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PDBsum entry 1jcz

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1jcz
Jmol
Contents
Protein chain
260 a.a. *
Ligands
ACY ×2
Metals
_ZN ×2
Waters ×537
* Residue conservation analysis
HEADER    LYASE                                   11-JUN-01   1JCZ
TITLE     CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN CARBONIC
TITLE    2 ANHYDRASE XII
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE XII;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND   5 SYNONYM: CARBONATE DEHYDRATASE XII, CA-XII, TUMOR ANTIGEN HOM-RCC-
COMPND   6 3.1.3;
COMPND   7 EC: 4.2.1.1;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-11D
KEYWDS    EXTRACELLULAR DOMAIN, HUMAN CARBONIC ANHYDRASE XII, BITOPIC MEMBRANE
KEYWDS   2 PROTEIN, TYPE I MEMBRANE PROTEIN, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.A.WHITTINGTON,A.WAHEED,B.ULMASOV,G.N.SHAH,J.H.GRUBB,W.S.SLY,
AUTHOR   2 D.W.CHRISTIANSON
REVDAT   3   16-NOV-11 1JCZ    1       VERSN  HETATM
REVDAT   2   24-FEB-09 1JCZ    1       VERSN
REVDAT   1   17-AUG-01 1JCZ    0
JRNL        AUTH   D.A.WHITTINGTON,A.WAHEED,B.ULMASOV,G.N.SHAH,J.H.GRUBB,
JRNL        AUTH 2 W.S.SLY,D.W.CHRISTIANSON
JRNL        TITL   CRYSTAL STRUCTURE OF THE DIMERIC EXTRACELLULAR DOMAIN OF
JRNL        TITL 2 HUMAN CARBONIC ANHYDRASE XII, A BITOPIC MEMBRANE PROTEIN
JRNL        TITL 3 OVEREXPRESSED IN CERTAIN CANCER TUMOR CELLS.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  98  9545 2001
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   11493685
JRNL        DOI    10.1073/PNAS.161301298
REMARK   2
REMARK   2 RESOLUTION.    1.55 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) : 1.55
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 519456.450
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.5
REMARK   3   NUMBER OF REFLECTIONS             : 74133
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) : 0.194
REMARK   3   FREE R VALUE                     : 0.221
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 5970
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003
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) : 1.55
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.65
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.40
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9204
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560
REMARK   3   BIN FREE R VALUE                    : 0.3000
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.80
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 776
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4176
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 537
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 15.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.90
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -5.59000
REMARK   3    B22 (A**2) : 7.50000
REMARK   3    B33 (A**2) : -1.91000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.02000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18
REMARK   3   ESD FROM SIGMAA              (A) : 0.14
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) : 0.21
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18
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) : 0.76
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) : 1.140 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.740 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.870 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.710 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.37
REMARK   3   BSOL        : 45.24
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_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : ACETATE.PARAM
REMARK   3  PARAMETER FILE  5  : 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   : ACETATE.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1JCZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-01.
REMARK 100 THE RCSB ID CODE IS RCSB013637.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-00
REMARK 200  TEMPERATURE           (KELVIN) : 97
REMARK 200  PH                             : 4.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL7-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5
REMARK 200  DATA REDUNDANCY                : 5.000
REMARK 200  R MERGE                    (I) : 0.04600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.3000
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     (%) : 79.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.28700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.100
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 1G0E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, PH 4.8,
REMARK 280  VAPOR DIFFUSION, HANGING DROP AT 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       73.36650
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.28900
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       73.36650
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.28900
REMARK 290   SMTRY3   4  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 DIMER CONSISTING OF CHAINS A
REMARK 300 AND B IN THE ASYMMETRIC UNIT
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH B1102  LIES ON A SPECIAL POSITION.
