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PDBsum entry 1g0f

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Lyase PDB id
1g0f
Jmol
Contents
Protein chain
258 a.a. *
Metals
_HG
_ZN
Waters ×212
* Residue conservation analysis
HEADER    LYASE                                   06-OCT-00   1G0F
TITLE     SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN
TITLE    2 CARBONIC ANHYDRASE II
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 TISSUE: BLOOD;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS    TWISTED BETA SHEET, ZINC METALLOENZYME, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.DUDA,R.MCKENNA
REVDAT   4   24-FEB-09 1G0F    1       VERSN
REVDAT   3   17-AUG-01 1G0F    1       DBREF
REVDAT   2   16-MAY-01 1G0F    1       JRNL
REVDAT   1   18-OCT-00 1G0F    0
JRNL        AUTH   D.DUDA,C.TU,M.QIAN,P.LAIPIS,M.AGBANDJE-MCKENNA,
JRNL        AUTH 2 D.N.SILVERMAN,R.MCKENNA
JRNL        TITL   STRUCTURAL AND KINETIC ANALYSIS OF THE CHEMICAL
JRNL        TITL 2 RESCUE OF THE PROTON TRANSFER FUNCTION OF CARBONIC
JRNL        TITL 3 ANHYDRASE II.
JRNL        REF    BIOCHEMISTRY                  V.  40  1741 2001
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   11327835
JRNL        DOI    10.1021/BI002295Z
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.HAKANSSON,M.CARLSSON,L.A.SVENSSON,A.LILJAS
REMARK   1  TITL   STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II
REMARK   1  TITL 2 AND STRUCTURE OF SOME OF ITS ANION-LIGAND
REMARK   1  TITL 3 COMPLEXES.
REMARK   1  REF    J.MOL.BIOL.                   V. 227  1192 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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 : BRUNGER & ADAMS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1004536.990
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.6
REMARK   3   NUMBER OF REFLECTIONS             : 26736
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 SET) : 0.179
REMARK   3   FREE R VALUE                     : 0.198
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 1299
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 65.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3370
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120
REMARK   3   BIN FREE R VALUE                    : 0.2280
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 179
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2054
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 212
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.90
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.76000
REMARK   3    B22 (A**2) : -1.36000
REMARK   3    B33 (A**2) : -0.41000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.07000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16
REMARK   3   ESD FROM SIGMAA              (A) : 0.07
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.18
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.07
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.34
REMARK   3   BSOL        : 51.60
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  : ION.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ION.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1G0F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-00.
REMARK 100 THE RCSB ID CODE IS RCSB012077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-00
REMARK 200  TEMPERATURE           (KELVIN) : 300.0
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 5
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
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27019
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.6
REMARK 200  DATA REDUNDANCY                : 5.170
REMARK 200  R MERGE                    (I) : 0.05200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 19.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 25.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.17
REMARK 200  R MERGE FOR SHELL          (I) : 0.05200
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MERCURY CHLORIDE,
REMARK 280  TRIS HCL, PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  277K
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       20.80800
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 CONSTRUCTED FROM
REMARK 300 CHAIN A
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     MET A     1
REMARK 465     SER A     2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    LEU A  57      -50.14   -123.25
REMARK 500    ALA A  65     -167.03   -169.62
REMARK 500    LYS A 111       -1.80     72.30
REMARK 500    GLU A 234     -130.81     25.07
REMARK 500    ASN A 244       50.23    -95.32
REMARK 500    LYS A 252     -142.41     56.35
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 272        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH A 405        DISTANCE =  6.98 ANGSTROMS
REMARK 525    HOH A 452        DISTANCE =  5.46 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                              ZN A 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 103.4
REMARK 620 3 HIS A 119   ND1 112.8  99.9
REMARK 620 4 HOH A 428   O   108.1 130.6 101.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              HG A 263  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 432   O
REMARK 620 2 CYS A 206   SG  177.3
REMARK 620 3 GLN A 137   O    89.6  91.0
REMARK 620 4 HOH A 389   O    94.3  86.7 145.6
REMARK 620 5 GLU A 205   O    89.9  87.4  96.7 117.4
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800 SITE_IDENTIFIER: HG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NONE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 263
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G0E   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II WITH 4-METHYLIMIDAZOLE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 125 AND 127 ARE COVALENTLY BOUND.
DBREF  1G0F A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQADV 1G0F ALA A   64  UNP  P00918    HIS    63 ENGINEERED
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 ALA 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 262       1
HET     HG  A 263       1
HETNAM      ZN ZINC ION
HETNAM      HG MERCURY (II) ION
FORMUL   2   ZN    ZN 2+
FORMUL   3   HG    HG 2+
FORMUL   4  HOH   *212(H2 O)
HELIX    1   A PRO A   13  LYS A   18  5                                   6
HELIX    2   B PRO A   21  LYS A   24  5                                   4
HELIX    3   C THR A  125  TYR A  128  5                                   3
HELIX    4   D PHE A  131  ALA A  134  1                                   4
HELIX    5  E1 PRO A  155  LEU A  157  5                                   3
HELIX    6  E2 GLN A  158  VAL A  163  1                                   6
HELIX    7  E3 LEU A  164  ILE A  167  5                                   4
HELIX    8   F PRO A  181  LEU A  184  5                                   4
HELIX    9   G SER A  220  PHE A  226  1                                   7
SHEET    1 B1A10 LYS A  39  TYR A  40  0
SHEET    2 B1A10 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3 B1A10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4 B1A10 VAL A 207  LEU A 212 -1  N  VAL A 211   O  TRP A 192
SHEET    5 B1A10 LEU A 141  GLY A 151  1  O  VAL A 143   N  ILE A 210
SHEET    6 B1A10 ALA A 116  ASN A 124 -1  N  LEU A 120   O  LEU A 144
SHEET    7 B1A10 TYR A  88  TRP A  97 -1  O  HIS A  94   N  HIS A 119
SHEET    8 B1A10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9 B1A10 SER A  56  ASN A  61 -1  O  ARG A  58   N  GLU A  69
SHEET   10 B1A10 SER A 173  ASP A 175 -1  O  SER A 173   N  ILE A  59
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.10
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.09
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.06
LINK        ZN    ZN A 262                 O   HOH A 428     1555   1555  2.27
LINK        HG    HG A 263                 O   HOH A 432     1555   1555  2.36
LINK        HG    HG A 263                 SG  CYS A 206     1555   1555  2.21
LINK        HG    HG A 263                 O   GLN A 137     1555   1555  2.87
LINK        HG    HG A 263                 O   HOH A 389     1555   1555  3.12
LINK        HG    HG A 263                 O   GLU A 205     1555   1555  3.16
CISPEP   1 SER A   29    PRO A   30          0         0.01
CISPEP   2 PRO A  201    PRO A  202          0         0.48
SITE     1  ZN  3 HIS A  94  HIS A  96  HIS A 119
SITE     1  HG  1 CYS A 206
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  THR A 199
SITE     2 AC1  5 HOH A 428
SITE     1 AC2  5 VAL A 135  GLN A 137  GLU A 205  CYS A 206
SITE     2 AC2  5 HOH A 432
CRYST1   42.484   41.616   72.658  90.00 104.52  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      0.023538  0.000000  0.006094        0.00000
SCALE2      0.000000  0.024029  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014217        0.00000
      
PROCHECK
Go to PROCHECK summary
 References