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PDBsum entry 1kh9

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1kh9
Jmol
Contents
Protein chains
444 a.a. *
Ligands
PO4 ×2
Metals
_ZN ×4
_MG
Waters ×147
* Residue conservation analysis
HEADER    HYDROLASE                               29-NOV-01   1KH9
TITLE     E. COLI ALKALINE PHOSPHATASE MUTANT (D153GD330N) COMPLEX WITH
TITLE    2 PHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALKALINE PHOSPHATASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.1.3.1;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 STRAIN: WCC118;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PLIP4.0D153HD330N
KEYWDS    ALKALINE PHOSPHATASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.H.LE DU,C.LAMOURE,B.H.MULLER,O.V.BULGAKOV,E.LAJEUNESSE
REVDAT   6   25-JUN-14 1KH9    1       JRNL   REMARK
REVDAT   5   27-JUL-11 1KH9    1       ATOM   HETNAM REMARK REVDAT
REVDAT   4   13-JUL-11 1KH9    1       VERSN
REVDAT   3   24-FEB-09 1KH9    1       VERSN
REVDAT   2   01-APR-03 1KH9    1       JRNL
REVDAT   1   13-MAR-02 1KH9    0
JRNL        AUTH   M.H.LE DU,C.LAMOURE,B.H.MULLER,O.V.BULGAKOV,E.LAJEUNESSE,
JRNL        AUTH 2 A.MENEZ,J.C.BOULAIN
JRNL        TITL   ARTIFICIAL EVOLUTION OF AN ENZYME ACTIVE SITE: STRUCTURAL
JRNL        TITL 2 STUDIES OF THREE HIGHLY ACTIVE MUTANTS OF ESCHERICHIA COLI
JRNL        TITL 3 ALKALINE PHOSPHATASE.
JRNL        REF    J.MOL.BIOL.                   V. 316   941 2002
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   11884134
JRNL        DOI    10.1006/JMBI.2001.5384
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   E.E.KIM,H.W.WYCKOFF
REMARK   1  TITL   REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED ON CRYSTAL
REMARK   1  TITL 2 STRUCTURES. TWO-METAL ION CATALYSIS
REMARK   1  REF    J.MOL.BIOL.                   V. 218   449 1991
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
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)   (%) : 83.4
REMARK   3   NUMBER OF REFLECTIONS             : 32077
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : IMPLOR-CYCLING TEST SETS
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.196
REMARK   3   FREE R VALUE                     : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1600
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           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.64
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3510
REMARK   3   BIN FREE R VALUE                    : 0.3830
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1600
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            : 6504
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 14
REMARK   3   SOLVENT ATOMS            : 147
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  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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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 1KH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-01.
REMARK 100 THE RCSB ID CODE IS RCSB014958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : JUL-96
REMARK 200  TEMPERATURE           (KELVIN) : 292
