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PDBsum entry 3d0n

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Metal binding protein PDB id
3d0n
Jmol
Contents
Protein chain
263 a.a.
Ligands
ACT ×2
GOL
Metals
_ZN ×2
Waters ×777
HEADER    METAL BINDING PROTEIN                   02-MAY-08   3D0N
TITLE     CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE XIII
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 13;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE XIII, CARBONATE DEHYDRATASE XIII, CA-
COMPND   5 XIII;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA13;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: BL21(DE3)PLYS;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS    CARBONIC ANHYDRASE, LYASE, METAL-BINDING, METAL BINDING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.DI FIORE,G.DE SIMONE
REVDAT   5   13-JUL-11 3D0N    1       VERSN
REVDAT   4   09-JUN-09 3D0N    1       REVDAT
REVDAT   3   24-FEB-09 3D0N    1       VERSN
REVDAT   2   02-DEC-08 3D0N    1       JRNL
REVDAT   1   29-JUL-08 3D0N    0
JRNL        AUTH   A.DI FIORE,S.M.MONTI,M.HILVO,S.PARKKILA,V.ROMANO,A.SCALONI,
JRNL        AUTH 2 C.PEDONE,A.SCOZZAFAVA,C.T.SUPURAN,G.DE SIMONE
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE XIII AND ITS
JRNL        TITL 2 COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE.
JRNL        REF    PROTEINS                      V.  74   164 2008
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   18618712
JRNL        DOI    10.1002/PROT.22144
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  PUBL   3151019
REMARK   1  REFN                   ISSN 0887-3585
REMARK   2
REMARK   2 RESOLUTION.    1.55 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) : 1.55
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)   (%) : 95.4
REMARK   3   NUMBER OF REFLECTIONS             : 66286
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) : 0.168
REMARK   3   FREE R VALUE                     : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 3356
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            : 4186
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 16
REMARK   3   SOLVENT ATOMS            : 777
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) : 0.006
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 : 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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3D0N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-08.
REMARK 100 THE RCSB ID CODE IS RCSB047442.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.6
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) : 0.999882
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   : 68200
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550
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     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05800
REMARK 200   FOR THE DATA SET  : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.25800
REMARK 200   FOR SHELL         : 3.800
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: PDB ENTRY 1CA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 39.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2 M AMMONIUM ACETATE,
REMARK 280  0.1 M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  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       29.10500
REMARK 290   SMTRY3   2  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     GLY A    -1
REMARK 465     GLY B    -1
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   1     -177.17   -170.66
REMARK 500    SER A  65     -171.54    174.29
REMARK 500    ASN A  75       42.52   -105.95
REMARK 500    ASN A 124       99.78    -69.01
REMARK 500    PRO A 202        2.30    -69.17
REMARK 500    ASN A 244       44.04   -147.36
REMARK 500    SER B  65     -176.28    169.55
REMARK 500    ASN B  75       40.66    -97.73
REMARK 500    PRO B 202        4.92    -69.58
REMARK 500    ASN B 244       42.98   -146.32
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 A1621        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH A1770        DISTANCE =  5.48 ANGSTROMS
REMARK 525    HOH B1556        DISTANCE =  5.95 ANGSTROMS
REMARK 525    HOH B1678        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH B1688        DISTANCE =  5.57 ANGSTROMS
REMARK 525    HOH B1775        DISTANCE =  5.02 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  99.8
REMARK 620 3 HIS A 119   ND1 113.9  93.5
