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PDBsum entry 1tw8

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Top Page protein dna_rna metals Protein-protein interface(s) links
Hydrolase/DNA PDB id
1tw8
Jmol
Contents
Protein chains
257 a.a.
DNA/RNA
Metals
_CA ×6
_NA ×4
Waters ×765
HEADER    HYDROLASE/DNA                           30-JUN-04   1TW8
TITLE     HINCII BOUND TO CA2+ AND COGNATE DNA GTCGAC
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*GP*CP*CP*GP*GP*TP*CP*GP*AP*CP*CP*GP*G)-3';
COMPND   3 CHAIN: E, F, G, H;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: HINC II ENDONUCLEASE;
COMPND   7 CHAIN: A, B, C, D;
COMPND   8 EC: 3.1.21.4;
COMPND   9 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: COMMERCIAL PHOSPHORAMIDITE CHEMISTRY;
SOURCE   4 MOL_ID: 2;
SOURCE   5 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE   6 ORGANISM_TAXID: 727;
SOURCE   7 GENE: HINC II;
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    RESTRICTION ENDONUCLEASE, HYDROLASE-DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.ETZKORN,N.C.HORTON
REVDAT   4   06-JUN-12 1TW8    1       COMPND SOURCE SEQADV VERSN
REVDAT   3   24-FEB-09 1TW8    1       VERSN
REVDAT   2   23-NOV-04 1TW8    1       JRNL
REVDAT   1   10-AUG-04 1TW8    0
JRNL        AUTH   C.ETZKORN,N.C.HORTON
JRNL        TITL   CA2+ BINDING IN THE ACTIVE SITE OF HINCII: IMPLICATIONS FOR
JRNL        TITL 2 THE CATALYTIC MECHANISM
JRNL        REF    BIOCHEMISTRY                  V.  43 13256 2004
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   15491133
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : CNS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.9
REMARK   3   NUMBER OF REFLECTIONS             : 36795
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 5%
REMARK   3   R VALUE            (WORKING SET) : 0.180
REMARK   3   FREE R VALUE                     : 0.286
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1840
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            : 8241
REMARK   3   NUCLEIC ACID ATOMS       : 1060
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 765
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 55.10
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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.14
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  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 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 1TW8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-04.
REMARK 100 THE RCSB ID CODE IS RCSB022961.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
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) : 0.9
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
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          : MOSFLM, CCP4 (SCALA, TRUNCATE)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36795
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9
REMARK 200  DATA REDUNDANCY                : 2.700
REMARK 200  R MERGE                    (I) : 0.06600
REMARK 200  R SYM                      (I) : 0.06600
REMARK 200   FOR THE DATA SET  : 5.3000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1KC6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, 0.1M CITRATE, 0.15M NACL, PH
REMARK 280  5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X,-Y+1/2,Z
REMARK 290       7555   -X+1/2,Y,-Z
REMARK 290       8555   X,-Y,-Z+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       33.47250
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      127.44500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       88.59000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      127.44500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.47250
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       88.59000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.47250
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       88.59000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      127.44500
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       88.59000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.47250
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      127.44500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 ONE HALF OF THE ASYMMETRIC UNIT
REMARK 300 INCLUDING TWO PROTEIN SUBUNITS AND TWO STRANDS OF DNA (IE. CHAINS A
REMARK 300 -B, E-F)
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: E, F, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, C, D
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 B   258
REMARK 465     ILE D   257