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : LURE BEAMLINE DW32
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
REMARK 200  MONOCHROMATOR                  : MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : SDMS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200  DATA SCALING SOFTWARE          : SDMS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32077
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.11800
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.69800
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: 1KH7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MAGNESIUM CHLORIDE,
REMARK 280  ZINC SULFATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/2
REMARK 290       6555   X-Y,X,Z+1/2
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z
REMARK 290      10555   -Y,-X,-Z+1/2
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+1/2
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       69.43900
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       69.43900
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       69.43900
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       69.43900
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       69.43900
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       69.43900
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.0 KCAL/MOL
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     THR A     1
REMARK 465     PRO A     2
REMARK 465     GLU A     3
REMARK 465     MET A     4
REMARK 465     PRO A     5
REMARK 465     THR B     1
REMARK 465     PRO B     2
REMARK 465     GLU B     3
REMARK 465     MET B     4
REMARK 465     PRO 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     VAL A   6    CG1  CG2
REMARK 470     GLU A   8    CG   CD   OE1  OE2
REMARK 470     ASP A 153    CB   CG   OD1  OD2
REMARK 470     LYS A 449    CG   CD   CE   NZ
REMARK 470     VAL B   6    CG1  CG2
REMARK 470     GLU B   8    CG   CD   OE1  OE2
REMARK 470     ASP B 153    CB   CG   OD1  OD2
REMARK 470     LYS B 449    CG   CD   CE   NZ
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   OG   SER B   102     P    PO4 B   453              2.03
REMARK 500   CE1  HIS A   412     O1   PO4 A   453              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    SER A 102   CA    SER A 102   C       0.183
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    LEU A  48   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    GLU A   8       14.59    -67.18
REMARK 500    PHE A  71      117.20   -176.59
REMARK 500    ALA A  88     -168.31   -104.27
REMARK 500    ALA A 241      -74.48    -48.50
REMARK 500    SER A 374      131.54    -36.62
REMARK 500    HIS B  86       28.61   -148.86
REMARK 500    ALA B 149     -169.36   -115.20
REMARK 500    LYS B 177      -30.51   -133.18
REMARK 500    SER B 311       11.27    -64.25
REMARK 500    THR B 367     -162.82   -162.73
REMARK 500    HIS B 372     -158.05   -131.85
REMARK 500    LYS B 382       76.07   -103.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    SER A 325        24.8      L          L   OUTSIDE RANGE
REMARK 500    SER B 325        24.6      L          L   OUTSIDE RANGE
