spacer
spacer

PDBsum entry 1v9e

Go to PDB code: 
Top Page protein metals links
Lyase PDB id
1v9e
Jmol
Contents
Protein chains
259 a.a. *
Metals
_ZN ×2
Waters ×576
* Residue conservation analysis
HEADER    LYASE                                   26-JAN-04   1V9E
TITLE     CRYSTAL STRUCTURE ANALYSIS OF BOVINE CARBONIC ANHYDRASE II
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CA-II;
COMPND   5 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: CATTLE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 CELL: ERYTHROCYTES
KEYWDS    HIGH-RESOLUTION, TWISTED BETA SHEET, ZINC METALLOENZYME,
KEYWDS   2 LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.SAITO,T.SATO,A.IKAI,N.TANAKA
REVDAT   3   24-FEB-09 1V9E    1       VERSN
REVDAT   2   13-APR-04 1V9E    1       JRNL
REVDAT   1   10-FEB-04 1V9E    0
JRNL        AUTH   R.SAITO,T.SATO,A.IKAI,N.TANAKA
JRNL        TITL   STRUCTURE OF BOVINE CARBONIC ANHYDRASE II AT 1.95
JRNL        TITL 2 A RESOLUTION.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  60   792 2004
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   15039588
JRNL        DOI    10.1107/S0907444904003166
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.95 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) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.87
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.100
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2158185.710
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.6
REMARK   3   NUMBER OF REFLECTIONS             : 39641
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) : 0.270
REMARK   3   FREE R VALUE                     : 0.298
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3989
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) : 1.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4831
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340
REMARK   3   BIN FREE R VALUE                    : 0.3620
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.80
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 584
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4108
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 576
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 14.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.30
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -3.02000
REMARK   3    B22 (A**2) : -3.02000
REMARK   3    B33 (A**2) : 6.03000
REMARK   3    B12 (A**2) : 1.32000
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) : 0.32
REMARK   3   ESD FROM SIGMAA              (A) : 0.31
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) : 0.37
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.70
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.83
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) : 1.320 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.960 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.940 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.740 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.37
REMARK   3   BSOL        : 62.37
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 1V9E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JAN-04.
REMARK 100 THE RCSB ID CODE IS RCSB006371.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
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) : 1.00
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   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950
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     (%) : 90.6
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07600
REMARK 200   FOR THE DATA SET  : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.28400
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: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS-HCL, 2.4M AMMONIUM
REMARK 280  SULFATE, PH 7.5, SMALL TUBES, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
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       80.00000
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      160.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      120.00000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      200.00000
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       40.00000
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 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 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 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    HIS A   2       51.13    159.25
REMARK 500    ARG A  56      -74.48   -112.98
REMARK 500    SER A  64     -151.03   -172.02
REMARK 500    ASP A  80     -134.88     59.60
REMARK 500    ARG A 110       -5.21     71.29
REMARK 500    PRO A 200        3.54    -68.81
REMARK 500    ASN A 242       36.66   -147.29