REMARK 465     LEU D   258
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     LYS A  21    CG   CD   CE   NZ
REMARK 470     LYS A  24    CG   CD   CE   NZ
REMARK 470     GLU A  35    CG   CD   OE1  OE2
REMARK 470     LYS A  39    CG   CD   CE   NZ
REMARK 470     SER A  50    OG
REMARK 470     GLU A 102    CG   CD   OE1  OE2
REMARK 470     LYS A 159    CG   CD   CE   NZ
REMARK 470     LYS A 228    CG   CD   CE   NZ
REMARK 470     LEU A 258    CG   CD1  CD2
REMARK 470     GLN B   9    CG   CD   OE1  NE2
REMARK 470     LYS B  78    CG   CD   CE   NZ
REMARK 470     GLN B 121    CG   CD   OE1  NE2
REMARK 470     GLU B 178    CG   CD   OE1  OE2
REMARK 470     GLN B 240    CG   CD   OE1  NE2
REMARK 470     LYS B 251    CG   CD   CE   NZ
REMARK 470     LYS C  21    CG   CD   CE   NZ
REMARK 470     LYS C  24    CG   CD   CE   NZ
REMARK 470     LYS C  39    CG   CD   CE   NZ
REMARK 470     PHE C  44    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS C  46    CG   CD   CE   NZ
REMARK 470     GLU C  47    CG   CD   OE1  OE2
REMARK 470     LYS C  66    CG   CD   CE   NZ
REMARK 470     LYS C  78    CG   CD   CE   NZ
REMARK 470     LYS C  93    CG   CD   CE   NZ
REMARK 470     GLU C  97    CG   CD   OE1  OE2
REMARK 470     GLU C 102    CG   CD   OE1  OE2
REMARK 470     LYS C 154    CG   CD   CE   NZ
REMARK 470     GLU C 160    CD   OE1  OE2
REMARK 470     GLN D   9    CG   CD   OE1  NE2
REMARK 470     LYS D  19    CG   CD   CE   NZ
REMARK 470     LYS D  24    CG   CD   CE   NZ
REMARK 470     LYS D  46    CG   CD   CE   NZ
REMARK 470     SER D  50    OG
REMARK 470     GLU D  74    CG   CD   OE1  OE2
REMARK 470     LYS D 119    CG   CD   CE   NZ
REMARK 470     ASP D 120    CG   OD1  OD2
REMARK 470     LYS D 159    CG   CD   CE   NZ
REMARK 470     LYS D 232    CG   CD   CE   NZ
REMARK 470     ASP D 247    CG   OD1  OD2
REMARK 470     LYS D 251    CG   CD   CE   NZ
REMARK 470     LYS D 255    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    ILE A    70     O    HOH A   910              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH B   972     O    HOH B   972     8556     1.91
REMARK 500   O    HOH B  1102     O    HOH B  1102     8556     2.05
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    THR A  27      -35.77   -131.41
REMARK 500    LEU A  28       15.30     49.83
REMARK 500    ALA A  33      -78.04    -41.24
REMARK 500    ASN A  48      -65.23    -90.97
REMARK 500    LEU A  49       49.03    -96.82
REMARK 500    ASN A  81       28.78     49.63
REMARK 500    SER A  82      120.62   -170.71
REMARK 500    SER A  90      178.28    -54.97
REMARK 500    LYS A  93      -66.66    -20.47
REMARK 500    LEU A 104     -178.86    -61.74
REMARK 500    LYS A 119      135.68   -177.15
REMARK 500    ILE A 142      -69.33    -96.07
REMARK 500    SER A 184      172.91    179.63
REMARK 500    ALA A 204       45.78    -73.93
REMARK 500    ALA A 205       31.40     70.22
REMARK 500    PHE A 210      138.51   -173.84
REMARK 500    GLN A 217       46.17   -140.74
REMARK 500    VAL A 250      -64.18   -121.25
REMARK 500    PRO A 252        4.33    -60.00
REMARK 500    ILE A 257      -30.55   -137.06
REMARK 500    GLN B  18      163.14    -49.98
REMARK 500    PRO B  23     -131.01    -50.38
REMARK 500    LYS B  24       12.38    -65.01
REMARK 500    THR B  27       89.59     34.31
REMARK 500    ALA B  33     -135.09    -93.28
REMARK 500    PRO B  36      -19.64    -45.42
REMARK 500    LEU B  49       52.20   -147.63
REMARK 500    LYS B  66       37.98    -99.28
REMARK 500    ASN B  67       52.58   -157.09
REMARK 500    GLU B  74      -80.95    -44.19
REMARK 500    SER B  82      116.59   -175.82
REMARK 500    ILE B 101        7.91    -65.21
REMARK 500    ASN B 103       61.72   -151.23
REMARK 500    LYS B 119      122.09   -172.52
REMARK 500    ASP B 162       79.78   -152.35
REMARK 500    LEU B 163      -33.60   -153.45
REMARK 500    ASN B 176       80.14   -152.09
REMARK 500    PHE B 191        6.83    -67.31
REMARK 500    PRO B 195       -7.41    -57.94
REMARK 500    ARG B 213       -9.37    -59.19
REMARK 500    VAL B 250      -61.32   -132.66
REMARK 500    ASP C  10      -68.87   -133.92
REMARK 500    ILE C  11      -37.22    -39.68
REMARK 500    PRO C  23      108.98    -53.13
REMARK 500    SER C  25      120.34     65.95
REMARK 500    SER C  29      142.58   -173.30
REMARK 500    LEU C  49       30.11   -149.57
REMARK 500    LEU C  52       29.98   -162.40
REMARK 500    LYS C  55       84.27   -153.11
REMARK 500    GLN C  56      -87.12     50.82
REMARK 500
REMARK 500 THIS ENTRY HAS      95 RAMACHANDRAN OUTLIERS.
