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PDBsum entry 3lxe

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3lxe
Jmol
Contents
Protein chains
256 a.a.
Ligands
TOR ×2
Metals
_ZN ×2
Waters ×470
HEADER    LYASE                                   25-FEB-10   3LXE
TITLE     HUMAN CARBONIC ANHYDRASE I IN COMPLEX WITH TOPIRAMATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE I, CA-I, CARBONATE DEHYDRATASE I,
COMPND   5 CARBONIC ANHYDRASE B, CAB;
COMPND   6 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 TISSUE: RED BLOOD CELL
KEYWDS    CARBONIC ANHYDRASE 1, TOPIRAMATE, ENZYME-INHIBITOR COMPLEX, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.ALTERIO,G.DE SIMONE,S.M.MONTI,E.TRUPPO
REVDAT   1   21-JUL-10 3LXE    0
JRNL        AUTH   V.ALTERIO,S.M.MONTI,E.TRUPPO,C.PEDONE,C.T.SUPURAN,
JRNL        AUTH 2 G.DE SIMONE
JRNL        TITL   THE FIRST EXAMPLE OF A SIGNIFICANT ACTIVE SITE
JRNL        TITL 2 CONFORMATIONAL REARRANGEMENT IN A CARBONIC
JRNL        TITL 3 ANHYDRASE-INHIBITOR ADDUCT: THE CARBONIC ANHYDRASE
JRNL        TITL 4 I-TOPIRAMATE COMPLEX.
JRNL        REF    ORG.BIOMOL.CHEM.                           2010
JRNL        REFN                   ESSN 1477-0539
JRNL        PMID   20505865
JRNL        DOI    10.1039/B926832D
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.2
REMARK   3   NUMBER OF REFLECTIONS             : 39341
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.228
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1956
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            : 4016
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 46
REMARK   3   SOLVENT ATOMS            : 470
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.00
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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 3LXE COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB057849.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ELETTRA
REMARK 200  BEAMLINE                       : 5.2R
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41817
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : 0.06700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.33400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.300
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: 2CAB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/V PEG 4000, 0.2M SODIUM ACETATE,
REMARK 280  0.1M TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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       31.66000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.33000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.53500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.33000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.66000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.53500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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     ALA A     1
REMARK 465     SER A     2
REMARK 465     PRO A     3
REMARK 465     ASP A     4
REMARK 465     ALA B     1
REMARK 465     SER B     2
REMARK 465     PRO B     3
REMARK 465     ASP B     4
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    SER A  65     -160.02   -162.69
REMARK 500    ASN A  75       43.83    -95.44
REMARK 500    PHE A  91      -11.04   -140.52
REMARK 500    ASN A 124       97.57    -69.71
REMARK 500    ASN A 244       33.65   -152.60
REMARK 500    SER B  65     -160.13   -168.39
REMARK 500    ASN B  75       45.78    -98.44
REMARK 500    PHE B  91      -13.19   -140.46
REMARK 500    ASN B 124       93.74    -68.33
REMARK 500    ASN B 244       35.03   -160.10
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 B 261  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TOR B 262   NAP
REMARK 620 2 HIS B  96   NE2 111.9
REMARK 620 3 HIS B  94   NE2 111.0 105.4
REMARK 620 4 HIS B 119   ND1 115.0  97.4 115.0
REMARK 620 5 TOR B 262   SAO  27.8 139.7  96.0 104.0
REMARK 620 N                    1     2     3     4
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 TOR A 262   NAP
REMARK 620 2 HIS A  96   NE2 108.9
REMARK 620 3 HIS A  94   NE2 115.4 107.3
REMARK 620 4 HIS A 119   ND1 115.0  98.2 110.5
