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PDBsum entry 1koq

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Top Page protein metals Protein-protein interface(s) links
Lyase PDB id
1koq
Jmol
Contents
Protein chains
222 a.a. *
Metals
_ZN ×2
Waters ×147
* Residue conservation analysis
HEADER    LYASE                                   22-MAR-98   1KOQ
TITLE     NEISSERIA GONORRHOEAE CARBONIC ANHYDRASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: NEISSERIA GONORRHOEAE;
SOURCE   3 ORGANISM_TAXID: 485;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    LYASE, CARBONIC ANHYDRASE, NEISSERIA GONORRHOEAE,
KEYWDS   2 STRUCTURAL TRIMMING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.HUANG,Y.XUE,L.CHIRICA,S.LINDSKOG,B.-H.JONSSON
REVDAT   3   24-FEB-09 1KOQ    1       VERSN
REVDAT   2   13-JAN-99 1KOQ    3       HET    COMPND REMARK TITLE
REVDAT   2 2                   3       HETATM HEADER TER    LINK
REVDAT   2 3                   3       ATOM   SOURCE SEQRES JRNL
REVDAT   2 4                   3       KEYWDS CONECT
REVDAT   1   09-DEC-98 1KOQ    0
JRNL        AUTH   S.HUANG,Y.XUE,E.SAUER-ERIKSSON,L.CHIRICA,
JRNL        AUTH 2 S.LINDSKOG,B.H.JONSSON
JRNL        TITL   CRYSTAL STRUCTURE OF CARBONIC ANHYDRASE FROM
JRNL        TITL 2 NEISSERIA GONORRHOEAE AND ITS COMPLEX WITH THE
JRNL        TITL 3 INHIBITOR ACETAZOLAMIDE.
JRNL        REF    J.MOL.BIOL.                   V. 283   301 1998
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9761692
JRNL        DOI    10.1006/JMBI.1998.2077
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   L.C.CHIRICA,B.ELLEBY,B.H.JONSSON,S.LINDSKOG
REMARK   1  TITL   THE COMPLETE SEQUENCE, EXPRESSION IN ESCHERICHIA
REMARK   1  TITL 2 COLI, PURIFICATION AND SOME PROPERTIES OF CARBONIC
REMARK   1  TITL 3 ANHYDRASE FROM NEISSERIA GONORRHOEAE
REMARK   1  REF    EUR.J.BIOCHEM.                V. 244   755 1997
REMARK   1  REFN                   ISSN 0014-2956
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 83.3
REMARK   3   NUMBER OF REFLECTIONS             : 26936
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : FREE-R
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.206
REMARK   3   FREE R VALUE                     : 0.271
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 3498
REMARK   3   NUCLEIC ACID ATOMS       : NULL
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 227
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.92
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) : 1.24
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.10
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.08
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1KOQ 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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.8
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          : ENRAF-NONIUS FR591
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28517
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.3
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.07200
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: REFINEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: NGCA COMPLEX WITH AZIME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 3,350; 50MM TRIS; 0.1 M
REMARK 280  LI2SO4;2.2 MM BME; 2.2 MM NAN3; 10% DMSO, PH 7.8
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       37.47000
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: 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 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     HIS A     4
REMARK 465     HIS B     4
REMARK 465     THR B     5
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     HIS B   6    CG   ND1  CD2  CE1  NE2
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    ALA A 148      106.26    -59.15
REMARK 500    ASP A 194     -159.69   -108.96
REMARK 500    ASN A 220     -118.19     57.18