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     ALA A     2
REMARK 465     SER A     3
REMARK 465     GLN A   262
REMARK 465     ALA B     2
REMARK 465     SER B     3
REMARK 465     GLN B   262
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  65     -177.46   -170.04
REMARK 500    THR A  91      -38.65   -133.54
REMARK 500    ASP A 102       77.53   -152.53
REMARK 500    GLN A 165        0.62    -68.66
REMARK 500    ASN A 244       58.68    -91.95
REMARK 500    ASP B 102       72.27   -152.66
REMARK 500    ASP B 252     -104.06    -60.95
REMARK 500    GLU B 253      157.21    -39.47
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 901  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 103.3
REMARK 620 3 HIS A 119   ND1 117.4  95.0
REMARK 620 4 ACY A 801   O    88.7 165.2  87.0
REMARK 620 5 HOH A1096   O   105.2  87.8 135.3  80.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 902  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACY B 802   O
REMARK 620 2 HIS B  96   NE2 166.1
REMARK 620 3 HIS B 119   ND1  81.9  96.3
REMARK 620 4 HOH B1071   O    81.9  90.1 136.0
REMARK 620 5 HIS B  94   NE2  90.6 102.5 116.4 104.4
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 802
DBREF  1JCZ A    2   262  UNP    O43570   CAH12_HUMAN     30    292
DBREF  1JCZ B    2   262  UNP    O43570   CAH12_HUMAN     30    292
SEQADV 1JCZ ALA A    2  UNP  O43570    GLY    30 CONFLICT
SEQADV 1JCZ ALA B    2  UNP  O43570    GLY    30 CONFLICT
SEQRES   1 A  263  ALA SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN
SEQRES   2 A  263  SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU
SEQRES   3 A  263  GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR
SEQRES   4 A  263  ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN
SEQRES   5 A  263  LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY
SEQRES   6 A  263  HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE
SEQRES   7 A  263  GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS
SEQRES   8 A  263  LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU
SEQRES   9 A  263  HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS
SEQRES  10 A  263  ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER
SEQRES  11 A  263  THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA
SEQRES  12 A  263  VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP
SEQRES  13 A  263  LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY
SEQRES  14 A  263  GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU
SEQRES  15 A  263  LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY
SEQRES  16 A  263  SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP
SEQRES  17 A  263  THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN
SEQRES  18 A  263  LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET
SEQRES  19 A  263  ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG
SEQRES  20 A  263  GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER
SEQRES  21 A  263  PHE SER GLN
SEQRES   1 B  263  ALA SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN
SEQRES   2 B  263  SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU
SEQRES   3 B  263  GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR
SEQRES   4 B  263  ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN
SEQRES   5 B  263  LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY
SEQRES   6 B  263  HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE
SEQRES   7 B  263  GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS
SEQRES   8 B  263  LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU
SEQRES   9 B  263  HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS
SEQRES  10 B  263  ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER
SEQRES  11 B  263  THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA
SEQRES  12 B  263  VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP
SEQRES  13 B  263  LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY
SEQRES  14 B  263  GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU
SEQRES  15 B  263  LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY
SEQRES  16 B  263  SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP
SEQRES  17 B  263  THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN
SEQRES  18 B  263  LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET
SEQRES  19 B  263  ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG
SEQRES  20 B  263  GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER
SEQRES  21 B  263  PHE SER GLN
HET     ZN  A 901       1
HET     ZN  B 902       1
HET    ACY  A 801       4
HET    ACY  B 802       4
HETNAM      ZN ZINC ION
HETNAM     ACY ACETIC ACID
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  ACY    2(C2 H4 O2)
FORMUL   7  HOH   *537(H2 O)
HELIX    1   1 GLY A   12  ASN A   14  5                                   3
HELIX    2   2 SER A   15  TYR A   20  1                                   6
HELIX    3   3 PRO A   21  GLY A   25  5                                   5
HELIX    4   4 HIS A   34  ASP A   36  5                                   3
HELIX    5   5 ASP A  130  SER A  135  1                                   6
