spacer
spacer

PDBsum entry 1elz

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1elz
Jmol
Contents
Protein chains
449 a.a. *
Ligands
PO4 ×2
Metals
_ZN ×4
_MG ×2
Waters ×676
* Residue conservation analysis
HEADER    HYDROLASE                               10-FEB-98   1ELZ
TITLE     E. COLI ALKALINE PHOSPHATASE MUTANT (S102G)
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;
COMPND   7 OTHER_DETAILS: ENZYME INHIBITED WITH PHOSPHATE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 STRAIN: SM547;
SOURCE   5 GENE: PHOA;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PEK307
KEYWDS    ALKALINE PHOSPHATASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.STEC,M.HEHIR,C.BRENNAN,M.NOLTE,E.R.KANTROWITZ
REVDAT   3   16-NOV-11 1ELZ    1       VERSN  HETATM
REVDAT   2   24-FEB-09 1ELZ    1       VERSN
REVDAT   1   27-MAY-98 1ELZ    0
JRNL        AUTH   B.STEC,M.J.HEHIR,C.BRENNAN,M.NOLTE,E.R.KANTROWITZ
JRNL        TITL   KINETIC AND X-RAY STRUCTURAL STUDIES OF THREE MUTANT E. COLI
JRNL        TITL 2 ALKALINE PHOSPHATASES: INSIGHTS INTO THE CATALYTIC MECHANISM
JRNL        TITL 3 WITHOUT THE NUCLEOPHILE SER102.
JRNL        REF    J.MOL.BIOL.                   V. 277   647 1998
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9533886
JRNL        DOI    10.1006/JMBI.1998.1635
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.    2.80 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) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.00
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)   (%) : 84.0
REMARK   3   NUMBER OF REFLECTIONS             : 22562
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) : 0.138
REMARK   3   FREE R VALUE                     : 0.173
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4
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) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.85
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 761
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2051
REMARK   3   BIN FREE R VALUE                    : 0.2285
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 4
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            : 6604
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 16
REMARK   3   SOLVENT ATOMS            : 676
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.92
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) : 0.20
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 9.00
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) : 0.015
REMARK   3   BOND ANGLES            (DEGREES) : 1.80
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.60
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ALL ATOMS
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; 2.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 3.500
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 3.500
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 3.500
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 1ELZ 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        : JUL-96
REMARK 200  TEMPERATURE           (KELVIN) : 292
REMARK 200  PH                             : 7.5
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          : RIGAKU RUH2R
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-NICOLET X100
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XDS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26363
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.13000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.37200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1ALK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 MG/ML PROTEIN IN 39% SATURATING
REMARK 280  (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2 100 MM ZNCL2, 2 MM NAH2PO4 AT
REMARK 280  PH 7.5, EQUILIBRATED AGAINST 55% SATURATING (NH4)2SO4
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 -0.499787 -0.866394  0.000000        0.00000
REMARK 290   SMTRY2   2  0.865657 -0.500213  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500213  0.866394  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.865657 -0.499787  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       69.29500