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     DC E   7         0.11    SIDE CHAIN
REMARK 500     DG E   8         0.08    SIDE CHAIN
REMARK 500     DA E   9         0.09    SIDE CHAIN
REMARK 500     DC E  10         0.08    SIDE CHAIN
REMARK 500     DC F   2         0.08    SIDE CHAIN
REMARK 500     DC F   7         0.12    SIDE CHAIN
REMARK 500     DG F   8         0.09    SIDE CHAIN
REMARK 500     DA F   9         0.07    SIDE CHAIN
REMARK 500     DC F  10         0.06    SIDE CHAIN
REMARK 500     DC G   7         0.06    SIDE CHAIN
REMARK 500     DG G   8         0.06    SIDE CHAIN
REMARK 500     DC H   7         0.08    SIDE CHAIN
REMARK 500     DG H   8         0.10    SIDE CHAIN
REMARK 500     DA H   9         0.05    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 915        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH A 916        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH A 938        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH A1076        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH A1090        DISTANCE =  6.19 ANGSTROMS
REMARK 525    HOH B 912        DISTANCE =  6.92 ANGSTROMS
REMARK 525    HOH B 916        DISTANCE =  8.22 ANGSTROMS
REMARK 525    HOH B 937        DISTANCE =  7.59 ANGSTROMS
REMARK 525    HOH B1048        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH B1077        DISTANCE =  5.49 ANGSTROMS
REMARK 525    HOH B1079        DISTANCE =  6.97 ANGSTROMS
REMARK 525    HOH B1084        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH B1094        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH B1095        DISTANCE =  8.46 ANGSTROMS
REMARK 525    HOH B1096        DISTANCE =  7.02 ANGSTROMS
REMARK 525    HOH B1097        DISTANCE =  8.50 ANGSTROMS
REMARK 525    HOH B1098        DISTANCE =  6.83 ANGSTROMS
REMARK 525    HOH C 983        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH C 987        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH C 991        DISTANCE =  6.40 ANGSTROMS
REMARK 525    HOH C 998        DISTANCE =  6.51 ANGSTROMS
REMARK 525    HOH D 924        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH E 116        DISTANCE =  8.60 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 801  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 128   O
REMARK 620 2 ASP A 114   OD1  86.8
REMARK 620 3 ASP A 127   OD1  90.2  80.6
REMARK 620 4 HOH F 806   O    81.0 166.4 105.4
REMARK 620 5 ASP A 114   OD2 131.5  45.8  91.0 144.2
REMARK 620 6 HOH A1058   O    90.9  82.8 163.3  91.3  75.8
REMARK 620 7  DG F   8   OP1 169.1 104.1  91.4  88.2  59.3  90.6
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA A 901  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 127   OD2
REMARK 620 2  DG F   8   OP2  80.3
REMARK 620 3 HOH A1060   O    89.9 117.2
REMARK 620 4 ILE A 142   O   103.1 123.5 119.2
REMARK 620 5 HOH A1066   O   159.2  79.0  97.8  90.0
REMARK 620 6 LYS A 129   NZ   60.9  66.3 150.4  67.1 111.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 802  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1006   O
REMARK 620 2  DG E   8   OP1 101.1
REMARK 620 3 HOH E 244   O   107.8  84.6
REMARK 620 4 ASP B 114   OD1  78.8  99.4 171.6
REMARK 620 5 VAL B 128   O    85.2 168.7  84.5  91.0
REMARK 620 6 ASP B 127   OD2 163.5  93.4  81.3  91.1  81.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B 902  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 142   O
REMARK 620 2 HOH B 998   O   117.7
REMARK 620 3  DG E   8   OP2 124.1 117.7
REMARK 620 4 ASP B 127   OD1  90.4 108.7  78.8
REMARK 620 5 HOH B 976   O    74.8  96.2  92.6 154.9
REMARK 620 6 HOH B1054   O    75.8  66.4 134.9  59.6 132.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA C 803  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1  DG H   8   OP1
REMARK 620 2 HOH C 971   O    87.4
REMARK 620 3 ASP C 114   OD2  78.9  84.1
REMARK 620 4 ASP C 127   OD1  97.4 168.8  86.8
