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PDBsum entry 1z97

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Lyase PDB id
1z97
Jmol
Contents
Protein chain
263 a.a.
Metals
_ZN
Waters ×97
HEADER    LYASE                                   31-MAR-05   1Z97
TITLE     HUMAN CARBONIC ANHYDRASE III: STRUCTURAL AND KINETIC STUDY
TITLE    2 OF CATALYSIS AND PROTON TRANSFER.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE III;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE III, CA- III;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA3;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-81F1
KEYWDS    CARBONIC ANHYDRASE, PROTON WIRE, CHEMICAL RESCUE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.M.DUDA,C.TU,S.Z.FISHER,H.AN,C.YOSHIOKA,L.GOVINDASAMY,
AUTHOR   2 P.J.LAIPIS,M.AGBANDJE-MCKENNA,D.N.SILVERMAN,R.MCKENNA
REVDAT   2   24-FEB-09 1Z97    1       VERSN
REVDAT   1   09-AUG-05 1Z97    0
JRNL        AUTH   D.M.DUDA,C.TU,S.Z.FISHER,H.AN,C.YOSHIOKA,
JRNL        AUTH 2 L.GOVINDASAMY,P.J.LAIPIS,M.AGBANDJE-MCKENNA,
JRNL        AUTH 3 D.N.SILVERMAN,R.MCKENNA
JRNL        TITL   HUMAN CARBONIC ANHYDRASE III: STRUCTURAL AND
JRNL        TITL 2 KINETIC STUDY OF CATALYSIS AND PROTON TRANSFER
JRNL        REF    BIOCHEMISTRY                  V.  44 10046 2005
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   16042381
JRNL        DOI    10.1021/BI050610H
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.8
REMARK   3   NUMBER OF REFLECTIONS             : 12911
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) : 0.186
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 653
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            : 2124
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 97
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) : 1.30
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 1Z97 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032456.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-JAN-02
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 9.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : OSMIC MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13525
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
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     (%) : 92.3
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08100
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.34100
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1FLJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 10MM TRIS, PH 9.2,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 273K
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       35.38750
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 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     MET A     1
REMARK 465     ALA A     2
REMARK 465     LYS A     3
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    LYS A  57      -56.78   -123.09
REMARK 500    ARG A  76      -72.28    -96.21
REMARK 500    ASN A 129      -38.48     65.98
REMARK 500    LYS A 178       70.16     53.80
REMARK 500    GLU A 236      156.17    -39.69
REMARK 500    ASN A 244       48.71   -100.57
REMARK 500    ASN A 252     -138.65     59.22
REMARK 500    LYS A 261      -70.89    -84.28
REMARK 500    HIS A 262       88.25     67.50
REMARK 500    HIS A 266     -142.26   -142.47
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 268  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 113.2
REMARK 620 3 HOH A 278   O   107.5 103.5
REMARK 620 4 HIS A 119   ND1 113.1 104.8 114.5
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 268
DBREF  1Z97 A    1   261  UNP    P07451   CAH3_HUMAN       0    259
SEQADV 1Z97 SER A  183  UNP  P07451    CYS   181 ENGINEERED
SEQADV 1Z97 SER A  188  UNP  P07451    CYS   186 ENGINEERED
SEQADV 1Z97 LEU A  198  UNP  P07451    PHE   196 ENGINEERED
SEQADV 1Z97 HIS A  262  UNP  P07451              EXPRESSION TAG
SEQADV 1Z97 HIS A  263  UNP  P07451              EXPRESSION TAG
SEQADV 1Z97 HIS A  264  UNP  P07451              EXPRESSION TAG
SEQADV 1Z97 HIS A  265  UNP  P07451              EXPRESSION TAG
SEQADV 1Z97 HIS A  266  UNP  P07451              EXPRESSION TAG
