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PDBsum entry 3znc

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Lyase PDB id
3znc
Jmol
Contents
Protein chain
250 a.a.
Ligands
BZ1
Metals
_ZN
Waters ×2
HEADER    LYASE                                   10-FEB-98   3ZNC
TITLE     MURINE CARBONIC ANHYDRASE IV COMPLEXED WITH BRINZOLAMIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE IV;
COMPND   3 CHAIN: A;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: MURINE CAIV;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_GENE: MURINE CAIV
KEYWDS    LYASE, ZINC, MURINE, MEMBRANE, INHIBITOR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.STAMS,Y.CHEN,D.W.CHRISTIANSON
REVDAT   2   24-FEB-09 3ZNC    1       VERSN
REVDAT   1   23-MAR-99 3ZNC    0
JRNL        AUTH   T.STAMS,Y.CHEN,P.A.BORIACK-SJODIN,J.D.HURT,J.LIAO,
JRNL        AUTH 2 J.A.MAY,T.DEAN,P.LAIPIS,D.N.SILVERMAN,
JRNL        AUTH 3 D.W.CHRISTIANSON
JRNL        TITL   STRUCTURES OF MURINE CARBONIC ANHYDRASE IV AND
JRNL        TITL 2 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
JRNL        TITL 3 BRINZOLAMIDE: MOLECULAR BASIS OF ISOZYME-DRUG
JRNL        TITL 4 DISCRIMINATION.
JRNL        REF    PROTEIN SCI.                  V.   7   556 1998
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   9541386
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   T.STAMS,S.K.NAIR,T.OKUYAMA,A.WAHEED,W.S.SLY,
REMARK   1  AUTH 2 D.W.CHRISTIANSON
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE SECRETORY FORM OF
REMARK   1  TITL 2 MEMBRANE-ASSOCIATED HUMAN CARBONIC ANHYDRASE IV AT
REMARK   1  TITL 3 2.8-A RESOLUTION
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  93 13589 1996
REMARK   1  REFN                   ISSN 0027-8424
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.4
REMARK   3   NUMBER OF REFLECTIONS             : 6506
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) : 0.191
REMARK   3   FREE R VALUE                     : 0.277
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 717
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            : 2018
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 25
REMARK   3   SOLVENT ATOMS            : 2
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.10
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  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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3ZNC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : OCT-96
REMARK 200  TEMPERATURE           (KELVIN) : 295
REMARK 200  PH                             : 7
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 RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7084
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9
REMARK 200  DATA REDUNDANCY                : 3.520
REMARK 200  R MERGE                    (I) : 0.09700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: MURINE CAIV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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       60.95000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.95000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       26.75000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.60000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       26.75000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.60000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       60.95000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       26.75000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.60000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       60.95000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       26.75000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.60000
REMARK 290   SMTRY3   8  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: DIMERIC
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   BIOMT1   2 -1.000000  0.000000  0.000000       53.50000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       60.95000
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     THR A   131
REMARK 465     SER A   132
REMARK 465     SER A   133
REMARK 465     LYS A   134
REMARK 465     GLU A   135
REMARK 465     ASP A   136
REMARK 465     SER A   137
REMARK 465     LYS A   138
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  11E     146.95     68.15
REMARK 500    PRO A  20      159.45    -40.27
REMARK 500    ALA A  22      -26.88     96.47
REMARK 500    GLN A  63       -4.33     86.58
REMARK 500    SER A  98     -143.42   -142.86
REMARK 500    ASN A 103       56.42   -158.18
REMARK 500    LYS A 140      -49.25    151.36
REMARK 500    SER A 174     -171.47   -170.57
REMARK 500    GLU A 178      107.86    -35.05
REMARK 500    TYR A 194      148.15   -175.56
REMARK 500    GLU A 205       46.74    -76.23
REMARK 500    ASN A 244       46.83    -89.21
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   1  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2  96.3
REMARK 620 3 HIS A 119   ND1 116.2  92.9
REMARK 620 4 BZ1 A 500   N2  104.4 113.0 128.8
REMARK 620 5 BZ1 A 500   S1   96.9 144.4 110.4  31.5
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE.
