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PDBsum entry 8xim

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Top Page protein ligands metals Protein-protein interface(s) links
Isomerase(intramolecular oxidoreductse) PDB id
8xim
Jmol
Contents
Protein chains
392 a.a. *
Ligands
XLS ×4
Metals
_MG ×4
Waters ×971
* Residue conservation analysis
HEADER    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 01-APR-92   8XIM
TITLE     PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM
TITLE    2 ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-
TITLE    3 DIRECTED MUTAGENESIS OF METAL BINDING SITES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-XYLOSE ISOMERASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 5.3.1.5;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ACTINOPLANES MISSOURIENSIS;
SOURCE   3 ORGANISM_TAXID: 1866
KEYWDS    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.JANIN
REVDAT   3   24-FEB-09 8XIM    1       VERSN
REVDAT   2   01-APR-03 8XIM    1       JRNL
REVDAT   1   15-JUL-93 8XIM    0
JRNL        AUTH   J.JENKINS,J.JANIN,F.REY,M.CHIADMI,H.VAN TILBEURGH,
JRNL        AUTH 2 I.LASTERS,M.DE MAEYER,D.VAN BELLE,S.J.WODAK,
JRNL        AUTH 3 M.LAUWEREYS,P.STANSSENS,G.MATTHYSSENS,A.M.LAMBEIR
JRNL        TITL   PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE
JRNL        TITL 2 FROM ACTINOPLANES MISSOURIENSIS. 1.
JRNL        TITL 3 CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF
JRNL        TITL 4 METAL BINDING SITES.
JRNL        REF    BIOCHEMISTRY                  V.  31  5449 1992
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   1610791
JRNL        DOI    10.1021/BI00139A005
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   A.-M.LAMBEIR,M.LAUWEREYS,P.STANSSENS,N.T.MRABET,
REMARK   1  AUTH 2 J.SNAUWAERT,H.VANTILBEURGH,G.MATTHYSSENS,I.LASTERS,
REMARK   1  AUTH 3 M.DEMAEYER,S.J.WODAK,J.JENKINS,M.CHIADMI,J.JANIN
REMARK   1  TITL   PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE
REMARK   1  TITL 2 FROM ACTINOPLANES MISSOURIENSIS. 2. SITE-DIRECTED
REMARK   1  TITL 3 MUTAGENESIS OF THE XYLOSE BINDING SITE
REMARK   1  REF    BIOCHEMISTRY                  V.  31  5459 1992
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 2
REMARK   1  AUTH   H.VANTILBEURGH,J.JENKINS,M.CHIADMI,
REMARK   1  AUTH 2 J.JANIN S.J.WODAK,N.T.MRABET,A.-M.LAMBEIR
REMARK   1  TITL   PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE
REMARK   1  TITL 2 FROM ACTINOPLANES MISSOURIENSIS. 3. CHANGING METAL
REMARK   1  TITL 3 SPECIFICITY AND THE PH PROFILE BY SITE-DIRECTED
REMARK   1  TITL 4 MUTAGENESIS
REMARK   1  REF    BIOCHEMISTRY                  V.  31  5467 1992
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 3
REMARK   1  AUTH   N.T.MRABET,A.VAN DENBROEK,I.VAN DEN BRANDE,
REMARK   1  AUTH 2 P.STANSSENS,Y.LAROCHE,A.-M.LAMBEIR,G.MATTHIJSSENS,
REMARK   1  AUTH 3 J.JENKINS,M.CHIADMI,H.VANTILBEURGH,F.REY,J.JANIN,
REMARK   1  AUTH 4 W.J.QUAX,I.LASTERS,M.DEMAEYER,S.J.WODAK
REMARK   1  TITL   ARGININE RESIDUES AS STABILIZING ELEMENTS IN
REMARK   1  TITL 2 PROTEINS
REMARK   1  REF    BIOCHEMISTRY                  V.  31  2239 1992
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 4
REMARK   1  AUTH   F.REY,J.JENKINS,J.JANIN,I.LASTERS,P.ALARD,
REMARK   1  AUTH 2 M.CLAESSENS,G.MATTHYSSENS,S.WODAK
REMARK   1  TITL   STRUCTURAL ANALYSIS OF THE 2.8 ANGSTROMS MODEL OF
REMARK   1  TITL 2 XYLOSE ISOMERASE FROM ACTINOPLANES MISSOURIENSIS
REMARK   1  REF    PROTEINS                      V.   4   165 1988
REMARK   1  REFN                   ISSN 0887-3585
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 97974
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 + TEST SET) : 0.146
REMARK   3   R VALUE            (WORKING SET) : NULL
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
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 12188
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 44
REMARK   3   SOLVENT ATOMS            : 971
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.010 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.036 ; 0.040
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.035 ; 0.040
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.009 ; 0.010
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.126 ; 0.150
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : 0.265 ; 0.500
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 8XIM 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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+1/3
REMARK 290       6555   -X,-X+Y,-Z+2/3
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      154.33333
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       77.16667
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       77.16667
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      154.33333
