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PDBsum entry 1f2w

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Lyase PDB id
1f2w
Jmol
Contents
Protein chain
257 a.a. *
Ligands
CNN
Metals
_ZN
_HG
HGB
Waters ×253
* Residue conservation analysis
HEADER    LYASE                                   30-MAY-00   1F2W
TITLE     THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC
TITLE    2 ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PACA/HCAII
KEYWDS    PROTEIN-INHIBITOR COMPLEX, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.GUERRI,F.BRIGANTI,A.SCOZZAFAVA,C.T.SUPURAN,S.MANGANI
REVDAT   3   24-FEB-09 1F2W    1       VERSN
REVDAT   2   29-NOV-00 1F2W    1       JRNL
REVDAT   1   08-JUN-00 1F2W    0
JRNL        AUTH   A.GUERRI,F.BRIGANTI,A.SCOZZAFAVA,C.T.SUPURAN,
JRNL        AUTH 2 S.MANGANI
JRNL        TITL   MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY
JRNL        TITL 2 CARBONIC ANHYDRASE II SUGGESTED BY CRYOGENIC X-RAY
JRNL        TITL 3 DIFFRACTION.
JRNL        REF    BIOCHEMISTRY                  V.  39 12391 2000
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   11015219
JRNL        DOI    10.1021/BI000937C
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 17716
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165
REMARK   3   R VALUE            (WORKING SET) : 0.166
REMARK   3   FREE R VALUE                     : 0.218
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 910
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2049
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 6
REMARK   3   SOLVENT ATOMS            : 253
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 6.60
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.014 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.034 ; 0.040
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.069 ; 0.050
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.012 ; 0.020
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.133 ; 0.150
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.180 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.230 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : 0.150 ; 0.300
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : 9.900 ; 7.000
REMARK   3    STAGGERED                 (DEGREES) : 17.200; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : 28.500; 20.000
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.640 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.240 ; 3.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.040 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.000 ; 3.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1F2W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-00.
REMARK 100 THE RCSB ID CODE IS RCSB011177.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-JAN-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.7
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          : MACSCIENCE M12X
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GOBEL MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : BRUKER SMART 1000
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200  DATA SCALING SOFTWARE          : SAINT
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17716
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0
REMARK 200  DATA REDUNDANCY                : 2.100
REMARK 200  R MERGE                    (I) : 0.05700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05
REMARK 200  COMPLETENESS FOR SHELL     (%) : 3902.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.09900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, 4-
REMARK 280  (HYDROXYMERCURY)BENZOATE, TRIS HCL , PH 7.7, VAPOR DIFFUSION,
REMARK 280  HANGING 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       20.87100
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     SER A     2
REMARK 465     HIS A     3
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    ARG A  27   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES
REMARK 500    PRO A  30   CA  -  N   -  CD  ANGL. DEV. =  -9.4 DEGREES
REMARK 500    PRO A  30   N   -  CD  -  CG  ANGL. DEV. =   8.0 DEGREES
REMARK 500    PHE A  66   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    PHE A  66   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    GLU A 239   OE1 -  CD  -  OE2 ANGL. DEV. = -10.2 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG A 254   NH1 -  CZ  -  NH2 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG A 254   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    ASN A  11       11.60   -142.70
REMARK 500    ARG A  27       52.59   -147.76
REMARK 500    PRO A  30      171.12    -53.31
REMARK 500    LYS A  76      -95.62    -98.90
REMARK 500    GLU A 106      -60.37    -93.01
REMARK 500    LYS A 111       -6.83     72.09
REMARK 500    PHE A 176       59.44   -147.70