REMARK 290   SMTRY1   5  0.499787  0.866394  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.865657  0.500213  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       69.29500
REMARK 290   SMTRY1   6  0.500213 -0.866394  0.000000        0.00000
REMARK 290   SMTRY2   6  0.865657  0.499787  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       69.29500
REMARK 290   SMTRY1   7 -0.499787  0.866640  0.000000        0.00000
REMARK 290   SMTRY2   7  0.865657  0.499787  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  1.000000 -0.000491  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 -0.500213 -0.866148  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.865657  0.500213  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  10  0.499787 -0.866640  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.865657 -0.499787  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       69.29500
REMARK 290   SMTRY1  11 -1.000000  0.000491  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       69.29500
REMARK 290   SMTRY1  12  0.500213  0.866148  0.000000        0.00000
REMARK 290   SMTRY2  12  0.865657 -0.500213  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       69.29500
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: 8840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -220.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 720  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 658  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 487  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 583  LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH B   483     O    HOH B   483     7556     0.32
REMARK 500   O    HOH B   523     O    HOH B   523     7556     0.47
REMARK 500   O    HOH A   647     O    HOH A   647    12555     0.81
REMARK 500   O    HOH A   705     O    HOH A   705    12555     0.82
REMARK 500   O    HOH B   482     OH   TYR B    64     7556     1.85
REMARK 500   O    HOH A   516     OE1  GLU A   406     2655     1.97
REMARK 500   O    HOH B   476     O    HOH B   774    10665     1.98
REMARK 500   O    GLU A    66     O    HOH A   486    12555     2.01
REMARK 500   O    HOH B   466     OG   SER A   295     3665     2.06
REMARK 500   CB   SER A   295     O    HOH B   485    12555     2.16
REMARK 500   O    ASP A   294     O    HOH B   484    12555     2.17
REMARK 500   O    HOH B   500     OE1  GLU A   308    12555     2.17
REMARK 500   O    HOH A   517     O    HOH B   664     2655     2.18
REMARK 500   O    HOH B   500     NZ   LYS A   305    12555     2.18
REMARK 500   O    HOH A   746     O    HOH A   543    12555     2.18
REMARK 500   O    HOH B   790     O    HOH B   503    10665     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    SER A 295   CB    SER A 295   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 323   N   -  CA  -  C   ANGL. DEV. = -15.4 DEGREES
REMARK 500    LEU B  48   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES
REMARK 500    GLY B  50   N   -  CA  -  C   ANGL. DEV. = -15.6 DEGREES
REMARK 500    LEU B 390   CA  -  CB  -  CG  ANGL. DEV. =  14.2 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   2       29.13    -78.33
REMARK 500    GLU A   8      -70.27    -64.43
REMARK 500    ALA A  88     -166.20   -101.57
REMARK 500    LYS A  92      -74.76    -68.67
REMARK 500    GLU A 126       14.25     87.62
REMARK 500    TYR A 169      -72.77    -60.24
REMARK 500    THR A 367     -167.84   -168.19
REMARK 500    ASN A 428        2.13    -66.59
REMARK 500    PRO B   2       26.51    -77.55
REMARK 500    PHE B  71      118.55   -172.15
REMARK 500    ALA B  88     -169.95   -101.74
REMARK 500    LYS B  92      -71.00    -67.20
REMARK 500    GLU B 126       13.87     88.57
REMARK 500    TYR B 169      -76.38    -55.85
REMARK 500    SER B 311        2.01    -66.30
REMARK 500    THR B 367     -166.51   -162.13
REMARK 500    ASN B 428        7.01    -69.99
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 497        DISTANCE =  7.99 ANGSTROMS
REMARK 525    HOH A 529        DISTANCE =  5.88 ANGSTROMS
REMARK 525    HOH A 540        DISTANCE =  7.65 ANGSTROMS
