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PDBsum entry 1avn

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Lyase PDB id
1avn
Jmol
Contents
Protein chain
257 a.a.
Ligands
AZI
HSM
Metals
_ZN
_HG
Waters ×155
HEADER    LYASE                                   17-SEP-97   1AVN
TITLE     HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH THE HISTAMINE
TITLE    2 ACTIVATOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: HCA II;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 OTHER_DETAILS: COMPLEX WITH HISTAMINE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELL_LINE: BL21;
SOURCE   6 CELL: ERYTHROCYTES;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACA/HCA II
KEYWDS    LYASE, OXO-ACID
EXPDTA    X-RAY DIFFRACTION
AUTHOR    F.BRIGANTI,S.MANGANI,P.ORIOLI,A.SCOZZAFAVA,G.VERNAGLIONE,
AUTHOR   2 C.T.SUPURAN
REVDAT   2   24-FEB-09 1AVN    1       VERSN
REVDAT   1   24-DEC-97 1AVN    0
JRNL        AUTH   F.BRIGANTI,S.MANGANI,P.ORIOLI,A.SCOZZAFAVA,
JRNL        AUTH 2 G.VERNAGLIONE,C.T.SUPURAN
JRNL        TITL   CARBONIC ANHYDRASE ACTIVATORS: X-RAY
JRNL        TITL 2 CRYSTALLOGRAPHIC AND SPECTROSCOPIC INVESTIGATIONS
JRNL        TITL 3 FOR THE INTERACTION OF ISOZYMES I AND II WITH
JRNL        TITL 4 HISTAMINE.
JRNL        REF    BIOCHEMISTRY                  V.  36 10384 1997
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   9265618
JRNL        DOI    10.1021/BI970760V
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CCP4
REMARK   3   AUTHORS     : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.6
REMARK   3   NUMBER OF REFLECTIONS             : 14464
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.154
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) : 0.1540
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) : 14464
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          : 4
REMARK   3   SOLVENT ATOMS            : 177
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.90
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) : 0.15
REMARK   3   ESD FROM SIGMAA              (A) : 0.15
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 30.00
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.018 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.056 ; 0.040
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.080 ; 0.050
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) : 0.174 ; 0.150
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.177 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.183 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : 0.211 ; 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) : 6.300 ; 3.000
REMARK   3    STAGGERED                 (DEGREES) : 17.900; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : 29.500; 20.000
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 1AVN 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        : NOV-96
REMARK 200  TEMPERATURE           (KELVIN) : 293
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 M18XH
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200  DATA SCALING SOFTWARE          : XENGEN
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14777
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.900
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.0
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.07600
REMARK 200  R SYM                      (I) : 0.09000
REMARK 200   FOR THE DATA SET  : 33.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.06400
REMARK 200  R SYM FOR SHELL            (I) : 0.17400
REMARK 200   FOR SHELL         : 10.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HCA II CRYSTALLIZED FROM 2.3 M
REMARK 280  AMMONIUM SULFATE, 50MM TRIS-HCL, 3MM SODIUM AZIDE, PH 7.7
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       20.84500
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 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 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 A   4    CB   CG   ND1  CD2  CE1  NE2
REMARK 470     GLU A  14    CB   CG   CD   OE1  OE2
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   313     O    HOH A   420              1.98
REMARK 500   OE2  GLU A   239     O    HOH A   312              2.14
