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PDBsum entry 1ckq

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Protein/DNA PDB id
1ckq
Jmol
Contents
Protein chain
261 a.a.
DNA/RNA
Waters ×151
HEADER    PROTEIN/DNA                             22-APR-99   1CKQ
TITLE     PRE-TRANSITION STATE ECO RI ENDONUCLEASE/COGNATE DNA
TITLE    2 (TCGCGAATTCGCG) COMPLEX
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-
COMPND   3 D(*TP*CP*GP*CP*GP*AP*AP*TP*TP*CP*GP*CP*G)-3');
COMPND   4 CHAIN: B;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: PROTEIN (ENDONUCLEASE);
COMPND   8 CHAIN: A
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    SEQUENCE-SPECIFIC DNA-PROTEIN COMPLEX, PROTEIN/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.HORVATH,J.M.ROSENBERG
REVDAT   2   24-FEB-09 1CKQ    1       VERSN
REVDAT   1   26-APR-99 1CKQ    0
JRNL        AUTH   M.HORVATH,J.CHOI,Y.KIM,P.A.WILKOSZ,K.CHANDRASEKHAR,
JRNL        AUTH 2 J.M.ROSENBERG
JRNL        TITL   THE INTEGRATION OF RECOGNITION AND CLEAVAGE: X-RAY
JRNL        TITL 2 STRUCTURES OF PRE- TRANSITION STATE AND
JRNL        TITL 3 POST-REACTIVE DNA-ECO RI ENDONUCLEASE COMPLEXES
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.85 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) : 1.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0
REMARK   3   NUMBER OF REFLECTIONS             : 27076
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : RFREE
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.235
REMARK   3   FREE R VALUE                     : 0.286
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3025
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.93
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 801
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3798
REMARK   3   BIN FREE R VALUE                    : 0.3858
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 12.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 109
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            : 2051
REMARK   3   NUCLEIC ACID ATOMS       : 263
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 151
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.30
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) : 0.30
REMARK   3   ESD FROM SIGMAA              (A) : 0.28
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 8.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.31
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.003
REMARK   3   BOND ANGLES            (DEGREES) : 1.03
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.89
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) : 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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : PARAM11.WAT
REMARK   3  PARAMETER FILE  3  : DNA-RNA.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPH19.PEP
REMARK   3  TOPOLOGY FILE  3   : TOPH11.WAT
REMARK   3  TOPOLOGY FILE  4   : DNA-RNA.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1CKQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-99.
REMARK 100 THE RCSB ID CODE IS RCSB000923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-98
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
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) : 1.100
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32270
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 10.600
REMARK 200  R MERGE                    (I) : 0.12400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.44600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1ERI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP
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 300 REMARK:
REMARK 300 ECO RI IS A DIMER. THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 CONSISTS OF A MONOMER AND THE COORDINATES OF THIS MONOMER
REMARK 300 ARE PRESENTED IN THIS ENTRY. TO GENERATE THE DIMER AND THE
REMARK 300 OTHER HALF OF THE DNA DUPLEX ONE MUST APPLY THE FOLLOWING
REMARK 300 CRYSTALLOGRAPHIC TWO-FOLD TRANSFORMATION TO THE COORDINATES
REMARK 300 IN THIS ENTRY - -.5 .866025 0.0 .866025 .5 0.0 0.0 0.0 -1.0
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: B, 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 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     SER A     2
REMARK 465     ASN A     3
REMARK 465     LYS A     4
REMARK 465     LYS A     5
REMARK 465     GLN A     6
REMARK 465     SER A     7
REMARK 465     ASN A     8
REMARK 465     ARG A     9
REMARK 465     LEU A    10
REMARK 465     THR A    11
REMARK 465     GLU A    12
REMARK 465     GLN A    13
REMARK 465     HIS A    14
REMARK 465     LYS A    15
REMARK 465     LEU A    16
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  81      111.78   -164.62
REMARK 500    ASN A  85       43.69   -103.43
REMARK 500    PRO A 164       48.40    -81.34
REMARK 500    ASN A 224      136.51   -174.42
REMARK 500    HIS A 225      -70.81    -84.22
REMARK 500    ASP A 227       74.58     51.83
REMARK 500    LYS A 228      -52.53   -141.11
REMARK 500    SER A 229      118.67     73.68
REMARK 500    SER A 276       44.87    -84.86
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 B   8         0.06    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 362        DISTANCE =  5.42 ANGSTROMS
REMARK 525    HOH A 391        DISTANCE =  7.91 ANGSTROMS
REMARK 525    HOH A 400        DISTANCE = 11.06 ANGSTROMS
REMARK 525    HOH A 401        DISTANCE = 12.37 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: HYD
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: PROTEIN RECOGNTION RESIDUES GROUPS THAT
REMARK 800  HYDROGEN BOND TO THE DNA BASES AND/OR PROVIDE PRIMARY
REMARK 800  BUTTRESSING.
REMARK 800 SITE_IDENTIFIER: DNA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: DNA RECOGNITION SEQUENCE THIS IS THE DNA
REMARK 800  TARGET RECOGNIZED BY THE PROTEIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FIRST 15 RESIDUES ARE DISORDERED IN THE CRYSTAL STRUCTURE
REMARK 999 AND NOT SEEN IN THE ELECTRON DENSITY.