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 B1070        DISTANCE =  5.12 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     PO4 A  453
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 450  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 327   OD2
REMARK 620 2 HIS A 331   NE2  99.2
REMARK 620 3 HIS A 412   NE2 141.9  94.3
REMARK 620 4 PO4 A 453   O1  120.4 133.6  69.9
REMARK 620 5 ASP A 327   OD1  53.0 109.1  88.9 113.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 451  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 370   NE2
REMARK 620 2 ASP A 369   OD1 108.3
REMARK 620 3 ASP A  51   OD2 129.1  81.4
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 452  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 322   OE2
REMARK 620 2 ASP A  51   OD1  75.6
REMARK 620 3 THR A 155   OG1  79.7  89.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 450  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 327   OD2
REMARK 620 2 HIS B 331   NE2 100.8
REMARK 620 3 HIS B 412   NE2 151.6  88.5
REMARK 620 4 PO4 B 453   O1  101.1 109.0 101.0
REMARK 620 5 PO4 B 453   O2   80.8 166.7  96.2  57.9
REMARK 620 6 ASP B 327   OD1  54.3  98.2  98.1 146.9  93.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 451  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  51   OD1
REMARK 620 2 ASP B 369   OD2  73.8
REMARK 620 3 HIS B 370   NE2 131.5 123.2
REMARK 620 4 PO4 B 453   O2   86.1 150.6  86.1
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 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 453
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I23   RELATED DB: PDB
REMARK 900 THIS ENTRY REPLACES 1I23
REMARK 900 RELATED ID: 1ALK   RELATED DB: PDB
REMARK 900 RELATED ID: 1KH7   RELATED DB: PDB
DBREF  1KH9 A    1   449  UNP    P00634   PPB_ECOLI       23    471
DBREF  1KH9 B    1   449  UNP    P00634   PPB_ECOLI       23    471
SEQADV 1KH9 ASN A   15  UNP  P00634    ASP    37 CONFLICT
SEQADV 1KH9 ASN A   35  UNP  P00634    ASP    57 CONFLICT
SEQADV 1KH9 GLN A  176  UNP  P00634    GLU   198 CONFLICT
SEQADV 1KH9 GLU A  228  UNP  P00634    GLN   250 CONFLICT
SEQADV 1KH9 GLU A  230  UNP  P00634    GLN   252 CONFLICT
SEQADV 1KH9 ASN A  330  UNP  P00634    ASP   352 ENGINEERED
SEQADV 1KH9 ASN B   15  UNP  P00634    ASP    37 CONFLICT
SEQADV 1KH9 ASN B   35  UNP  P00634    ASP    57 CONFLICT
SEQADV 1KH9 GLN B  176  UNP  P00634    GLU   198 CONFLICT
SEQADV 1KH9 GLU B  228  UNP  P00634    GLN   250 CONFLICT
SEQADV 1KH9 GLU B  230  UNP  P00634    GLN   252 CONFLICT
SEQADV 1KH9 ASN B  330  UNP  P00634    ASP   352 ENGINEERED
SEQRES   1 A  449  THR PRO GLU MET PRO VAL LEU GLU ASN ARG ALA ALA GLN
SEQRES   2 A  449  GLY ASN ILE THR ALA PRO GLY GLY ALA ARG ARG LEU THR
SEQRES   3 A  449  GLY ASP GLN THR ALA ALA LEU ARG ASN SER LEU SER ASP
SEQRES   4 A  449  LYS PRO ALA LYS ASN ILE ILE LEU LEU ILE GLY ASP GLY
SEQRES   5 A  449  MET GLY ASP SER GLU ILE THR ALA ALA ARG ASN TYR ALA
SEQRES   6 A  449  GLU GLY ALA GLY GLY PHE PHE LYS GLY ILE ASP ALA LEU
SEQRES   7 A  449  PRO LEU THR GLY GLN TYR THR HIS TYR ALA LEU ASN LYS
SEQRES   8 A  449  LYS THR GLY LYS PRO ASP TYR VAL THR ASP SER ALA ALA