REMARK 620 5 VAL C 128   O   166.1  79.3 103.3  96.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA C 903  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE C 142   O
REMARK 620 2 HOH C 967   O   106.6
REMARK 620 3  DG H   8   OP2 120.5  98.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA D 804  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 114   OD2
REMARK 620 2 ASP D 127   OD2  99.7
REMARK 620 3 VAL D 128   O    95.2  84.7
REMARK 620 4 HOH D 922   O    61.3 152.4  77.9
REMARK 620 5  DG G   8   OP2 122.9  78.5 140.2 128.0
REMARK 620 6  DG G   8   OP1  80.9 112.2 163.1  85.8  50.1
REMARK 620 7 ASP D 114   OD1  44.2  64.0 115.0 104.4  89.4  73.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA D 904  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS D 129   NZ
REMARK 620 2 ILE D 142   O    79.8
REMARK 620 3 HOH G 551   O   170.5  92.7
REMARK 620 4 HOH D 989   O   110.0  72.5  72.7
REMARK 620 5  DG G   8   OP2  69.8 138.2 119.6  91.4
REMARK 620 6 ASP D 127   OD1  68.2 106.2 108.9 178.0  88.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA F 805  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1059   O
REMARK 620 2 HOH F 841   O    72.9
REMARK 620 3  DG F   1   O6  121.3  53.8
REMARK 620 4  DC F   2   N4  125.0  76.1  67.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA H 806  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1  DG H   1   O6
REMARK 620 2 HOH H  43   O   142.9
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 904
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KC6   RELATED DB: PDB
REMARK 900 HINCII BOUND TO COGNATE DNA GTCGAC
DBREF  1TW8 A    2   258  UNP    E1B6R0   E1B6R0_HAEIF     2    258
DBREF  1TW8 B    2   258  UNP    E1B6R0   E1B6R0_HAEIF     2    258
DBREF  1TW8 C    2   258  UNP    E1B6R0   E1B6R0_HAEIF     2    258
DBREF  1TW8 D    2   258  UNP    E1B6R0   E1B6R0_HAEIF     2    258
DBREF  1TW8 E    1    13  PDB    1TW8     1TW8             1     13
DBREF  1TW8 F    1    13  PDB    1TW8     1TW8             1     13
DBREF  1TW8 G    1    13  PDB    1TW8     1TW8             1     13
DBREF  1TW8 H    1    13  PDB    1TW8     1TW8             1     13
SEQRES   1 E   13   DG  DC  DC  DG  DG  DT  DC  DG  DA  DC  DC  DG  DG
SEQRES   1 F   13   DG  DC  DC  DG  DG  DT  DC  DG  DA  DC  DC  DG  DG
SEQRES   1 G   13   DG  DC  DC  DG  DG  DT  DC  DG  DA  DC  DC  DG  DG
SEQRES   1 H   13   DG  DC  DC  DG  DG  DT  DC  DG  DA  DC  DC  DG  DG
SEQRES   1 A  257  SER PHE ILE LYS PRO ILE TYR GLN ASP ILE ASN SER ILE
SEQRES   2 A  257  LEU ILE GLY GLN LYS VAL LYS ARG PRO LYS SER GLY THR
SEQRES   3 A  257  LEU SER GLY HIS ALA ALA GLY GLU PRO PHE GLU LYS LEU
SEQRES   4 A  257  VAL TYR LYS PHE LEU LYS GLU ASN LEU SER ASP LEU THR
SEQRES   5 A  257  PHE LYS GLN TYR GLU TYR LEU ASN ASP LEU PHE MET LYS
SEQRES   6 A  257  ASN PRO ALA ILE ILE GLY HIS GLU ALA ARG TYR LYS LEU
SEQRES   7 A  257  PHE ASN SER PRO THR LEU LEU PHE LEU LEU SER ARG GLY
SEQRES   8 A  257  LYS ALA ALA THR GLU ASN TRP SER ILE GLU ASN LEU PHE
SEQRES   9 A  257  GLU GLU LYS GLN ASN ASP THR ALA ASP ILE LEU LEU VAL
SEQRES  10 A  257  LYS ASP GLN PHE TYR GLU LEU LEU ASP VAL LYS THR ARG
SEQRES  11 A  257  ASN ILE SER LYS SER ALA GLN ALA PRO ASN ILE ILE SER
SEQRES  12 A  257  ALA TYR LYS LEU ALA GLN THR CYS ALA LYS MET ILE ASP
SEQRES  13 A  257  ASN LYS GLU PHE ASP LEU PHE ASP ILE ASN TYR LEU GLU
SEQRES  14 A  257  VAL ASP TRP GLU LEU ASN GLY GLU ASP LEU VAL CYS VAL
SEQRES  15 A  257  SER THR SER PHE ALA GLU LEU PHE LYS SER GLU PRO SER
SEQRES  16 A  257  GLU LEU TYR ILE ASN TRP ALA ALA ALA MET GLN ILE GLN
SEQRES  17 A  257  PHE HIS VAL ARG ASP LEU ASP GLN GLY PHE ASN GLY THR
SEQRES  18 A  257  ARG GLU GLU TRP ALA LYS SER TYR LEU LYS HIS PHE VAL
SEQRES  19 A  257  THR GLN ALA GLU GLN ARG ALA ILE SER MET ILE ASP LYS
SEQRES  20 A  257  PHE VAL LYS PRO PHE LYS LYS TYR ILE LEU
SEQRES   1 B  257  SER PHE ILE LYS PRO ILE TYR GLN ASP ILE ASN SER ILE
SEQRES   2 B  257  LEU ILE GLY GLN LYS VAL LYS ARG PRO LYS SER GLY THR
SEQRES   3 B  257  LEU SER GLY HIS ALA ALA GLY GLU PRO PHE GLU LYS LEU