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
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TOR A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TOR B 262
DBREF  3LXE A    1   260  UNP    P00915   CAH1_HUMAN       2    261
DBREF  3LXE B    1   260  UNP    P00915   CAH1_HUMAN       2    261
SEQRES   1 A  260  ALA SER PRO ASP TRP GLY TYR ASP ASP LYS ASN GLY PRO
SEQRES   2 A  260  GLU GLN TRP SER LYS LEU TYR PRO ILE ALA ASN GLY ASN
SEQRES   3 A  260  ASN GLN SER PRO VAL ASP ILE LYS THR SER GLU THR LYS
SEQRES   4 A  260  HIS ASP THR SER LEU LYS PRO ILE SER VAL SER TYR ASN
SEQRES   5 A  260  PRO ALA THR ALA LYS GLU ILE ILE ASN VAL GLY HIS SER
SEQRES   6 A  260  PHE HIS VAL ASN PHE GLU ASP ASN ASP ASN ARG SER VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES  10 A  260  LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES  11 A  260  LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES  12 A  260  ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES  13 A  260  LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES  14 A  260  LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES  15 A  260  THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES  16 A  260  GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES  17 A  260  TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES  18 A  260  GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES  19 A  260  GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES  20 A  260  THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
SEQRES   1 B  260  ALA SER PRO ASP TRP GLY TYR ASP ASP LYS ASN GLY PRO
SEQRES   2 B  260  GLU GLN TRP SER LYS LEU TYR PRO ILE ALA ASN GLY ASN
SEQRES   3 B  260  ASN GLN SER PRO VAL ASP ILE LYS THR SER GLU THR LYS
SEQRES   4 B  260  HIS ASP THR SER LEU LYS PRO ILE SER VAL SER TYR ASN
SEQRES   5 B  260  PRO ALA THR ALA LYS GLU ILE ILE ASN VAL GLY HIS SER
SEQRES   6 B  260  PHE HIS VAL ASN PHE GLU ASP ASN ASP ASN ARG SER VAL
SEQRES   7 B  260  LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES   8 B  260  GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES   9 B  260  SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES  10 B  260  LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES  11 B  260  LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES  12 B  260  ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES  13 B  260  LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES  14 B  260  LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES  15 B  260  THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES  16 B  260  GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES  17 B  260  TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES  18 B  260  GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES  19 B  260  GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES  20 B  260  THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
HET     ZN  A 261       1
HET    TOR  A 262      22
HET     ZN  B 261       1
HET    TOR  B 262      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   3   ZN    2(ZN 2+)
FORMUL   4  TOR    2(C12 H21 N O8 S)
FORMUL   7  HOH   *470(H2 O)
HELIX    1   1 GLY A   12  LEU A   19  5                                   8
HELIX    2   2 TYR A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A   34  THR A   38  5                                   5
HELIX    4   4 ASN A   52  ALA A   54  5                                   3
HELIX    5   5 SER A  130  ALA A  135  1                                   6
HELIX    6   6 ASN A  154  LYS A  156  5                                   3
HELIX    7   7 LEU A  157  LEU A  164  1                                   8
HELIX    8   8 GLN A  165  ILE A  167  5                                   3
HELIX    9   9 ASP A  180  LEU A  185  5                                   6
HELIX   10  10 SER A  219  SER A  228  1                                  10
HELIX   11  11 GLY B   12  GLU B   14  5                                   3
HELIX   12  12 GLN B   15  TYR B   20  1                                   6
HELIX   13  13 PRO B   21  GLY B   25  5                                   5
HELIX   14  14 ASN B   52  ALA B   54  5                                   3