REMARK 525    HOH A 570        DISTANCE =  6.07 ANGSTROMS
REMARK 525    HOH A 647        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH B 462        DISTANCE =  5.92 ANGSTROMS
REMARK 525    HOH B 463        DISTANCE =  6.62 ANGSTROMS
REMARK 525    HOH B 628        DISTANCE =  6.39 ANGSTROMS
REMARK 525    HOH B 630        DISTANCE =  5.92 ANGSTROMS
REMARK 525    HOH B 665        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH B 673        DISTANCE =  7.64 ANGSTROMS
REMARK 525    HOH B 675        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH B 789        DISTANCE =  5.38 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                              ZN A 450  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 327   OD2
REMARK 620 2 HIS A 331   NE2 105.4
REMARK 620 3 HIS A 412   NE2  96.0  98.5
REMARK 620 4 PO4 A 453   O1  117.9 111.7 124.2
REMARK 620 5 ASP A 327   OD1  52.3  90.5 148.2  79.1
REMARK 620 6 PO4 A 453   O2   77.8 166.2  94.5  56.2  80.9
REMARK 620 N                    1     2     3     4     5
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 ASP A  51   OD1
REMARK 620 2 ASP A 369   OD2 113.0
REMARK 620 3 HIS A 370   NE2 120.5  99.6
REMARK 620 4 PO4 A 453   O2   89.6 146.6  88.4
REMARK 620 N                    1     2     3
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 ASP A  51   OD2
REMARK 620 2 THR A 155   OG1  85.8
REMARK 620 3 GLU A 322   OE2  87.5 100.3
REMARK 620 4 HOH A 454   O    96.2  96.4 163.1
REMARK 620 5 HOH A 455   O   164.6 109.6  88.5  83.7
REMARK 620 6 HOH A 456   O    81.5 160.4  94.0  70.4  84.0
REMARK 620 N                    1     2     3     4     5
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 100.7
REMARK 620 3 HIS B 412   NE2  94.7  96.7
REMARK 620 4 PO4 B 453   O1  125.5 110.5 123.3
REMARK 620 5 ASP B 327   OD1  54.0  85.0 148.2  84.9
REMARK 620 6 PO4 B 453   O2   82.7 170.8  91.4  61.1  90.3
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  98.8
REMARK 620 3 HIS B 370   NE2 123.8  98.4
REMARK 620 4 PO4 B 453   O2  101.6 145.8  92.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 452  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  51   OD2
REMARK 620 2 THR B 155   OG1  96.4
REMARK 620 3 GLU B 322   OE2  83.7  99.4
REMARK 620 4 HOH B 454   O    97.6 102.2 158.0
REMARK 620 5 HOH B 455   O   157.1 104.4  83.7  87.2
REMARK 620 6 HOH B 456   O    74.6 170.6  77.1  82.0  84.0
REMARK 620 N                    1     2     3     4     5
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 MG B 452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 453
DBREF  1ELZ A    1   449  UNP    P00634   PPB_ECOLI       23    471
DBREF  1ELZ B    1   449  UNP    P00634   PPB_ECOLI       23    471
SEQADV 1ELZ GLY A  102  UNP  P00634    SER   124 ENGINEERED
SEQADV 1ELZ GLY B  102  UNP  P00634    SER   124 ENGINEERED
SEQRES   1 A  449  THR PRO GLU MET PRO VAL LEU GLU ASN ARG ALA ALA GLN
SEQRES   2 A  449  GLY ASP ILE THR ALA PRO GLY GLY ALA ARG ARG LEU THR
SEQRES   3 A  449  GLY ASP GLN THR ALA ALA LEU ARG ASP 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 GLY 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 GLU 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 GLN ALA GLN 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 ASP 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 ASP ILE THR ALA PRO GLY GLY ALA ARG ARG LEU THR
SEQRES   3 B  449  GLY ASP GLN THR ALA ALA LEU ARG ASP 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 GLY 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 GLU 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 GLN ALA GLN 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 ASP 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       5
HET     ZN  B 450       1
HET     ZN  B 451       1
HET     MG  B 452       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    2(MG 2+)
FORMUL   6  PO4    2(O4 P 3-)
FORMUL  11  HOH   *676(H2 O)
HELIX    1   1 THR A   30  SER A   36  1                                   7
HELIX    2   2 ASP A   55  ALA A   65  1                                  11