SEQRES   9 A  449  SER ALA THR ALA TRP SER THR GLY VAL LYS THR TYR ASN
SEQRES  10 A  449  GLY ALA LEU GLY VAL ASP ILE HIS GLU LYS ASP HIS PRO
SEQRES  11 A  449  THR ILE LEU GLU MET ALA LYS ALA ALA GLY LEU ALA THR
SEQRES  12 A  449  GLY ASN VAL SER THR ALA GLU LEU GLN ASP ALA THR PRO
SEQRES  13 A  449  ALA ALA LEU VAL ALA HIS VAL THR SER ARG LYS CYS TYR
SEQRES  14 A  449  GLY PRO SER ALA THR SER GLN LYS CYS PRO GLY ASN ALA
SEQRES  15 A  449  LEU GLU LYS GLY GLY LYS GLY SER ILE THR GLU GLN LEU
SEQRES  16 A  449  LEU ASN ALA ARG ALA ASP VAL THR LEU GLY GLY GLY ALA
SEQRES  17 A  449  LYS THR PHE ALA GLU THR ALA THR ALA GLY GLU TRP GLN
SEQRES  18 A  449  GLY LYS THR LEU ARG GLU GLU ALA GLU ALA ARG GLY TYR
SEQRES  19 A  449  GLN LEU VAL SER ASP ALA ALA SER LEU ASN SER VAL THR
SEQRES  20 A  449  GLU ALA ASN GLN GLN LYS PRO LEU LEU GLY LEU PHE ALA
SEQRES  21 A  449  ASP GLY ASN MET PRO VAL ARG TRP LEU GLY PRO LYS ALA
SEQRES  22 A  449  THR TYR HIS GLY ASN ILE ASP LYS PRO ALA VAL THR CYS
SEQRES  23 A  449  THR PRO ASN PRO GLN ARG ASN ASP SER VAL PRO THR LEU
SEQRES  24 A  449  ALA GLN MET THR ASP LYS ALA ILE GLU LEU LEU SER LYS
SEQRES  25 A  449  ASN GLU LYS GLY PHE PHE LEU GLN VAL GLU GLY ALA SER
SEQRES  26 A  449  ILE ASP LYS GLN ASN HIS ALA ALA ASN PRO CYS GLY GLN
SEQRES  27 A  449  ILE GLY GLU THR VAL ASP LEU ASP GLU ALA VAL GLN ARG
SEQRES  28 A  449  ALA LEU GLU PHE ALA LYS LYS GLU GLY ASN THR LEU VAL
SEQRES  29 A  449  ILE VAL THR ALA ASP HIS ALA HIS ALA SER GLN ILE VAL
SEQRES  30 A  449  ALA PRO ASP THR LYS ALA PRO GLY LEU THR GLN ALA LEU
SEQRES  31 A  449  ASN THR LYS ASP GLY ALA VAL MET VAL MET SER TYR GLY
SEQRES  32 A  449  ASN SER GLU GLU ASP SER GLN GLU HIS THR GLY SER GLN
SEQRES  33 A  449  LEU ARG ILE ALA ALA TYR GLY PRO HIS ALA ALA ASN VAL
SEQRES  34 A  449  VAL GLY LEU THR ASP GLN THR ASP LEU PHE TYR THR MET
SEQRES  35 A  449  LYS ALA ALA LEU GLY LEU LYS
SEQRES   1 B  449  THR PRO GLU MET PRO VAL LEU GLU ASN ARG ALA ALA GLN
SEQRES   2 B  449  GLY ASN ILE THR ALA PRO GLY GLY ALA ARG ARG LEU THR
SEQRES   3 B  449  GLY ASP GLN THR ALA ALA LEU ARG ASN SER LEU SER ASP
SEQRES   4 B  449  LYS PRO ALA LYS ASN ILE ILE LEU LEU ILE GLY ASP GLY
SEQRES   5 B  449  MET GLY ASP SER GLU ILE THR ALA ALA ARG ASN TYR ALA
SEQRES   6 B  449  GLU GLY ALA GLY GLY PHE PHE LYS GLY ILE ASP ALA LEU
SEQRES   7 B  449  PRO LEU THR GLY GLN TYR THR HIS TYR ALA LEU ASN LYS
SEQRES   8 B  449  LYS THR GLY LYS PRO ASP TYR VAL THR ASP SER ALA ALA
SEQRES   9 B  449  SER ALA THR ALA TRP SER THR GLY VAL LYS THR TYR ASN
SEQRES  10 B  449  GLY ALA LEU GLY VAL ASP ILE HIS GLU LYS ASP HIS PRO
SEQRES  11 B  449  THR ILE LEU GLU MET ALA LYS ALA ALA GLY LEU ALA THR
SEQRES  12 B  449  GLY ASN VAL SER THR ALA GLU LEU GLN ASP ALA THR PRO
SEQRES  13 B  449  ALA ALA LEU VAL ALA HIS VAL THR SER ARG LYS CYS TYR
SEQRES  14 B  449  GLY PRO SER ALA THR SER GLN LYS CYS PRO GLY ASN ALA
SEQRES  15 B  449  LEU GLU LYS GLY GLY LYS GLY SER ILE THR GLU GLN LEU
SEQRES  16 B  449  LEU ASN ALA ARG ALA ASP VAL THR LEU GLY GLY GLY ALA
SEQRES  17 B  449  LYS THR PHE ALA GLU THR ALA THR ALA GLY GLU TRP GLN
SEQRES  18 B  449  GLY LYS THR LEU ARG GLU GLU ALA GLU ALA ARG GLY TYR