SEQADV 1Z97 HIS A  267  UNP  P07451              EXPRESSION TAG
SEQRES   1 A  266  MET ALA LYS GLU TRP GLY TYR ALA SER HIS ASN GLY PRO
SEQRES   2 A  266  ASP HIS TRP HIS GLU LEU PHE PRO ASN ALA LYS GLY GLU
SEQRES   3 A  266  ASN GLN SER PRO ILE GLU LEU HIS THR LYS ASP ILE ARG
SEQRES   4 A  266  HIS ASP PRO SER LEU GLN PRO TRP SER VAL SER TYR ASP
SEQRES   5 A  266  GLY GLY SER ALA LYS THR ILE LEU ASN ASN GLY LYS THR
SEQRES   6 A  266  CYS ARG VAL VAL PHE ASP ASP THR TYR ASP ARG SER MET
SEQRES   7 A  266  LEU ARG GLY GLY PRO LEU PRO GLY PRO TYR ARG LEU ARG
SEQRES   8 A  266  GLN PHE HIS LEU HIS TRP GLY SER SER ASP ASP HIS GLY
SEQRES   9 A  266  SER GLU HIS THR VAL ASP GLY VAL LYS TYR ALA ALA GLU
SEQRES  10 A  266  LEU HIS LEU VAL HIS TRP ASN PRO LYS TYR ASN THR PHE
SEQRES  11 A  266  LYS GLU ALA LEU LYS GLN ARG ASP GLY ILE ALA VAL ILE
SEQRES  12 A  266  GLY ILE PHE LEU LYS ILE GLY HIS GLU ASN GLY GLU PHE
SEQRES  13 A  266  GLN ILE PHE LEU ASP ALA LEU ASP LYS ILE LYS THR LYS
SEQRES  14 A  266  GLY LYS GLU ALA PRO PHE THR LYS PHE ASP PRO SER SER
SEQRES  15 A  266  LEU PHE PRO ALA SER ARG ASP TYR TRP THR TYR GLN GLY
SEQRES  16 A  266  SER LEU THR THR PRO PRO CYS GLU GLU CYS ILE VAL TRP
SEQRES  17 A  266  LEU LEU LEU LYS GLU PRO MET THR VAL SER SER ASP GLN
SEQRES  18 A  266  MET ALA LYS LEU ARG SER LEU LEU SER SER ALA GLU ASN
SEQRES  19 A  266  GLU PRO PRO VAL PRO LEU VAL SER ASN TRP ARG PRO PRO
SEQRES  20 A  266  GLN PRO ILE ASN ASN ARG VAL VAL ARG ALA SER PHE LYS
SEQRES  21 A  266  HIS HIS HIS HIS HIS HIS
HET     ZN  A 268       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  HOH   *97(H2 O)
HELIX    1   1 GLY A   12  HIS A   17  1                                   6
HELIX    2   2 GLU A   18  LEU A   19  5                                   2
HELIX    3   3 PHE A   20  GLY A   25  5                                   6
HELIX    4   4 ASP A   52  GLY A   54  5                                   3
HELIX    5   5 PRO A  125  ASN A  129  5                                   4
HELIX    6   6 THR A  130  LEU A  135  1                                   6
HELIX    7   7 ASN A  154  LEU A  164  1                                  11
HELIX    8   8 ASP A  165  LYS A  168  5                                   4
HELIX    9   9 ASP A  180  PHE A  185  5                                   6
HELIX   10  10 SER A  219  ARG A  227  1                                   9
SHEET    1   A 2 GLU 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   B10 ARG A  39  HIS A  40  0
SHEET    2   B10 ARG A 257  ALA A 258  1  O  ALA A 258   N  ARG A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  ARG A 257
SHEET    4   B10 ILE A 207  LEU A 212 -1  O  ILE A 207   N  GLY A 196
SHEET    5   B10 ILE A 141  ILE A 150  1  N  ILE A 141   O  VAL A 208
SHEET    6   B10 ALA A 116  TRP A 123 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  ARG A  91   O  VAL A 121
SHEET    8   B10 CYS A  66  PHE A  70 -1  N  PHE A  70   O  ARG A  91
SHEET    9   B10 ALA A  56  ASN A  61 -1  N  THR A  58   O  VAL A  69
SHEET   10   B10 GLU A 173  PRO A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 TRP A  47  SER A  50  0
SHEET    2   C 6 MET 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  TRP A 123 -1  O  VAL A 121   N  ARG A  91
SHEET    5   C 6 ILE A 141  ILE A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 MET A 216  VAL A 218  1  O  MET A 216   N  PHE A 147
LINK        ZN    ZN A 268                 NE2 HIS A  94     1555   1555  2.19
LINK        ZN    ZN A 268                 NE2 HIS A  96     1555   1555  2.19
LINK        ZN    ZN A 268                 O   HOH A 278     1555   1555  1.98
LINK        ZN    ZN A 268                 ND1 HIS A 119     1555   1555  2.12
CISPEP   1 SER A   29    PRO A   30          0        -0.21
CISPEP   2 PRO A  201    PRO A  202          0         0.32
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  HOH A 278
CRYST1   44.105   70.775   44.487  90.00 115.07  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      0.022673  0.000000  0.010606        0.00000
SCALE2      0.000000  0.014129  0.000000        0.00000
SCALE3      0.000000  0.000000  0.024816        0.00000
      
PROCHECK
Go to PROCHECK summary
 References