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PDBsum entry 1aja

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Top Page protein Protein-protein interface(s) links
Non specific mono-esterase PDB id
1aja
Jmol
Contents
Protein chains
435 a.a. *
* Residue conservation analysis
HEADER    NON SPECIFIC MONO-ESTERASE              19-AUG-95   1AJA
TITLE     THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI
TITLE    2 ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM
TITLE    3 BINDING AND INCREASED CATALYTIC ACTIVITY
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: APO ENZYME
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 GENE: PHOA;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: LAC;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PWM528 AS BAMH1/HINDIII
SOURCE   9 RESTRICTION FRAGMENT;
SOURCE  10 EXPRESSION_SYSTEM_GENE: PHOA;
SOURCE  11 OTHER_DETAILS: LAC PROMOTER. FOR MORE INFORMATION ABOUT
SOURCE  12 THE EXPRESSION SYSTEM CONSULT MANDECKI ET AL. GENE 94, 103-
SOURCE  13 107; (1990).
KEYWDS    NON SPECIFIC MONO-ESTERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.G.DEALWIS,L.CHEN,C.ABAD-ZAPATERO
REVDAT   2   24-FEB-09 1AJA    1       VERSN
REVDAT   1   14-NOV-95 1AJA    0
JRNL        AUTH   C.G.DEALWIS,C.BRENNAN,K.CHRISTIANSON,W.MANDECKI,
JRNL        AUTH 2 C.ABAD-ZAPATERO
JRNL        TITL   CRYSTALLOGRAPHIC ANALYSIS OF REVERSIBLE METAL
JRNL        TITL 2 BINDING OBSERVED IN A MUTANT (ASP153-->GLY) OF
JRNL        TITL 3 ESCHERICHIA COLI ALKALINE PHOSPHATASE.
JRNL        REF    BIOCHEMISTRY                  V.  34 13967 1995
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   7577993
JRNL        DOI    10.1021/BI00043A001
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   C.DEALWIS,C.BRENNAN,K.CHRISTIANSON,W.MANDECKI,
REMARK   1  AUTH 2 A.ABAD-ZAPATERO
REMARK   1  TITL   CRYSTALLOGRAPHIC ANALYSIS OF REVERSIBLE METAL
REMARK   1  TITL 2 BINDING OBSERVED IN A MUTANT (ASP 153--> GLY) OF
REMARK   1  TITL 3 E. COLI ALKALINE PHOSPHATASE
REMARK   1  REF    TO BE PUBLISHED
REMARK   1  REFN
REMARK   1 REFERENCE 2
REMARK   1  AUTH   L.CHEN,D.NEIDHART,M.KOHLBRENNER,W.MANDECKI,S.BELL,
REMARK   1  AUTH 2 J.SOWADSKI,C.ABAD-ZAPATERO
REMARK   1  TITL   3-D STRUCTURE OF THE (ASP 101-->SER) OF E.COLI
REMARK   1  TITL 2 ALKALINE PHOSPHATASE WITH HIGHER CATALYTIC ACTIVITY
REMARK   1  REF    PROTEIN ENG.                  V.   5   605 1992
REMARK   1  REFN                   ISSN 0269-2139
REMARK   2
REMARK   2 RESOLUTION.    2.50 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) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
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             : 34945
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) : 0.162
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            : 6352
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
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) : 11.00
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) : 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) : 0.015
REMARK   3   BOND ANGLES            (DEGREES) : 2.70
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 1AJA 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        : 06-JAN-94
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) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40175
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.0
REMARK 200  DATA REDUNDANCY                : 1.650
REMARK 200  R MERGE                    (I) : 0.08000
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   (%): 62.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       97.51000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       83.46500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       38.22000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       97.51000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       83.46500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       38.22000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       97.51000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       83.46500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       38.22000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       97.51000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       83.46500
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       38.22000
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: 6690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 450
REMARK 450 SOURCE
REMARK 450 FOR MORE INFORMATION ABOUT THE EXPRESSION SYSTEM CONSULT
REMARK 450 MANDECKI ET AL. GENE 94, 103-107; (1990).