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    PRO A  30   CD    PRO A  30   N       0.138
REMARK 500    THR A 125   C     LYS A 127   N       0.315
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    TRP A  16   O   -  C   -  N   ANGL. DEV. =   9.9 DEGREES
REMARK 500    ASP A  19   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    GLU A  26   CB  -  CG  -  CD  ANGL. DEV. =  17.8 DEGREES
REMARK 500    GLU A  26   OE1 -  CD  -  OE2 ANGL. DEV. = -10.4 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    SER A  29   CA  -  C   -  O   ANGL. DEV. = -15.0 DEGREES
REMARK 500    PRO A  30   CA  -  N   -  CD  ANGL. DEV. = -25.7 DEGREES
REMARK 500    PRO A  30   N   -  CA  -  CB  ANGL. DEV. =  24.4 DEGREES
REMARK 500    PRO A  30   N   -  CD  -  CG  ANGL. DEV. =  15.3 DEGREES
REMARK 500    SER A  29   CA  -  C   -  N   ANGL. DEV. = -23.6 DEGREES
REMARK 500    SER A  29   O   -  C   -  N   ANGL. DEV. =  39.4 DEGREES
REMARK 500    PRO A  30   C   -  N   -  CA  ANGL. DEV. =  47.9 DEGREES
REMARK 500    PRO A  30   C   -  N   -  CD  ANGL. DEV. = -31.5 DEGREES
REMARK 500    ASP A  34   CB  -  CG  -  OD1 ANGL. DEV. =   7.8 DEGREES
REMARK 500    LYS A  39   CA  -  CB  -  CG  ANGL. DEV. =  20.9 DEGREES
REMARK 500    TYR A  40   CB  -  CG  -  CD2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ASP A  41   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    SER A  43   CA  -  CB  -  OG  ANGL. DEV. =  18.3 DEGREES
REMARK 500    ASP A  52   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG A  58   CD  -  NE  -  CZ  ANGL. DEV. =  18.6 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    PHE A  66   N   -  CA  -  CB  ANGL. DEV. =  10.8 DEGREES
REMARK 500    LYS A  76   C   -  N   -  CA  ANGL. DEV. =  16.6 DEGREES
REMARK 500    PRO A  83   N   -  CA  -  CB  ANGL. DEV. =  -7.0 DEGREES
REMARK 500    PRO A  83   O   -  C   -  N   ANGL. DEV. =  -9.6 DEGREES
REMARK 500    TYR A  88   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ASP A 101   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    LYS A 112   CB  -  CG  -  CD  ANGL. DEV. =  15.9 DEGREES
REMARK 500    TYR A 114   CB  -  CG  -  CD2 ANGL. DEV. =   3.7 DEGREES
REMARK 500    LYS A 127   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES
REMARK 500    TYR A 128   CB  -  CG  -  CD2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ASP A 130   OD1 -  CG  -  OD2 ANGL. DEV. = -18.9 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD2 ANGL. DEV. =  12.0 DEGREES
REMARK 500    ASP A 139   CB  -  CG  -  OD1 ANGL. DEV. =   8.4 DEGREES
REMARK 500    ASP A 162   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    SER A 173   N   -  CA  -  CB  ANGL. DEV. =   9.5 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD1 ANGL. DEV. =  13.1 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD2 ANGL. DEV. =  -8.4 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    GLU A 187   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES
REMARK 500    ASP A 190   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TYR A 191   CB  -  CG  -  CD2 ANGL. DEV. =   8.2 DEGREES
REMARK 500    TYR A 194   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    GLU A 221   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    PHE A 226   CB  -  CG  -  CD1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG A 227   NE  -  CZ  -  NH2 ANGL. DEV. =   6.6 DEGREES
REMARK 500    LYS A 228   CB  -  CG  -  CD  ANGL. DEV. =  20.0 DEGREES
REMARK 500    GLN A 255   CA  -  CB  -  CG  ANGL. DEV. =  20.3 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    PRO A  30      152.87    115.69
REMARK 500    LYS A 111       -0.84     80.92
REMARK 500    ASN A 244       42.50    -92.25
REMARK 500    LYS A 252     -131.18     53.20
REMARK 500    ASN A 253       46.66    -81.73
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    THR A 125        -16.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615   M RES C SSEQI
REMARK 615     HOH A  301
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  94   NE2
REMARK 620 2 HIS A  96   NE2 100.3
REMARK 620 3 HIS A 119   ND1 116.3 102.8
REMARK 620 4 AZI A 265   N2  109.6 134.3  94.1
REMARK 620 5 HOH A 407   O   104.8 137.8  95.8   4.9
REMARK 620 6 AZI A 265   N3  103.4 115.5 117.7  25.1  25.4
REMARK 620 N                    1     2     3     4     5