SEQRES  19 B  449  GLN LEU VAL SER ASP ALA ALA SER LEU ASN SER VAL THR
SEQRES  20 B  449  GLU ALA ASN GLN GLN LYS PRO LEU LEU GLY LEU PHE ALA
SEQRES  21 B  449  ASP GLY ASN MET PRO VAL ARG TRP LEU GLY PRO LYS ALA
SEQRES  22 B  449  THR TYR HIS GLY ASN ILE ASP LYS PRO ALA VAL THR CYS
SEQRES  23 B  449  THR PRO ASN PRO GLN ARG ASN ASP SER VAL PRO THR LEU
SEQRES  24 B  449  ALA GLN MET THR ASP LYS ALA ILE GLU LEU LEU SER LYS
SEQRES  25 B  449  ASN GLU LYS GLY PHE PHE LEU GLN VAL GLU GLY ALA SER
SEQRES  26 B  449  ILE ASP LYS GLN ASN HIS ALA ALA ASN PRO CYS GLY GLN
SEQRES  27 B  449  ILE GLY GLU THR VAL ASP LEU ASP GLU ALA VAL GLN ARG
SEQRES  28 B  449  ALA LEU GLU PHE ALA LYS LYS GLU GLY ASN THR LEU VAL
SEQRES  29 B  449  ILE VAL THR ALA ASP HIS ALA HIS ALA SER GLN ILE VAL
SEQRES  30 B  449  ALA PRO ASP THR LYS ALA PRO GLY LEU THR GLN ALA LEU
SEQRES  31 B  449  ASN THR LYS ASP GLY ALA VAL MET VAL MET SER TYR GLY
SEQRES  32 B  449  ASN SER GLU GLU ASP SER GLN GLU HIS THR GLY SER GLN
SEQRES  33 B  449  LEU ARG ILE ALA ALA TYR GLY PRO HIS ALA ALA ASN VAL
SEQRES  34 B  449  VAL GLY LEU THR ASP GLN THR ASP LEU PHE TYR THR MET
SEQRES  35 B  449  LYS ALA ALA LEU GLY LEU LYS
HET     ZN  A 450       1
HET     ZN  A 451       1
HET     MG  A 452       1
HET    PO4  A 453       4
HET     ZN  B 450       1
HET     ZN  B 451       1
HET    PO4  B 453       5
HETNAM      ZN ZINC ION
HETNAM      MG MAGNESIUM ION
HETNAM     PO4 PHOSPHATE ION
FORMUL   3   ZN    4(ZN 2+)
FORMUL   5   MG    MG 2+
FORMUL   6  PO4    2(O4 P 3-)
FORMUL  10  HOH   *147(H2 O)
HELIX    1   1 ASP A   28  ASN A   35  1                                   8
HELIX    2   2 GLY A   54  GLU A   66  1                                  13
HELIX    3   3 ASP A  101  GLY A  112  1                                  12
HELIX    4   4 THR A  131  GLY A  140  1                                  10
HELIX    5   5 ASP A  153  ALA A  161  1                                   9
HELIX    6   6 GLY A  170  CYS A  178  1                                   9
HELIX    7   7 ALA A  182  GLY A  186  5                                   5
HELIX    8   8 SER A  190  ARG A  199  1                                  10
HELIX    9   9 ALA A  208  GLU A  213  5                                   6
HELIX   10  10 THR A  224  ARG A  232  1                                   9
HELIX   11  11 ASP A  239  VAL A  246  1                                   8
HELIX   12  12 HIS A  276  LYS A  281  1                                   6
HELIX   13  13 THR A  298  SER A  311  1                                  14
HELIX   14  14 ALA A  324  ALA A  332  1                                   9
HELIX   15  15 ASN A  334  GLY A  360  1                                  27
HELIX   16  16 HIS A  425  VAL A  430  5                                   6
HELIX   17  17 GLN A  435  GLY A  447  1                                  13
HELIX   18  18 ASP B   28  ASN B   35  1                                   8
HELIX   19  19 GLY B   54  GLU B   66  1                                  13
HELIX   20  20 ASP B  101  GLY B  112  1                                  12
HELIX   21  21 THR B  131  ALA B  139  1                                   9