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     ILE A   326
REMARK 465     ASP A   327
REMARK 465     LYS A   328
REMARK 465     GLN A   329
REMARK 465     ASP A   330
REMARK 465     HIS A   331
REMARK 465     GLY A   403
REMARK 465     ASN A   404
REMARK 465     SER A   405
REMARK 465     GLU A   406
REMARK 465     GLU A   407
REMARK 465     ASP A   408
REMARK 465     SER A   409
REMARK 465     GLN A   410
REMARK 465     ILE B   326
REMARK 465     ASP B   327
REMARK 465     LYS B   328
REMARK 465     GLN B   329
REMARK 465     ASP B   330
REMARK 465     HIS B   331
REMARK 465     ALA B   332
REMARK 465     GLY B   403
REMARK 465     ASN B   404
REMARK 465     SER B   405
REMARK 465     GLU B   406
REMARK 465     GLU B   407
REMARK 465     ASP B   408
REMARK 465     SER B   409
REMARK 465     GLN B   410
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ALA A 332    CB
REMARK 470     GLU A 411    CG   CD   OE1  OE2
REMARK 470     ASP B  51    CG   OD1  OD2
REMARK 470     GLN B 252    CG   CD   OE1  NE2
REMARK 470     GLU B 411    CG   CD   OE1  OE2
REMARK 470     HIS B 412    CG   ND1  CD2  CE1  NE2
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    HIS A 162   NE2   HIS A 162   CD2    -0.072
REMARK 500    HIS A 370   NE2   HIS A 370   CD2    -0.068
REMARK 500    HIS B 125   NE2   HIS B 125   CD2    -0.069
REMARK 500    HIS B 129   NE2   HIS B 129   CD2    -0.069
REMARK 500    HIS B 162   NE2   HIS B 162   CD2    -0.078
REMARK 500    HIS B 276   NE2   HIS B 276   CD2    -0.067
REMARK 500    HIS B 370   NE2   HIS B 370   CD2    -0.069
REMARK 500    HIS B 425   NE2   HIS B 425   CD2    -0.079
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  34   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    TYR A  84   CA  -  CB  -  CG  ANGL. DEV. =  12.5 DEGREES
REMARK 500    TYR A  84   CB  -  CG  -  CD2 ANGL. DEV. =  -5.2 DEGREES
REMARK 500    TRP A 220   CD1 -  CG  -  CD2 ANGL. DEV. =   7.4 DEGREES
REMARK 500    TRP A 220   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.4 DEGREES
REMARK 500    TRP A 268   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP A 268   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A 351   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 351   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ARG A 418   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 418   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    MET B   4   CG  -  SD  -  CE  ANGL. DEV. =   9.6 DEGREES
REMARK 500    LEU B   7   CA  -  C   -  N   ANGL. DEV. = -14.3 DEGREES
REMARK 500    ARG B  34   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    LEU B  48   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES
REMARK 500    TYR B  84   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    TRP B 109   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG B 166   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    LEU B 195   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    ARG B 199   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG B 199   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    TRP B 220   CD1 -  CG  -  CD2 ANGL. DEV. =   7.8 DEGREES
REMARK 500    TRP B 220   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.7 DEGREES
REMARK 500    ARG B 226   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG B 226   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    TRP B 268   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    TRP B 268   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.8 DEGREES
REMARK 500    TRP B 268   CG  -  CD2 -  CE3 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG B 292   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG B 292   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ASN B 293   CB  -  CA  -  C   ANGL. DEV. = -12.0 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  51       95.20    -59.19
REMARK 500    HIS A  86       40.95   -148.71
REMARK 500    GLU A 184       21.20    -72.22
REMARK 500    ASN A 250     -167.83   -162.80
REMARK 500    PRO A 288      135.52    -35.70
REMARK 500    ASN A 293      161.50     77.33
REMARK 500    ALA A 333       53.98     30.97
REMARK 500    HIS A 425       -0.90     72.11
REMARK 500    PRO B   2       81.23    -50.60
REMARK 500    MET B   4      107.34     21.05
REMARK 500    HIS B  86       31.03   -147.19
REMARK 500    GLU B 126       17.91     51.44
REMARK 500    GLN B 291       37.91    -85.64
REMARK 500    ASN B 293      143.64     80.42
REMARK 500    ASN B 361       35.61   -143.81
REMARK 500    HIS B 372     -167.42   -106.64
REMARK 500    THR B 433     -168.50   -123.64
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     ASN B 293        23.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEET
REMARK 700  DETERMINATION METHOD: KABSCH & SANDER;
REMARK 700  SHEET_ID: S1A; SAME AS 1ALK.
