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PDBsum entry 1v9i

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Lyase PDB id
1v9i
Jmol
Contents
Protein chain
261 a.a. *
Metals
_ZN
* Residue conservation analysis
HEADER    LYASE                                   26-JAN-04   1V9I
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE SITE SPECIFIC MUTANT
TITLE    2 (Q253C) OF BOVINE CARBONIC ANHYDRASE II
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: C;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CA-II;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: CATTLE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 CELL: ERYTHROCYTES;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PRSETB;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSETB
KEYWDS    BETA SHEET, ZINC METALLOENZYME, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.SAITO,T.SATO,A.IKAI,N.TANAKA
REVDAT   2   24-FEB-09 1V9I    1       VERSN
REVDAT   1   10-FEB-04 1V9I    0
JRNL        AUTH   R.SAITO,T.SATO,A.IKAI,N.TANAKA
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF THE SITE SPECIFIC
JRNL        TITL 2 MUTANT (Q253C) OF BOVINE CARBONIC ANHYDRASE II
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.95 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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.100
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 945099.600
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7
REMARK   3   NUMBER OF REFLECTIONS             : 7798
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) : 0.247
REMARK   3   FREE R VALUE                     : 0.346
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 799
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.012
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) : 2.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.13
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1078
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080
REMARK   3   BIN FREE R VALUE                    : 0.3750
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 11.20
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 136
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2068
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 0.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.60
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 8.08000
REMARK   3    B22 (A**2) : 8.08000
REMARK   3    B33 (A**2) : -16.16000
REMARK   3    B12 (A**2) : 12.38000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38
REMARK   3   ESD FROM SIGMAA              (A) : 0.55
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) : 0.59
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.73
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.07
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) : 8.140 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 12.610; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 9.780 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 13.980; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.40
REMARK   3   BSOL        : 62.53
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   : ION.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1V9I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-04.
REMARK 100 THE RCSB ID CODE IS RCSB006375.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-6A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978
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          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7798
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950
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     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07500
REMARK 200   FOR THE DATA SET  : NULL
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: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS-HCL, 3MM NAN3, 2.3M
REMARK 280  AMMONIUM SULFATE, PH 7.5, SMALL TUBES, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.66667
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       77.33333
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       77.33333
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       38.66667
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 APPLY THE FOLLOWING TO CHAINS: C
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 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    CYS C   2      100.51    161.21
REMARK 500    SER C   3     -160.92    -60.07
REMARK 500    HIS C   4      115.57    179.29
REMARK 500    TRP C   6     -177.68    -55.74
REMARK 500    LYS C  19      -85.02    -61.28
REMARK 500    ALA C  24       -3.49    -58.25
REMARK 500    LEU C  50       64.20   -107.86
REMARK 500    VAL C  51       74.92    -68.26
REMARK 500    ALA C  55      130.83    -34.14
REMARK 500    ARG C  58      -89.01   -103.85
REMARK 500    HIS C  65       16.38   -140.24
REMARK 500    SER C  66      178.07    163.71
REMARK 500    ASP C  76       26.31    -78.99
REMARK 500    LYS C  77      -55.37    -29.60
REMARK 500    ASP C  82     -124.19     43.34
REMARK 500    ARG C 112       -2.84     60.74
REMARK 500    ALA C 116      -76.66    -62.24
REMARK 500    LEU C 157       12.92    -61.21
REMARK 500    ASP C 162      -86.65    -59.55
REMARK 500    ALA C 163      -12.63    -35.92
