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PDBsum entry 1alj

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Hydrolase (phosphoric monoester) PDB id
1alj
Jmol
Contents
Protein chains
446 a.a. *
Ligands
PO4 ×2
Metals
_ZN ×2
_MG ×2
Waters ×219
* Residue conservation analysis
HEADER    HYDROLASE (PHOSPHORIC MONOESTER)        02-JUN-95   1ALJ
TITLE     ALKALINE PHOSPHATASE MUTANT (H412N)
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: EK1498;
SOURCE   5 GENE: PHOA;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PEK202;
SOURCE   9 EXPRESSION_SYSTEM_GENE: PHOA
KEYWDS    HYDROLASE (PHOSPHORIC MONOESTER), TRANSFERASE (PHOSPHO,
KEYWDS   2 ALCOHOL ACCEPTOR)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.MA,T.T.TIBBITTS,E.R.KANTROWITZ
REVDAT   2   24-FEB-09 1ALJ    1       VERSN
REVDAT   1   14-NOV-95 1ALJ    0
JRNL        AUTH   L.MA,T.T.TIBBITTS,E.R.KANTROWITZ
JRNL        TITL   ESCHERICHIA COLI ALKALINE PHOSPHATASE: X-RAY
JRNL        TITL 2 STRUCTURAL STUDIES OF A MUTANT ENZYME
JRNL        TITL 3 (HIS-412-->ASN) AT ONE OF THE CATALYTICALLY
JRNL        TITL 4 IMPORTANT ZINC BINDING SITES.
JRNL        REF    PROTEIN SCI.                  V.   4  1498 1995
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   8520475
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   E.E.KIM,H.W.WYCKOFF
REMARK   1  TITL   REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED
REMARK   1  TITL 2 ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS
REMARK   1  REF    J.MOL.BIOL.                   V. 218   449 1991
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 2
REMARK   1  AUTH   L.MA,E.R.KANTROWITZ
REMARK   1  TITL   MUTATIONS AT HISTIDINE 412 ALTER ZINC BINDING AND
REMARK   1  TITL 2 ELIMINATE TRANSFERASE ACTIVITY IN ESCHERICHIA COLI
REMARK   1  TITL 3 ALKALINE PHOSPHATASE
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 31614 1994
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
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             : 38875
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.166
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   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            : 6558
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 14
REMARK   3   SOLVENT ATOMS            : 219
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) : 0.27
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) : 0.020
REMARK   3   BOND ANGLES            (DEGREES) : 2.01
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.80
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.67
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 1ALJ 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        : 14-MAY-93
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36882
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.300
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : 0.10800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THIS ENTRY IS A MUTANT ALKALINE
REMARK 280  PHOSPHATE (H412N) IN WHICH HIS 412 IS REPLACED BY ASN,
REMARK 280  DETERMINED WITH CRYSTALS SOAKED IN STABILIZATION BUFFER
REMARK 280  CONTAINING NO ADDED ZINC. THERE IS ONE ZINC AND ONE MAGNESIUM
REMARK 280  COMPLEXED WITH INORGANIC PHOSPHATE BOUND IN EACH OF THE TWO
REMARK 280  ACTIVE SITES.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-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 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  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        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       97.38000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       83.87000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       38.11500
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       97.38000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       83.87000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       38.11500
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       97.38000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       83.87000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       38.11500
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       97.38000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       83.87000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       38.11500
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 300 REMARK: THERE IS A DIMER (IDENTICAL CHAINS OF 449 RESIDUES) PER
REMARK 300 ASYMMETRIC UNIT. THESE SUBUNITS, DESIGNATED "A" AND "B".
REMARK 300 THE FIRST THREE RESIDUES WERE DELETED DURING THE
REMARK 300 REFINEMENT.
