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PDBsum entry 1hea

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Lyase(oxo-acid) PDB id
1hea
Jmol
Contents
Protein chain
256 a.a.
Metals
_HG
_ZN
Waters ×110
HEADER    LYASE(OXO-ACID)                         16-JUL-92   1HEA
TITLE     CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
TITLE    2 (E.C.4.2.1.1) MUTANT WITH LEU 198 REPLACED BY ARG (L198R)
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
KEYWDS    LYASE(OXO-ACID)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.K.NAIR,D.W.CHRISTIANSON
REVDAT   2   24-FEB-09 1HEA    1       VERSN
REVDAT   1   15-OCT-92 1HEA    0
JRNL        AUTH   S.K.NAIR,D.W.CHRISTIANSON
JRNL        TITL   STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO ACID
JRNL        TITL 2 SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN
JRNL        TITL 3 CARBONIC ANHYDRASE II.
JRNL        REF    BIOCHEMISTRY                  V.  32  4506 1993
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   8485129
JRNL        DOI    10.1021/BI00068A005
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2042
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 110
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.011 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 2.300 ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
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) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1HEA 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) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
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: 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   (%): 42.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       20.85000
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 SECONDARY STRUCTURE ELEMENTS WERE DEFINED USING THE PROGRAM
REMARK 400 *DSSP* (W. KABSCH, C. SANDER, BIOPOLYMERS, V. 22, P. 2577,
REMARK 400 1983).
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH A   345     O    HOH A   348              2.09
REMARK 500   OE2  GLU A    14     O    HOH A   349              2.15
REMARK 500   OD2  ASP A   162     O    HOH A   295              2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    HIS A 107   CG    HIS A 107   CD2     0.057
REMARK 500    GLU A 205   CD    GLU A 205   OE2     0.066
REMARK 500    GLU A 214   CD    GLU A 214   OE1     0.086
REMARK 500    GLU A 236   CD    GLU A 236   OE2     0.101
REMARK 500    GLU A 239   CD    GLU A 239   OE2     0.069
REMARK 500
REMARK 500 REMARK: NULL
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    LYS A  24   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    PRO A  30   CA  -  N   -  CD  ANGL. DEV. = -13.3 DEGREES
REMARK 500    PRO A  30   N   -  CA  -  CB  ANGL. DEV. =  11.0 DEGREES
REMARK 500    PRO A  30   N   -  CD  -  CG  ANGL. DEV. =  12.6 DEGREES
REMARK 500    SER A  29   O   -  C   -  N   ANGL. DEV. =  12.5 DEGREES
REMARK 500    THR A  35   O   -  C   -  N   ANGL. DEV. =  10.6 DEGREES
REMARK 500    TYR A  51   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    TYR A  51   CB  -  CG  -  CD1 ANGL. DEV. =   5.2 DEGREES
REMARK 500    ARG A  58   CD  -  NE  -  CZ  ANGL. DEV. =  -9.5 DEGREES
REMARK 500    GLY A  63   O   -  C   -  N   ANGL. DEV. =   9.6 DEGREES
REMARK 500    ASP A  72   CB  -  CG  -  OD2 ANGL. DEV. =   7.6 DEGREES
REMARK 500    ARG A  89   CB  -  CA  -  C   ANGL. DEV. = -12.6 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    LEU A 100   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES
REMARK 500    TYR A 128   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    PHE A 131   CB  -  CG  -  CD1 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD1 ANGL. DEV. =   9.9 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES
REMARK 500    PRO A 201   CA  -  C   -  O   ANGL. DEV. = -18.7 DEGREES
REMARK 500    PRO A 202   CA  -  N   -  CD  ANGL. DEV. = -10.0 DEGREES
REMARK 500    PRO A 202   N   -  CD  -  CG  ANGL. DEV. =   9.1 DEGREES