SEQRES   4 B  257  VAL TYR LYS PHE LEU LYS GLU ASN LEU SER ASP LEU THR
SEQRES   5 B  257  PHE LYS GLN TYR GLU TYR LEU ASN ASP LEU PHE MET LYS
SEQRES   6 B  257  ASN PRO ALA ILE ILE GLY HIS GLU ALA ARG TYR LYS LEU
SEQRES   7 B  257  PHE ASN SER PRO THR LEU LEU PHE LEU LEU SER ARG GLY
SEQRES   8 B  257  LYS ALA ALA THR GLU ASN TRP SER ILE GLU ASN LEU PHE
SEQRES   9 B  257  GLU GLU LYS GLN ASN ASP THR ALA ASP ILE LEU LEU VAL
SEQRES  10 B  257  LYS ASP GLN PHE TYR GLU LEU LEU ASP VAL LYS THR ARG
SEQRES  11 B  257  ASN ILE SER LYS SER ALA GLN ALA PRO ASN ILE ILE SER
SEQRES  12 B  257  ALA TYR LYS LEU ALA GLN THR CYS ALA LYS MET ILE ASP
SEQRES  13 B  257  ASN LYS GLU PHE ASP LEU PHE ASP ILE ASN TYR LEU GLU
SEQRES  14 B  257  VAL ASP TRP GLU LEU ASN GLY GLU ASP LEU VAL CYS VAL
SEQRES  15 B  257  SER THR SER PHE ALA GLU LEU PHE LYS SER GLU PRO SER
SEQRES  16 B  257  GLU LEU TYR ILE ASN TRP ALA ALA ALA MET GLN ILE GLN
SEQRES  17 B  257  PHE HIS VAL ARG ASP LEU ASP GLN GLY PHE ASN GLY THR
SEQRES  18 B  257  ARG GLU GLU TRP ALA LYS SER TYR LEU LYS HIS PHE VAL
SEQRES  19 B  257  THR GLN ALA GLU GLN ARG ALA ILE SER MET ILE ASP LYS
SEQRES  20 B  257  PHE VAL LYS PRO PHE LYS LYS TYR ILE LEU
SEQRES   1 C  257  SER PHE ILE LYS PRO ILE TYR GLN ASP ILE ASN SER ILE
SEQRES   2 C  257  LEU ILE GLY GLN LYS VAL LYS ARG PRO LYS SER GLY THR
SEQRES   3 C  257  LEU SER GLY HIS ALA ALA GLY GLU PRO PHE GLU LYS LEU
SEQRES   4 C  257  VAL TYR LYS PHE LEU LYS GLU ASN LEU SER ASP LEU THR
SEQRES   5 C  257  PHE LYS GLN TYR GLU TYR LEU ASN ASP LEU PHE MET LYS
SEQRES   6 C  257  ASN PRO ALA ILE ILE GLY HIS GLU ALA ARG TYR LYS LEU
SEQRES   7 C  257  PHE ASN SER PRO THR LEU LEU PHE LEU LEU SER ARG GLY
SEQRES   8 C  257  LYS ALA ALA THR GLU ASN TRP SER ILE GLU ASN LEU PHE
SEQRES   9 C  257  GLU GLU LYS GLN ASN ASP THR ALA ASP ILE LEU LEU VAL
SEQRES  10 C  257  LYS ASP GLN PHE TYR GLU LEU LEU ASP VAL LYS THR ARG
SEQRES  11 C  257  ASN ILE SER LYS SER ALA GLN ALA PRO ASN ILE ILE SER
SEQRES  12 C  257  ALA TYR LYS LEU ALA GLN THR CYS ALA LYS MET ILE ASP
SEQRES  13 C  257  ASN LYS GLU PHE ASP LEU PHE ASP ILE ASN TYR LEU GLU
SEQRES  14 C  257  VAL ASP TRP GLU LEU ASN GLY GLU ASP LEU VAL CYS VAL
SEQRES  15 C  257  SER THR SER PHE ALA GLU LEU PHE LYS SER GLU PRO SER
SEQRES  16 C  257  GLU LEU TYR ILE ASN TRP ALA ALA ALA MET GLN ILE GLN
SEQRES  17 C  257  PHE HIS VAL ARG ASP LEU ASP GLN GLY PHE ASN GLY THR
SEQRES  18 C  257  ARG GLU GLU TRP ALA LYS SER TYR LEU LYS HIS PHE VAL
SEQRES  19 C  257  THR GLN ALA GLU GLN ARG ALA ILE SER MET ILE ASP LYS
SEQRES  20 C  257  PHE VAL LYS PRO PHE LYS LYS TYR ILE LEU
SEQRES   1 D  257  SER PHE ILE LYS PRO ILE TYR GLN ASP ILE ASN SER ILE
SEQRES   2 D  257  LEU ILE GLY GLN LYS VAL LYS ARG PRO LYS SER GLY THR
SEQRES   3 D  257  LEU SER GLY HIS ALA ALA GLY GLU PRO PHE GLU LYS LEU
SEQRES   4 D  257  VAL TYR LYS PHE LEU LYS GLU ASN LEU SER ASP LEU THR
SEQRES   5 D  257  PHE LYS GLN TYR GLU TYR LEU ASN ASP LEU PHE MET LYS
SEQRES   6 D  257  ASN PRO ALA ILE ILE GLY HIS GLU ALA ARG TYR LYS LEU
SEQRES   7 D  257  PHE ASN SER PRO THR LEU LEU PHE LEU LEU SER ARG GLY
SEQRES   8 D  257  LYS ALA ALA THR GLU ASN TRP SER ILE GLU ASN LEU PHE
SEQRES   9 D  257  GLU GLU LYS GLN ASN ASP THR ALA ASP ILE LEU LEU VAL
SEQRES  10 D  257  LYS ASP GLN PHE TYR GLU LEU LEU ASP VAL LYS THR ARG
SEQRES  11 D  257  ASN ILE SER LYS SER ALA GLN ALA PRO ASN ILE ILE SER
SEQRES  12 D  257  ALA TYR LYS LEU ALA GLN THR CYS ALA LYS MET ILE ASP
SEQRES  13 D  257  ASN LYS GLU PHE ASP LEU PHE ASP ILE ASN TYR LEU GLU
SEQRES  14 D  257  VAL ASP TRP GLU LEU ASN GLY GLU ASP LEU VAL CYS VAL
SEQRES  15 D  257  SER THR SER PHE ALA GLU LEU PHE LYS SER GLU PRO SER
SEQRES  16 D  257  GLU LEU TYR ILE ASN TRP ALA ALA ALA MET GLN ILE GLN
SEQRES  17 D  257  PHE HIS VAL ARG ASP LEU ASP GLN GLY PHE ASN GLY THR
SEQRES  18 D  257  ARG GLU GLU TRP ALA LYS SER TYR LEU LYS HIS PHE VAL
SEQRES  19 D  257  THR GLN ALA GLU GLN ARG ALA ILE SER MET ILE ASP LYS
SEQRES  20 D  257  PHE VAL LYS PRO PHE LYS LYS TYR ILE LEU