REMARK 700  SHEET_ID: S2A; SAME AS 1ALK.
REMARK 700  SHEET_ID: S1B; SAME AS 1ALK.
REMARK 700  SHEET_ID: S2B; SAME AS 1ALK.
DBREF  1AJA A    1   449  UNP    P00634   PPB_ECOLI       23    471
DBREF  1AJA B    1   449  UNP    P00634   PPB_ECOLI       23    471
SEQADV 1AJA GLY A  153  UNP  P00634    ASP   175 ENGINEERED
SEQADV 1AJA GLU A  230  UNP  P00634    GLN   252 CONFLICT
SEQADV 1AJA GLY B  153  UNP  P00634    ASP   175 ENGINEERED
SEQADV 1AJA GLU B  230  UNP  P00634    GLN   252 CONFLICT
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 GLY 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 GLU ALA ARG GLY TYR
SEQRES  19 A  449  GLN LEU VAL SER ASP ALA ALA SER LEU ASN SER VAL THR
SEQRES  20 A  449  GLU ALA ASN GLN GLN LYS PRO LEU LEU GLY LEU PHE ALA
SEQRES  21 A  449  ASP GLY ASN MET PRO VAL ARG TRP LEU GLY PRO LYS ALA
SEQRES  22 A  449  THR TYR HIS GLY ASN ILE ASP LYS PRO ALA VAL THR CYS
SEQRES  23 A  449  THR PRO ASN PRO GLN ARG ASN ASP SER VAL PRO THR LEU
SEQRES  24 A  449  ALA GLN MET THR ASP LYS ALA ILE GLU LEU LEU SER LYS
SEQRES  25 A  449  ASN GLU LYS GLY PHE PHE LEU GLN VAL GLU GLY ALA SER
SEQRES  26 A  449  ILE ASP LYS GLN 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 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 GLY 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 GLU ALA ARG GLY TYR
SEQRES  19 B  449  GLN LEU VAL SER ASP ALA ALA SER LEU ASN SER VAL THR
SEQRES  20 B  449  GLU ALA ASN GLN GLN LYS PRO LEU LEU GLY LEU PHE ALA
SEQRES  21 B  449  ASP GLY ASN MET PRO VAL ARG TRP LEU GLY PRO LYS ALA
SEQRES  22 B  449  THR TYR HIS GLY ASN ILE ASP LYS PRO ALA VAL THR CYS
SEQRES  23 B  449  THR PRO ASN PRO GLN ARG ASN ASP SER VAL PRO THR LEU
SEQRES  24 B  449  ALA GLN MET THR ASP LYS ALA ILE GLU LEU LEU SER LYS
SEQRES  25 B  449  ASN GLU LYS GLY PHE PHE LEU GLN VAL GLU GLY ALA SER
SEQRES  26 B  449  ILE ASP LYS GLN 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
HELIX    1  H1 GLN A   29  LEU A   37  1                                   9
HELIX    2  H2 GLY A   54  GLU A   66  1                                  13
HELIX    3  H3 PHE A   72  LEU A   78  1                                   7
HELIX    4  H4 ASP A  101  GLY A  112  1                                  12
HELIX    5  H5 THR A  131  GLY A  140  1                                  10
HELIX    6  H6 GLY A  153  VAL A  160  1                                   8
HELIX    7  H7 GLY A  170  LYS A  177  1                                   8
HELIX    8  H8 SER A  190  ARG A  199  1                                  10
HELIX    9  H9 GLY A  207  GLU A  213  1                                   7
HELIX   10 H10 THR A  224  GLY A  233  1                                  10
HELIX   11 H11 ASP A  239  VAL A  246  1                                   8
HELIX   12 H12 HIS A  276  LYS A  281  1                                   6
HELIX   13 H13 THR A  298  ASN A  313  1                                  16
