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PDBsum entry 2hoc

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Top Page protein ligands metals links
Lyase PDB id
2hoc
Jmol
Contents
Protein chain
258 a.a.
Ligands
1CN ×2
MBO
GOL
Metals
_ZN
Waters ×161
HEADER    LYASE                                   14-JUL-06   2HOC
TITLE     CRYSTAL STRUCTURE OF THE HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH
TITLE    2 THE 5-(4-AMINO-3-CHLORO-5-FLUOROPHENYLSULFONAMIDO)-1,3,4-THIADIAZOLE-
TITLE    3 2-SULFONAMIDE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CARBONATE DEHYDRATASE II, CA-II,
COMPND   5 CARBONIC ANHYDRASE C;
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 OTHER_DETAILS: HUMAN ERYTHROCYTES
KEYWDS    PROTEIN-INHIBITOR COMPLEX, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.MENCHISE,A.DI FIORE,G.DE SIMONE
REVDAT   5   21-SEP-11 2HOC    1       HETATM
REVDAT   4   13-JUL-11 2HOC    1       VERSN
REVDAT   3   24-FEB-09 2HOC    1       VERSN
REVDAT   2   28-NOV-06 2HOC    1       JRNL
REVDAT   1   10-OCT-06 2HOC    0
JRNL        AUTH   V.MENCHISE,G.D.SIMONE,A.D.FIORE,A.SCOZZAFAVA,C.T.SUPURAN
JRNL        TITL   CARBONIC ANHYDRASE INHIBITORS: X-RAY CRYSTALLOGRAPHIC
JRNL        TITL 2 STUDIES FOR THE BINDING OF
JRNL        TITL 3 5-AMINO-1,3,4-THIADIAZOLE-2-SULFONAMIDE AND
JRNL        TITL 4 5-(4-AMINO-3-CHLORO-5-FLUOROPHENYLSULFONAMIDO)-1,3,4-
JRNL        TITL 5 THIADIAZOLE-2-SULFONAMIDE TO HUMAN ISOFORM II.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  6204 2006
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   17000110
JRNL        DOI    10.1016/J.BMCL.2006.09.022
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   A.E.ERIKSSON,T.A.JONES,A.LILJAS
REMARK   1  TITL   REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 A
REMARK   1  TITL 2 RESOLUTION.
REMARK   1  REF    PROTEINS:                     V.   4   274 1988
REMARK   1  REF  2 STRUCT.,FUNCT.,GENET.
REMARK   1  REFN                   ISSN 0887-3585
REMARK   1  PMID   3151019
REMARK   1  DOI    10.1002/PROT.340040406
REMARK   2
REMARK   2 RESOLUTION.    2.10 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) : 2.10
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 11351
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.184
REMARK   3   FREE R VALUE                     : 0.223
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 616
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            : 2059
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 61
REMARK   3   SOLVENT ATOMS            : 161
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
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) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_TRIS.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : INI10.PAR
REMARK   3  PARAMETER FILE  5  : GOL_LOW.PAR
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2HOC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB038573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.2
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) : 1.2
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12269
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
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     (%) : 87.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08000
REMARK 200   FOR THE DATA SET  : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.23600
REMARK 200   FOR SHELL         : 4.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1CA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, SODIUM CHLORIDE,
REMARK 280  TRIS-HCL, 4-(HYDROXYMERCURYBENZOATE), PH 8.2, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293K
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       20.70000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER.