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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     SER A     2
REMARK 465     SER B     2
REMARK 465     SER C     2
REMARK 465     VAL C     3
REMARK 465     SER D     2
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     GLN A   4    CG   CD   OE1  NE2
REMARK 470     GLU A   8    CG   CD   OE1  OE2
REMARK 470     GLN A  66    CG   CD   OE1  NE2
REMARK 470     ASP A 280    CG   OD1  OD2
REMARK 470     GLN B   4    CG   CD   OE1  NE2
REMARK 470     GLU B   8    CG   CD   OE1  OE2
REMARK 470     GLN B  66    CG   CD   OE1  NE2
REMARK 470     ASP B 280    CG   OD1  OD2
REMARK 470     GLN C   4    CG   CD   OE1  NE2
REMARK 470     GLU C   8    CG   CD   OE1  OE2
REMARK 470     GLN C  66    CG   CD   OE1  NE2
REMARK 470     ASP C 280    CG   OD1  OD2
REMARK 470     GLN D   4    CG   CD   OE1  NE2
REMARK 470     GLU D   8    CG   CD   OE1  OE2
REMARK 470     GLN D  66    CG   CD   OE1  NE2
REMARK 470     PRO D 209    CB
REMARK 470     ASP D 280    CG   OD1  OD2
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   OE1  GLN A   204     OE1  GLN C   204              1.54
REMARK 500   OE1  GLN B   204     OE1  GLN D   204              1.66
REMARK 500   OE2  GLU D   217     O    HOH D   429              2.14
REMARK 500   NH1  ARG D   394     O    HOH D   614              2.14
REMARK 500   OE2  GLU D   141     O    HOH D   595              2.17
REMARK 500   O    HOH C   416     O    HOH C   540              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    SER D 169   C     GLU D 170   N      -0.214
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  23   CD  -  NE  -  CZ  ANGL. DEV. =  10.9 DEGREES
REMARK 500    ARG A  23   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ASP A  24   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    PHE A  26   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ASP A  80   CB  -  CG  -  OD1 ANGL. DEV. =  -8.1 DEGREES
REMARK 500    ARG A 109   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG A 109   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 113   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG A 117   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG A 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ASP A 146   CB  -  CG  -  OD1 ANGL. DEV. =   8.7 DEGREES
REMARK 500    ASP A 150   CB  -  CG  -  OD1 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ARG A 157   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG A 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ASP A 171   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG A 172   CD  -  NE  -  CZ  ANGL. DEV. =  11.5 DEGREES
REMARK 500    ARG A 172   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 188   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    GLU A 205   OE1 -  CD  -  OE2 ANGL. DEV. = -11.0 DEGREES
REMARK 500    ASP A 292   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG A 321   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ASP A 328   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    GLU A 330   OE1 -  CD  -  OE2 ANGL. DEV. =   8.5 DEGREES
REMARK 500    ARG A 361   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 361   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 394   NH1 -  CZ  -  NH2 ANGL. DEV. =  10.8 DEGREES
REMARK 500    ARG A 394   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ARG A 394   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG B  23   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ASP B  28   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ASP B  55   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG B  68   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ASP B  80   CB  -  CG  -  OD1 ANGL. DEV. =  -8.2 DEGREES
REMARK 500    ARG B 113   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG B 117   NE  -  CZ  -  NH1 ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG B 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ARG B 121   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG B 140   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG B 140   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ASP B 156   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    ARG B 157   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    TYR B 158   CB  -  CG  -  CD2 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ASP B 257   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ARG B 313   CD  -  NE  -  CZ  ANGL. DEV. =  23.1 DEGREES
REMARK 500    ARG B 313   NE  -  CZ  -  NH1 ANGL. DEV. =   7.9 DEGREES
REMARK 500    ARG B 313   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ARG B 321   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    GLU B 330   OE1 -  CD  -  OE2 ANGL. DEV. =  12.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     109 ANGLE DEVIATIONS.