REMARK 500    ASN A 244       53.02    -98.42
REMARK 500    LYS A 252     -137.74     53.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 SER A   29     PRO A   30                  -33.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    SER A  29        -16.76
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 458        DISTANCE =  5.39 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     HGB A  263
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  96   NE2
REMARK 620 2 HIS A 119   ND1 103.7
REMARK 620 3 HIS A  94   NE2 100.7 122.2
REMARK 620 4 CNN A 264   N2  103.4 110.2 113.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              HG A 265  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  64   ND1
REMARK 620 2 HOH A 503   O    94.0
REMARK 620 3 HOH A 328   O   111.8  94.4
REMARK 620 4 ASN A  62   O    94.4 145.1 113.6
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 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 265
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HGB A 263
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CNN A 264
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BV3   RELATED DB: PDB
REMARK 900 1BV3 CONTAINS THE SAME PROTEIN WITH UREA
DBREF  1F2W A    2   261  UNP    P00918   CAH2_HUMAN       1    259
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
HET     HG  A 265       1
HET    HGB  A 263       1
HET    CNN  A 264       3
HETNAM      ZN ZINC ION
HETNAM      HG MERCURY (II) ION
HETNAM     HGB 4-(HYDROXYMERCURY)BENZOIC ACID
HETNAM     CNN CYANAMIDE
FORMUL   2   ZN    ZN 2+
FORMUL   3   HG    HG 2+
FORMUL   4  HGB    C7 H6 HG O3
FORMUL   5  CNN    C H2 N2
FORMUL   6  HOH   *253(H2 O)
HELIX    1   1 PHE A   20  GLY A   25  5                                   6
HELIX    2   2 LYS A  127  GLY A  129  5                                   3
HELIX    3   3 ASP A  130  VAL A  135  1                                   6
HELIX    4   4 LYS A  154  GLY A  156  5                                   3
HELIX    5   5 LEU A  157  LEU A  164  1                                   8
HELIX    6   6 ASP A  165  LYS A  168  5                                   4
HELIX    7   7 ASP A  180  LEU A  185  5                                   6
HELIX    8   8 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   B16 LYS A  39  TYR A  40  0
SHEET    2   B16 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3   B16 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B16 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B16 LEU A 141  VAL A 150  1  O  LEU A 141   N  THR A 208
SHEET    6   B16 ILE A 216  VAL A 218  1  N  ILE A 216   O  PHE A 147
SHEET    7   B16 LEU A 141  VAL A 150  1  O  PHE A 147   N  ILE A 216
SHEET    8   B16 ALA A 116  ASN A 124 -1  O  ALA A 116   N  LEU A 148
SHEET    9   B16 TYR A  88  TRP A  97 -1  N  ARG A  89   O  TRP A 123
SHEET   10   B16 VAL A  78  GLY A  81 -1  N  LEU A  79   O  TYR A  88
SHEET   11   B16 LEU A  47  SER A  50 -1  N  SER A  48   O  LYS A  80
SHEET   12   B16 VAL A  78  GLY A  81 -1  O  VAL A  78   N  SER A  50
SHEET   13   B16 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET   14   B16 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET   15   B16 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   16   B16 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
LINK        ZN    ZN A 262                 NE2 HIS A  96     1555   1555  2.15
LINK        ZN    ZN A 262                 ND1 HIS A 119     1555   1555  2.01
LINK        ZN    ZN A 262                 NE2 HIS A  94     1555   1555  2.00
LINK        ZN    ZN A 262                 N2  CNN A 264     1555   1555  2.09
LINK        HG    HG A 265                 ND1 HIS A  64     1555   1555  2.47
LINK        HG    HG A 265                 O   HOH A 503     1555   1555  2.61
LINK        HG    HG A 265                 O   HOH A 328     1555   1555  2.81
LINK        HG    HG A 265                 O   ASN A  62     1555   1555  2.87
LINK        HG   HGB A 263                 O   HOH A 298     1555   1555  2.27
CISPEP   1 PRO A  201    PRO A  202          0        13.69
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  CNN A 264
SITE     2 AC1  5 HOH A 316
SITE     1 AC2  4 ASN A  62  HIS A  64  HOH A 328  HOH A 503
SITE     1 AC3  5 GLN A 137  GLU A 205  CYS A 206  HOH A 298
SITE     2 AC3  5 HOH A 497
SITE     1 AC4  8 HIS A  94  HIS A  96  HIS A 119  THR A 199
SITE     2 AC4  8 THR A 200   ZN A 262  HOH A 316  HOH A 500
CRYST1   42.158   41.742   72.307  90.00 104.42  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      0.023720  0.000000  0.006100        0.00000
SCALE2      0.000000  0.023960  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014280        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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