REMARK 500    ASP B  13       57.97   -113.66
REMARK 500    THR B  40      -70.51   -117.58
REMARK 500    MET B 144      108.91    -53.38
REMARK 500    ASP B 194     -164.21   -103.90
REMARK 500    SER B 210      170.84    176.08
REMARK 500    ASN B 220     -118.23     59.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 422        DISTANCE =  5.09 ANGSTROMS
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 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  92   NE2
REMARK 620 2 HIS A  94   NE2 107.4
REMARK 620 3 HIS A 111   ND1 118.9 103.5
REMARK 620 4 HOH A 303   O    98.1 101.9 125.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 302  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  92   NE2
REMARK 620 2 HIS B  94   NE2 111.0
REMARK 620 3 HIS B 111   ND1 112.9 103.0
REMARK 620 4 HOH B 305   O    94.7 100.5 133.6
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 301
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302
DBREF  1KOQ A    4   226  UNP    Q50940   CAH_NEIGO       30    252
DBREF  1KOQ B    4   226  UNP    Q50940   CAH_NEIGO       30    252
SEQRES   1 A  223  HIS THR HIS TRP GLY TYR THR GLY HIS ASP SER PRO GLU
SEQRES   2 A  223  SER TRP GLY ASN LEU SER GLU GLU PHE ARG LEU CYS SER
SEQRES   3 A  223  THR GLY LYS ASN GLN SER PRO VAL ASN ILE THR GLU THR
SEQRES   4 A  223  VAL SER GLY LYS LEU PRO ALA ILE LYS VAL ASN TYR LYS
SEQRES   5 A  223  PRO SER MET VAL ASP VAL GLU ASN ASN GLY HIS THR ILE
SEQRES   6 A  223  GLN VAL ASN TYR PRO GLU GLY GLY ASN THR LEU THR VAL
SEQRES   7 A  223  ASN GLY ARG THR TYR THR LEU LYS GLN PHE HIS PHE HIS
SEQRES   8 A  223  VAL PRO SER GLU ASN GLN ILE LYS GLY ARG THR PHE PRO
SEQRES   9 A  223  MET GLU ALA HIS PHE VAL HIS LEU ASP GLU ASN LYS GLN
SEQRES  10 A  223  PRO LEU VAL LEU ALA VAL LEU TYR GLU ALA GLY LYS THR
SEQRES  11 A  223  ASN GLY ARG LEU SER SER ILE TRP ASN VAL MET PRO MET
SEQRES  12 A  223  THR ALA GLY LYS VAL LYS LEU ASN GLN PRO PHE ASP ALA
SEQRES  13 A  223  SER THR LEU LEU PRO LYS ARG LEU LYS TYR TYR ARG PHE
SEQRES  14 A  223  ALA GLY SER LEU THR THR PRO PRO CYS THR GLU GLY VAL
SEQRES  15 A  223  SER TRP LEU VAL LEU LYS THR TYR ASP HIS ILE ASP GLN
SEQRES  16 A  223  ALA GLN ALA GLU LYS PHE THR ARG ALA VAL GLY SER GLU
SEQRES  17 A  223  ASN ASN ARG PRO VAL GLN PRO LEU ASN ALA ARG VAL VAL
SEQRES  18 A  223  ILE GLU
SEQRES   1 B  223  HIS THR HIS TRP GLY TYR THR GLY HIS ASP SER PRO GLU
SEQRES   2 B  223  SER TRP GLY ASN LEU SER GLU GLU PHE ARG LEU CYS SER
SEQRES   3 B  223  THR GLY LYS ASN GLN SER PRO VAL ASN ILE THR GLU THR
SEQRES   4 B  223  VAL SER GLY LYS LEU PRO ALA ILE LYS VAL ASN TYR LYS
SEQRES   5 B  223  PRO SER MET VAL ASP VAL GLU ASN ASN GLY HIS THR ILE
SEQRES   6 B  223  GLN VAL ASN TYR PRO GLU GLY GLY ASN THR LEU THR VAL
SEQRES   7 B  223  ASN GLY ARG THR TYR THR LEU LYS GLN PHE HIS PHE HIS
SEQRES   8 B  223  VAL PRO SER GLU ASN GLN ILE LYS GLY ARG THR PHE PRO
SEQRES   9 B  223  MET GLU ALA HIS PHE VAL HIS LEU ASP GLU ASN LYS GLN
SEQRES  10 B  223  PRO LEU VAL LEU ALA VAL LEU TYR GLU ALA GLY LYS THR
SEQRES  11 B  223  ASN GLY ARG LEU SER SER ILE TRP ASN VAL MET PRO MET
SEQRES  12 B  223  THR ALA GLY LYS VAL LYS LEU ASN GLN PRO PHE ASP ALA
SEQRES  13 B  223  SER THR LEU LEU PRO LYS ARG LEU LYS TYR TYR ARG PHE
SEQRES  14 B  223  ALA GLY SER LEU THR THR PRO PRO CYS THR GLU GLY VAL
SEQRES  15 B  223  SER TRP LEU VAL LEU LYS THR TYR ASP HIS ILE ASP GLN
SEQRES  16 B  223  ALA GLN ALA GLU LYS PHE THR ARG ALA VAL GLY SER GLU
SEQRES  17 B  223  ASN ASN ARG PRO VAL GLN PRO LEU ASN ALA ARG VAL VAL
SEQRES  18 B  223  ILE GLU
HET     ZN  A 301       1
HET     ZN  B 302       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  HOH   *147(H2 O)
HELIX    1   1 GLY A   11  ASP A   13  5                                   3
HELIX    2   2 PRO A   15  LEU A   21  5                                   7
HELIX    3   3 GLU A   23  THR A   30  5                                   8