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    THR A  17      -77.12    -80.07
REMARK 500    PHE A  94      -31.26   -138.20
REMARK 500    GLN A 186       99.89     77.45
REMARK 500    LEU A 193       63.95     60.87
REMARK 500    ASN A 247     -172.47   -170.59
REMARK 500    HIS A 250       72.48   -111.19
REMARK 500    PHE A 364      -74.99   -159.19
REMARK 500    THR B  17      -74.33    -80.77
REMARK 500    ALA B  22       33.53     73.44
REMARK 500    GLN B 186      101.06     73.14
REMARK 500    LEU B 193       63.58     65.51
REMARK 500    HIS B 250       73.94   -114.48
REMARK 500    PRO B 252       94.06    -65.76
REMARK 500    PHE B 364      -78.10   -154.46
REMARK 500    THR C  17      -71.02    -84.99
REMARK 500    GLN C 186      105.02     73.91
REMARK 500    LEU C 193       61.69     65.47
REMARK 500    ASN C 247     -174.40   -171.61
REMARK 500    HIS C 250       74.93   -112.04
REMARK 500    PRO C 279      -71.89    -31.90
REMARK 500    ASP C 280      -96.16    -59.64
REMARK 500    PHE C 364      -71.65   -162.41
REMARK 500    THR D  17      -75.60    -82.95
REMARK 500    ALA D  22       39.96     70.44
REMARK 500    ASP D  24     -163.35   -103.23
REMARK 500    GLN D 186      101.36     77.60
REMARK 500    LEU D 193       61.91     63.07
REMARK 500    HIS D 250       72.57   -111.72
REMARK 500    PRO D 252       96.86    -66.59
REMARK 500    ASN D 277       57.13    -97.39
REMARK 500    ASP D 280       43.24     78.93
REMARK 500    PHE D 364      -70.72   -158.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 MG 395 IS AT METAL SITE 1 IN ALL FOUR SUBUNITS.  THE
REMARK 600 MG AT METAL SITE 2 HAS BEEN REPLACED WITH WATER HOH 396 IN
REMARK 600 ALL FOUR SUBUNITS.
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                              MG A 395  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 292   OD2
REMARK 620 2 GLU A 217   OE1  87.8
REMARK 620 3 XLS A 397   O2   76.8  81.0
REMARK 620 4 XLS A 397   O4   87.4 164.4  83.4
REMARK 620 5 GLU A 181   OE1 135.5 136.5 107.8  50.7
REMARK 620 6 GLU A 181   OE2 161.0  95.8  85.2  84.1  45.0
REMARK 620 7 ASP A 245   OD2  97.7  96.5 174.0  98.9  77.8 100.5
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 395  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 XLS B 397   O4
REMARK 620 2 GLU B 181   OE2  85.1
REMARK 620 3 ASP B 245   OD2  92.0  84.1
REMARK 620 4 XLS B 397   O2   89.6  88.1 171.9
REMARK 620 5 ASP B 292   OD2  88.7 171.3 102.2  85.8
REMARK 620 6 GLU B 217   OE1 172.5  87.5  88.6  88.8  98.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 395  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 217   OE1
REMARK 620 2 ASP C 245   OD2  92.4
REMARK 620 3 XLS C 397   O2   94.5 172.9
REMARK 620 4 XLS C 397   O4  173.6  93.4  79.7
REMARK 620 5 ASP C 292   OD2  93.8  92.2  85.7  83.1
REMARK 620 6 GLU C 181   OE2  98.0  95.7  85.0  84.2 165.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 395  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 181   OE2
REMARK 620 2 ASP D 245   OD2  89.4
REMARK 620 3 XLS D 397   O4   77.0  89.6
REMARK 620 4 ASP D 292   OD2 162.5 101.1  89.0
REMARK 620 5 XLS D 397   O2   78.7 166.9  82.4  89.2
REMARK 620 6 GLU D 217   OE1  95.4  99.9 167.8  96.5  86.8
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XLS A 397
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XLS B 397
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XLS C 397