REMARK 620 4 HOH A1026   O   109.8  88.2 135.2
REMARK 620 5 ACT A 263   O    88.7 171.2  84.7  87.1
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  94   NE2
REMARK 620 2 HIS B  96   NE2 101.7
REMARK 620 3 HIS B 119   ND1 115.0  91.5
REMARK 620 4 ACT B 263   OXT  91.8 166.5  83.6
REMARK 620 5 HOH B1497   O   104.5  88.1 139.7  87.5
REMARK 620 N                    1     2     3     4
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 264
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CA2   RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE HUMAN CARBONIC ANHYDRASE II
DBREF  3D0N A    0B  261  UNP    Q8N1Q1   CAH13_HUMAN      1    262
DBREF  3D0N B    0B  261  UNP    Q8N1Q1   CAH13_HUMAN      1    262
SEQADV 3D0N GLY A   -1  UNP  Q8N1Q1              EXPRESSION TAG
SEQADV 3D0N SER A    0A UNP  Q8N1Q1              EXPRESSION TAG
SEQADV 3D0N GLY B   -1  UNP  Q8N1Q1              EXPRESSION TAG
SEQADV 3D0N SER B    0A UNP  Q8N1Q1              EXPRESSION TAG
SEQRES   1 A  264  GLY SER MET SER ARG LEU SER TRP GLY TYR ARG GLU HIS
SEQRES   2 A  264  ASN GLY PRO ILE HIS TRP LYS GLU PHE PHE PRO ILE ALA
SEQRES   3 A  264  ASP GLY ASP GLN GLN SER PRO ILE GLU ILE LYS THR LYS
SEQRES   4 A  264  GLU VAL LYS TYR ASP SER SER LEU ARG PRO LEU SER ILE
SEQRES   5 A  264  LYS TYR ASP PRO SER SER ALA LYS ILE ILE SER ASN SER
SEQRES   6 A  264  GLY HIS SER PHE ASN VAL ASP PHE ASP ASP THR GLU ASN
SEQRES   7 A  264  LYS SER VAL LEU ARG GLY GLY PRO LEU THR GLY SER TYR
SEQRES   8 A  264  ARG LEU ARG GLN VAL HIS LEU HIS TRP GLY SER ALA ASP
SEQRES   9 A  264  ASP HIS GLY SER GLU HIS ILE VAL ASP GLY VAL SER TYR
SEQRES  10 A  264  ALA ALA GLU LEU HIS VAL VAL HIS TRP ASN SER ASP LYS
SEQRES  11 A  264  TYR PRO SER PHE VAL GLU ALA ALA HIS GLU PRO ASP GLY
SEQRES  12 A  264  LEU ALA VAL LEU GLY VAL PHE LEU GLN ILE GLY GLU PRO
SEQRES  13 A  264  ASN SER GLN LEU GLN LYS ILE THR ASP THR LEU ASP SER
SEQRES  14 A  264  ILE LYS GLU LYS GLY LYS GLN THR ARG PHE THR ASN PHE
SEQRES  15 A  264  ASP LEU LEU SER LEU LEU PRO PRO SER TRP ASP TYR TRP
SEQRES  16 A  264  THR TYR PRO GLY SER LEU THR VAL PRO PRO LEU LEU GLU
SEQRES  17 A  264  SER VAL THR TRP ILE VAL LEU LYS GLN PRO ILE ASN ILE
SEQRES  18 A  264  SER SER GLN GLN LEU ALA LYS PHE ARG SER LEU LEU CYS
SEQRES  19 A  264  THR ALA GLU GLY GLU ALA ALA ALA PHE LEU VAL SER ASN
SEQRES  20 A  264  HIS ARG PRO PRO GLN PRO LEU LYS GLY ARG LYS VAL ARG
SEQRES  21 A  264  ALA SER PHE HIS
SEQRES   1 B  264  GLY SER MET SER ARG LEU SER TRP GLY TYR ARG GLU HIS
SEQRES   2 B  264  ASN GLY PRO ILE HIS TRP LYS GLU PHE PHE PRO ILE ALA
SEQRES   3 B  264  ASP GLY ASP GLN GLN SER PRO ILE GLU ILE LYS THR LYS
SEQRES   4 B  264  GLU VAL LYS TYR ASP SER SER LEU ARG PRO LEU SER ILE
SEQRES   5 B  264  LYS TYR ASP PRO SER SER ALA LYS ILE ILE SER ASN SER
SEQRES   6 B  264  GLY HIS SER PHE ASN VAL ASP PHE ASP ASP THR GLU ASN
SEQRES   7 B  264  LYS SER VAL LEU ARG GLY GLY PRO LEU THR GLY SER TYR
SEQRES   8 B  264  ARG LEU ARG GLN VAL HIS LEU HIS TRP GLY SER ALA ASP
SEQRES   9 B  264  ASP HIS GLY SER GLU HIS ILE VAL ASP GLY VAL SER TYR
SEQRES  10 B  264  ALA ALA GLU LEU HIS VAL VAL HIS TRP ASN SER ASP LYS
SEQRES  11 B  264  TYR PRO SER PHE VAL GLU ALA ALA HIS GLU PRO ASP GLY
SEQRES  12 B  264  LEU ALA VAL LEU GLY VAL PHE LEU GLN ILE GLY GLU PRO
SEQRES  13 B  264  ASN SER GLN LEU GLN LYS ILE THR ASP THR LEU ASP SER
SEQRES  14 B  264  ILE LYS GLU LYS GLY LYS GLN THR ARG PHE THR ASN PHE
SEQRES  15 B  264  ASP LEU LEU SER LEU LEU PRO PRO SER TRP ASP TYR TRP
SEQRES  16 B  264  THR TYR PRO GLY SER LEU THR VAL PRO PRO LEU LEU GLU
SEQRES  17 B  264  SER VAL THR TRP ILE VAL LEU LYS GLN PRO ILE ASN ILE
SEQRES  18 B  264  SER SER GLN GLN LEU ALA LYS PHE ARG SER LEU LEU CYS
SEQRES  19 B  264  THR ALA GLU GLY GLU ALA ALA ALA PHE LEU VAL SER ASN
SEQRES  20 B  264  HIS ARG PRO PRO GLN PRO LEU LYS GLY ARG LYS VAL ARG
SEQRES  21 B  264  ALA SER PHE HIS
HET     ZN  A 262       1
HET    ACT  A 263       4
HET     ZN  B 262       1
HET    ACT  B 263       4
HET    GOL  B 264      12
HETNAM      ZN ZINC ION
HETNAM     ACT ACETATE ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  ACT    2(C2 H3 O2 1-)
FORMUL   7  GOL    C3 H8 O3
FORMUL   8  HOH   *777(H2 O)
HELIX    1   1 GLY A   12  PHE A   19  5                                   8
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 SER A  130  ALA A  135  1                                   6
HELIX    4   4 ASN A  154  ASP A  162  1                                   9
HELIX    5   5 THR A  163  LYS A  168  5                                   6