HELIX   22  22 ASP B  153  ALA B  158  1                                   6
HELIX   23  23 GLY B  170  CYS B  178  1                                   9
HELIX   24  24 SER B  190  ARG B  199  1                                  10
HELIX   25  25 GLY B  207  GLU B  213  5                                   7
HELIX   26  26 THR B  224  ARG B  232  1                                   9
HELIX   27  27 ASP B  239  VAL B  246  1                                   8
HELIX   28  28 HIS B  276  LYS B  281  1                                   6
HELIX   29  29 THR B  298  SER B  311  1                                  14
HELIX   30  30 ALA B  324  ALA B  332  1                                   9
HELIX   31  31 ASN B  334  GLY B  360  1                                  27
HELIX   32  32 HIS B  425  VAL B  429  5                                   5
HELIX   33  33 GLN B  435  GLY B  447  1                                  13
SHEET    1   A10 GLN A 235  VAL A 237  0
SHEET    2   A10 LEU A 255  LEU A 258  1  O  LEU A 256   N  GLN A 235
SHEET    3   A10 VAL A 202  GLY A 206  1  N  THR A 203   O  GLY A 257
SHEET    4   A10 ALA A 142  GLU A 150  1  N  ALA A 149   O  GLY A 206
SHEET    5   A10 PHE A 317  GLY A 323  1  O  GLN A 320   N  VAL A 146
SHEET    6   A10 ASN A  44  GLY A  50  1  N  ILE A  49   O  VAL A 321
SHEET    7   A10 THR A 362  THR A 367  1  O  THR A 367   N  GLY A  50
SHEET    8   A10 LEU A 417  TYR A 422 -1  O  TYR A 422   N  VAL A 364
SHEET    9   A10 LEU A  80  THR A  85 -1  N  LEU A  80   O  ALA A 421
SHEET   10   A10 GLY A 431  ASP A 434  1  O  GLY A 431   N  GLN A  83
SHEET    1   B 2 ALA A  88  LEU A  89  0
SHEET    2   B 2 PRO A  96  ASP A  97 -1  O  ASP A  97   N  ALA A  88
SHEET    1   C 2 TRP A 268  LEU A 269  0
SHEET    2   C 2 THR A 287  PRO A 288 -1  O  THR A 287   N  LEU A 269
SHEET    1   D 4 THR A 274  TYR A 275  0
SHEET    2   D 4 LEU A 386  ASN A 391 -1  O  THR A 387   N  THR A 274
SHEET    3   D 4 VAL A 397  TYR A 402 -1  O  MET A 398   N  LEU A 390
SHEET    4   D 4 GLN A 375  VAL A 377 -1  N  GLN A 375   O  SER A 401
SHEET    1   E10 GLN B 235  VAL B 237  0
SHEET    2   E10 LEU B 255  LEU B 258  1  O  LEU B 256   N  GLN B 235
SHEET    3   E10 VAL B 202  GLY B 206  1  N  THR B 203   O  GLY B 257
SHEET    4   E10 ALA B 142  GLU B 150  1  N  ALA B 149   O  GLY B 206
SHEET    5   E10 PHE B 317  GLY B 323  1  O  GLN B 320   N  VAL B 146
SHEET    6   E10 ASN B  44  GLY B  50  1  N  ILE B  49   O  VAL B 321
SHEET    7   E10 THR B 362  THR B 367  1  O  ILE B 365   N  LEU B  48
SHEET    8   E10 LEU B 417  TYR B 422 -1  O  ALA B 420   N  VAL B 366
SHEET    9   E10 LEU B  80  THR B  85 -1  N  TYR B  84   O  LEU B 417
SHEET   10   E10 GLY B 431  ASP B 434  1  O  THR B 433   N  THR B  85
SHEET    1   F 2 ALA B  88  LEU B  89  0
SHEET    2   F 2 PRO B  96  ASP B  97 -1  O  ASP B  97   N  ALA B  88
SHEET    1   G 2 TRP B 268  LEU B 269  0
SHEET    2   G 2 THR B 287  PRO B 288 -1  O  THR B 287   N  LEU B 269
SHEET    1   H 4 THR B 274  TYR B 275  0
SHEET    2   H 4 LEU B 386  ASN B 391 -1  O  THR B 387   N  THR B 274
SHEET    3   H 4 VAL B 397  TYR B 402 -1  O  MET B 398   N  LEU B 390
SHEET    4   H 4 SER B 374  VAL B 377 -1  N  GLN B 375   O  SER B 401
