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PDBsum entry 4km4

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4km4
Jmol
Contents
Protein chains
445 a.a.
Ligands
PO4 ×2
Metals
_ZN ×6
HEADER    HYDROLASE                               08-MAY-13   4KM4
TITLE     E. COLI ALKALINE PHOSPHATASE MUTANT S102G/R166S IN COMPLEX WITH
TITLE    2 INORGANIC PHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALKALINE PHOSPHATASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: APASE;
COMPND   5 EC: 3.1.3.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 83333;
SOURCE   4 STRAIN: K12;
SOURCE   5 GENE: PHOA, B0383, JW0374;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    PHOSPHATE MONOESTER HYDROLASE, PERIPLASMIC, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.D.ANDREWS,T.D.FENN,D.HERSCHLAG
REVDAT   1   24-JUL-13 4KM4    0
JRNL        AUTH   L.D.ANDREWS,T.D.FENN,D.HERSCHLAG
JRNL        TITL   GROUND STATE DESTABILIZATION BY ANIONIC NUCLEOPHILES
JRNL        TITL 2 CONTRIBUTES TO THE ACTIVITY OF PHOSPHORYL TRANSFER ENZYMES.
JRNL        REF    PLOS BIOL.                    V.  11 01599 2013
JRNL        REFN                   ISSN 1544-9173
JRNL        PMID   23843744
JRNL        DOI    10.1371/JOURNAL.PBIO.1001599
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : FFX
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 26488
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.232
REMARK   3   FREE R VALUE                     : 0.296
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1335
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           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 6530
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 16
REMARK   3   SOLVENT ATOMS            : 0
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 4KM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079510.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26488
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 20.400
REMARK 200  R MERGE                    (I) : 0.33700
REMARK 200  R SYM                      (I) : 0.41000
REMARK 200   FOR THE DATA SET  : 13.8000
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) : 2.91
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1ALK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL PARTS 23.5 MG/ML ENZYME IN 10 MM
REMARK 280  NAMOPS AND 50 MM NACL AND 0.2 M NH4F, 17-21% PEG 3350, AND 500 UM
REMARK 280  ZNCL2, PH 8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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       69.77450
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       69.77450
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       69.77450
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       69.77450
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       69.77450
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       69.77450
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: 26680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -284.0 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 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   HZ1  LYS A    91     OE2  GLU A   126              1.59
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    ARG A  62   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG A  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    TYR A  84   CA  -  CB  -  CG  ANGL. DEV. =  12.6 DEGREES