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 CYS A 206   SG
REMARK 620 2 GLN A 137   O    87.7
REMARK 620 3 HOH A 347   O   154.8  99.6
REMARK 620 4 HOH A 420   O   157.8  95.9  45.9
REMARK 620 5 GLU A 205   O    91.4  94.2  64.2 110.1
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 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
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 265
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HSM A 264
DBREF  1AVN 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 263       1
HET    AZI  A 265       3
HET    HSM  A 264       8
HETNAM      ZN ZINC ION
HETNAM      HG MERCURY (II) ION
HETNAM     AZI AZIDE ION
HETNAM     HSM HISTAMINE
FORMUL   2   ZN    ZN 2+
FORMUL   3   HG    HG 2+
FORMUL   4  AZI    N3 1-
FORMUL   5  HSM    C5 H9 N3
FORMUL   6  HOH   *155(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  E1 PRO A  155  LEU A  157  5                                   3
HELIX    6  E2 GLN A  158  VAL A  163  1                                   6
HELIX    7  E3 LEU A  164  ILE A  167  5                                   4
HELIX    8   F PRO A  181  LEU A  184  5                                   4
HELIX    9   G SER A  220  PHE A  226  1                                   7
SHEET    1 B1A10 LYS A  39  TYR A  40  0
SHEET    2 B1A10 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3 B1A10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4 B1A10 VAL A 207  LEU A 212 -1  N  VAL A 211   O  TRP A 192
SHEET    5 B1A10 LEU A 141  GLY A 151  1  O  VAL A 143   N  ILE A 210
SHEET    6 B1A10 ALA A 116  ASN A 124 -1  N  LEU A 120   O  LEU A 144
SHEET    7 B1A10 TYR A  88  TRP A  97 -1  O  HIS A  94   N  HIS A 119
SHEET    8 B1A10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9 B1A10 SER A  56  ASN A  61 -1  O  ARG A  58   N  GLU A  69
SHEET   10 B1A10 SER A 173  ASP A 175 -1  O  SER A 173   N  ILE A  59
SHEET    1 B1B 7 ILE A 216  SER A 219  0
SHEET    2 B1B 7 LEU A 141  GLY A 151  1  N  GLY A 151   O  VAL A 218
SHEET    3 B1B 7 ALA A 116  ASN A 124 -1  N  LEU A 120   O  LEU A 144
SHEET    4 B1B 7 TYR A  88  TRP A  97 -1  O  HIS A  94   N  HIS A 119
SHEET    5 B1B 7 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    6 B1B 7 SER A  56  ASN A  61 -1  O  ARG A  58   N  GLU A  69
SHEET    7 B1B 7 SER A 173  ASP A 175 -1  O  SER A 173   N  ILE A  59
SHEET    1  B2 2 LEU A  47  SER A  50  0
SHEET    2  B2 2 VAL A  78  GLY A  81 -1  N  LYS A  80   O  SER A  48
SHEET    1  B3 2 ASP A  32  ILE A  33  0
SHEET    2  B3 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
LINK        ZN    ZN A 262                 NE2 HIS A  94     1555   1555  2.05
LINK        ZN    ZN A 262                 NE2 HIS A  96     1555   1555  2.13
LINK        ZN    ZN A 262                 ND1 HIS A 119     1555   1555  2.00
LINK        ZN    ZN A 262                 N2  AZI A 265     1555   1555  2.70
LINK        ZN    ZN A 262                 O   HOH A 407     1555   1555  2.46
LINK        ZN    ZN A 262                 N3  AZI A 265     1555   1555  2.05
LINK        HG    HG A 263                 SG  CYS A 206     1555   1555  2.19
LINK        HG    HG A 263                 O   GLN A 137     1555   1555  3.13
LINK        HG    HG A 263                 O   HOH A 347     1555   1555  3.40
LINK        HG    HG A 263                 O   HOH A 420     1555   1555  3.14
LINK        HG    HG A 263                 O   GLU A 205     1555   1555  3.35
CISPEP   1 PRO A  201    PRO A  202          0         3.99
SITE     1  ZN  3 HIS A  94  HIS A  96  HIS A 119
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  AZI A 265
SITE     2 AC1  5 HOH A 407
SITE     1 AC2  3 GLN A 137  GLU A 205  CYS A 206
SITE     1 AC3  9 HIS A  94  HIS A  96  HIS A 119  LEU A 198
SITE     2 AC3  9 THR A 199  TRP A 209   ZN A 262  HOH A 392
SITE     3 AC3  9 HOH A 407
SITE     1 AC4  5 ASN A  62  HIS A  64  ASN A  67  GLN A  92
SITE     2 AC4  5 HOH A 396
CRYST1   42.610   41.690   72.780  90.00 104.24  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      0.023469  0.000000  0.005956        0.00000
SCALE2      0.000000  0.023987  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014176        0.00000
      
PROCHECK
Go to PROCHECK summary
 References