HELIX    3   3 GLY A  102  THR A  111  1                                  10
HELIX    4   4 ILE A  132  ALA A  139  1                                   8
HELIX    5   5 ALA A  154  LEU A  159  1                                   6
HELIX    6   6 PRO A  171  LYS A  177  1                                   7
HELIX    7   7 LEU A  183  LYS A  185  5                                   3
HELIX    8   8 ILE A  191  ALA A  198  1                                   8
HELIX    9   9 THR A  210  ALA A  212  5                                   3
HELIX   10  10 LEU A  225  ARG A  232  1                                   8
HELIX   11  11 ALA A  240  SER A  245  1                                   6
HELIX   12  12 GLY A  277  ASP A  280  1                                   4
HELIX   13  13 LEU A  299  LYS A  312  1                                  14
HELIX   14  14 SER A  325  HIS A  331  1                                   7
HELIX   15  15 PRO A  335  GLU A  359  1                                  25
HELIX   16  16 ALA A  426  VAL A  429  5                                   4
HELIX   17  17 GLN A  435  LEU A  446  1                                  12
HELIX   18  18 THR B   30  ARG B   34  1                                   5
HELIX   19  19 ASP B   55  ALA B   65  1                                  11
HELIX   20  20 GLY B  102  THR B  111  1                                  10
HELIX   21  21 ILE B  132  ALA B  139  1                                   8
HELIX   22  22 ALA B  154  LEU B  159  1                                   6
HELIX   23  23 PRO B  171  LYS B  177  1                                   7
HELIX   24  24 LEU B  183  LYS B  185  5                                   3
HELIX   25  25 ILE B  191  ALA B  198  1                                   8
HELIX   26  26 ALA B  208  ALA B  212  5                                   5
HELIX   27  27 LEU B  225  ARG B  232  1                                   8
HELIX   28  28 ALA B  240  SER B  245  1                                   6
HELIX   29  29 GLY B  277  ASP B  280  1                                   4
HELIX   30  30 LEU B  299  LYS B  312  1                                  14
HELIX   31  31 SER B  325  HIS B  331  1                                   7
HELIX   32  32 PRO B  335  GLU B  359  1                                  25
HELIX   33  33 ALA B  426  VAL B  429  5                                   4
HELIX   34  34 GLN B  435  LEU B  446  1                                  12
SHEET    1   A10 GLY A 431  ASP A 434  0
SHEET    2   A10 LEU A  80  THR A  85  1  N  GLN A  83   O  GLY A 431
SHEET    3   A10 LEU A 417  TYR A 422 -1  N  ALA A 421   O  LEU A  80
SHEET    4   A10 THR A 362  THR A 367 -1  N  VAL A 366   O  ALA A 420
SHEET    5   A10 ASN A  44  GLY A  50  1  N  ASN A  44   O  LEU A 363
SHEET    6   A10 PHE A 317  GLY A 323  1  N  PHE A 317   O  ILE A  45
SHEET    7   A10 ALA A 142  SER A 147  1  N  ALA A 142   O  PHE A 318
SHEET    8   A10 VAL A 202  GLY A 205  1  N  VAL A 202   O  ASN A 145
SHEET    9   A10 LEU A 255  LEU A 258  1  N  LEU A 255   O  THR A 203
SHEET   10   A10 GLN A 235  VAL A 237  1  N  GLN A 235   O  LEU A 256
SHEET    1   B 3 GLN A 375  VAL A 377  0
SHEET    2   B 3 VAL A 397  TYR A 402 -1  N  SER A 401   O  GLN A 375
SHEET    3   B 3 LEU A 386  ASN A 391 -1  N  LEU A 390   O  MET A 398
SHEET    1   C10 GLY B 431  ASP B 434  0
SHEET    2   C10 LEU B  80  THR B  85  1  N  GLN B  83   O  GLY B 431
SHEET    3   C10 LEU B 417  TYR B 422 -1  N  ALA B 421   O  LEU B  80
SHEET    4   C10 THR B 362  THR B 367 -1  N  VAL B 366   O  ALA B 420
SHEET    5   C10 ASN B  44  GLY B  50  1  N  ASN B  44   O  LEU B 363
SHEET    6   C10 PHE B 317  GLY B 323  1  N  PHE B 317   O  ILE B  45
SHEET    7   C10 ALA B 142  SER B 147  1  N  ALA B 142   O  PHE B 318
SHEET    8   C10 VAL B 202  GLY B 205  1  N  VAL B 202   O  ASN B 145
SHEET    9   C10 LEU B 255  LEU B 258  1  N  LEU B 255   O  THR B 203
SHEET   10   C10 GLN B 235  VAL B 237  1  N  GLN B 235   O  LEU B 256
SHEET    1   D 3 GLN B 375  VAL B 377  0
SHEET    2   D 3 VAL B 397  TYR B 402 -1  N  SER B 401   O  GLN B 375
SHEET    3   D 3 LEU B 386  ASN B 391 -1  N  LEU B 390   O  MET B 398