REMARK 500    TYR A  84   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    TYR A  84   CB  -  CG  -  CD1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG A 267   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 292   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 292   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 418   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG B  34   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG B  62   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG B  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    TYR B  84   CA  -  CB  -  CG  ANGL. DEV. =  13.1 DEGREES
REMARK 500    TYR B  84   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    TYR B  84   CB  -  CG  -  CD1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG B 232   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG B 292   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG B 292   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG B 418   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG B 418   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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    ASP A 153      150.50    -45.12
REMARK 500    HIS A 372     -160.12   -128.51
REMARK 500    ASP A 408       38.49    -76.15
REMARK 500    ASN A 428        3.82    -65.14
REMARK 500    ASP B 153      154.19    -46.70
REMARK 500    ASN B 250     -175.79   -173.99
REMARK 500    HIS B 372     -156.59   -126.75
REMARK 500    ASN B 428        2.20    -67.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A  23         0.08    SIDE CHAIN
REMARK 500    TYR A  64         0.10    SIDE CHAIN
REMARK 500    TYR B  64         0.08    SIDE CHAIN
REMARK 500    HIS B 370         0.09    SIDE CHAIN
REMARK 500    ARG B 418         0.09    SIDE CHAIN
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    ARG A 267        23.7      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 502  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  51   OD1
REMARK 620 2 ASP B 369   OD2  99.4
REMARK 620 3 HIS B 370   NE2 115.1  96.3
REMARK 620 4 PO4 B 501   O2  120.4 125.4  98.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 502  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  51   OD1
REMARK 620 2 ASP A 369   OD2  97.5
REMARK 620 3 HIS A 370   NE2 112.6  98.1
REMARK 620 4 PO4 A 501   O2  119.9 124.3 102.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 504  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 322   OE2
REMARK 620 2 ASP B  51   OD2  90.2
REMARK 620 3 ASP B 153   OD2 111.6 156.6
REMARK 620 4 THR B 155   OG1  84.9  90.9  99.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 503  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 327   OD1
REMARK 620 2 HIS B 331   NE2 107.0
REMARK 620 3 HIS B 412   NE2 102.3 102.9
REMARK 620 4 PO4 B 501   O1  119.0 106.6 117.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 504  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 322   OE2
REMARK 620 2 ASP A  51   OD2  89.0
REMARK 620 3 ASP A 153   OD2 113.7 152.5
REMARK 620 4 THR A 155   OG1  85.5  97.9  99.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 503  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 327   OD1
REMARK 620 2 HIS A 331   NE2 105.3
REMARK 620 3 HIS A 412   NE2  98.1 100.7
REMARK 620 4 PO4 A 501   O1  118.5 114.5 117.0
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 PO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 504
DBREF  4KM4 A    4   448  UNP    P00634   PPB_ECOLI       26    470
DBREF  4KM4 B    4   448  UNP    P00634   PPB_ECOLI       26    470
SEQADV 4KM4 GLY A  102  UNP  P00634    SER   124 ENGINEERED MUTATION
SEQADV 4KM4 SER A  166  UNP  P00634    ARG   188 ENGINEERED MUTATION
SEQADV 4KM4 GLY B  102  UNP  P00634    SER   124 ENGINEERED MUTATION