HET     CA  A 801       1
HET     CA  B 802       1
HET     CA  C 803       1
HET     CA  D 804       1
HET     CA  F 805       1
HET     CA  H 806       1
HET     NA  A 901       1
HET     NA  B 902       1
HET     NA  C 903       1
HET     NA  D 904       1
HETNAM      CA CALCIUM ION
HETNAM      NA SODIUM ION
FORMUL   9   CA    6(CA 2+)
FORMUL  15   NA    4(NA 1+)
FORMUL  19  HOH   *765(H2 O)
HELIX    1   1 ILE A    4  PRO A    6  5                                   3
HELIX    2   2 ILE A    7  ILE A   16  1                                  10
HELIX    3   3 SER A   29  ALA A   33  5                                   5
HELIX    4   4 GLY A   34  LEU A   49  1                                  16
HELIX    5   5 GLN A   56  LYS A   66  1                                  11
HELIX    6   6 ILE A   71  LYS A   78  1                                   8
HELIX    7   7 LEU A   79  ASN A   81  5                                   3
HELIX    8   8 SER A   82  SER A   90  1                                   9
HELIX    9   9 GLY A   92  TRP A   99  1                                   8
HELIX   10  10 ALA A  145  LYS A  159  1                                  15
HELIX   11  11 PHE A  191  SER A  193  5                                   3
HELIX   12  12 GLU A  194  LEU A  198  5                                   5
HELIX   13  13 HIS A  211  LEU A  215  5                                   5
HELIX   14  14 THR A  222  VAL A  250  1                                  29
HELIX   15  15 LYS A  251  ILE A  257  5                                   7
HELIX   16  16 ILE B    4  PRO B    6  5                                   3
HELIX   17  17 ILE B    7  ILE B   16  1                                  10
HELIX   18  18 SER B   29  ALA B   33  5                                   5
HELIX   19  19 GLY B   34  PRO B   36  5                                   3
HELIX   20  20 PHE B   37  LEU B   49  1                                  13
HELIX   21  21 LYS B   55  LYS B   66  1                                  12
HELIX   22  22 GLY B   72  LEU B   79  1                                   8
HELIX   23  23 SER B   82  SER B   90  1                                   9
HELIX   24  24 GLY B   92  ASN B   98  1                                   7
HELIX   25  25 ALA B  145  ASN B  158  1                                  14
HELIX   26  26 PHE B  191  SER B  193  5                                   3
HELIX   27  27 HIS B  211  LEU B  215  5                                   5
HELIX   28  28 THR B  222  VAL B  250  1                                  29
HELIX   29  29 LYS B  251  LYS B  254  5                                   4
HELIX   30  30 ILE C    4  PRO C    6  5                                   3
HELIX   31  31 ILE C    7  ILE C   16  1                                  10
HELIX   32  32 GLY C   34  LEU C   49  1                                  16
HELIX   33  33 GLN C   56  LYS C   66  1                                  11
HELIX   34  34 GLU C   74  PHE C   80  5                                   7
HELIX   35  35 SER C   82  SER C   90  1                                   9
HELIX   36  36 ALA C   94  ASN C   98  5                                   5
HELIX   37  37 ALA C  145  ASP C  157  1                                  13
HELIX   38  38 PHE C  191  SER C  193  5                                   3
HELIX   39  39 THR C  222  VAL C  250  1                                  29
HELIX   40  40 ILE D    4  GLN D    9  5                                   6
HELIX   41  41 ASP D   10  ILE D   16  1                                   7
HELIX   42  42 GLY D   30  LEU D   49  1                                  20
HELIX   43  43 LYS D   55  LYS D   66  1                                  12
HELIX   44  44 GLY D   72  LEU D   79  1                                   8
HELIX   45  45 SER D   82  SER D   90  1                                   9
HELIX   46  46 GLY D   92  ASN D   98  1                                   7
HELIX   47  47 ALA D  145  ASN D  158  1                                  14