HELIX   15  15 SER B  130  ALA B  135  1                                   6
HELIX   16  16 ASN B  154  LYS B  156  5                                   3
HELIX   17  17 LEU B  157  LEU B  164  1                                   8
HELIX   18  18 GLN B  165  ILE B  167  5                                   3
HELIX   19  19 ASP B  180  LEU B  185  5                                   6
HELIX   20  20 SER B  219  SER B  228  1                                  10
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  HIS A  40  0
SHEET    2   B10 ARG A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 PHE A 191  GLY A 196 -1  N  THR A 193   O  ARG A 257
SHEET    4   B10 VAL A 207  CYS A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  HIS A 122   O  ALA A 142
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  ARG A  89   O  TRP A 123
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 ALA A  56  ASN A  61 -1  N  GLU A  58   O  ASN A  69
SHEET   10   B10 ARG A 173  PRO A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 ILE 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  TRP A 123   N  ARG A  89
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ALA A 142   N  HIS A 122
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  LYS A 149
SHEET    1   D 2 ASP B  32  ILE B  33  0
SHEET    2   D 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1   E10 LYS B  39  HIS B  40  0
SHEET    2   E10 ARG B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   E10 PHE B 191  GLY B 196 -1  N  THR B 193   O  ARG B 257
SHEET    4   E10 VAL B 207  CYS B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   E10 LEU B 141  VAL B 150  1  N  GLY B 145   O  ILE B 210
SHEET    6   E10 ALA B 116  ASN B 124 -1  N  ALA B 116   O  MET B 148
SHEET    7   E10 TYR B  88  TRP B  97 -1  N  ARG B  89   O  TRP B 123
SHEET    8   E10 PHE B  66  PHE B  70 -1  N  VAL B  68   O  PHE B  93
SHEET    9   E10 ALA B  56  ASN B  61 -1  N  GLU B  58   O  ASN B  69
SHEET   10   E10 ARG B 173  PRO B 175 -1  O  ALA B 174   N  ILE B  59
SHEET    1   F 6 ILE B  47  SER B  50  0
SHEET    2   F 6 VAL B  78  GLY B  81 -1  O  LYS B  80   N  SER B  48
SHEET    3   F 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  LEU B  79
SHEET    4   F 6 ALA B 116  ASN B 124 -1  O  TRP B 123   N  ARG B  89
SHEET    5   F 6 LEU B 141  VAL B 150 -1  O  MET B 148   N  ALA B 116
SHEET    6   F 6 ILE B 216  VAL B 218  1  O  ILE B 216   N  LYS B 149
LINK        ZN    ZN B 261                 NAP TOR B 262     1555   1555  1.89
LINK         NE2 HIS B  96                ZN    ZN B 261     1555   1555  1.98
LINK        ZN    ZN A 261                 NAP TOR A 262     1555   1555  2.00
LINK         NE2 HIS A  96                ZN    ZN A 261     1555   1555  2.02
LINK         NE2 HIS B  94                ZN    ZN B 261     1555   1555  2.06
LINK         NE2 HIS A  94                ZN    ZN A 261     1555   1555  2.09
LINK         ND1 HIS A 119                ZN    ZN A 261     1555   1555  2.10
LINK         ND1 HIS B 119                ZN    ZN B 261     1555   1555  2.13
LINK        ZN    ZN B 261                 SAO TOR B 262     1555   1555  3.00
CISPEP   1 SER A   29    PRO A   30          0         0.16
CISPEP   2 PRO A  201    PRO A  202          0         0.97
CISPEP   3 SER B   29    PRO B   30          0        -0.42
CISPEP   4 PRO B  201    PRO B  202          0         0.13
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  TOR A 262
SITE     1 AC2  4 HIS B  94  HIS B  96  HIS B 119  TOR B 262
SITE     1 AC3 11 HIS A  64  SER A  65  GLN A  92  HIS A  94
SITE     2 AC3 11 HIS A  96  HIS A 119  LEU A 198  THR A 199
SITE     3 AC3 11 HIS A 200   ZN A 261  HOH A 442
SITE     1 AC4 11 HIS B  64  SER B  65  GLN B  92  HIS B  94
SITE     2 AC4 11 HIS B  96  HIS B 119  LEU B 198  THR B 199
SITE     3 AC4 11 HIS B 200   ZN B 261  HOH B 469
CRYST1   63.320   71.070  120.660  90.00  90.00  90.00 P 21 21 21    8
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      0.015793  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014071  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008288        0.00000
      
PROCHECK
Go to PROCHECK summary
 References