SEQADV 4KM4 SER B  166  UNP  P00634    ARG   188 ENGINEERED MUTATION
SEQRES   1 A  445  MET PRO VAL LEU GLU ASN ARG ALA ALA GLN GLY ASP ILE
SEQRES   2 A  445  THR ALA PRO GLY GLY ALA ARG ARG LEU THR GLY ASP GLN
SEQRES   3 A  445  THR ALA ALA LEU ARG ASP SER LEU SER ASP LYS PRO ALA
SEQRES   4 A  445  LYS ASN ILE ILE LEU LEU ILE GLY ASP GLY MET GLY ASP
SEQRES   5 A  445  SER GLU ILE THR ALA ALA ARG ASN TYR ALA GLU GLY ALA
SEQRES   6 A  445  GLY GLY PHE PHE LYS GLY ILE ASP ALA LEU PRO LEU THR
SEQRES   7 A  445  GLY GLN TYR THR HIS TYR ALA LEU ASN LYS LYS THR GLY
SEQRES   8 A  445  LYS PRO ASP TYR VAL THR ASP GLY ALA ALA SER ALA THR
SEQRES   9 A  445  ALA TRP SER THR GLY VAL LYS THR TYR ASN GLY ALA LEU
SEQRES  10 A  445  GLY VAL ASP ILE HIS GLU LYS ASP HIS PRO THR ILE LEU
SEQRES  11 A  445  GLU MET ALA LYS ALA ALA GLY LEU ALA THR GLY ASN VAL
SEQRES  12 A  445  SER THR ALA GLU LEU GLN ASP ALA THR PRO ALA ALA LEU
SEQRES  13 A  445  VAL ALA HIS VAL THR SER SER LYS CYS TYR GLY PRO SER
SEQRES  14 A  445  ALA THR SER GLU LYS CYS PRO GLY ASN ALA LEU GLU LYS
SEQRES  15 A  445  GLY GLY LYS GLY SER ILE THR GLU GLN LEU LEU ASN ALA
SEQRES  16 A  445  ARG ALA ASP VAL THR LEU GLY GLY GLY ALA LYS THR PHE
SEQRES  17 A  445  ALA GLU THR ALA THR ALA GLY GLU TRP GLN GLY LYS THR
SEQRES  18 A  445  LEU ARG GLU GLN ALA GLN ALA ARG GLY TYR GLN LEU VAL
SEQRES  19 A  445  SER ASP ALA ALA SER LEU ASN SER VAL THR GLU ALA ASN
SEQRES  20 A  445  GLN GLN LYS PRO LEU LEU GLY LEU PHE ALA ASP GLY ASN
SEQRES  21 A  445  MET PRO VAL ARG TRP LEU GLY PRO LYS ALA THR TYR HIS
SEQRES  22 A  445  GLY ASN ILE ASP LYS PRO ALA VAL THR CYS THR PRO ASN
SEQRES  23 A  445  PRO GLN ARG ASN ASP SER VAL PRO THR LEU ALA GLN MET
SEQRES  24 A  445  THR ASP LYS ALA ILE GLU LEU LEU SER LYS ASN GLU LYS
SEQRES  25 A  445  GLY PHE PHE LEU GLN VAL GLU GLY ALA SER ILE ASP LYS
SEQRES  26 A  445  GLN ASP HIS ALA ALA ASN PRO CYS GLY GLN ILE GLY GLU
SEQRES  27 A  445  THR VAL ASP LEU ASP GLU ALA VAL GLN ARG ALA LEU GLU
SEQRES  28 A  445  PHE ALA LYS LYS GLU GLY ASN THR LEU VAL ILE VAL THR
SEQRES  29 A  445  ALA ASP HIS ALA HIS ALA SER GLN ILE VAL ALA PRO ASP
SEQRES  30 A  445  THR LYS ALA PRO GLY LEU THR GLN ALA LEU ASN THR LYS
SEQRES  31 A  445  ASP GLY ALA VAL MET VAL MET SER TYR GLY ASN SER GLU
SEQRES  32 A  445  GLU ASP SER GLN GLU HIS THR GLY SER GLN LEU ARG ILE
SEQRES  33 A  445  ALA ALA TYR GLY PRO HIS ALA ALA ASN VAL VAL GLY LEU
SEQRES  34 A  445  THR ASP GLN THR ASP LEU PHE TYR THR MET LYS ALA ALA
SEQRES  35 A  445  LEU GLY LEU
SEQRES   1 B  445  MET PRO VAL LEU GLU ASN ARG ALA ALA GLN GLY ASP ILE
SEQRES   2 B  445  THR ALA PRO GLY GLY ALA ARG ARG LEU THR GLY ASP GLN
SEQRES   3 B  445  THR ALA ALA LEU ARG ASP SER LEU SER ASP LYS PRO ALA
SEQRES   4 B  445  LYS ASN ILE ILE LEU LEU ILE GLY ASP GLY MET GLY ASP
SEQRES   5 B  445  SER GLU ILE THR ALA ALA ARG ASN TYR ALA GLU GLY ALA
SEQRES   6 B  445  GLY GLY PHE PHE LYS GLY ILE ASP ALA LEU PRO LEU THR
SEQRES   7 B  445  GLY GLN TYR THR HIS TYR ALA LEU ASN LYS LYS THR GLY
SEQRES   8 B  445  LYS PRO ASP TYR VAL THR ASP GLY ALA ALA SER ALA THR
SEQRES   9 B  445  ALA TRP SER THR GLY VAL LYS THR TYR ASN GLY ALA LEU
SEQRES  10 B  445  GLY VAL ASP ILE HIS GLU LYS ASP HIS PRO THR ILE LEU
SEQRES  11 B  445  GLU MET ALA LYS ALA ALA GLY LEU ALA THR GLY ASN VAL
SEQRES  12 B  445  SER THR ALA GLU LEU GLN ASP ALA THR PRO ALA ALA LEU
SEQRES  13 B  445  VAL ALA HIS VAL THR SER SER LYS CYS TYR GLY PRO SER
SEQRES  14 B  445  ALA THR SER GLU LYS CYS PRO GLY ASN ALA LEU GLU LYS
SEQRES  15 B  445  GLY GLY LYS GLY SER ILE THR GLU GLN LEU LEU ASN ALA
SEQRES  16 B  445  ARG ALA ASP VAL THR LEU GLY GLY GLY ALA LYS THR PHE
SEQRES  17 B  445  ALA GLU THR ALA THR ALA GLY GLU TRP GLN GLY LYS THR