REMARK 500    LYS A 250     -132.71     61.92
REMARK 500    ASN A 251       35.88    -90.65
REMARK 500    ASN B  10       20.37   -141.04
REMARK 500    ARG B  56      -79.94   -109.29
REMARK 500    SER B  64     -150.04   -169.48
REMARK 500    LYS B  75     -102.02    -63.27
REMARK 500    ASP B  80     -142.56     61.23
REMARK 500    ARG B 110       -2.91     68.76
REMARK 500    PRO B 200        0.12    -67.29
REMARK 500    ASN B 242       38.23   -144.30
REMARK 500    LYS B 250     -110.02     70.44
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                              ZN A 260  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  93   NE2
REMARK 620 2 HIS A  95   NE2 109.4
REMARK 620 3 HOH A 462   O   101.3 123.0
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 260  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  93   NE2
REMARK 620 2 HIS B  95   NE2 104.3
REMARK 620 3 HIS B 118   ND1 118.2 104.2
REMARK 620 4 HOH B 478   O   104.6 121.5 105.0
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 260
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 260
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V9I   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, Q253C MUTANT
DBREF  1V9E A    1   259  UNP    P00921   CAH2_BOVIN       1    259
DBREF  1V9E B    1   259  UNP    P00921   CAH2_BOVIN       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 ASN GLY GLU ARG
SEQRES   3 A  259  GLN SER PRO VAL ASP ILE ASP THR LYS ALA VAL VAL GLN
SEQRES   4 A  259  ASP PRO ALA LEU LYS PRO LEU ALA LEU VAL TYR GLY GLU
SEQRES   5 A  259  ALA THR SER ARG ARG MET VAL ASN ASN GLY HIS SER PHE
SEQRES   6 A  259  ASN VAL GLU TYR ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES   7 A  259  LYS ASP GLY PRO LEU THR GLY THR TYR ARG LEU VAL GLN
SEQRES   8 A  259  PHE HIS PHE HIS TRP GLY SER SER ASP ASP GLN GLY SER
SEQRES   9 A  259  GLU HIS THR VAL ASP ARG 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  THR ALA ALA GLN GLN PRO ASP GLY LEU ALA VAL VAL GLY
SEQRES  12 A  259  VAL PHE LEU LYS VAL GLY ASP ALA ASN PRO ALA LEU GLN
SEQRES  13 A  259  LYS VAL LEU ASP ALA LEU ASP SER ILE LYS THR LYS GLY
SEQRES  14 A  259  LYS SER THR ASP PHE PRO ASN PHE ASP PRO GLY SER LEU
SEQRES  15 A  259  LEU PRO ASN VAL LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES  16 A  259  LEU THR THR PRO PRO LEU LEU GLU SER VAL THR TRP ILE
SEQRES  17 A  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLN GLN MET
SEQRES  18 A  259  LEU LYS PHE ARG THR LEU ASN PHE ASN ALA GLU GLY GLU
SEQRES  19 A  259  PRO GLU LEU LEU MET LEU ALA ASN TRP ARG PRO ALA GLN
SEQRES  20 A  259  PRO LEU LYS ASN ARG GLN VAL ARG GLY PHE PRO LYS
SEQRES   1 B  259  SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU
SEQRES   2 B  259  HIS TRP HIS LYS ASP PHE PRO ILE ALA ASN GLY GLU ARG
SEQRES   3 B  259  GLN SER PRO VAL ASP ILE ASP THR LYS ALA VAL VAL GLN
SEQRES   4 B  259  ASP PRO ALA LEU LYS PRO LEU ALA LEU VAL TYR GLY GLU
SEQRES   5 B  259  ALA THR SER ARG ARG MET VAL ASN ASN GLY HIS SER PHE
SEQRES   6 B  259  ASN VAL GLU TYR ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES   7 B  259  LYS ASP GLY PRO LEU THR GLY THR TYR ARG LEU VAL GLN
SEQRES   8 B  259  PHE HIS PHE HIS TRP GLY SER SER ASP ASP GLN GLY SER
SEQRES   9 B  259  GLU HIS THR VAL ASP ARG LYS LYS TYR ALA ALA GLU LEU
SEQRES  10 B  259  HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES  11 B  259  THR ALA ALA GLN GLN PRO ASP GLY LEU ALA VAL VAL GLY
SEQRES  12 B  259  VAL PHE LEU LYS VAL GLY ASP ALA ASN PRO ALA LEU GLN
SEQRES  13 B  259  LYS VAL LEU ASP ALA LEU ASP SER ILE LYS THR LYS GLY
SEQRES  14 B  259  LYS SER THR ASP PHE PRO ASN PHE ASP PRO GLY SER LEU
SEQRES  15 B  259  LEU PRO ASN VAL LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES  16 B  259  LEU THR THR PRO PRO LEU LEU GLU SER VAL THR TRP ILE
SEQRES  17 B  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLN GLN MET
SEQRES  18 B  259  LEU LYS PHE ARG THR LEU ASN PHE ASN ALA GLU GLY GLU
SEQRES  19 B  259  PRO GLU LEU LEU MET LEU ALA ASN TRP ARG PRO ALA GLN
SEQRES  20 B  259  PRO LEU LYS ASN ARG GLN VAL ARG GLY PHE PRO LYS
HET     ZN  A 260       1
HET     ZN  B 260       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  HOH   *576(H2 O)
HELIX    1   1 HIS A   14  ASP A   18  5                                   5
HELIX    2   2 PHE A   19  GLY A   24  5                                   6
HELIX    3   3 ASP A   33  VAL A   37  5                                   5
HELIX    4   4 LYS A  125  GLY A  127  5                                   3
HELIX    5   5 ASP A  128  ALA A  133  1                                   6
HELIX    6   6 ASN A  152  ALA A  154  5                                   3
HELIX    7   7 LEU A  155  LEU A  162  1                                   8