DBREF  1CKQ A    2   277  UNP    P00642   T2E1_ECOLI       1    276
DBREF  1CKQ B    1    13  PDB    1CKQ     1CKQ             1     13
SEQRES   1 B   13   DT  DC  DG  DC  DG  DA  DA  DT  DT  DC  DG  DC  DG
SEQRES   1 A  276  SER ASN LYS LYS GLN SER ASN ARG LEU THR GLU GLN HIS
SEQRES   2 A  276  LYS LEU SER GLN GLY VAL ILE GLY ILE PHE GLY ASP TYR
SEQRES   3 A  276  ALA LYS ALA HIS ASP LEU ALA VAL GLY GLU VAL SER LYS
SEQRES   4 A  276  LEU VAL LYS LYS ALA LEU SER ASN GLU TYR PRO GLN LEU
SEQRES   5 A  276  SER PHE ARG TYR ARG ASP SER ILE LYS LYS THR GLU ILE
SEQRES   6 A  276  ASN GLU ALA LEU LYS LYS ILE ASP PRO ASP LEU GLY GLY
SEQRES   7 A  276  THR LEU PHE VAL SER ASN SER SER ILE LYS PRO ASP GLY
SEQRES   8 A  276  GLY ILE VAL GLU VAL LYS ASP ASP TYR GLY GLU TRP ARG
SEQRES   9 A  276  VAL VAL LEU VAL ALA GLU ALA LYS HIS GLN GLY LYS ASP
SEQRES  10 A  276  ILE ILE ASN ILE ARG ASN GLY LEU LEU VAL GLY LYS ARG
SEQRES  11 A  276  GLY ASP GLN ASP LEU MET ALA ALA GLY ASN ALA ILE GLU
SEQRES  12 A  276  ARG SER HIS LYS ASN ILE SER GLU ILE ALA ASN PHE MET
SEQRES  13 A  276  LEU SER GLU SER HIS PHE PRO TYR VAL LEU PHE LEU GLU
SEQRES  14 A  276  GLY SER ASN PHE LEU THR GLU ASN ILE SER ILE THR ARG
SEQRES  15 A  276  PRO ASP GLY ARG VAL VAL ASN LEU GLU TYR ASN SER GLY
SEQRES  16 A  276  ILE LEU ASN ARG LEU ASP ARG LEU THR ALA ALA ASN TYR
SEQRES  17 A  276  GLY MET PRO ILE ASN SER ASN LEU CYS ILE ASN LYS PHE
SEQRES  18 A  276  VAL ASN HIS LYS ASP LYS SER ILE MET LEU GLN ALA ALA
SEQRES  19 A  276  SER ILE TYR THR GLN GLY ASP GLY ARG GLU TRP ASP SER
SEQRES  20 A  276  LYS ILE MET PHE GLU ILE MET PHE ASP ILE SER THR THR
SEQRES  21 A  276  SER LEU ARG VAL LEU GLY ARG ASP LEU PHE GLU GLN LEU
SEQRES  22 A  276  THR SER LYS
FORMUL   3  HOH   *151(H2 O)
HELIX    1   1 GLY A   19  HIS A   31  5                                  13
HELIX    2   2 VAL A   35  GLU A   49  1                                  15
HELIX    3   3 LYS A   63  ILE A   73  1                                  11
HELIX    4   4 ASP A  118  ARG A  123  1                                   6
HELIX    5   5 ALA A  142  PHE A  156  5                                  15
HELIX    6   6 LEU A  201  ARG A  203  5                                   3
HELIX    7   7 THR A  205  ASN A  208  5                                   4
HELIX    8   8 SER A  248  VAL A  265  1                                  18
HELIX    9   9 GLY A  267  ASP A  269  5                                   3
HELIX   10  10 PHE A  271  THR A  275  1                                   5
SHEET    1   A 5 PHE A  55  ARG A  58  0
SHEET    2   A 5 ILE A  94  LYS A  98 -1  N  GLU A  96   O  ARG A  56
SHEET    3   A 5 TRP A 104  HIS A 114 -1  N  LEU A 108   O  VAL A  95
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  N  SER A 236   O  LEU A 167
SHEET    1   B 2 ILE A 179  THR A 182  0
SHEET    2   B 2 VAL A 188  LEU A 191 -1  N  LEU A 191   O  ILE A 179
SHEET    1   C 2 LYS A 221  VAL A 223  0
SHEET    2   C 2 ILE A 230  LEU A 232 -1  N  LEU A 232   O  LYS A 221
SITE     1 HYD  9 ALA A 138  ASN A 141  ALA A 142  GLU A 144
SITE     2 HYD  9 ARG A 145  ARG A 200  ARG A 203  HOH A 278
SITE     3 HYD  9 HOH B  14
SITE     1 DNA  6  DG B   5   DA B   6   DA B   7   DT B   8
SITE     2 DNA  6  DT B   9   DC B  10
CRYST1  118.110  118.110   49.450  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      0.008467  0.004888  0.000000        0.00000
SCALE2      0.000000  0.009776  0.000000        0.00000
SCALE3      0.000000  0.000000  0.020222        0.00000
      
PROCHECK
Go to PROCHECK summary
 References