HELIX    6   6 ASP A  180  LEU A  185  5                                   6
HELIX    7   7 SER A  219  ARG A  227  1                                   9
HELIX    8   8 GLY B   12  PHE B   19  5                                   8
HELIX    9   9 PHE B   20  GLY B   25  5                                   6
HELIX   10  10 LYS B   34  VAL B   38  5                                   5
HELIX   11  11 SER B  130  ALA B  135  1                                   6
HELIX   12  12 ASN B  154  ASP B  162  1                                   9
HELIX   13  13 THR B  163  LYS B  168  5                                   6
HELIX   14  14 ASP B  180  LEU B  185  5                                   6
HELIX   15  15 SER B  219  ARG B  227  1                                   9
SHEET    1   A 2 GLU A  32  ILE A  33  0
SHEET    2   A 2 ILE A 108  VAL A 109  1  O  ILE A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 ARG 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  ARG 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  ILE 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  VAL 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  VAL A  68   O  VAL A  93
SHEET    9   B10 ALA A  56  ASN A  61 -1  N  ILE A  58   O  ASP A  69
SHEET   10   B10 GLN A 173  ARG A 175 -1  O  THR A 174   N  ILE A  59
SHEET    1   C 6 LEU A  47  LYS A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  ARG 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  ILE A 150 -1  O  VAL A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  ILE A 218  1  O  ILE A 216   N  PHE A 147
SHEET    1   D 2 GLU B  32  ILE B  33  0
SHEET    2   D 2 ILE B 108  VAL B 109  1  O  ILE B 108   N  ILE B  33
SHEET    1   E10 LYS B  39  TYR B  40  0
SHEET    2   E10 ARG B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   E10 TYR B 191  GLY B 196 -1  N  THR B 193   O  ARG B 257
SHEET    4   E10 VAL B 207  LEU B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   E10 LEU B 141  ILE B 150  1  N  GLY B 145   O  ILE B 210
SHEET    6   E10 ALA B 116  ASN B 124 -1  N  LEU B 118   O  VAL B 146
SHEET    7   E10 TYR B  88  TRP B  97 -1  N  ARG B  91   O  VAL B 121
SHEET    8   E10 PHE B  66  PHE B  70 -1  N  VAL B  68   O  VAL B  93
SHEET    9   E10 ALA B  56  ASN B  61 -1  N  SER B  60   O  ASN B  67
SHEET   10   E10 GLN B 173  ARG B 175 -1  O  THR B 174   N  ILE B  59
SHEET    1   F 6 LEU B  47  LYS B  50  0
SHEET    2   F 6 VAL B  78  GLY B  81 -1  O  ARG 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  VAL B 121   N  ARG B  91
SHEET    5   F 6 LEU B 141  ILE B 150 -1  O  VAL B 146   N  LEU B 118
SHEET    6   F 6 ILE B 216  ILE B 218  1  O  ILE B 216   N  PHE B 147
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.03
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.10
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.06
LINK         NE2 HIS B  94                ZN    ZN B 262     1555   1555  1.99
LINK         NE2 HIS B  96                ZN    ZN B 262     1555   1555  2.13
LINK         ND1 HIS B 119                ZN    ZN B 262     1555   1555  2.06
LINK        ZN    ZN A 262                 O   HOH A1026     1555   1555  2.05
LINK        ZN    ZN A 262                 O   ACT A 263     1555   1555  2.15
LINK        ZN    ZN B 262                 OXT ACT B 263     1555   1555  2.10
LINK        ZN    ZN B 262                 O   HOH B1497     1555   1555  2.06
CISPEP   1 SER A   29    PRO A   30          0         0.14
CISPEP   2 PRO A  201    PRO A  202          0         0.45
CISPEP   3 SER B   29    PRO B   30          0         0.02
CISPEP   4 PRO B  201    PRO B  202          0         0.60
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  THR A 199
SITE     2 AC1  5 HOH A1026
SITE     1 AC2  5 HIS B  94  HIS B  96  HIS B 119  THR B 199
SITE     2 AC2  5 HOH B1497
SITE     1 AC3  5 HIS A  94  HIS A 119  LEU A 198  THR A 199
SITE     2 AC3  5 HOH A1026
SITE     1 AC4  6 HIS B  94  HIS B 119  LEU B 198  THR B 199
SITE     2 AC4  6 HOH B1497  HOH B1498
SITE     1 AC5  9 SER A  48  LEU B 182  LEU B 185  PRO B 186
SITE     2 AC5  9 PRO B 187  TRP B 189  HOH B1331  HOH B1335
SITE     3 AC5  9 HOH B1573
CRYST1   57.780   58.210   72.120  90.00  92.36  90.00 P 1 21 1      4
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      0.017307  0.000000  0.000713        0.00000
SCALE2      0.000000  0.017179  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013878        0.00000
      
PROCHECK
Go to PROCHECK summary
 References