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PDBsum entry 3ca2

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Top Page protein ligands metals links
Lyase(oxo-acid) PDB id
3ca2
Jmol
Contents
Protein chain
256 a.a.
Ligands
AMS
Metals
_HG ×2
_ZN
Waters ×160
HEADER    LYASE(OXO-ACID)                         02-OCT-89   3CA2
TITLE     CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN
TITLE    2 HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF
TITLE    3 THE SCN-ION TO THE ZINC AT HIGH P*H
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    A.E.ERIKSSON,T.A.JONES,A.LILJAS
REVDAT   4   24-FEB-09 3CA2    1       VERSN
REVDAT   3   01-APR-03 3CA2    1       JRNL
REVDAT   2   15-APR-90 3CA2    3       COMPND REMARK HET    FORMUL
REVDAT   2 2                   3       HETATM CONECT
REVDAT   1   15-JAN-90 3CA2    0
JRNL        AUTH   A.E.ERIKSSON,P.M.KYLSTEN,T.A.JONES,A.LILJAS
JRNL        TITL   CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING
JRNL        TITL 2 SITES IN HUMAN CARBONIC ANHYDRASE II: A
JRNL        TITL 3 PENTACOORDINATED BINDING OF THE SCN- ION TO THE
JRNL        TITL 4 ZINC AT HIGH PH.
JRNL        REF    PROTEINS                      V.   4   283 1988
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   3151020
JRNL        DOI    10.1002/PROT.340040407
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   A.E.ERIKSSON,T.A.JONES,A.LILJAS
REMARK   1  TITL   REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II
REMARK   1  TITL 2 AT 2.0 ANGSTROMS RESOLUTION
REMARK   1  REF    PROTEINS                      V.   4   274 1988
REMARK   1  REFN                   ISSN 0887-3585
REMARK   1 REFERENCE 2
REMARK   1  AUTH   B.NOTSTRAND,I.VAARA,K.K.KANNAN
REMARK   1  TITL   STRUCTURAL RELATIONSHIP OF HUMAN ERYTHROCYTE
REMARK   1  TITL 2 CARBONIC ANHYDRASE ISOZYMES B AND C
REMARK   1  EDIT   C.L.MARKERT
REMARK   1  REF    ISOZYMES-MOLECULAR STRUCTURE  V.   1   575 1975
REMARK   1  PUBL   ACADEMIC PRESS,NEW YORK
REMARK   1  REFN
REMARK   1 REFERENCE 3
REMARK   1  AUTH   K.K.KANNAN,A.LILJAS,I.WAARA,P.-C.BERGSTEN,
REMARK   1  AUTH 2 S.LOVGREN,B.STRANDBERG,U.BENGTSSON,U.CARLBOM,
REMARK   1  AUTH 3 K.FRIDBORG,L.JARUP,M.PETEF
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CARBONIC
REMARK   1  TITL 2 ANHYDRASE C. VI. THE THREE-DIMENSIONAL STRUCTURE
REMARK   1  TITL 3 AT HIGH RESOLUTION IN RELATION TO OTHER MAMMALIAN
REMARK   1  TITL 4 CARBONIC ANHYDRASES
REMARK   1  REF    COLD SPRING HARBOR            V.  36   221 1972
REMARK   1  REF  2 SYMP.QUANT.BIOL.
REMARK   1  REFN                   ISSN 0091-7451
REMARK   1 REFERENCE 4
REMARK   1  AUTH   A.LILJAS,K.K.KANNAN,P.-C.BERGSTEN,I.WAARA,
REMARK   1  AUTH 2 K.FRIDBORG,B.STRANDBERG,U.CARLBOM,L.JARUP,
REMARK   1  AUTH 3 S.LOVGREN,M.PETEF
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE C
REMARK   1  REF    NATURE NEW BIOL.              V. 235   131 1972
REMARK   1  REFN                   ISSN 0369-4887
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) : 0.192
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            : 2039
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 15
REMARK   3   SOLVENT ATOMS            : 160
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) : 0.028 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.041 ; 0.030
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.046 ; 0.040
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.014 ; 0.020
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.153 ; 0.150
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) : 0.850 ; 1.000
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.365 ; 1.500
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.001 ; 1.000
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 1.636 ; 1.500
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:  THE ELECTRON DENSITY IS WEAK FOR
REMARK   3  RESIDUES LYS 9, SER 43, LYS 159, ASN 253, AND LYS 257.