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XLS D 397
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 395
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 395
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 395
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 395
DBREF  8XIM A    2   394  UNP    P12851   XYLA_ACTMI       1    393
DBREF  8XIM B    2   394  UNP    P12851   XYLA_ACTMI       1    393
DBREF  8XIM C    2   394  UNP    P12851   XYLA_ACTMI       1    393
DBREF  8XIM D    2   394  UNP    P12851   XYLA_ACTMI       1    393
SEQADV 8XIM GLN A  186  UNP  P12851    GLU   185 CONFLICT
SEQADV 8XIM GLN B  186  UNP  P12851    GLU   185 CONFLICT
SEQADV 8XIM GLN C  186  UNP  P12851    GLU   185 CONFLICT
SEQADV 8XIM GLN D  186  UNP  P12851    GLU   185 CONFLICT
SEQRES   1 A  393  SER VAL GLN ALA THR ARG GLU ASP LYS PHE SER PHE GLY
SEQRES   2 A  393  LEU TRP THR VAL GLY TRP GLN ALA ARG ASP ALA PHE GLY
SEQRES   3 A  393  ASP ALA THR ARG THR ALA LEU ASP PRO VAL GLU ALA VAL
SEQRES   4 A  393  HIS LYS LEU ALA GLU ILE GLY ALA TYR GLY ILE THR PHE
SEQRES   5 A  393  HIS ASP ASP ASP LEU VAL PRO PHE GLY SER ASP ALA GLN
SEQRES   6 A  393  THR ARG ASP GLY ILE ILE ALA GLY PHE LYS LYS ALA LEU
SEQRES   7 A  393  ASP GLU THR GLY LEU ILE VAL PRO MET VAL THR THR ASN
SEQRES   8 A  393  LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 A  393  SER ASN ASP ARG SER VAL ARG ARG TYR ALA ILE ARG LYS
SEQRES  10 A  393  VAL LEU ARG GLN MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES  11 A  393  LYS THR LEU VAL LEU TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES  12 A  393  TYR ASP SER ALA LYS ASP VAL SER ALA ALA LEU ASP ARG
SEQRES  13 A  393  TYR ARG GLU ALA LEU ASN LEU LEU ALA GLN TYR SER GLU
SEQRES  14 A  393  ASP ARG GLY TYR GLY LEU ARG PHE ALA ILE GLU PRO LYS
SEQRES  15 A  393  PRO ASN GLN PRO ARG GLY ASP ILE LEU LEU PRO THR ALA
SEQRES  16 A  393  GLY HIS ALA ILE ALA PHE VAL GLN GLU LEU GLU ARG PRO
SEQRES  17 A  393  GLU LEU PHE GLY ILE ASN PRO GLU THR GLY HIS GLU GLN
SEQRES  18 A  393  MET SER ASN LEU ASN PHE THR GLN GLY ILE ALA GLN ALA
SEQRES  19 A  393  LEU TRP HIS LYS LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 A  393  GLN HIS GLY PRO LYS PHE ASP GLN ASP LEU VAL PHE GLY
SEQRES  21 A  393  HIS GLY ASP LEU LEU ASN ALA PHE SER LEU VAL ASP LEU
SEQRES  22 A  393  LEU GLU ASN GLY PRO ASP GLY ALA PRO ALA TYR ASP GLY
SEQRES  23 A  393  PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR GLU ASP
SEQRES  24 A  393  TYR ASP GLY VAL TRP GLU SER ALA LYS ALA ASN ILE ARG
SEQRES  25 A  393  MET TYR LEU LEU LEU LYS GLU ARG ALA LYS ALA PHE ARG
SEQRES  26 A  393  ALA ASP PRO GLU VAL GLN GLU ALA LEU ALA ALA SER LYS
SEQRES  27 A  393  VAL ALA GLU LEU LYS THR PRO THR LEU ASN PRO GLY GLU
SEQRES  28 A  393  GLY TYR ALA GLU LEU LEU ALA ASP ARG SER ALA PHE GLU
SEQRES  29 A  393  ASP TYR ASP ALA ASP ALA VAL GLY ALA LYS GLY PHE GLY
SEQRES  30 A  393  PHE VAL LYS LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU
SEQRES  31 A  393  GLY ALA ARG
SEQRES   1 B  393  SER VAL GLN ALA THR ARG GLU ASP LYS PHE SER PHE GLY
SEQRES   2 B  393  LEU TRP THR VAL GLY TRP GLN ALA ARG ASP ALA PHE GLY
SEQRES   3 B  393  ASP ALA THR ARG THR ALA LEU ASP PRO VAL GLU ALA VAL
SEQRES   4 B  393  HIS LYS LEU ALA GLU ILE GLY ALA TYR GLY ILE THR PHE
SEQRES   5 B  393  HIS ASP ASP ASP LEU VAL PRO PHE GLY SER ASP ALA GLN
SEQRES   6 B  393  THR ARG ASP GLY ILE ILE ALA GLY PHE LYS LYS ALA LEU