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: 8300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 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     THR B     1
REMARK 465     PRO B     2
REMARK 465     GLU B     3
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    ALA A  88   CA    ALA A  88   CB     -0.131
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    ASN A   9      117.72   -161.70
REMARK 500    HIS A  86       38.50   -143.03
REMARK 500    ASN A 293      145.43     64.60
REMARK 500    SER A 325       -8.88    -49.90
REMARK 500    ALA A 332       10.27    -68.50
REMARK 500    HIS A 372     -168.14   -121.62
REMARK 500    GLU A 407       45.93    -82.11
REMARK 500    ASP A 408      -72.80     63.04
REMARK 500    SER A 409      105.03    -53.81
REMARK 500    ALA B  88     -167.54   -103.01
REMARK 500    TYR B  98      -19.39    -48.86
REMARK 500    ASN B 293      144.76     57.46
REMARK 500    SER B 325       -8.11    -50.59
REMARK 500    ALA B 332        6.52    -68.25
REMARK 500    GLU B 407       45.36    -82.50
REMARK 500    ASP B 408      -74.31     63.91
REMARK 500    SER B 409      106.49    -53.06
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 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: (11X,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        25.0      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 A 455        DISTANCE =  8.88 ANGSTROMS
REMARK 525    HOH A 491        DISTANCE =  5.58 ANGSTROMS
REMARK 525    HOH A 493        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH B 498        DISTANCE =  6.82 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 451  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  51   OD2
REMARK 620 2 ASP A 369   OD2  96.4
REMARK 620 3 SER A 102   OG   96.1  85.3
REMARK 620 4 HIS A 370   NE2 172.6  90.0  80.6
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   OD1
REMARK 620 2 HOH A 500   O   147.7
REMARK 620 3 HOH A 454   O   116.9  60.0
REMARK 620 4 GLU A 322   OE2  61.7 138.7 150.2
REMARK 620 5 THR A 155   OG1  74.2  90.9 142.1  67.7
REMARK 620 6 ASP A  51   OD2  43.5 133.4  77.0  87.9 116.5
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   OD2
REMARK 620 2 HIS B 370   NE2 158.0
REMARK 620 3 ASP B 369   OD2 102.6  98.3
REMARK 620 4 SER B 102   OG  102.9  83.0  92.0
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 GLU B 322   OE2
REMARK 620 2 HOH B 519   O   138.5
REMARK 620 3 ASP B  51   OD1  54.3 109.2
REMARK 620 4 THR B 155   OG1  66.4 150.8  70.3
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: A
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTICALLY ACTIVE SITE ON A SUBUNIT
REMARK 800 SITE_IDENTIFIER: B
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTICALLY ACTIVE SITE ON B SUBUNIT
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 451
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 452
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 453
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 451
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 452
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 453
DBREF  1ALJ A    1   449  UNP    P00634   PPB_ECOLI       23    471
DBREF  1ALJ B    1   449  UNP    P00634   PPB_ECOLI       23    471
SEQADV 1ALJ ASN A  412  UNP  P00634    HIS   434 ENGINEERED
SEQADV 1ALJ ASN B  412  UNP  P00634    HIS   434 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 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 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 ASN 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 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 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 ASN 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 451       1