HELIX   14 H14 SER A  325  ALA A  333  1                                   3
HELIX   15 H15 ASN A  334  GLY A  360  1                                  27
HELIX   16 H16 ASP A  434  GLY A  447  1                                  14
HELIX   17  G1 GLN B   29  LEU B   37  1                                   9
HELIX   18  G2 GLY B   54  GLU B   66  1                                  13
HELIX   19  G3 PHE B   72  LEU B   78  1                                   7
HELIX   20  G4 ASP B  101  GLY B  112  1                                  12
HELIX   21  G5 THR B  131  GLY B  140  1                                  10
HELIX   22  G6 GLY B  153  VAL B  160  1                                   8
HELIX   23  G7 GLY B  170  LYS B  177  1                                   8
HELIX   24  G8 SER B  190  ARG B  199  1                                  10
HELIX   25  G9 GLY B  207  GLU B  213  1                                   7
HELIX   26 G10 THR B  224  GLY B  233  1                                  10
HELIX   27 G11 ASP B  239  VAL B  246  1                                   8
HELIX   28 G12 HIS B  276  LYS B  281  1                                   6
HELIX   29 G13 THR B  298  ASN B  313  1                                  16
HELIX   30 G14 SER B  325  ALA B  333  1                                   2
HELIX   31 G15 ASN B  334  GLY B  360  1                                  27
HELIX   32 G16 ASP B  434  GLY B  447  1                                  14
SHEET    1 S1A10 GLY A 431  ASP A 434  0
SHEET    2 S1A10 LEU A  80  THR A  85  1
SHEET    3 S1A10 LEU A 417  TYR A 422 -1
SHEET    4 S1A10 ASN A 361  THR A 367 -1
SHEET    5 S1A10 ASN A  44  GLY A  50  1
SHEET    6 S1A10 GLY A 316  GLY A 323  1
SHEET    7 S1A10 ALA A 142  THR A 148  1
SHEET    8 S1A10 ASP A 201  GLY A 205  1
SHEET    9 S1A10 PRO A 254  PHE A 259  1
SHEET   10 S1A10 GLN A 235  VAL A 237  1
SHEET    1 S2A 3 GLN A 375  VAL A 377  0
SHEET    2 S2A 3 VAL A 397  TYR A 402 -1
SHEET    3 S2A 3 LEU A 386  ASN A 391 -1
SHEET    1 S1B10 GLY B 431  ASP B 434  0
SHEET    2 S1B10 LEU B  80  THR B  85  1
SHEET    3 S1B10 LEU B 417  TYR B 422 -1
SHEET    4 S1B10 ASN B 361  THR B 367 -1
SHEET    5 S1B10 ASN B  44  GLY B  50  1
SHEET    6 S1B10 GLY B 316  GLY B 323  1
SHEET    7 S1B10 ALA B 142  THR B 148  1
SHEET    8 S1B10 ASP B 201  GLY B 205  1
SHEET    9 S1B10 PRO B 254  PHE B 259  1
SHEET   10 S1B10 GLN B 235  VAL B 237  1
SHEET    1 S2B 3 GLN B 375  VAL B 377  0
SHEET    2 S2B 3 VAL B 397  TYR B 402 -1
SHEET    3 S2B 3 LEU B 386  ASN B 391 -1
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  2.02
SSBOND   4 CYS B  286    CYS B  336                          1555   1555  2.00
CRYST1  195.020  166.930   76.440  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      0.005128  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005991  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013082        0.00000
      
PROCHECK
Go to PROCHECK summary
 References