REMARK   4
REMARK   4 3CA2 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   (%): 42.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
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     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   369     O    HOH A   393              2.19
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  94   CG    HIS A  94   ND1    -0.095
REMARK 500    ARG A 246   CD    ARG A 246   NE      0.114
REMARK 500    SER A 259   CB    SER A 259   OG      0.080
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    GLY A  12   C   -  N   -  CA  ANGL. DEV. =  15.5 DEGREES
REMARK 500    GLU A  26   CG  -  CD  -  OE1 ANGL. DEV. =  13.1 DEGREES
REMARK 500    GLU A  26   CG  -  CD  -  OE2 ANGL. DEV. = -12.8 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ASP A  34   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ASP A  41   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    LEU A  44   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES
REMARK 500    TYR A  51   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES
REMARK 500    TYR A  51   CB  -  CG  -  CD1 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A  58   CD  -  NE  -  CZ  ANGL. DEV. =  12.1 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    HIS A  64   CG  -  ND1 -  CE1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASP A  71   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP A  72   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ASP A  75   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ALA A  77   CB  -  CA  -  C   ANGL. DEV. =   9.3 DEGREES
REMARK 500    ARG A  89   CD  -  NE  -  CZ  ANGL. DEV. =  -8.7 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    LEU A 100   CA  -  CB  -  CG  ANGL. DEV. =  17.3 DEGREES
REMARK 500    GLU A 106   CG  -  CD  -  OE2 ANGL. DEV. = -12.3 DEGREES
REMARK 500    ALA A 116   O   -  C   -  N   ANGL. DEV. =   9.6 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    LYS A 172   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD1 ANGL. DEV. =  13.2 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    GLU A 214   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.7 DEGREES
REMARK 500    GLU A 221   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES
REMARK 500    VAL A 223   CG1 -  CB  -  CG2 ANGL. DEV. = -11.2 DEGREES
REMARK 500    ARG A 227   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES
REMARK 500    GLU A 238   CG  -  CD  -  OE1 ANGL. DEV. =  13.0 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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    ALA A  65     -175.61   -172.90
REMARK 500    PHE A 176       68.50   -150.10
REMARK 500    ASN A 244       51.63    -94.38
REMARK 500    LYS A 252     -128.49     57.58
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 381        DISTANCE =  5.27 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                              HG A 262  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A  62   O
REMARK 620 2 HIS A  64   ND1  91.0
REMARK 620 3 HOH A 333   O   140.9  85.2
REMARK 620 N                    1     2
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 GLN A 137   O
REMARK 620 2 GLU A 205   O    96.5
REMARK 620 3 CYS A 206   SG   75.9  88.0
REMARK 620 4 HOH A 332   O   161.8  79.5  86.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 264  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 119   ND1
REMARK 620 2 HIS A  94   NE2 116.5
REMARK 620 3 AMS A 265   N1  106.6 111.6
REMARK 620 4 HIS A  96   NE2 100.6 104.1 117.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             AMS A 265  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  64   NE2
REMARK 620 2 HOH A 368   O    80.9
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 263
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 264
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMS A 265
DBREF  3CA2 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     HG  A 262       1
HET     HG  A 263       1
HET     ZN  A 264       1
HET    AMS  A 265      12
HETNAM      HG MERCURY (II) ION
HETNAM      ZN ZINC ION
HETNAM     AMS 3-MERCURI-4-AMINOBENZENESULFONAMIDE
FORMUL   2   HG    2(HG 2+)
FORMUL   4   ZN    ZN 2+
FORMUL   5  AMS    C6 H7 HG N2 O2 S
FORMUL   6  HOH   *160(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        HG    HG A 262                 O   ASN A  62     1555   1555  3.12
LINK        HG    HG A 262                 ND1 HIS A  64     1555   1555  2.23
LINK        HG    HG A 262                 O   HOH A 333     1555   1555  3.01
LINK        HG    HG A 263                 O   GLN A 137     1555   1555  3.01
LINK        HG    HG A 263                 O   GLU A 205     1555   1555  3.08
LINK        HG    HG A 263                 SG  CYS A 206     1555   1555  2.24
LINK        HG    HG A 263                 O   HOH A 332     1555   1555  3.53
LINK        ZN    ZN A 264                 ND1 HIS A 119     1555   1555  1.93
LINK        ZN    ZN A 264                 NE2 HIS A  94     1555   1555  1.98
LINK        ZN    ZN A 264                 N1  AMS A 265     1555   1555  2.02
LINK        ZN    ZN A 264                 NE2 HIS A  96     1555   1555  2.09
LINK        HG   AMS A 265                 NE2 HIS A  64     1555   1555  2.67
LINK        HG   AMS A 265                 O   HOH A 368     1555   1555  3.13
CISPEP   1 SER A   29    PRO A   30          0        -0.29
CISPEP   2 PRO A  201    PRO A  202          0         2.57
SITE     1 AC1  3 ASN A  62  HIS A  64  HOH A 333
SITE     1 AC2  3 GLN A 137  GLU A 205  CYS A 206
SITE     1 AC3  4 HIS A  94  HIS A  96  HIS A 119  AMS A 265
SITE     1 AC4 10 HIS A  64  GLN A  92  HIS A  94  HIS A  96
SITE     2 AC4 10 HIS A 119  LEU A 198  THR A 199  THR A 200
SITE     3 AC4 10  ZN A 264  HOH A 320
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
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 References