SEQRES  18 B  445  LEU ARG GLU GLN ALA GLN ALA ARG GLY TYR GLN LEU VAL
SEQRES  19 B  445  SER ASP ALA ALA SER LEU ASN SER VAL THR GLU ALA ASN
SEQRES  20 B  445  GLN GLN LYS PRO LEU LEU GLY LEU PHE ALA ASP GLY ASN
SEQRES  21 B  445  MET PRO VAL ARG TRP LEU GLY PRO LYS ALA THR TYR HIS
SEQRES  22 B  445  GLY ASN ILE ASP LYS PRO ALA VAL THR CYS THR PRO ASN
SEQRES  23 B  445  PRO GLN ARG ASN ASP SER VAL PRO THR LEU ALA GLN MET
SEQRES  24 B  445  THR ASP LYS ALA ILE GLU LEU LEU SER LYS ASN GLU LYS
SEQRES  25 B  445  GLY PHE PHE LEU GLN VAL GLU GLY ALA SER ILE ASP LYS
SEQRES  26 B  445  GLN ASP HIS ALA ALA ASN PRO CYS GLY GLN ILE GLY GLU
SEQRES  27 B  445  THR VAL ASP LEU ASP GLU ALA VAL GLN ARG ALA LEU GLU
SEQRES  28 B  445  PHE ALA LYS LYS GLU GLY ASN THR LEU VAL ILE VAL THR
SEQRES  29 B  445  ALA ASP HIS ALA HIS ALA SER GLN ILE VAL ALA PRO ASP
SEQRES  30 B  445  THR LYS ALA PRO GLY LEU THR GLN ALA LEU ASN THR LYS
SEQRES  31 B  445  ASP GLY ALA VAL MET VAL MET SER TYR GLY ASN SER GLU
SEQRES  32 B  445  GLU ASP SER GLN GLU HIS THR GLY SER GLN LEU ARG ILE
SEQRES  33 B  445  ALA ALA TYR GLY PRO HIS ALA ALA ASN VAL VAL GLY LEU
SEQRES  34 B  445  THR ASP GLN THR ASP LEU PHE TYR THR MET LYS ALA ALA
SEQRES  35 B  445  LEU GLY LEU
HET    PO4  A 501       5
HET     ZN  A 502       1
HET     ZN  A 503       1
HET     ZN  A 504       1
HET    PO4  B 501       5
HET     ZN  B 502       1
HET     ZN  B 503       1
HET     ZN  B 504       1
HETNAM     PO4 PHOSPHATE ION
HETNAM      ZN ZINC ION
FORMUL   3  PO4    2(O4 P 3-)
FORMUL   4   ZN    6(ZN 2+)
HELIX    1   1 GLN A   29  ASP A   35  1                                   7
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  ALA A  139  1                                   9
HELIX    5   5 ASP A  153  ALA A  158  1                                   6
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 GLY A  207  GLU A  213  5                                   7
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 THR A  298  SER A  311  1                                  14
HELIX   13  13 ALA A  324  ALA A  333  1                                  10
HELIX   14  14 ASN A  334  GLY A  360  1                                  27
HELIX   15  15 HIS A  425  VAL A  430  5                                   6
HELIX   16  16 GLN A  435  GLY A  447  1                                  13
HELIX   17  17 GLN B   29  ASP B   35  1                                   7
HELIX   18  18 GLY B   54  GLU B   66  1                                  13
HELIX   19  19 ASP B  101  GLY B  112  1                                  12
HELIX   20  20 THR B  131  ALA B  139  1                                   9
HELIX   21  21 ASP B  153  ALA B  158  1                                   6
HELIX   22  22 GLY B  170  CYS B  178  1                                   9
HELIX   23  23 ALA B  182  GLY B  186  5                                   5
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  430  5                                   6
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  ASN A 145   O  VAL A 202
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  ALA A 368  1  O  ILE A 365   N  LEU A  48
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  THR A 433   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 3 GLN A 375  VAL A 377  0
SHEET    2   D 3 VAL A 397  TYR A 402 -1  O  SER A 401   N  GLN A 375
SHEET    3   D 3 LEU A 386  ASN A 391 -1  N  LEU A 386   O  TYR A 402
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  GLY B 205   O  GLY B 257
SHEET    4   E10 ALA B 142  GLU B 150  1  N  SER B 147   O  LEU B 204