SEQRES   7 B  393  ASP GLU THR GLY LEU ILE VAL PRO MET VAL THR THR ASN
SEQRES   8 B  393  LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 B  393  SER ASN ASP ARG SER VAL ARG ARG TYR ALA ILE ARG LYS
SEQRES  10 B  393  VAL LEU ARG GLN MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES  11 B  393  LYS THR LEU VAL LEU TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES  12 B  393  TYR ASP SER ALA LYS ASP VAL SER ALA ALA LEU ASP ARG
SEQRES  13 B  393  TYR ARG GLU ALA LEU ASN LEU LEU ALA GLN TYR SER GLU
SEQRES  14 B  393  ASP ARG GLY TYR GLY LEU ARG PHE ALA ILE GLU PRO LYS
SEQRES  15 B  393  PRO ASN GLN PRO ARG GLY ASP ILE LEU LEU PRO THR ALA
SEQRES  16 B  393  GLY HIS ALA ILE ALA PHE VAL GLN GLU LEU GLU ARG PRO
SEQRES  17 B  393  GLU LEU PHE GLY ILE ASN PRO GLU THR GLY HIS GLU GLN
SEQRES  18 B  393  MET SER ASN LEU ASN PHE THR GLN GLY ILE ALA GLN ALA
SEQRES  19 B  393  LEU TRP HIS LYS LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 B  393  GLN HIS GLY PRO LYS PHE ASP GLN ASP LEU VAL PHE GLY
SEQRES  21 B  393  HIS GLY ASP LEU LEU ASN ALA PHE SER LEU VAL ASP LEU
SEQRES  22 B  393  LEU GLU ASN GLY PRO ASP GLY ALA PRO ALA TYR ASP GLY
SEQRES  23 B  393  PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR GLU ASP
SEQRES  24 B  393  TYR ASP GLY VAL TRP GLU SER ALA LYS ALA ASN ILE ARG
SEQRES  25 B  393  MET TYR LEU LEU LEU LYS GLU ARG ALA LYS ALA PHE ARG
SEQRES  26 B  393  ALA ASP PRO GLU VAL GLN GLU ALA LEU ALA ALA SER LYS
SEQRES  27 B  393  VAL ALA GLU LEU LYS THR PRO THR LEU ASN PRO GLY GLU
SEQRES  28 B  393  GLY TYR ALA GLU LEU LEU ALA ASP ARG SER ALA PHE GLU
SEQRES  29 B  393  ASP TYR ASP ALA ASP ALA VAL GLY ALA LYS GLY PHE GLY
SEQRES  30 B  393  PHE VAL LYS LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU
SEQRES  31 B  393  GLY ALA ARG
SEQRES   1 C  393  SER VAL GLN ALA THR ARG GLU ASP LYS PHE SER PHE GLY
SEQRES   2 C  393  LEU TRP THR VAL GLY TRP GLN ALA ARG ASP ALA PHE GLY
SEQRES   3 C  393  ASP ALA THR ARG THR ALA LEU ASP PRO VAL GLU ALA VAL
SEQRES   4 C  393  HIS LYS LEU ALA GLU ILE GLY ALA TYR GLY ILE THR PHE
SEQRES   5 C  393  HIS ASP ASP ASP LEU VAL PRO PHE GLY SER ASP ALA GLN
SEQRES   6 C  393  THR ARG ASP GLY ILE ILE ALA GLY PHE LYS LYS ALA LEU
SEQRES   7 C  393  ASP GLU THR GLY LEU ILE VAL PRO MET VAL THR THR ASN
SEQRES   8 C  393  LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 C  393  SER ASN ASP ARG SER VAL ARG ARG TYR ALA ILE ARG LYS
SEQRES  10 C  393  VAL LEU ARG GLN MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES  11 C  393  LYS THR LEU VAL LEU TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES  12 C  393  TYR ASP SER ALA LYS ASP VAL SER ALA ALA LEU ASP ARG
SEQRES  13 C  393  TYR ARG GLU ALA LEU ASN LEU LEU ALA GLN TYR SER GLU
SEQRES  14 C  393  ASP ARG GLY TYR GLY LEU ARG PHE ALA ILE GLU PRO LYS
SEQRES  15 C  393  PRO ASN GLN PRO ARG GLY ASP ILE LEU LEU PRO THR ALA
SEQRES  16 C  393  GLY HIS ALA ILE ALA PHE VAL GLN GLU LEU GLU ARG PRO
SEQRES  17 C  393  GLU LEU PHE GLY ILE ASN PRO GLU THR GLY HIS GLU GLN
SEQRES  18 C  393  MET SER ASN LEU ASN PHE THR GLN GLY ILE ALA GLN ALA
SEQRES  19 C  393  LEU TRP HIS LYS LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 C  393  GLN HIS GLY PRO LYS PHE ASP GLN ASP LEU VAL PHE GLY
SEQRES  21 C  393  HIS GLY ASP LEU LEU ASN ALA PHE SER LEU VAL ASP LEU
SEQRES  22 C  393  LEU GLU ASN GLY PRO ASP GLY ALA PRO ALA TYR ASP GLY
SEQRES  23 C  393  PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR GLU ASP