HET     MG  A 452       1
HET    PO4  A 453       5
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    2(ZN 2+)
FORMUL   4   MG    2(MG 2+)
FORMUL   5  PO4    2(O4 P 3-)
FORMUL   9  HOH   *219(H2 O)
HELIX    1   1 THR A   30  SER A   36  1                                   7
HELIX    2   2 ASP A   55  GLU A   66  1                                  12
HELIX    3   3 ILE A   75  ALA A   77  5                                   3
HELIX    4   4 SER A  102  THR A  111  1                                  10
HELIX    5   5 ILE A  132  ALA A  138  1                                   7
HELIX    6   6 ALA A  154  LEU A  159  1                                   6
HELIX    7   7 PRO A  171  LYS A  177  1                                   7
HELIX    8   8 LEU A  183  LYS A  185  5                                   3
HELIX    9   9 ILE A  191  ALA A  198  1                                   8
HELIX   10  10 THR A  210  ALA A  212  5                                   3
HELIX   11  11 LEU A  225  ARG A  232  1                                   8
HELIX   12  12 ALA A  240  SER A  245  1                                   6
HELIX   13  13 GLY A  277  ASP A  280  1                                   4
HELIX   14  14 PRO A  290  ARG A  292  5                                   3
HELIX   15  15 LEU A  299  LYS A  312  1                                  14
HELIX   16  16 SER A  325  HIS A  331  1                                   7
HELIX   17  17 PRO A  335  GLU A  359  1                                  25
HELIX   18  18 ALA A  426  VAL A  429  5                                   4
HELIX   19  19 GLN A  435  ALA A  445  1                                  11
HELIX   20  20 THR B   30  SER B   36  1                                   7
HELIX   21  21 ASP B   55  GLU B   66  1                                  12
HELIX   22  22 SER B  102  THR B  111  1                                  10
HELIX   23  23 ILE B  132  ALA B  138  1                                   7
HELIX   24  24 ALA B  154  LEU B  159  1                                   6
HELIX   25  25 PRO B  171  LYS B  177  1                                   7
HELIX   26  26 LEU B  183  LYS B  185  5                                   3
HELIX   27  27 ILE B  191  ALA B  198  1                                   8
HELIX   28  28 ALA B  208  ALA B  212  5                                   5
HELIX   29  29 LEU B  225  ARG B  232  1                                   8
HELIX   30  30 ALA B  240  SER B  245  1                                   6
HELIX   31  31 GLY B  277  ASP B  280  1                                   4
HELIX   32  32 PRO B  290  ARG B  292  5                                   3
HELIX   33  33 LEU B  299  LYS B  312  1                                  14
HELIX   34  34 SER B  325  HIS B  331  1                                   7
HELIX   35  35 PRO B  335  GLU B  359  1                                  25
HELIX   36  36 ALA B  426  VAL B  429  5                                   4
HELIX   37  37 GLN B  435  ALA B  445  1                                  11
SHEET    1   A10 GLN A 235  VAL A 237  0
SHEET    2   A10 LEU A 255  LEU A 258  1  N  LEU A 256   O  GLN A 235
SHEET    3   A10 VAL A 202  GLY A 205  1  N  THR A 203   O  LEU A 255
SHEET    4   A10 ALA A 142  SER A 147  1  N  ASN A 145   O  VAL A 202
SHEET    5   A10 PHE A 317  GLY A 323  1  N  PHE A 318   O  ALA A 142
SHEET    6   A10 ASN A  44  GLY A  50  1  N  ILE A  45   O  LEU A 319
SHEET    7   A10 THR A 362  ALA A 368  1  N  LEU A 363   O  ASN A  44
SHEET    8   A10 LEU A 417  TYR A 422 -1  N  TYR A 422   O  VAL A 364
SHEET    9   A10 LEU A  80  THR A  85 -1  N  TYR A  84   O  LEU A 417
SHEET   10   A10 GLY A 431  ASP A 434  1  N  GLY A 431   O  GLN A  83
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 GLN B 235  VAL B 237  0