HELIX   48  48 PHE D  191  SER D  193  5                                   3
HELIX   49  49 THR D  222  ASP D  247  1                                  26
HELIX   50  50 PHE D  249  LYS D  254  1                                   6
SHEET    1   A 6 VAL A  20  LYS A  21  0
SHEET    2   A 6 ASP A 179  GLU A 189 -1  O  LEU A 180   N  VAL A  20
SHEET    3   A 6 PHE A 164  ASN A 176 -1  N  ASP A 172   O  VAL A 183
SHEET    4   A 6 PHE A 122  ASN A 132  1  N  LEU A 125   O  ASP A 165
SHEET    5   A 6 ILE A 115  LYS A 119 -1  N  ILE A 115   O  LEU A 126
SHEET    6   A 6 THR A  53  LYS A  55 -1  N  PHE A  54   O  LEU A 116
SHEET    1   B 3 ASN A 141  SER A 144  0
SHEET    2   B 3 GLN A 207  GLN A 209 -1  O  ILE A 208   N  ILE A 142
SHEET    3   B 3 ILE A 200  ASN A 201 -1  N  ASN A 201   O  GLN A 207
SHEET    1   C 6 LYS B  19  VAL B  20  0
SHEET    2   C 6 LEU B 180  GLU B 189 -1  O  LEU B 180   N  VAL B  20
SHEET    3   C 6 PHE B 164  LEU B 175 -1  N  TYR B 168   O  ALA B 188
SHEET    4   C 6 TYR B 123  ASN B 132  1  N  LYS B 129   O  VAL B 171
SHEET    5   C 6 ILE B 115  LEU B 117 -1  N  ILE B 115   O  LEU B 126
SHEET    6   C 6 THR B  53  PHE B  54 -1  N  PHE B  54   O  LEU B 116
SHEET    1   D 3 ASN B 141  SER B 144  0
SHEET    2   D 3 GLN B 207  GLN B 209 -1  O  ILE B 208   N  ILE B 143
SHEET    3   D 3 TYR B 199  ASN B 201 -1  N  ASN B 201   O  GLN B 207
SHEET    1   E 5 THR C  53  PHE C  54  0
SHEET    2   E 5 ILE C 115  VAL C 118 -1  O  LEU C 116   N  PHE C  54
SHEET    3   E 5 TYR C 123  ASN C 132 -1  O  LEU C 126   N  ILE C 115
SHEET    4   E 5 PHE C 164  ASN C 176  1  O  ASP C 165   N  LEU C 125
SHEET    5   E 5 ASP C 179  GLU C 189 -1  O  SER C 186   N  GLU C 170
SHEET    1   F 3 ASN C 141  SER C 144  0
SHEET    2   F 3 GLN C 207  GLN C 209 -1  O  ILE C 208   N  ILE C 143
SHEET    3   F 3 ILE C 200  ASN C 201 -1  N  ASN C 201   O  GLN C 207
SHEET    1   G 5 LYS D  19  LYS D  21  0
SHEET    2   G 5 ASP D 179  GLU D 189 -1  O  LEU D 180   N  VAL D  20
SHEET    3   G 5 PHE D 164  TRP D 173 -1  N  ASP D 172   O  VAL D 183
SHEET    4   G 5 PHE D 122  ASN D 132  1  N  LEU D 125   O  ASP D 165
SHEET    5   G 5 ILE D 115  LYS D 119 -1  N  ILE D 115   O  LEU D 126
SHEET    1   H 3 ASN D 141  SER D 144  0
SHEET    2   H 3 GLN D 207  GLN D 209 -1  O  ILE D 208   N  ILE D 143
SHEET    3   H 3 ILE D 200  ASN D 201 -1  N  ASN D 201   O  GLN D 207
LINK        CA    CA A 801                 O   VAL A 128     1555   1555  2.36
LINK        CA    CA A 801                 OD1 ASP A 114     1555   1555  2.32
LINK        CA    CA A 801                 OD1 ASP A 127     1555   1555  2.18
LINK        CA    CA A 801                 O   HOH F 806     1555   1555  2.21
LINK        CA    CA A 801                 OD2 ASP A 114     1555   1555  3.11
LINK        CA    CA A 801                 O   HOH A1058     1555   1555  2.23
LINK        CA    CA A 801                 OP1  DG F   8     1555   1555  2.24
LINK        NA    NA A 901                 OD2 ASP A 127     1555   1555  2.41
LINK        NA    NA A 901                 OP2  DG F   8     1555   1555  2.44
LINK        NA    NA A 901                 O   HOH A1060     1555   1555  2.55
LINK        NA    NA A 901                 O   ILE A 142     1555   1555  2.24
LINK        NA    NA A 901                 O   HOH A1066     1555   1555  2.49
LINK        CA    CA B 802                 O   HOH B1006     1555   1555  2.12
LINK        CA    CA B 802                 OP1  DG E   8     1555   1555  2.18
LINK        CA    CA B 802                 O   HOH E 244     1555   1555  2.56
LINK        CA    CA B 802                 OD1 ASP B 114     1555   1555  2.34
LINK        CA    CA B 802                 O   VAL B 128     1555   1555  2.39
LINK        CA    CA B 802                 OD2 ASP B 127     1555   1555  2.28
LINK        NA    NA B 902                 O   ILE B 142     1555   1555  2.35
LINK        NA    NA B 902                 O   HOH B 998     1555   1555  2.15
LINK        NA    NA B 902                 OP2  DG E   8     1555   1555  2.47