HELIX    8   8 ASP A  163  ILE A  165  5                                   3
HELIX    9   9 ASP A  178  LEU A  183  5                                   6
HELIX   10  10 SER A  217  ARG A  225  1                                   9
HELIX   11  11 GLY B   11  GLU B   13  5                                   3
HELIX   12  12 HIS B   14  PHE B   19  1                                   6
HELIX   13  13 PRO B   20  GLY B   24  5                                   5
HELIX   14  14 ASP B   33  VAL B   37  5                                   5
HELIX   15  15 ASP B  128  ALA B  133  1                                   6
HELIX   16  16 ASN B  152  ALA B  154  5                                   3
HELIX   17  17 LEU B  155  LEU B  162  1                                   8
HELIX   18  18 ASP B  163  LYS B  166  5                                   4
HELIX   19  19 ASP B  178  LEU B  183  5                                   6
HELIX   20  20 SER B  217  ARG B  225  1                                   9
SHEET    1   A 2 ASP A  31  ILE A  32  0
SHEET    2   A 2 THR A 107  VAL A 108  1  O  THR A 107   N  ILE A  32
SHEET    1   B10 VAL A  38  GLN A  39  0
SHEET    2   B10 ARG A 255  PHE A 257  1  O  GLY A 256   N  VAL A  38
SHEET    3   B10 TYR A 189  GLY A 194 -1  N  TYR A 189   O  PHE A 257
SHEET    4   B10 VAL A 205  LEU A 210 -1  O  VAL A 205   N  GLY A 194
SHEET    5   B10 LEU A 139  VAL A 148  1  N  GLY A 143   O  LEU A 210
SHEET    6   B10 ALA A 115  ASN A 123 -1  N  LEU A 117   O  VAL A 144
SHEET    7   B10 TYR A  87  TRP A  96 -1  N  HIS A  93   O  HIS A 118
SHEET    8   B10 PHE A  65  TYR A  69 -1  N  TYR A  69   O  VAL A  90
SHEET    9   B10 SER A  55  ASN A  60 -1  N  ARG A  56   O  GLU A  68
SHEET   10   B10 SER A 171  ASP A 173 -1  O  THR A 172   N  MET A  58
SHEET    1   C 6 LEU A  46  VAL A  49  0
SHEET    2   C 6 VAL A  77  ASP A  80 -1  O  LYS A  79   N  ALA A  47
SHEET    3   C 6 TYR A  87  TRP A  96 -1  O  TYR A  87   N  LEU A  78
SHEET    4   C 6 ALA A 115  ASN A 123 -1  O  HIS A 118   N  HIS A  93
SHEET    5   C 6 LEU A 139  VAL A 148 -1  O  VAL A 144   N  LEU A 117
SHEET    6   C 6 ILE A 214  VAL A 216  1  O  ILE A 214   N  PHE A 145
SHEET    1   D 2 ASP B  31  ILE B  32  0
SHEET    2   D 2 THR B 107  VAL B 108  1  O  THR B 107   N  ILE B  32
SHEET    1   E10 VAL B  38  GLN B  39  0
SHEET    2   E10 ARG B 255  PHE B 257  1  O  GLY B 256   N  VAL B  38
SHEET    3   E10 TYR B 189  GLY B 194 -1  N  TYR B 189   O  PHE B 257
SHEET    4   E10 VAL B 205  LEU B 210 -1  O  VAL B 205   N  GLY B 194
SHEET    5   E10 LEU B 139  VAL B 148  1  N  GLY B 143   O  LEU B 210
SHEET    6   E10 ALA B 115  ASN B 123 -1  N  LEU B 117   O  VAL B 144
SHEET    7   E10 TYR B  87  TRP B  96 -1  N  HIS B  93   O  HIS B 118
SHEET    8   E10 PHE B  65  TYR B  69 -1  N  TYR B  69   O  VAL B  90
SHEET    9   E10 SER B  55  ASN B  60 -1  N  ARG B  56   O  GLU B  68
SHEET   10   E10 SER B 171  ASP B 173 -1  O  THR B 172   N  MET B  58
SHEET    1   F 6 LEU B  46  VAL B  49  0
SHEET    2   F 6 VAL B  77  ASP B  80 -1  O  LYS B  79   N  ALA B  47
SHEET    3   F 6 TYR B  87  TRP B  96 -1  O  TYR B  87   N  LEU B  78
SHEET    4   F 6 ALA B 115  ASN B 123 -1  O  HIS B 118   N  HIS B  93
SHEET    5   F 6 LEU B 139  VAL B 148 -1  O  VAL B 144   N  LEU B 117
SHEET    6   F 6 ILE B 214  VAL B 216  1  O  ILE B 214   N  PHE B 145
LINK        ZN    ZN A 260                 NE2 HIS A  93     1555   1555  2.12
LINK        ZN    ZN A 260                 NE2 HIS A  95     1555   1555  2.16
LINK        ZN    ZN B 260                 NE2 HIS B  93     1555   1555  2.13
LINK        ZN    ZN B 260                 NE2 HIS B  95     1555   1555  2.13
LINK        ZN    ZN B 260                 ND1 HIS B 118     1555   1555  2.18
LINK        ZN    ZN A 260                 O   HOH A 462     1555   1555  2.19
LINK        ZN    ZN B 260                 O   HOH B 478     1555   1555  2.29
CISPEP   1 SER A   28    PRO A   29          0         0.24
CISPEP   2 PRO A  199    PRO A  200          0         0.39
CISPEP   3 PHE A  257    PRO A  258          0        -0.07
CISPEP   4 SER B   28    PRO B   29          0         0.23
CISPEP   5 PRO B  199    PRO B  200          0         0.37
CISPEP   6 PHE B  257    PRO B  258          0        -0.12
SITE     1 AC1  5 HIS A  93  HIS A  95  HIS A 118  THR A 197
SITE     2 AC1  5 HOH A 462
SITE     1 AC2  5 HIS B  93  HIS B  95  HIS B 118  THR B 197
SITE     2 AC2  5 HOH B 478
CRYST1   66.700   66.700  240.000  90.00  90.00 120.00 P 61         12
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      0.014993  0.008656  0.000000        0.00000
SCALE2      0.000000  0.017312  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004167        0.00000
      
PROCHECK
Go to PROCHECK summary
 References