SHEET    2   C10 LEU B 255  LEU B 258  1  N  LEU B 256   O  GLN B 235
SHEET    3   C10 VAL B 202  GLY B 205  1  N  THR B 203   O  LEU B 255
SHEET    4   C10 ALA B 142  SER B 147  1  N  ASN B 145   O  VAL B 202
SHEET    5   C10 PHE B 317  GLY B 323  1  N  PHE B 318   O  ALA B 142
SHEET    6   C10 ASN B  44  GLY B  50  1  N  ILE B  45   O  LEU B 319
SHEET    7   C10 THR B 362  ALA B 368  1  N  LEU B 363   O  ASN B  44
SHEET    8   C10 LEU B 417  TYR B 422 -1  N  TYR B 422   O  VAL B 364
SHEET    9   C10 LEU B  80  THR B  85 -1  N  TYR B  84   O  LEU B 417
SHEET   10   C10 GLY B 431  ASP B 434  1  N  GLY B 431   O  GLN B  83
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  2.01
SSBOND   2 CYS A  286    CYS A  336                          1555   1555  2.02
SSBOND   3 CYS B  168    CYS B  178                          1555   1555  2.00
SSBOND   4 CYS B  286    CYS B  336                          1555   1555  2.06
LINK        ZN    ZN A 451                 OD2 ASP A  51     1555   1555  2.76
LINK        ZN    ZN A 451                 OD2 ASP A 369     1555   1555  2.17
LINK        ZN    ZN A 451                 OG  SER A 102     1555   1555  2.67
LINK        ZN    ZN A 451                 NE2 HIS A 370     1555   1555  2.17
LINK        MG    MG A 452                 OD1 ASP A  51     1555   1555  2.74
LINK        MG    MG A 452                 O   HOH A 500     1555   1555  2.47
LINK        MG    MG A 452                 O   HOH A 454     1555   1555  2.92
LINK        MG    MG A 452                 OE2 GLU A 322     1555   1555  2.73
LINK        MG    MG A 452                 OG1 THR A 155     1555   1555  2.72
LINK        MG    MG A 452                 OD2 ASP A  51     1555   1555  3.11
LINK        ZN    ZN B 451                 OD2 ASP B  51     1555   1555  2.59
LINK        ZN    ZN B 451                 NE2 HIS B 370     1555   1555  2.27
LINK        ZN    ZN B 451                 OD2 ASP B 369     1555   1555  1.97
LINK        ZN    ZN B 451                 OG  SER B 102     1555   1555  2.70
LINK        MG    MG B 452                 OE2 GLU B 322     1555   1555  3.00
LINK        MG    MG B 452                 O   HOH B 519     1555   1555  3.00
LINK        MG    MG B 452                 OD1 ASP B  51     1555   1555  3.08
LINK        MG    MG B 452                 OG1 THR B 155     1555   1555  2.52
SITE     1   A 13 ASP A 327  HIS A 331  ASN A 412   ZN A 451
SITE     2   A 13  MG A 452  PO4 A 453  ASP A  51  ASP A 369
SITE     3   A 13 HIS A 370  THR A 155  GLU A 322  ARG A 166
SITE     4   A 13 SER A 102
SITE     1   B 13 ASP B 327  HIS B 331  ASN B 412   ZN B 451
SITE     2   B 13  MG B 452  PO4 B 453  ASP B  51  ASP B 369
SITE     3   B 13 HIS B 370  THR B 155  GLU B 322  ARG B 166
SITE     4   B 13 SER B 102
SITE     1 AC1  6 ASP A  51  SER A 102  ASP A 327  ASP A 369
SITE     2 AC1  6 HIS A 370  PO4 A 453
SITE     1 AC2  6 ASP A  51  ASP A 153  THR A 155  GLU A 322
SITE     2 AC2  6 HOH A 454  HOH A 500
SITE     1 AC3  9 ASP A 101  SER A 102  ARG A 166  ASP A 327
SITE     2 AC3  9 HIS A 331  HIS A 370  ASN A 412   ZN A 451
SITE     3 AC3  9 HOH A 454
SITE     1 AC4  5 ASP B  51  SER B 102  ASP B 327  ASP B 369
SITE     2 AC4  5 HIS B 370
SITE     1 AC5  5 ASP B  51  ASP B 153  THR B 155  GLU B 322
SITE     2 AC5  5 HOH B 519
SITE     1 AC6  8 ASP B 101  SER B 102  ARG B 166  ASP B 327
SITE     2 AC6  8 HIS B 331  HIS B 370  ASN B 412  HOH B 519
CRYST1  194.760  167.740   76.230  90.00  90.00  90.00 I 2 2 2      16
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      0.005135  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005962  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013118        0.00000
      
PROCHECK
Go to PROCHECK summary
 References