SEQRES  24 C  393  TYR ASP GLY VAL TRP GLU SER ALA LYS ALA ASN ILE ARG
SEQRES  25 C  393  MET TYR LEU LEU LEU LYS GLU ARG ALA LYS ALA PHE ARG
SEQRES  26 C  393  ALA ASP PRO GLU VAL GLN GLU ALA LEU ALA ALA SER LYS
SEQRES  27 C  393  VAL ALA GLU LEU LYS THR PRO THR LEU ASN PRO GLY GLU
SEQRES  28 C  393  GLY TYR ALA GLU LEU LEU ALA ASP ARG SER ALA PHE GLU
SEQRES  29 C  393  ASP TYR ASP ALA ASP ALA VAL GLY ALA LYS GLY PHE GLY
SEQRES  30 C  393  PHE VAL LYS LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU
SEQRES  31 C  393  GLY ALA ARG
SEQRES   1 D  393  SER VAL GLN ALA THR ARG GLU ASP LYS PHE SER PHE GLY
SEQRES   2 D  393  LEU TRP THR VAL GLY TRP GLN ALA ARG ASP ALA PHE GLY
SEQRES   3 D  393  ASP ALA THR ARG THR ALA LEU ASP PRO VAL GLU ALA VAL
SEQRES   4 D  393  HIS LYS LEU ALA GLU ILE GLY ALA TYR GLY ILE THR PHE
SEQRES   5 D  393  HIS ASP ASP ASP LEU VAL PRO PHE GLY SER ASP ALA GLN
SEQRES   6 D  393  THR ARG ASP GLY ILE ILE ALA GLY PHE LYS LYS ALA LEU
SEQRES   7 D  393  ASP GLU THR GLY LEU ILE VAL PRO MET VAL THR THR ASN
SEQRES   8 D  393  LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 D  393  SER ASN ASP ARG SER VAL ARG ARG TYR ALA ILE ARG LYS
SEQRES  10 D  393  VAL LEU ARG GLN MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES  11 D  393  LYS THR LEU VAL LEU TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES  12 D  393  TYR ASP SER ALA LYS ASP VAL SER ALA ALA LEU ASP ARG
SEQRES  13 D  393  TYR ARG GLU ALA LEU ASN LEU LEU ALA GLN TYR SER GLU
SEQRES  14 D  393  ASP ARG GLY TYR GLY LEU ARG PHE ALA ILE GLU PRO LYS
SEQRES  15 D  393  PRO ASN GLN PRO ARG GLY ASP ILE LEU LEU PRO THR ALA
SEQRES  16 D  393  GLY HIS ALA ILE ALA PHE VAL GLN GLU LEU GLU ARG PRO
SEQRES  17 D  393  GLU LEU PHE GLY ILE ASN PRO GLU THR GLY HIS GLU GLN
SEQRES  18 D  393  MET SER ASN LEU ASN PHE THR GLN GLY ILE ALA GLN ALA
SEQRES  19 D  393  LEU TRP HIS LYS LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 D  393  GLN HIS GLY PRO LYS PHE ASP GLN ASP LEU VAL PHE GLY
SEQRES  21 D  393  HIS GLY ASP LEU LEU ASN ALA PHE SER LEU VAL ASP LEU
SEQRES  22 D  393  LEU GLU ASN GLY PRO ASP GLY ALA PRO ALA TYR ASP GLY
SEQRES  23 D  393  PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR GLU ASP
SEQRES  24 D  393  TYR ASP GLY VAL TRP GLU SER ALA LYS ALA ASN ILE ARG
SEQRES  25 D  393  MET TYR LEU LEU LEU LYS GLU ARG ALA LYS ALA PHE ARG
SEQRES  26 D  393  ALA ASP PRO GLU VAL GLN GLU ALA LEU ALA ALA SER LYS
SEQRES  27 D  393  VAL ALA GLU LEU LYS THR PRO THR LEU ASN PRO GLY GLU
SEQRES  28 D  393  GLY TYR ALA GLU LEU LEU ALA ASP ARG SER ALA PHE GLU
SEQRES  29 D  393  ASP TYR ASP ALA ASP ALA VAL GLY ALA LYS GLY PHE GLY
SEQRES  30 D  393  PHE VAL LYS LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU
SEQRES  31 D  393  GLY ALA ARG
HET    XLS  A 397      10
HET    XLS  B 397      10
HET    XLS  C 397      10
HET    XLS  D 397      10
HET     MG  A 395       1
HET     MG  B 395       1
HET     MG  C 395       1
HET     MG  D 395       1
HETNAM     XLS D-XYLOSE (LINEAR FORM)
HETNAM      MG MAGNESIUM ION
FORMUL   5  XLS    4(C5 H10 O5)
FORMUL   9   MG    4(MG 2+)
FORMUL  13  HOH   *971(H2 O)
HELIX    1   1 THR A    6  ASP A    9  5                                   4
HELIX    2   2 LEU A   15  GLY A   19  1                                   5
HELIX    3   3 ASP A   35  GLY A   47  1                                  13
HELIX    4   4 HIS A   54  VAL A   59  1                                   6
