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PDBsum entry 2q1b

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Lyase PDB id
2q1b
Jmol
Contents
Protein chain
256 a.a.
Ligands
BEZ
LSA
Metals
_ZN ×2
_HG
Waters ×285
HEADER    LYASE                                   24-MAY-07   2Q1B
TITLE     CARBONIC ANHYDRASE II IN COMPLEX WITH SACCHARIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CARBONATE DEHYDRATASE II,
COMPND   5 CA-II, CARBONIC ANHYDRASE C;
COMPND   6 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 OTHER_DETAILS: FROM HUMAN ERYTHROCYTES
KEYWDS    10-STRANDED, TWISTED BETA-SHEET, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.KLEBE,A.HEINE,K.KOEHLER
REVDAT   3   24-FEB-09 2Q1B    1       VERSN
REVDAT   2   09-OCT-07 2Q1B    1       JRNL
REVDAT   1   04-SEP-07 2Q1B    0
JRNL        AUTH   K.KOHLER,A.HILLEBRECHT,J.SCHULZE WISCHELER,
JRNL        AUTH 2 A.INNOCENTI,A.HEINE,C.T.SUPURAN,G.KLEBE
JRNL        TITL   SACCHARIN INHIBITS CARBONIC ANHYDRASES: POSSIBLE
JRNL        TITL 2 EXPLANATION FOR ITS UNPLEASANT METALLIC AFTERTASTE.
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  46  7697 2007
JRNL        REFN                   ISSN 1433-7851
JRNL        PMID   17705204
JRNL        DOI    10.1002/ANIE.200701189
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.70 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) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.7
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
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) : 0.148
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.147
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.218
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1168
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 24041
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.147
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.146
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.215
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1135
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 23282
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2105
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 24
REMARK   3   SOLVENT ATOMS      : 285
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2348.31
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1991.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 14
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 9664
REMARK   3   NUMBER OF RESTRAINTS                     : 9067
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.008
REMARK   3   ANGLE DISTANCES                      (A) : 0.026
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.053
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.056
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.019
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.065
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2Q1B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-07.
REMARK 100 THE RCSB ID CODE IS RCSB043024.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 103
REMARK 200  PH                             : 8.5
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 RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178
REMARK 200  MONOCHROMATOR                  : FOCUSSING MIRRORS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24239
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
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     (%) : 89.9
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04100
REMARK 200   FOR THE DATA SET  : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.09600
REMARK 200   FOR SHELL         : 9.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1OQ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.6-2.8M AMMONIUM SULFATE, 0.1M
REMARK 280  TRIS-HCL, 0.001M CHLORO-MERCURY-BENZOATE, PH 8.5, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K
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       20.80500
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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     SER A     2
REMARK 465     HIS A     3
REMARK 465     LYS A   261
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 114   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 227   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 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       56.50   -146.06
REMARK 500    ALA A  65     -168.11   -161.11
REMARK 500    LYS A  76      -93.98   -119.88
REMARK 500    GLU A 106      -67.30    -91.91
REMARK 500    PHE A 176       68.94   -153.95
REMARK 500    ASN A 244       47.99    -90.81
REMARK 500    LYS A 252     -136.69     55.21
REMARK 500    ASN A 253       59.24    -94.53
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 400  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A 119   ND1  96.8
REMARK 620 3 HIS A  94   NE2 105.3 116.4
REMARK 620 4 LSA A 500   N9  122.2 121.5  94.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              HG A 450  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 206   SG
REMARK 620 2 GLN A 137   O    85.7
REMARK 620 3 GLU A 205   O    95.1  90.7
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 400
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 430
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 450
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A 455
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LSA A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OQ5   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH NANOMOLAR INHIBITOR
REMARK 900 RELATED ID: 1Z9Y   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH FUROSEMIDE AS
REMARK 900 SULFONAMIDE INHIBITOR
DBREF  2Q1B A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 A  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 400       1
HET     ZN  A 430       1
HET     HG  A 450       1
HET    BEZ  A 455       9
HET    LSA  A 500      12
HETNAM      ZN ZINC ION
HETNAM      HG MERCURY (II) ION
HETNAM     BEZ BENZOIC ACID
HETNAM     LSA 1,2-BENZISOTHIAZOL-3(2H)-ONE 1,1-DIOXIDE
HETSYN     LSA SACCHARIN
FORMUL   2   ZN    2(ZN 2+)
FORMUL   4   HG    HG 2+
FORMUL   5  BEZ    C7 H6 O2
FORMUL   6  LSA    C7 H5 N O3 S
FORMUL   7  HOH   *285(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
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 ALA A 116  ASN A 124 -1
SHEET    3   B10 THR A  87  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    4   B10 PHE A  66  PHE A  70 -1  N  PHE A  70   O  ILE A  91
SHEET    5   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
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 THR A  87  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
LINK        ZN    ZN A 400                 NE2 HIS A  96     1555   1555  2.03
LINK        ZN    ZN A 400                 ND1 HIS A 119     1555   1555  2.10
LINK        ZN    ZN A 400                 NE2 HIS A  94     1555   1555  2.04
LINK        ZN    ZN A 400                 N9  LSA A 500     1555   1555  2.05
LINK        HG    HG A 450                 SG  CYS A 206     1555   1555  1.94
LINK        HG    HG A 450                 O   GLN A 137     1555   1555  2.92
LINK        HG    HG A 450                 O   GLU A 205     1555   1555  3.23
CISPEP   1 SER A   29    PRO A   30          0         1.99
CISPEP   2 PRO A  201    PRO A  202          0        13.77
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  LSA A 500
SITE     1 AC2  3 ASN A  62  HIS A  64  HOH A 752
SITE     1 AC3  4 GLN A 137  GLU A 205  CYS A 206  BEZ A 455
SITE     1 AC4  7 GLN A 136  GLN A 137  PRO A 138  GLU A 205
SITE     2 AC4  7  HG A 450  HOH A 658  HOH A 783
SITE     1 AC5 10 HIS A  94  HIS A  96  HIS A 119  VAL A 143
SITE     2 AC5 10 LEU A 198  THR A 199  THR A 200  TRP A 209
SITE     3 AC5 10  ZN A 400  HOH A 755
CRYST1   42.220   41.610   72.160  90.00 104.44  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      0.023685  0.000000  0.006099        0.00000
SCALE2      0.000000  0.024033  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014310        0.00000
      
PROCHECK
Go to PROCHECK summary
 References