HELIX    6   6 TYR A  157  SER A  162  1                                   6
HELIX    7   7 HIS A  163  VAL A  167  5                                   5
HELIX    8   8 ILE A  181  LEU A  185  5                                   5
HELIX    9   9 SER A  219  ALA A  229  1                                  11
HELIX   10  10 GLY B   12  ASN B   14  5                                   3
HELIX   11  11 SER B   15  TYR B   20  1                                   6
HELIX   12  12 PRO B   21  GLY B   25  5                                   5
HELIX   13  13 HIS B   34  ASP B   36  5                                   3
HELIX   14  14 ASP B  130  SER B  135  1                                   6
HELIX   15  15 ASN B  154  SER B  162  1                                   9
HELIX   16  16 HIS B  163  LYS B  168  5                                   6
HELIX   17  17 ILE B  181  LEU B  185  5                                   5
HELIX   18  18 SER B  219  LEU B  230  1                                  12
SHEET    1   A 2 ASP A  32  LEU A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  LEU A  33
SHEET    1   B15 GLU A 173  PRO A 177  0
SHEET    2   B15 GLN A  56  ASN A  61 -1  O  PHE A  57   N  VAL A 176
SHEET    3   B15 VAL A  66  ASN A  69 -1  N  LYS A  67   O  THR A  60
SHEET    4   B15 TYR A  88  TRP A  97 -1  O  LEU A  93   N  LEU A  68
SHEET    5   B15 ALA A 116  ASN A 124 -1  N  GLU A 117   O  HIS A  96
SHEET    6   B15 LEU A 141  MET A 150 -1  O  ALA A 142   N  HIS A 122
SHEET    7   B15 VAL A 207  PHE A 212  1  N  LEU A 208   O  LEU A 141
SHEET    8   B15 TYR A 191  GLY A 196 -1  N  TYR A 192   O  VAL A 211
SHEET    9   B15 VAL A 256  THR A 258 -1  O  TYR A 257   N  ARG A 193
SHEET   10   B15 LEU A  38  TYR A  40  1  O  GLN A  39   N  THR A 258
SHEET   11   B15 VAL A 256  THR A 258  1  O  VAL A 256   N  GLN A  39
SHEET   12   B15 TYR A 191  GLY A 196 -1  N  ARG A 193   O  TYR A 257
SHEET   13   B15 VAL A 207  PHE A 212 -1  O  VAL A 207   N  GLY A 196
SHEET   14   B15 LEU A 141  MET A 150  1  O  LEU A 141   N  LEU A 208
SHEET   15   B15 VAL A 216  ILE A 218  1  O  VAL A 216   N  GLU A 149
SHEET    1   C 2 ASP B  32  LEU B  33  0
SHEET    2   C 2 THR B 108  VAL B 109  1  O  THR B 108   N  LEU B  33
SHEET    1   D15 GLU B 173  PRO B 177  0
SHEET    2   D15 GLN B  56  ASN B  61 -1  O  PHE B  57   N  VAL B 176
SHEET    3   D15 VAL B  66  ASN B  69 -1  N  LYS B  67   O  THR B  60
SHEET    4   D15 TYR B  88  TRP B  97 -1  O  LEU B  93   N  LEU B  68
SHEET    5   D15 ALA B 116  ASN B 124 -1  N  GLU B 117   O  HIS B  96
SHEET    6   D15 LEU B 141  MET B 150 -1  O  ALA B 142   N  HIS B 122
SHEET    7   D15 VAL B 207  PHE B 212  1  N  LEU B 208   O  LEU B 141
SHEET    8   D15 TYR B 191  GLY B 196 -1  N  TYR B 192   O  VAL B 211
SHEET    9   D15 VAL B 256  THR B 258 -1  O  TYR B 257   N  ARG B 193
SHEET   10   D15 LEU B  38  TYR B  40  1  O  GLN B  39   N  THR B 258
SHEET   11   D15 VAL B 256  THR B 258  1  O  VAL B 256   N  GLN B  39
SHEET   12   D15 TYR B 191  GLY B 196 -1  N  ARG B 193   O  TYR B 257
SHEET   13   D15 VAL B 207  PHE B 212 -1  O  VAL B 207   N  GLY B 196
SHEET   14   D15 LEU B 141  MET B 150  1  O  LEU B 141   N  LEU B 208
SHEET   15   D15 VAL B 216  ILE B 218  1  O  VAL B 216   N  GLU B 149
SSBOND   1 CYS A   23    CYS A  203                          1555   1555  2.04
SSBOND   2 CYS B   23    CYS B  203                          1555   1555  2.03
LINK        ZN    ZN A 901                 NE2 HIS A  94     1555   1555  2.04
LINK        ZN    ZN A 901                 NE2 HIS A  96     1555   1555  2.09
LINK        ZN    ZN A 901                 ND1 HIS A 119     1555   1555  2.12
LINK        ZN    ZN A 901                 O   ACY A 801     1555   1555  2.28
LINK        ZN    ZN A 901                 O   HOH A1096     1555   1555  2.12
LINK        ZN    ZN B 902                 O   ACY B 802     1555   1555  2.33
LINK        ZN    ZN B 902                 NE2 HIS B  96     1555   1555  2.05
LINK        ZN    ZN B 902                 ND1 HIS B 119     1555   1555  2.07
LINK        ZN    ZN B 902                 O   HOH B1071     1555   1555  1.98
LINK        ZN    ZN B 902                 NE2 HIS B  94     1555   1555  2.02
CISPEP   1 SER A   29    PRO A   30          0         0.11
CISPEP   2 PRO A  201    PRO A  202          0         0.30
CISPEP   3 SER B   29    PRO B   30          0         0.06
CISPEP   4 PRO B  201    PRO B  202          0         0.22
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  ACY A 801
SITE     2 AC1  5 HOH A1096
SITE     1 AC2  5 HIS B  94  HIS B  96  HIS B 119  ACY B 802
SITE     2 AC2  5 HOH B1071
SITE     1 AC3  8 HIS A  94  HIS A 119  VAL A 143  LEU A 198
SITE     2 AC3  8 THR A 199   ZN A 901  HOH A1057  HOH A1096
SITE     1 AC4  8 HIS B  94  HIS B 119  VAL B 143  LEU B 198
SITE     2 AC4  8 THR B 199   ZN B 902  HOH B1071  HOH B1079
CRYST1  146.733   44.578   85.167  90.00  94.10  90.00 C 1 2 1       8
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      0.006815  0.000000  0.000488        0.00000
SCALE2      0.000000  0.022433  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011772        0.00000
      
PROCHECK
Go to PROCHECK summary
 References