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 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     SER A     2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     HIS A    3   CB   CG   ND1  CD2  CE1  NE2
REMARK 480     HIS A    4   C    CB   CG   ND1  CD2  CE1  NE2
REMARK 480     LYS A    9   CG   CD   CE   NZ
REMARK 480     LYS A   45   C    CG   CD   CE   NZ
REMARK 480     LYS A   80   CG   CD   CE   NZ
REMARK 480     LYS A  159   CD   CE   NZ
REMARK 480     GLU A  236   OE2
REMARK 480     LYS A  257   CE   NZ
REMARK 480     LYS A  261   CG   CD   CE   NZ
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    ASN A  11       18.46   -141.36
REMARK 500    ILE A  22       -9.35    -59.60
REMARK 500    ALA A  65     -170.20   -172.31
REMARK 500    LYS A 111       -6.32     72.23
REMARK 500    ASN A 244       45.96    -90.88
REMARK 500    LYS A 252     -128.40     51.60
REMARK 500    ASN A 253       59.37    -90.44
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                             MBO A 267  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 206   SG
REMARK 620 2 MBO A 267   CE1 171.0
REMARK 620 3 GLN A 137   O    84.5 100.0
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 263  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 107.1
REMARK 620 3 HIS A 119   ND1 116.2 105.5
REMARK 620 4 1CN A 265   N1  109.6 108.0 110.1
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 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CN A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBO A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HNC   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CARBONIC ANHYDRASE II IN
REMARK 900 COMPLEX WITH THE 5-AMINO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1CA2   RELATED DB: PDB
REMARK 900 REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0
REMARK 900 ANGSTROMS RESOLUTION
DBREF  2HOC A    2   260  UNP    P00918   CAH2_HUMAN       1    259
SEQRES   1 A  259  SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU
SEQRES   2 A  259  HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG
SEQRES   3 A  259  GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES   4 A  259  ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES   5 A  259  ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES   6 A  259  ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES   7 A  259  LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES   8 A  259  PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES   9 A  259  GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU
SEQRES  10 A  259  HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES  11 A  259  LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES  12 A  259  ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES  13 A  259  LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES  14 A  259  LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES  15 A  259  LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES  16 A  259  LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES  17 A  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES  18 A  259  LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES  19 A  259  PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES  20 A  259  PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 263       1
HET    1CN  A 265      22
HET    1CN  A 266      22
HET    MBO  A 267      10
HET    GOL  A 702       6
HETNAM      ZN ZINC ION
HETNAM     1CN 5-{[(4-AMINO-3-CHLORO-5-FLUOROPHENYL)SULFONYL]AMINO}-1,
HETNAM   2 1CN  3,4-THIADIAZOLE-2-SULFONAMIDE
HETNAM     MBO MERCURIBENZOIC ACID
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  1CN    2(C8 H7 CL F N5 O4 S3)
FORMUL   5  MBO    C7 H5 HG O2
FORMUL   6  GOL    C3 H8 O3
FORMUL   7  HOH   *161(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  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 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU 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  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  GLN A  92   O  VAL A 121
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  PHE A  70   O  ILE A  91
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LYS A  45  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  82 -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  VAL A 121   N  GLN A  92
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  VAL A 218   N  LYS A 149
LINK         SG  CYS A 206                HG   MBO A 267     1555   1555  2.11
LINK         NE2 HIS A  94                ZN    ZN A 263     1555   1555  2.07
LINK         NE2 HIS A  96                ZN    ZN A 263     1555   1555  2.04
LINK         ND1 HIS A 119                ZN    ZN A 263     1555   1555  1.99
LINK        ZN    ZN A 263                 N1  1CN A 265     1555   1555  1.98
LINK         O   GLN A 137                HG   MBO A 267     1555   1555  2.97
CISPEP   1 SER A   29    PRO A   30          0        -0.09
CISPEP   2 PRO A  201    PRO A  202          0         1.78
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  1CN A 265
SITE     1 AC2 13 HIS A  94  HIS A  96  HIS A 119  PHE A 131
SITE     2 AC2 13 VAL A 135  LEU A 198  THR A 199  THR A 200
SITE     3 AC2 13 LEU A 204  TRP A 209   ZN A 263  HOH A 525
SITE     4 AC2 13 GOL A 702
SITE     1 AC3 10 PHE A  20  PRO A  21  ILE A  22  VAL A 135
SITE     2 AC3 10 GLN A 136  PRO A 202  LEU A 204  GLU A 205
SITE     3 AC3 10 MBO A 267  HOH A 404
SITE     1 AC4  6 GLN A 137  PRO A 138  GLU A 205  CYS A 206
SITE     2 AC4  6 1CN A 266  HOH A 413
SITE     1 AC5  7 ASN A  62  HIS A  64  ASN A  67  GLN A  92
SITE     2 AC5  7 HIS A  94  1CN A 265  HOH A 411
CRYST1   42.100   41.400   71.730  90.00 104.31  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      0.023753  0.000000  0.006059        0.00000
SCALE2      0.000000  0.024155  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014388        0.00000
      
PROCHECK
Go to PROCHECK summary
 References