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PDBsum entry 3gz0

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Lyase PDB id
3gz0
Jmol
Contents
Protein chain
257 a.a.
Metals
_ZN
Waters ×249
HEADER    LYASE                                   06-APR-09   3GZ0
TITLE     APO-HUMAN CARBONIC ANHYDRASE II REVISITED: IMPLICATIONS OF
TITLE    2 THE LOSS OF A METAL IN PROTEIN STRUCTURE, STABILITY AND
TITLE    3 SOLVENT NETWORK
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE
COMPND   5 DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC;
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: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS    APO, CARBONIC ANHYDRASE, ACETYLATION, CYTOPLASM, DISEASE
KEYWDS   2 MUTATION, LYASE, METAL-BINDING, POLYMORPHISM, ZINC
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.S.AVVARU,R.MCKENNA
REVDAT   3   15-SEP-09 3GZ0    1       JRNL
REVDAT   2   04-AUG-09 3GZ0    1       REMARK
REVDAT   1   21-JUL-09 3GZ0    0
JRNL        AUTH   B.S.AVVARU,S.A.BUSBY,M.J.CHALMERS,P.R.GRIFFIN,
JRNL        AUTH 2 B.VENKATAKRISHNAN,M.AGBANDJE-MCKENNA,D.N.SILVERMAN,
JRNL        AUTH 3 R.MCKENNA
JRNL        TITL   APO-HUMAN CARBONIC ANHYDRASE II REVISITED:
JRNL        TITL 2 IMPLICATIONS OF THE LOSS OF A METAL IN PROTEIN
JRNL        TITL 3 STRUCTURE, STABILITY, AND SOLVENT NETWORK .
JRNL        REF    BIOCHEMISTRY                  V.  48  7365 2009
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   19583303
JRNL        DOI    10.1021/BI9007512
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.26 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.26
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4
REMARK   3   CROSS-VALIDATION METHOD           : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.140
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.187
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2087
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 1
REMARK   3   SOLVENT ATOMS      : 249
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL
REMARK   3   NUMBER OF RESTRAINTS                     : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : NULL
REMARK   3   ANGLE DISTANCES                      (A) : NULL
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : NULL
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3GZ0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052483.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : A1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9772
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91749
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.260
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.4
REMARK 200  DATA REDUNDANCY                : 7.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08500
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.08500
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2CBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RYSTALS OF APO-HCA II WERE OBTAINED
REMARK 280  THROUGH HANGING DROP METHOD. 10 UL DROPS OF EQUAL AMOUNTS OF
REMARK 280  PROTEIN AND PRECIPITANT WERE EQUILIBRATED AGAINST PRECIPITANT
REMARK 280  SOLUTION (1.3 M SODIUM CITRATE, 100MM TRIS-HCL, PH 7.0) BY
REMARK 280  VAPOR DIFFUSION AT ROOM TEMPERATURE (~20 C). A CRYSTAL WAS
REMARK 280  CRYOPROTECTED BY QUICK IMMERSION INTO 20% GLYCEROL MOTHER
REMARK 280  LIQUOR AND FLASH-COOLED BY EXPOSING IT TO A GAS STREAM OF
REMARK 280  NITROGEN AT 100K, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  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       20.81150
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 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 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     SER A     2
REMARK 465     HIS A     3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500  ZN    ZN  A   262     O    HOH A  2001              1.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    TYR A   7   CB  -  CG  -  CD2 ANGL. DEV. =   3.6 DEGREES
REMARK 500    HIS A  15   CG  -  ND1 -  CE1 ANGL. DEV. =   9.5 DEGREES
REMARK 500    HIS A  15   ND1 -  CE1 -  NE2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    TYR A  51   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A  58   CD  -  NE  -  CZ  ANGL. DEV. =  23.6 DEGREES
REMARK 500    TYR A 114   CB  -  CG  -  CD2 ANGL. DEV. =   4.1 DEGREES
REMARK 500    LEU A 141   CB  -  CG  -  CD2 ANGL. DEV. =  10.5 DEGREES
REMARK 500    LYS A 159   CA  -  CB  -  CG  ANGL. DEV. =  23.1 DEGREES
REMARK 500    LYS A 213   CA  -  CB  -  CG  ANGL. DEV. =  18.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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    ARG A  27       53.01   -141.49
REMARK 500    ALA A  65     -166.27   -161.48
REMARK 500    LYS A 111       -1.87     73.94
REMARK 500    ASN A 244       51.00    -95.58
REMARK 500    LYS A 252     -136.56     52.19
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 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2  94.9
REMARK 620 3 HIS A 119   ND1 120.1 104.8
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 A 262
DBREF  3GZ0 A    2   261  UNP    P00918   CAH2_HUMAN       2    260
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 LYS GLY GLU ARG
SEQRES   3 A  259  GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES   4 A  259  ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES   5 A  259  ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES   6 A  259  ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES   7 A  259  LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES   8 A  259  PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES   9 A  259  GLU HIS THR VAL ASP LYS 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  LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES  12 A  259  ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES  13 A  259  LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES  14 A  259  LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES  15 A  259  LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES  16 A  259  LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES  17 A  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES  18 A  259  LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES  19 A  259  PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES  20 A  259  PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 262       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  HOH   *249(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS 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  LYS 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  VAL A 150  1  N  GLY A 145   O  LEU A 212
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  VAL A  78   N  SER A  50
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  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  1.98
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.19
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.21
CISPEP   1 SER A   29    PRO A   30          0        -2.83
CISPEP   2 PRO A  201    PRO A  202          0        11.99
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  THR A 199
SITE     2 AC1  5 HOH A2001
CRYST1   42.737   41.623   72.821  90.00 104.59  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      0.023399  0.000000  0.006091        0.00000
SCALE2      0.000000  0.024025  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014190        0.00000
      
PROCHECK
Go to PROCHECK summary
 References