SSBOND   1 CYS A  168    CYS A  178                          1555   1555  2.03
SSBOND   2 CYS A  286    CYS A  336                          1555   1555  2.03
SSBOND   3 CYS B  168    CYS B  178                          1555   1555  2.02
SSBOND   4 CYS B  286    CYS B  336                          1555   1555  2.03
LINK        ZN    ZN A 450                 OD2 ASP A 327     1555   1555  2.31
LINK        ZN    ZN A 450                 NE2 HIS A 331     1555   1555  2.07
LINK        ZN    ZN A 450                 NE2 HIS A 412     1555   1555  2.00
LINK        ZN    ZN A 450                 O1  PO4 A 453     1555   1555  1.89
LINK        ZN    ZN A 451                 NE2 HIS A 370     1555   1555  2.09
LINK        MG    MG A 452                 OE2 GLU A 322     1555   1555  2.04
LINK        ZN    ZN B 450                 OD2 ASP B 327     1555   1555  2.40
LINK        ZN    ZN B 450                 NE2 HIS B 331     1555   1555  1.92
LINK        ZN    ZN B 450                 NE2 HIS B 412     1555   1555  2.04
LINK        ZN    ZN B 450                 O1  PO4 B 453     1555   1555  2.49
LINK        ZN    ZN B 451                 OD1 ASP B  51     1555   1555  2.72
LINK        ZN    ZN B 451                 OD2 ASP B 369     1555   1555  2.23
LINK        ZN    ZN B 451                 NE2 HIS B 370     1555   1555  2.11
LINK        ZN    ZN B 451                 O2  PO4 B 453     1555   1555  2.83
LINK        ZN    ZN B 450                 O2  PO4 B 453     1555   1555  1.88
LINK         OD1 ASP A  51                MG    MG A 452     1555   1555  2.16
LINK         OD1 ASP A 369                ZN    ZN A 451     1555   1555  2.32
LINK         OG1 THR A 155                MG    MG A 452     1555   1555  2.34
LINK         OD1 ASP B 327                ZN    ZN B 450     1555   1555  2.47
LINK         OD2 ASP A  51                ZN    ZN A 451     1555   1555  2.49
LINK         OD1 ASP A 327                ZN    ZN A 450     1555   1555  2.57
LINK         OG  SER A 102                 P   PO4 A 453     1555   1555  1.60
SITE     1 AC1  4 ASP A 327  HIS A 331  HIS A 412  PO4 A 453
SITE     1 AC2  5 ASP A  51  SER A 102  ASP A 327  ASP A 369
SITE     2 AC2  5 HIS A 370
SITE     1 AC3  3 ASP A  51  THR A 155  GLU A 322
SITE     1 AC4  6 SER A 102  ARG A 166  ASP A 327  HIS A 331
SITE     2 AC4  6 HIS A 412   ZN A 450
SITE     1 AC5  4 ASP B 327  HIS B 331  HIS B 412  PO4 B 453
SITE     1 AC6  5 ASP B  51  SER B 102  ASP B 369  HIS B 370
SITE     2 AC6  5 PO4 B 453
SITE     1 AC7  9 SER B 102  ARG B 166  ASP B 327  HIS B 331
SITE     2 AC7  9 HIS B 370  HIS B 412   ZN B 450   ZN B 451
SITE     3 AC7  9 HOH B1125
CRYST1  164.010  164.010  138.878  90.00  90.00 120.00 P 63 2 2     24
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      0.006097  0.003520  0.000000        0.00000
SCALE2      0.000000  0.007040  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007201        0.00000
MTRIX1   1  0.007130  0.999974 -0.001354       -0.11190    1
MTRIX2   1  0.999974 -0.007132 -0.001395        0.26200    1
MTRIX3   1 -0.001404 -0.001344 -0.999998      104.46890    1
      
PROCHECK
Go to PROCHECK summary
 References