LINK        NA    NA B 902                 OD1 ASP B 127     1555   1555  2.20
LINK        NA    NA B 902                 O   HOH B 976     1555   1555  2.39
LINK        CA    CA C 803                 OP1  DG H   8     1555   1555  2.29
LINK        CA    CA C 803                 O   HOH C 971     1555   1555  2.07
LINK        CA    CA C 803                 OD2 ASP C 114     1555   1555  2.37
LINK        CA    CA C 803                 OD1 ASP C 127     1555   1555  2.17
LINK        CA    CA C 803                 O   VAL C 128     1555   1555  2.43
LINK        NA    NA C 903                 O   ILE C 142     1555   1555  2.08
LINK        CA    CA D 804                 OD2 ASP D 114     1555   1555  2.52
LINK        CA    CA D 804                 OD2 ASP D 127     1555   1555  2.24
LINK        CA    CA D 804                 O   VAL D 128     1555   1555  2.31
LINK        CA    CA D 804                 O   HOH D 922     1555   1555  2.35
LINK        CA    CA D 804                 OP2  DG G   8     1555   1555  3.34
LINK        CA    CA D 804                 OP1  DG G   8     1555   1555  2.33
LINK        CA    CA D 804                 OD1 ASP D 114     1555   1555  3.11
LINK        NA    NA D 904                 NZ  LYS D 129     1555   1555  2.60
LINK        NA    NA D 904                 O   ILE D 142     1555   1555  2.24
LINK        NA    NA D 904                 O   HOH G 551     1555   1555  2.52
LINK        NA    NA D 904                 O   HOH D 989     1555   1555  2.43
LINK        NA    NA D 904                 OP2  DG G   8     1555   1555  2.31
LINK        NA    NA D 904                 OD1 ASP D 127     1555   1555  2.15
LINK        CA    CA F 805                 O   HOH B1059     1555   1555  2.95
LINK        CA    CA F 805                 O   HOH F 841     1555   1555  2.28
LINK        CA    CA F 805                 O6   DG F   1     1555   1555  3.04
LINK        CA    CA F 805                 N4   DC F   2     1555   1555  2.87
LINK        CA    CA H 806                 O6   DG H   1     1555   1555  1.98
LINK        CA    CA H 806                 O   HOH H  43     1555   1555  2.76
LINK        CA    CA F 805                 O6   DG F   1     1555   6655  2.31
LINK        CA    CA F 805                 O   HOH F 841     1555   6655  2.39
LINK        CA    CA H 806                 O6   DG H   1     1555   7557  2.96
LINK        CA    CA H 806                 O   HOH H  43     1555   7557  3.17
LINK         NZ  LYS A 129                NA    NA A 901     1555   1555  2.67
LINK        NA    NA C 903                 O   HOH C 967     1555   1555  2.90
LINK         OP2  DG H   8                NA    NA C 903     1555   1555  3.09
LINK        NA    NA B 902                 O   HOH B1054     1555   1555  3.18
SITE     1 AC1  6 ASP A 114  ASP A 127  VAL A 128  HOH A1058
SITE     2 AC1  6  DG F   8  HOH F 806
SITE     1 AC2  6 ASP B 114  ASP B 127  VAL B 128  HOH B1006
SITE     2 AC2  6  DG E   8  HOH E 244
SITE     1 AC3  5 ASP C 114  ASP C 127  VAL C 128  HOH C 971
SITE     2 AC3  5  DG H   8
SITE     1 AC4  5 ASP D 114  ASP D 127  VAL D 128  HOH D 922
SITE     2 AC4  5  DG G   8
SITE     1 AC5  5 HOH B1059   DG E  12   DG F   1   DC F   2
SITE     2 AC5  5 HOH F 841
SITE     1 AC6  2  DG H   1  HOH H  43
SITE     1 AC7  6 ASP A 127  LYS A 129  ILE A 142  HOH A1060
SITE     2 AC7  6 HOH A1066   DG F   8
SITE     1 AC8  6 ASP B 127  LYS B 129  ILE B 142  HOH B 976
SITE     2 AC8  6 HOH B 998   DG E   8
SITE     1 AC9  7 ASP C 127  LYS C 129  ILE C 142  ILE C 143
SITE     2 AC9  7 HOH C 967   DC H   7   DG H   8
SITE     1 BC1  6 ASP D 127  LYS D 129  ILE D 142  HOH D 989
SITE     2 BC1  6  DG G   8  HOH G 551
CRYST1   66.945  177.180  254.890  90.00  90.00  90.00 I 21 21 21   32
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      0.014938  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005644  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003923        0.00000
      
PROCHECK
Go to PROCHECK summary
 References