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BZ1 A 500
DBREF  3ZNC A    5   261  UNP    Q64444   CAH4_MOUSE      22    279
SEQADV 3ZNC GLU A   11A UNP  Q64444    LYS    29 CONFLICT
SEQRES   1 A  258  TRP CYS TYR GLU ILE GLN THR GLU ASP PRO ARG SER SER
SEQRES   2 A  258  CYS LEU GLY PRO GLU LYS TRP PRO GLY ALA CYS LYS GLU
SEQRES   3 A  258  ASN GLN GLN SER PRO ILE ASN ILE VAL THR ALA ARG THR
SEQRES   4 A  258  LYS VAL ASN PRO ARG LEU THR PRO PHE ILE LEU VAL GLY
SEQRES   5 A  258  TYR ASP GLN LYS GLN GLN TRP PRO ILE LYS ASN ASN GLN
SEQRES   6 A  258  HIS THR VAL GLU MET THR LEU GLY GLY GLY ALA CYS ILE
SEQRES   7 A  258  ILE GLY GLY ASP LEU PRO ALA ARG TYR GLU ALA VAL GLN
SEQRES   8 A  258  LEU HIS LEU HIS TRP SER ASN GLY ASN ASP ASN GLY SER
SEQRES   9 A  258  GLU HIS SER ILE ASP GLY ARG HIS PHE ALA MET GLU MET
SEQRES  10 A  258  HIS ILE VAL HIS LYS LYS LEU THR SER SER LYS GLU ASP
SEQRES  11 A  258  SER LYS ASP LYS PHE ALA VAL LEU ALA PHE MET ILE GLU
SEQRES  12 A  258  VAL GLY ASP LYS VAL ASN LYS GLY PHE GLN PRO LEU VAL
SEQRES  13 A  258  GLU ALA LEU PRO SER ILE SER LYS PRO HIS SER THR SER
SEQRES  14 A  258  THR VAL ARG GLU SER SER LEU GLN ASP MET LEU PRO PRO
SEQRES  15 A  258  SER THR LYS MET TYR THR TYR PHE ARG TYR ASN GLY SER
SEQRES  16 A  258  LEU THR THR PRO ASN CYS ASP GLU THR VAL ILE TRP THR
SEQRES  17 A  258  VAL TYR LYS GLN PRO ILE LYS ILE HIS LYS ASN GLN PHE
SEQRES  18 A  258  LEU GLU PHE SER LYS ASN LEU TYR TYR ASP GLU ASP GLN
SEQRES  19 A  258  LYS LEU ASN MET LYS ASP ASN VAL ARG PRO LEU GLN PRO
SEQRES  20 A  258  LEU GLY LYS ARG GLN VAL PHE LYS SER HIS ALA
HET     ZN  A   1       1
HET    BZ1  A 500      24
HETNAM      ZN ZINC ION
HETNAM     BZ1 (+)-4-ETHYLAMINO-3,4-DIHYDRO-2-(METHOXY)PROPYL-2H-
HETNAM   2 BZ1  THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE-1,1-DIOXIDE
FORMUL   2   ZN    ZN 2+
FORMUL   3  BZ1    C12 H21 N3 O5 S3
FORMUL   4  HOH   *2(H2 O)
HELIX    1   1 GLU A    8  THR A   11  1                                   4
HELIX    2   2 PRO A   13  LYS A   15  5                                   3
HELIX    3   3 THR A   35  ARG A   37  5                                   3
HELIX    4   4 LYS A  155  GLU A  162  1                                   8
HELIX    5   5 LEU A  164  SER A  166  5                                   3
HELIX    6   6 LEU A  181  MET A  184  5                                   4
HELIX    7   7 SER A  187A LYS A  188  5                                   3
HELIX    8   8 LYS A  220  ASN A  228  1                                  10
SHEET    1   A 2 ILE A  48  VAL A  50  0
SHEET    2   A 2 CYS A  78  ILE A  80 -1  N  ILE A  80   O  ILE A  48
SHEET    1   B 3 THR A 173  VAL A 176  0
SHEET    2   B 3 TRP A  57  ASN A  61 -1  N  ILE A  59   O  SER A 174
SHEET    3   B 3 VAL A  66  MET A  68 -1  N  GLU A  67   O  LYS A  60
SHEET    1   C 5 TYR A 191  GLY A 196  0
SHEET    2   C 5 VAL A 207  TYR A 212 -1  N  VAL A 211   O  PHE A 192
SHEET    3   C 5 PHE A 141  ILE A 148  1  N  PHE A 141   O  ILE A 208
SHEET    4   C 5 MET A 116  LYS A 124 -1  N  HIS A 122   O  ALA A 142
SHEET    5   C 5 TYR A  88  TRP A  97 -1  N  HIS A  96   O  GLU A 117
SHEET    1   D 2 ILE A 148  GLY A 151  0
SHEET    2   D 2 ILE A 216  HIS A 219  1  N  ILE A 216   O  GLU A 149
SSBOND   1 CYS A    6    CYS A   11G                         1555   1555  2.46
SSBOND   2 CYS A   23    CYS A  203                          1555   1555  2.42
LINK        ZN    ZN A   1                 NE2 HIS A  94     1555   1555  2.02
LINK        ZN    ZN A   1                 NE2 HIS A  96     1555   1555  2.06
LINK        ZN    ZN A   1                 ND1 HIS A 119     1555   1555  2.25
LINK        ZN    ZN A   1                 N2  BZ1 A 500     1555   1555  1.91
LINK        ZN    ZN A   1                 S1  BZ1 A 500     1555   1555  2.97
CISPEP   1 SER A   29    PRO A   30          0         0.03
CISPEP   2 PRO A  201    ASN A  202          0        -0.09
SITE     1  ZN  3 HIS A  94  HIS A  96  HIS A 119
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  BZ1 A 500
SITE     1 AC2 11  ZN A   1  GLN A  92  HIS A  94  HIS A  96
SITE     2 AC2 11 HIS A 119  VAL A 121  PHE A 141  LEU A 198
SITE     3 AC2 11 THR A 199  THR A 200  TRP A 209
CRYST1   53.500   85.200  121.900  90.00  90.00  90.00 C 2 2 21      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      0.018692  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011737  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008203        0.00000
      
PROCHECK
Go to PROCHECK summary
 References