SSBOND   1 CYS A  168    CYS A  178                          1555   1555  2.02
SSBOND   2 CYS A  286    CYS A  336                          1555   1555  2.03
SSBOND   3 CYS B  168    CYS B  178                          1555   1555  2.03
SSBOND   4 CYS B  286    CYS B  336                          1555   1555  2.00
LINK        ZN    ZN A 450                 OD2 ASP A 327     1555   1555  2.25
LINK        ZN    ZN A 450                 NE2 HIS A 331     1555   1555  1.78
LINK        ZN    ZN A 450                 NE2 HIS A 412     1555   1555  1.88
LINK        ZN    ZN A 450                 O1  PO4 A 453     1555   1555  2.72
LINK        ZN    ZN A 451                 OD1 ASP A  51     1555   1555  1.92
LINK        ZN    ZN A 451                 OD2 ASP A 369     1555   1555  1.96
LINK        ZN    ZN A 451                 NE2 HIS A 370     1555   1555  2.15
LINK        ZN    ZN A 451                 O2  PO4 A 453     1555   1555  2.27
LINK        MG    MG A 452                 OD2 ASP A  51     1555   1555  2.16
LINK        MG    MG A 452                 OG1 THR A 155     1555   1555  1.93
LINK        MG    MG A 452                 OE2 GLU A 322     1555   1555  1.92
LINK        MG    MG A 452                 O   HOH A 454     1555   1555  2.13
LINK        MG    MG A 452                 O   HOH A 455     1555   1555  2.08
LINK        MG    MG A 452                 O   HOH A 456     1555   1555  2.22
LINK        ZN    ZN B 450                 OD2 ASP B 327     1555   1555  2.25
LINK        ZN    ZN B 450                 NE2 HIS B 331     1555   1555  1.86
LINK        ZN    ZN B 450                 NE2 HIS B 412     1555   1555  1.96
LINK        ZN    ZN B 450                 O1  PO4 B 453     1555   1555  2.49
LINK        ZN    ZN B 451                 OD1 ASP B  51     1555   1555  1.83
LINK        ZN    ZN B 451                 OD2 ASP B 369     1555   1555  1.96
LINK        ZN    ZN B 451                 NE2 HIS B 370     1555   1555  1.99
LINK        ZN    ZN B 451                 O2  PO4 B 453     1555   1555  2.16
LINK        MG    MG B 452                 OD2 ASP B  51     1555   1555  2.10
LINK        MG    MG B 452                 OG1 THR B 155     1555   1555  1.78
LINK        MG    MG B 452                 OE2 GLU B 322     1555   1555  2.23
LINK        MG    MG B 452                 O   HOH B 454     1555   1555  1.92
LINK        MG    MG B 452                 O   HOH B 455     1555   1555  2.00
LINK        MG    MG B 452                 O   HOH B 456     1555   1555  2.15
LINK        ZN    ZN A 450                 OD1 ASP A 327     1555   1555  2.62
LINK        ZN    ZN A 450                 O2  PO4 A 453     1555   1555  2.58
LINK        ZN    ZN B 450                 OD1 ASP B 327     1555   1555  2.55
LINK        ZN    ZN B 450                 O2  PO4 B 453     1555   1555  2.50
SITE     1 AC1  4 ASP A 327  HIS A 331  HIS A 412  PO4 A 453
SITE     1 AC2  4 ASP A  51  ASP A 369  HIS A 370  PO4 A 453
SITE     1 AC3  6 ASP A  51  THR A 155  GLU A 322  HOH A 454
SITE     2 AC3  6 HOH A 455  HOH A 456
SITE     1 AC4 13 ASP A  51  ASP A 101  GLY A 102  ARG A 166
SITE     2 AC4 13 ASP A 327  HIS A 370  HIS A 412   ZN A 450
SITE     3 AC4 13  ZN A 451  HOH A 454  HOH A 724  HOH A 755
SITE     4 AC4 13 HOH A 780
SITE     1 AC5  4 ASP B 327  HIS B 331  HIS B 412  PO4 B 453
SITE     1 AC6  4 ASP B  51  ASP B 369  HIS B 370  PO4 B 453
SITE     1 AC7  6 ASP B  51  THR B 155  GLU B 322  HOH B 454
SITE     2 AC7  6 HOH B 455  HOH B 456
SITE     1 AC8 13 ASP B  51  ASP B 101  GLY B 102  ARG B 166
SITE     2 AC8 13 ASP B 327  HIS B 331  HIS B 370  HIS B 412
SITE     3 AC8 13  ZN B 450   ZN B 451  HOH B 454  HOH B 613
SITE     4 AC8 13 HOH B 647
CRYST1  164.570  164.500  138.590  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      0.006076  0.003508  0.000000        0.00000
SCALE2      0.000000  0.007019  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007216        0.00000
MTRIX1   1  0.005904  0.999966 -0.005775        0.14810    1
MTRIX2   1  0.999964 -0.005939 -0.006044        0.45330    1
MTRIX3   1 -0.006078 -0.005739 -0.999965      104.51500    1
      
PROCHECK
Go to PROCHECK summary
 References