HELIX    5   5 ASP A   64  GLY A   83  1                                  20
HELIX    6   6 HIS A   96  LYS A  100  5                                   5
HELIX    7   7 ASP A  108  LEU A  129  1                                  22
HELIX    8   8 TYR A  145  LYS A  149  5                                   5
HELIX    9   9 ASP A  150  GLY A  173  1                                  24
HELIX   10  10 THR A  195  GLN A  204  1                                  10
HELIX   11  11 ARG A  208  GLU A  210  5                                   3
HELIX   12  12 GLU A  217  MET A  223  1                                   7
HELIX   13  13 ASN A  227  LYS A  239  1                                  13
HELIX   14  14 ASP A  264  ASN A  277  1                                  14
HELIX   15  15 GLY A  278  ALA A  282  5                                   5
HELIX   16  16 ASP A  300  ASP A  328  1                                  29
HELIX   17  17 ASP A  328  SER A  338  1                                  11
HELIX   18  18 LYS A  339  THR A  345  5                                   7
HELIX   19  19 GLY A  353  ALA A  359  1                                   7
HELIX   20  20 ASP A  360  PHE A  364  5                                   5
HELIX   21  21 ASP A  368  ALA A  374  1                                   7
HELIX   22  22 GLY A  378  LEU A  391  1                                  14
HELIX   23  23 THR B    6  ASP B    9  5                                   4
HELIX   24  24 LEU B   15  GLY B   19  1                                   5
HELIX   25  25 ASP B   35  GLY B   47  1                                  13
HELIX   26  26 HIS B   54  VAL B   59  1                                   6
HELIX   27  27 ASP B   64  GLY B   83  1                                  20
HELIX   28  28 HIS B   96  LYS B  100  5                                   5
HELIX   29  29 ASP B  108  GLY B  130  1                                  23
HELIX   30  30 TYR B  145  LYS B  149  5                                   5
HELIX   31  31 ASP B  150  ARG B  172  1                                  23
HELIX   32  32 THR B  195  GLN B  204  1                                  10
HELIX   33  33 ARG B  208  GLU B  210  5                                   3
HELIX   34  34 GLU B  217  MET B  223  1                                   7
HELIX   35  35 ASN B  227  LYS B  239  1                                  13
HELIX   36  36 ASP B  264  ASN B  277  1                                  14
HELIX   37  37 ASP B  300  ASP B  328  1                                  29
HELIX   38  38 ASP B  328  SER B  338  1                                  11
HELIX   39  39 LYS B  339  THR B  345  5                                   7
HELIX   40  40 GLY B  353  ASP B  360  1                                   8
HELIX   41  41 ARG B  361  PHE B  364  5                                   4
HELIX   42  42 ASP B  368  LYS B  375  1                                   8
HELIX   43  43 GLY B  378  LEU B  391  1                                  14
HELIX   44  44 THR C    6  ASP C    9  5                                   4
HELIX   45  45 LEU C   15  GLY C   19  1                                   5
HELIX   46  46 ASP C   35  GLY C   47  1                                  13
HELIX   47  47 HIS C   54  VAL C   59  1                                   6
HELIX   48  48 ASP C   64  GLY C   83  1                                  20
HELIX   49  49 HIS C   96  LYS C  100  5                                   5