REMARK 500    ILE C 167       47.82   -157.40
REMARK 500    PHE C 176       67.69   -115.20
REMARK 500    SER C 183        2.07    -62.77
REMARK 500    PRO C 186     -170.99    -58.08
REMARK 500    SER C 220      -30.66    -37.12
REMARK 500    PHE C 226      -34.07    -39.98
REMARK 500    LEU C 229      152.59    -44.86
REMARK 500    ASN C 232     -168.64    -72.85
REMARK 500    GLU C 234       84.22    -26.08
REMARK 500    GLU C 238      117.98    -31.88
REMARK 500    ASN C 244       47.78   -167.57
REMARK 500    LYS C 252     -128.74     60.88
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 C 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C  95   NE2
REMARK 620 2 HIS C  97   NE2  85.1
REMARK 620 3 HIS C 120   ND1  93.5  86.7
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 262
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V9E   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, WILD TYPE
DBREF  1V9I C    3   261  UNP    P00921   CAH2_BOVIN       1    259
SEQADV 1V9I ARG C    1  UNP  P00921              CLONING ARTIFACT
SEQADV 1V9I CYS C    2  UNP  P00921              CLONING ARTIFACT
SEQADV 1V9I CYS C  255  UNP  P00921    GLN   253 ENGINEERED
SEQRES   1 C  261  ARG CYS SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY
SEQRES   2 C  261  PRO GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA ASN GLY
SEQRES   3 C  261  GLU ARG GLN SER PRO VAL ASP ILE ASP THR LYS ALA VAL
SEQRES   4 C  261  VAL GLN ASP PRO ALA LEU LYS PRO LEU ALA LEU VAL TYR
SEQRES   5 C  261  GLY GLU ALA THR SER ARG ARG MET VAL ASN ASN GLY HIS
SEQRES   6 C  261  SER PHE ASN VAL GLU TYR ASP ASP SER GLN ASP LYS ALA
SEQRES   7 C  261  VAL LEU LYS ASP GLY PRO LEU THR GLY THR TYR ARG LEU
SEQRES   8 C  261  VAL GLN PHE HIS PHE HIS TRP GLY SER SER ASP ASP GLN
SEQRES   9 C  261  GLY SER GLU HIS THR VAL ASP ARG LYS LYS TYR ALA ALA
SEQRES  10 C  261  GLU LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP
SEQRES  11 C  261  PHE GLY THR ALA ALA GLN GLN PRO ASP GLY LEU ALA VAL
SEQRES  12 C  261  VAL GLY VAL PHE LEU LYS VAL GLY ASP ALA ASN PRO ALA
SEQRES  13 C  261  LEU GLN LYS VAL LEU ASP ALA LEU ASP SER ILE LYS THR
SEQRES  14 C  261  LYS GLY LYS SER THR ASP PHE PRO ASN PHE ASP PRO GLY
SEQRES  15 C  261  SER LEU LEU PRO ASN VAL LEU ASP TYR TRP THR TYR PRO
SEQRES  16 C  261  GLY SER LEU THR THR PRO PRO LEU LEU GLU SER VAL THR
SEQRES  17 C  261  TRP ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLN
SEQRES  18 C  261  GLN MET LEU LYS PHE ARG THR LEU ASN PHE ASN ALA GLU
SEQRES  19 C  261  GLY GLU PRO GLU LEU LEU MET LEU ALA ASN TRP ARG PRO
SEQRES  20 C  261  ALA GLN PRO LEU LYS ASN ARG CYS VAL ARG GLY PHE PRO
SEQRES  21 C  261  LYS
HET     ZN  C 262       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
HELIX    1   1 PHE C   21  GLY C   26  5                                   6
HELIX    2   2 ASP C   35  VAL C   39  5                                   5
HELIX    3   3 LYS C  127  GLY C  129  5                                   3
HELIX    4   4 ASP C  130  ALA C  135  1                                   6
HELIX    5   5 PRO C  155  LEU C  164  1                                  10
HELIX    6   6 ASP C  165  LYS C  168  5                                   4
HELIX    7   7 ASP C  180  LEU C  185  5                                   6
HELIX    8   8 SER C  219  LEU C  229  1                                  11
SHEET    1   A 2 ASP C  33  ILE C  34  0
SHEET    2   A 2 THR C 109  VAL C 110  1  O  THR C 109   N  ILE C  34
SHEET    1   B10 VAL C  40  GLN C  41  0
SHEET    2   B10 ARG C 257  PHE C 259  1  O  GLY C 258   N  VAL C  40
SHEET    3   B10 TYR C 191  GLY C 196 -1  N  THR C 193   O  ARG C 257
SHEET    4   B10 VAL C 207  LEU C 212 -1  O  VAL C 211   N  TRP C 192
SHEET    5   B10 LEU C 141  VAL C 150  1  N  GLY C 145   O  ILE C 210
SHEET    6   B10 GLU C 118  ASN C 125 -1  N  HIS C 123   O  ALA C 142
SHEET    7   B10 TYR C  89  PHE C  96 -1  N  HIS C  95   O  HIS C 120
SHEET    8   B10 PHE C  67  TYR C  71 -1  N  VAL C  69   O  PHE C  94
SHEET    9   B10 SER C  57  ASN C  62 -1  N  ARG C  58   O  GLU C  70
SHEET   10   B10 SER C 173  ASP C 175 -1  O  THR C 174   N  MET C  60
SHEET    1   C 6 LEU C  48  ALA C  49  0
SHEET    2   C 6 VAL C  79  ASP C  82 -1  O  LYS C  81   N  ALA C  49
SHEET    3   C 6 TYR C  89  PHE C  96 -1  O  TYR C  89   N  LEU C  80
SHEET    4   C 6 GLU C 118  ASN C 125 -1  O  HIS C 120   N  HIS C  95
SHEET    5   C 6 LEU C 141  VAL C 150 -1  O  ALA C 142   N  HIS C 123
SHEET    6   C 6 ILE C 216  VAL C 218  1  O  ILE C 216   N  PHE C 147
LINK        ZN    ZN C 262                 NE2 HIS C  95     1555   1555  2.27
LINK        ZN    ZN C 262                 NE2 HIS C  97     1555   1555  2.30
LINK        ZN    ZN C 262                 ND1 HIS C 120     1555   1555  2.25
CISPEP   1 SER C   30    PRO C   31          0         0.17
CISPEP   2 PRO C  201    PRO C  202          0         0.20
CISPEP   3 PHE C  259    PRO C  260          0         0.38
SITE     1 AC1  4 HIS C  95  HIS C  97  HIS C 120  THR C 199
CRYST1   73.100   73.100  116.000  90.00  90.00 120.00 P 31 2 1      6
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      0.013680  0.007898  0.000000        0.00000
SCALE2      0.000000  0.015796  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008621        0.00000
      
PROCHECK
Go to PROCHECK summary
 References