU MET LEU ALA THR ASN LEU THR ASP
SEQRES  24 A  576  LYS GLU TYR VAL ARG THR ARG ARG ALA LEU ILE LEU GLU
SEQRES  25 A  576  ILE LEU ILE LYS ALA GLY SER LEU LYS ILE GLU GLN ILE
SEQRES  26 A  576  GLN ASP ASN LEU LYS LYS LEU GLY PHE ASP GLU VAL ILE
SEQRES  27 A  576  GLU THR ILE GLU ASN ASP ILE LYS GLY LEU ILE ASN THR
SEQRES  28 A  576  GLY ILE PHE ILE GLU ILE LYS GLY ARG PHE TYR GLN LEU
SEQRES  29 A  576  LYS ASP HIS ILE LEU GLN PHE VAL ILE PRO ASN ARG GLY
SEQRES  30 A  576  VAL THR LYS GLN LEU VAL LYS SER GLU LEU GLU GLU LYS
SEQRES  31 A  576  LYS SER GLU LEU ARG HIS LYS LEU LYS TYR VAL PRO HIS
SEQRES  32 A  576  GLU TYR ILE GLU LEU ILE GLU ILE ALA ARG ASN SER THR
SEQRES  33 A  576  GLN ASP ARG ILE LEU GLU MET LYS VAL MET GLU PHE PHE
SEQRES  34 A  576  MET LYS VAL TYR GLY TYR ARG GLY LYS HIS LEU GLY GLY
SEQRES  35 A  576  SER ARG LYS PRO ASP GLY ALA ILE TYR THR VAL GLY SER
SEQRES  36 A  576  PRO ILE ASP TYR GLY VAL ILE VAL ASP THR LYS ALA TYR
SEQRES  37 A  576  SER GLY GLY TYR ASN LEU PRO ILE GLY GLN ALA ASP GLU
SEQRES  38 A  576  MET GLN ARG TYR VAL GLU GLU ASN GLN THR ARG ASN LYS
SEQRES  39 A  576  HIS ILE ASN PRO ASN GLU TRP TRP LYS VAL TYR PRO SER
SEQRES  40 A  576  SER VAL THR GLU PHE LYS PHE LEU PHE VAL SER GLY HIS
SEQRES  41 A  576  PHE LYS GLY ASN TYR LYS ALA GLN LEU THR ARG LEU ASN
SEQRES  42 A  576  HIS ILE THR ASN CYS ASN GLY ALA VAL LEU SER VAL GLU
SEQRES  43 A  576  GLU LEU LEU ILE GLY GLY GLU MET ILE LYS ALA GLY THR
SEQRES  44 A  576  LEU THR LEU GLU GLU VAL ARG ARG LYS PHE ASN ASN GLY
SEQRES  45 A  576  GLU ILE ASN PHE
FORMUL   4  HOH   *172(H2 O)
HELIX    1   1 PHE A   17  PHE A   27  1                                  11
HELIX    2   2 LYS A   32  ASN A   39  1                                   8
HELIX    3   3 LYS A   41  LEU A   45  1                                   5
HELIX    4   4 SER A   49  ASN A   60  1                                  12
HELIX    5   5 TYR A   68  VAL A   72  1                                   5
HELIX    6   6 ARG A   79  GLU A   81  5                                   3
HELIX    7   7 ILE A   87  THR A   91  1                                   5
HELIX    8   8 ASN A  104  ALA A  116  1                                  13
HELIX    9   9 ASP A  133  LYS A  140  1                                   8
HELIX   10  10 ALA A  146  SER A  158  1                                  13
HELIX   11  11 PRO A  160  LEU A  169  1                                  10
HELIX   12  12 LYS A  177  ASN A  183  1                                   7
HELIX   13  13 GLU A  197  ALA A  205  1                                   9
HELIX   14  14 GLU A  214  ASN A  217  1                                   4
HELIX   15  15 SER A  222  LYS A  236  1                                  15
HELIX   16  16 GLY A  269  LYS A  279  1                                  11
HELIX   17  17 TRP A  293  MET A  295  5                                   3
HELIX   18  18 LYS A  303  LYS A  319  1                                  17
HELIX   19  19 ILE A  325  LEU A  335  1                                  11
HELIX   20  20 ILE A  341  ASN A  353  1                                  13
HELIX   21  21 THR A  382  GLN A  384  5                                   3
HELIX   22  22 GLU A  389  LYS A  400  1                                  12
HELIX   23  23 HIS A  406  ARG A  416  5                                  11
HELIX   24  24 SER A  418  LYS A  434  5                                  17
HELIX   25  25 ILE A  479  GLU A  491  1                                  13
HELIX   26  26 TRP A  504  VAL A  507  5                                   4
HELIX   27  27 ALA A  530  THR A  539  1                                  10
HELIX   28  28 VAL A  548  ALA A  560  1                                  13
SHEET    1   A 2 ILE A 120  ILE A 123  0
SHEET    2   A 2 SER A 128  ILE A 131 -1  N  VAL A 130   O  GLU A 121
SHEET    1   B 2 VAL A 240  GLN A 242  0
SHEET    2   B 2 PHE A 265  ILE A 267 -1  N  LYS A 266   O  LYS A 241
SHEET    1   C 2 LYS A 245  ILE A 248  0
SHEET    2   C 2 LYS A 258  ILE A 261 -1  N  ILE A 261   O  LYS A 245
SHEET    1   D 2 ILE A 358  LYS A 361  0
SHEET    2   D 2 PHE A 364  LEU A 367 -1  N  GLN A 366   O  GLU A 359
SHEET    1   E 5 ARG A 439  HIS A 442  0
SHEET    2   E 5 GLY A 451  TYR A 454 -1  N  TYR A 454   O  ARG A 439
SHEET    3   E 5 TYR A 462  LYS A 469 -1  N  VAL A 466   O  GLY A 451
SHEET    4   E 5 GLU A 514  SER A 521  1  N  GLU A 514   O  GLY A 463
SHEET    5   E 5 GLY A 543  SER A 547  1  N  ALA A 544   O  PHE A 517
CRYST1   65.590  119.340   71.520  90.00 101.42  90.00 P 1 21 1      2
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      0.015246  0.000000  0.003080        0.00000
SCALE2      0.000000  0.008379  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014265        0.00000
      
PROCHECK
Go to PROCHECK summary
 References