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  ALA B 368  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  LEU B  80   O  ALA B 421
SHEET   10   E10 GLY B 431  ASP B 434  1  O  THR B 433   N  GLN B  83
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  TYR B 402   N  LEU B 386
SHEET    4   H 4 GLN B 375  VAL B 377 -1  N  GLN B 375   O  SER B 401
SSBOND   1 CYS A  168    CYS A  178                          1555   1555  2.04
SSBOND   2 CYS A  286    CYS A  336                          1555   1555  2.05
SSBOND   3 CYS B  168    CYS B  178                          1555   1555  2.05
SSBOND   4 CYS B  286    CYS B  336                          1555   1555  2.03
LINK         OD1 ASP B  51                ZN    ZN B 502     1555   1555  1.85
LINK         OD1 ASP A  51                ZN    ZN A 502     1555   1555  1.86
LINK         OE2 GLU B 322                ZN    ZN B 504     1555   1555  1.90
LINK         OD1 ASP B 327                ZN    ZN B 503     1555   1555  1.90
LINK         OE2 GLU A 322                ZN    ZN A 504     1555   1555  1.90
LINK         OD2 ASP B 369                ZN    ZN B 502     1555   1555  1.91
LINK         OD2 ASP B  51                ZN    ZN B 504     1555   1555  1.91
LINK         OD2 ASP A  51                ZN    ZN A 504     1555   1555  1.92
LINK         OD2 ASP A 369                ZN    ZN A 502     1555   1555  1.93
LINK         OD1 ASP A 327                ZN    ZN A 503     1555   1555  1.93
LINK         NE2 HIS B 331                ZN    ZN B 503     1555   1555  1.94
LINK         OD2 ASP B 153                ZN    ZN B 504     1555   1555  1.94
LINK         NE2 HIS B 412                ZN    ZN B 503     1555   1555  1.97
LINK         NE2 HIS A 331                ZN    ZN A 503     1555   1555  1.97
LINK         NE2 HIS A 412                ZN    ZN A 503     1555   1555  1.97
LINK         OD2 ASP A 153                ZN    ZN A 504     1555   1555  1.99
LINK         OG1 THR A 155                ZN    ZN A 504     1555   1555  1.99
LINK         NE2 HIS A 370                ZN    ZN A 502     1555   1555  2.00
LINK         OG1 THR B 155                ZN    ZN B 504     1555   1555  2.04
LINK         NE2 HIS B 370                ZN    ZN B 502     1555   1555  2.05
LINK         O2  PO4 A 501                ZN    ZN A 502     1555   1555  2.08
LINK         O2  PO4 B 501                ZN    ZN B 502     1555   1555  2.12
LINK         O1  PO4 A 501                ZN    ZN A 503     1555   1555  2.24
LINK         O1  PO4 B 501                ZN    ZN B 503     1555   1555  2.29
SITE     1 AC1 12 ASP A  51  GLY A 102  ASP A 153  ASP A 327
SITE     2 AC1 12 LYS A 328  HIS A 331  ASP A 369  HIS A 370
SITE     3 AC1 12 HIS A 412   ZN A 502   ZN A 503   ZN A 504
SITE     1 AC2  5 ASP A  51  ASP A 327  ASP A 369  HIS A 370
SITE     2 AC2  5 PO4 A 501
SITE     1 AC3  4 ASP A 327  HIS A 331  HIS A 412  PO4 A 501
SITE     1 AC4  5 ASP A  51  ASP A 153  THR A 155  GLU A 322
SITE     2 AC4  5 PO4 A 501
SITE     1 AC5 11 ASP B  51  GLY B 102  ASP B 153  ASP B 327
SITE     2 AC5 11 LYS B 328  HIS B 331  ASP B 369  HIS B 370
SITE     3 AC5 11 HIS B 412   ZN B 502   ZN B 503
SITE     1 AC6  5 ASP B  51  ASP B 327  ASP B 369  HIS B 370
SITE     2 AC6  5 PO4 B 501
SITE     1 AC7  4 ASP B 327  HIS B 331  HIS B 412  PO4 B 501
SITE     1 AC8  4 ASP B  51  ASP B 153  THR B 155  GLU B 322
CRYST1  160.935  160.935  139.549  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      0.006214  0.003587  0.000000        0.00000
SCALE2      0.000000  0.007175  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007166        0.00000
      
PROCHECK
Go to PROCHECK summary
 References