HELIX    4   4 SER A  138  VAL A  143  1                                   6
HELIX    5   5 ALA A  159  LEU A  162  5                                   4
HELIX    6   6 GLN A  198  VAL A  208  1                                  11
HELIX    7   7 PRO B   15  ASN B   20  5                                   6
HELIX    8   8 GLU B   23  THR B   30  5                                   8
HELIX    9   9 SER B  138  VAL B  143  1                                   6
HELIX   10  10 ALA B  159  LEU B  162  5                                   4
HELIX   11  11 GLN B  198  VAL B  208  1                                  11
SHEET    1   A 7 ILE A  50  ASN A  53  0
SHEET    2   A 7 THR A  78  VAL A  81 -1  N  THR A  80   O  LYS A  51
SHEET    3   A 7 ARG A  84  HIS A  94 -1  N  TYR A  86   O  LEU A  79
SHEET    4   A 7 MET A 108  LEU A 115 -1  N  LEU A 115   O  THR A  87
SHEET    5   A 7 PRO A 121  TYR A 128 -1  N  TYR A 128   O  MET A 108
SHEET    6   A 7 GLU A 183  LEU A 190  1  N  SER A 186   O  VAL A 123
SHEET    7   A 7 TYR A 169  SER A 175 -1  N  GLY A 174   O  GLY A 184
SHEET    1   B 4 GLY A 149  LYS A 152  0
SHEET    2   B 4 VAL A  59  ASN A  63 -1  N  ASN A  63   O  GLY A 149
SHEET    3   B 4 ILE A  68  TYR A  72 -1  N  ASN A  71   O  ASP A  60
SHEET    4   B 4 GLN A  90  HIS A  92 -1  N  PHE A  91   O  VAL A  70
SHEET    1   C 2 TYR A 128  ALA A 130  0
SHEET    2   C 2 ASP A 194  ILE A 196  1  N  ASP A 194   O  GLU A 129
SHEET    1   D 7 LYS B  51  ASN B  53  0
SHEET    2   D 7 THR B  78  VAL B  81 -1  N  THR B  80   O  LYS B  51
SHEET    3   D 7 ARG B  84  HIS B  94 -1  N  TYR B  86   O  LEU B  79
SHEET    4   D 7 MET B 108  LEU B 115 -1  N  LEU B 115   O  THR B  87
SHEET    5   D 7 PRO B 121  TYR B 128 -1  N  TYR B 128   O  MET B 108
SHEET    6   D 7 GLU B 183  LEU B 190  1  N  SER B 186   O  VAL B 123
SHEET    7   D 7 TYR B 169  SER B 175 -1  N  GLY B 174   O  GLY B 184
SHEET    1   E 4 GLY B 149  LYS B 152  0
SHEET    2   E 4 ASP B  60  ASN B  63 -1  N  ASN B  63   O  GLY B 149
SHEET    3   E 4 ILE B  68  ASN B  71 -1  N  ASN B  71   O  ASP B  60
SHEET    4   E 4 GLN B  90  HIS B  92 -1  N  PHE B  91   O  VAL B  70
SHEET    1   F 2 TYR B 128  ALA B 130  0
SHEET    2   F 2 ASP B 194  ILE B 196  1  N  ASP B 194   O  GLU B 129
SSBOND   1 CYS A   28    CYS A  181                          1555   1555  2.02
SSBOND   2 CYS B   28    CYS B  181                          1555   1555  2.02
LINK        ZN    ZN A 301                 NE2 HIS A  92     1555   1555  2.10
LINK        ZN    ZN A 301                 NE2 HIS A  94     1555   1555  2.21
LINK        ZN    ZN A 301                 ND1 HIS A 111     1555   1555  2.03
LINK        ZN    ZN A 301                 O   HOH A 303     1555   1555  2.15
LINK        ZN    ZN B 302                 NE2 HIS B  92     1555   1555  2.12
LINK        ZN    ZN B 302                 NE2 HIS B  94     1555   1555  2.29
LINK        ZN    ZN B 302                 ND1 HIS B 111     1555   1555  2.16
LINK        ZN    ZN B 302                 O   HOH B 305     1555   1555  2.10
CISPEP   1 SER A   35    PRO A   36          0        -0.09
CISPEP   2 VAL A   95    PRO A   96          0        -0.44
CISPEP   3 PRO A  179    PRO A  180          0         0.42
CISPEP   4 SER B   35    PRO B   36          0        -0.04
CISPEP   5 VAL B   95    PRO B   96          0        -0.50
CISPEP   6 PRO B  179    PRO B  180          0         0.35
SITE     1 AC1  4 HIS A  92  HIS A  94  HIS A 111  HOH A 303
SITE     1 AC2  4 HIS B  92  HIS B  94  HIS B 111  HOH B 305
CRYST1   47.230   74.940   62.380  90.00  93.87  90.00 P 1 21 1      4
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      0.021173  0.000000  0.001432        0.00000
SCALE2      0.000000  0.013344  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016067        0.00000
      
PROCHECK
Go to PROCHECK summary
 References