REMARK 500    PRO A 201   O   -  C   -  N   ANGL. DEV. =  14.6 DEGREES
REMARK 500    GLU A 236   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.2 DEGREES
REMARK 500    GLU A 236   CG  -  CD  -  OE1 ANGL. DEV. =  13.6 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       11.12   -141.21
REMARK 500    ARG A  27       50.44   -140.72
REMARK 500    ALA A  65     -173.73   -172.45
REMARK 500    PHE A 176       73.96   -151.94
REMARK 500    PRO A 202        4.90    -59.76
REMARK 500    ASN A 244       50.70    -94.96
REMARK 500    ASN A 253      -32.36     88.22
REMARK 500    ARG A 254      158.21    -43.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A  58         0.26    SIDE_CHAIN
REMARK 500    ARG A  89         0.14    SIDE_CHAIN
REMARK 500    ARG A 254         0.10    SIDE_CHAIN
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 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A 119   ND1  96.1
REMARK 620 3 HIS A  94   NE2 116.3 112.1
REMARK 620 4 HOH A 357   O   111.8 116.0 105.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              HG A 263  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 205   O
REMARK 620 2 CYS A 206   SG   88.2
REMARK 620 3 GLN A 137   O    89.1  90.6
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 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 263
DBREF  1HEA A    2   261  UNP    P00918   CAH2_HUMAN       1    259
SEQADV 1HEA ARG A  198  UNP  P00918    LEU   196 CONFLICT
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 ARG 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 262       1
HET     HG  A 263       1
HETNAM      ZN ZINC ION
HETNAM      HG MERCURY (II) ION
FORMUL   2   ZN    ZN 2+
FORMUL   3   HG    HG 2+
FORMUL   4  HOH   *110(H2 O)
HELIX    1   A PRO A   13  LYS A   18  5                                   6
HELIX    2   B PRO A   21  LYS A   24  5                                   4
HELIX    3   C THR A  125  TYR A  128  5                                   3
HELIX    4   D PHE A  131  ALA A  134  1                                   4
HELIX    5   E PRO A  155  ILE A  167  5158-163 RIGHT HANDED ALPHA        13
HELIX    6   F PRO A  181  LEU A  184  5                                   4
HELIX    7   G SER A  220  PHE A  226  1                                   7
SHEET    1   S10 SER A 173  ASP A 175  0
SHEET    2   S10 SER A  56  ASN A  61 -1  O  ILE A  59   N  ALA A 174
SHEET    3   S10 PHE A  66  PHE A  70 -1  O  ASN A  67   N  LEU A  60
SHEET    4   S10 TYR A  88  TRP A  97 -1  O  PHE A  93   N  VAL A  68
SHEET    5   S10 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94
SHEET    6   S10 LEU A 141  VAL A 150 -1  O  LEU A 144   N  LEU A 120
SHEET    7   S10 VAL A 207  LEU A 212  1  O  ILE A 210   N  GLY A 145
SHEET    8   S10 TYR A 191  GLY A 196 -1  O  TRP A 192   N  VAL A 211
SHEET    9   S10 LYS A 257  ALA A 258 -1  O  LYS A 257   N  THR A 193
SHEET   10   S10 LYS A  39  TYR A  40  1  O  LYS A  39   N  ALA A 258
LINK        ZN    ZN A 262                 NE2 HIS A  96     1555   1555  2.10
LINK        ZN    ZN A 262                 ND1 HIS A 119     1555   1555  1.93
LINK        ZN    ZN A 262                 NE2 HIS A  94     1555   1555  2.14
LINK        ZN    ZN A 262                 O   HOH A 357     1555   1555  2.22
LINK        HG    HG A 263                 O   GLU A 205     1555   1555  3.51
LINK        HG    HG A 263                 SG  CYS A 206     1555   1555  2.05
LINK        HG    HG A 263                 O   GLN A 137     1555   1555  2.89
CISPEP   1 SER A   29    PRO A   30          0        18.17
CISPEP   2 PRO A  201    PRO A  202          0       -12.28
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  HOH A 357
SITE     1 AC2  3 GLN A 137  GLU A 205  CYS A 206
CRYST1   42.700   41.700   73.000  90.00 104.60  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      0.023419  0.000000  0.006100        0.00000
SCALE2      0.000000  0.023981  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014156        0.00000
      
PROCHECK
Go to PROCHECK summary
 References