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PDBsum entry 3hku

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Lyase PDB id
3hku
Jmol
Contents
Protein chain
257 a.a.
Ligands
TOR
Metals
_ZN
Waters ×354
HEADER    LYASE                                   25-MAY-09   3HKU
TITLE     HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH TOPIRAMATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE
COMPND   5 DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLSMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET8C
KEYWDS    CARBONIC ANHYDRASE DRUG DESIGN, ACETYLATION, CYTOPLASM,
KEYWDS   2 DISEASE MUTATION, LYASE, METAL-BINDING, POLYMORPHISM, ZINC
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.PAUL,S.-A.POULSEN,A.HOFMANN
REVDAT   1   13-OCT-09 3HKU    0
JRNL        AUTH   M.LOPEZ,B.PAUL,A.HOFMANN,J.MORIZZI,Q.WU,
JRNL        AUTH 2 S.A.CHARMAN,A.INNOCENTI,D.VULLO,C.T.SUPURAN,
JRNL        AUTH 3 S.-A.POULSEN
JRNL        TITL   S-GLYCOSYL PRIMARY SULFONAMIDES-A NEW STRUCTURAL
JRNL        TITL 2 CLASS FOR SELECTIVE INHIBITION OF CANCER-ASSOCIATED
JRNL        TITL 3 CARBONIC ANHYDRASES
JRNL        REF    J.MED.CHEM.                                2009
JRNL        REFN                   ISSN 0022-2623
JRNL        DOI    10.1021/JM900914E
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.19
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 21463
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 + TEST SET) : 0.155
REMARK   3   R VALUE            (WORKING SET) : 0.152
REMARK   3   FREE R VALUE                     : 0.198
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1156
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1544
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.09
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1670
REMARK   3   BIN FREE R VALUE SET COUNT          : 76
REMARK   3   BIN FREE R VALUE                    : 0.2790
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2049
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 23
REMARK   3   SOLVENT ATOMS            : 354
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 13.63
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.83
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.06000
REMARK   3    B22 (A**2) : 0.04000
REMARK   3    B33 (A**2) : -0.03000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.14000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.127
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.122
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.259
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2134 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2905 ; 1.368 ; 1.967
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   256 ; 6.441 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    98 ;35.007 ;24.694
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   352 ;13.298 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;20.609 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   306 ; 0.096 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1627 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1050 ; 0.201 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1418 ; 0.307 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   297 ; 0.149 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.079 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    49 ; 0.185 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    43 ; 0.204 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1320 ; 0.802 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2065 ; 1.335 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   944 ; 2.210 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   840 ; 3.394 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3HKU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 9.5
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 MICROMAX-007 HF
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21463
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.200
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.03300
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) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.05800
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.6M (NH4)2SO4, PH 9.5, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K
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       20.71300
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MET A     1
REMARK 465     SER A     2
REMARK 465     HIS A     3
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    HOH A   361     O    HOH A   403              2.04
REMARK 500   O    HOH A   365     O    HOH A   489              2.11
REMARK 500   O    HOH A   441     O    HOH A   584              2.12
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 A   469     O    HOH A   580     1455     2.18
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    ARG A  27       59.68   -145.22
REMARK 500    LEU A  57      -54.73   -123.31
REMARK 500    HIS A  64      -50.80   -121.16
REMARK 500    ALA A  65     -149.15   -149.02
REMARK 500    GLU A 106      -61.58    -90.21
REMARK 500    LYS A 111       -3.87     72.58
REMARK 500    PHE A 175       50.81   -145.99
REMARK 500    ASN A 243       51.66    -96.67
REMARK 500    LYS A 251     -137.51     54.57
REMARK 500
REMARK 500 REMARK: NULL
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                              ZN A 261  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 107.7
REMARK 620 3 HIS A 119   ND1 113.2  98.2
REMARK 620 4 TOR A 300   NAP 111.3 112.7 112.9
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 261
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TOR A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HKQ   RELATED DB: PDB
REMARK 900 RELATED ID: 3HKT   RELATED DB: PDB
DBREF  3HKU A    1   260  UNP    P00918   CAH2_HUMAN       1    260
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 A  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 261       1
HET    TOR  A 300      22
HETNAM      ZN ZINC ION
HETNAM     TOR [(3AS,5AR,8AR,8BS)-2,2,7,7-TETRAMETHYLTETRAHYDRO-3AH-
HETNAM   2 TOR  BIS[1,3]DIOXOLO[4,5-B:4',5'-D]PYRAN-3A-YL]METHYL
HETNAM   3 TOR  SULFAMATE
HETSYN     TOR TOPIRAMATE
FORMUL   2   ZN    ZN 2+
FORMUL   3  TOR    C12 H21 N O8 S
FORMUL   4  HOH   *354(H2 O)
HELIX    1   1 PHE A   20  GLY A   25  5                                   6
HELIX    2   2 LYS A  126  GLY A  128  5                                   3
HELIX    3   3 ASP A  129  VAL A  134  1                                   6
HELIX    4   4 LYS A  153  GLY A  155  5                                   3
HELIX    5   5 LEU A  156  LEU A  163  1                                   8
HELIX    6   6 ASP A  164  LYS A  167  5                                   4
HELIX    7   7 ASP A  179  LEU A  184  5                                   6
HELIX    8   8 SER A  218  ARG A  226  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 256  ALA A 257  1  O  ALA A 257   N  LYS A  39
SHEET    3   B10 TYR A 190  GLY A 195 -1  N  THR A 192   O  LYS A 256
SHEET    4   B10 VAL A 206  LEU A 211 -1  O  VAL A 206   N  GLY A 195
SHEET    5   B10 LEU A 140  VAL A 149  1  N  GLY A 144   O  ILE A 209
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 145
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  ARG A  58   O  GLU A  69
SHEET   10   B10 SER A 172  ASP A 174 -1  O  ALA A 173   N  ILE A  59
SHEET    1   C 6 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  LYS A  80   N  SER A  48
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 140  VAL A 149 -1  O  ILE A 145   N  LEU A 118
SHEET    6   C 6 ILE A 215  VAL A 217  1  O  ILE A 215   N  PHE A 146
LINK         NE2 HIS A  94                ZN    ZN A 261     1555   1555  1.98
LINK         NE2 HIS A  96                ZN    ZN A 261     1555   1555  2.05
LINK         ND1 HIS A 119                ZN    ZN A 261     1555   1555  2.09
LINK        ZN    ZN A 261                 NAP TOR A 300     1555   1555  1.95
CISPEP   1 SER A   29    PRO A   30          0        -0.91
CISPEP   2 PRO A  200    PRO A  201          0         8.80
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  TOR A 300
SITE     1 AC2 13 ASN A  62  ALA A  65  ASN A  67  GLN A  92
SITE     2 AC2 13 HIS A  94  HIS A  96  HIS A 119  VAL A 142
SITE     3 AC2 13 LEU A 197  THR A 198  THR A 199   ZN A 261
SITE     4 AC2 13 HOH A 343
CRYST1   42.264   41.426   72.440  90.00 104.59  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      0.023661  0.000000  0.006158        0.00000
SCALE2      0.000000  0.024139  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014264        0.00000
      
PROCHECK
Go to PROCHECK summary
 References