HELIX   50  50 ASP C  108  GLY C  130  1                                  23
HELIX   51  51 TYR C  145  LYS C  149  5                                   5
HELIX   52  52 ASP C  150  GLY C  173  1                                  24
HELIX   53  53 THR C  195  GLN C  204  1                                  10
HELIX   54  54 ARG C  208  GLU C  210  5                                   3
HELIX   55  55 GLU C  217  MET C  223  1                                   7
HELIX   56  56 ASN C  227  HIS C  238  1                                  12
HELIX   57  57 ASP C  264  ASN C  277  1                                  14
HELIX   58  58 ASP C  300  ASP C  328  1                                  29
HELIX   59  59 ASP C  328  SER C  338  1                                  11
HELIX   60  60 LYS C  339  THR C  345  5                                   7
HELIX   61  61 GLY C  353  ASP C  360  1                                   8
HELIX   62  62 ARG C  361  PHE C  364  5                                   4
HELIX   63  63 ASP C  368  LYS C  375  1                                   8
HELIX   64  64 GLY C  378  LEU C  391  1                                  14
HELIX   65  65 THR D    6  ASP D    9  5                                   4
HELIX   66  66 LEU D   15  GLY D   19  1                                   5
HELIX   67  67 ASP D   35  ILE D   46  1                                  12
HELIX   68  68 HIS D   54  VAL D   59  1                                   6
HELIX   69  69 ASP D   64  GLY D   83  1                                  20
HELIX   70  70 HIS D   96  LYS D  100  5                                   5
HELIX   71  71 ASP D  108  GLY D  130  1                                  23
HELIX   72  72 TYR D  145  LYS D  149  5                                   5
HELIX   73  73 ASP D  150  GLY D  173  1                                  24
HELIX   74  74 THR D  195  GLN D  204  1                                  10
HELIX   75  75 ARG D  208  GLU D  210  5                                   3
HELIX   76  76 GLU D  217  MET D  223  1                                   7
HELIX   77  77 ASN D  227  LYS D  239  1                                  13
HELIX   78  78 ASP D  264  ASN D  277  1                                  14
HELIX   79  79 ASP D  300  ALA D  327  1                                  28
HELIX   80  80 ASP D  328  SER D  338  1                                  11
HELIX   81  81 VAL D  340  THR D  345  5                                   6
HELIX   82  82 GLY D  353  ASP D  360  1                                   8
HELIX   83  83 ARG D  361  PHE D  364  5                                   4
HELIX   84  84 ASP D  368  ALA D  374  1                                   7
HELIX   85  85 GLY D  378  LEU D  391  1                                  14
SHEET    1   A 4 GLY A  50  THR A  52  0
SHEET    2   A 4 PHE A  11  GLY A  14  1  O  PHE A  11   N  GLY A  50
SHEET    3   A 4 ARG A 289  PHE A 291  1  O  ARG A 289   N  SER A  12
SHEET    4   A 4 ASP A 245  LEU A 246  1  N  LEU A 246   O  HIS A 290
SHEET    1   B 4 MET A  88  THR A  90  0
SHEET    2   B 4 THR A 133  TRP A 137  1  O  THR A 133   N  VAL A  89
SHEET    3   B 4 ARG A 177  GLU A 181  1  O  ARG A 177   N  LEU A 134
SHEET    4   B 4 PHE A 212  ILE A 214  1  N  GLY A 213   O  PHE A 178
SHEET    1   C 2 GLY A 142  ALA A 143  0
SHEET    2   C 2 ASP A 190  ILE A 191 -1  O  ASP A 190   N  ALA A 143
SHEET    1   D 4 GLY B  50  THR B  52  0
SHEET    2   D 4 PHE B  11  GLY B  14  1  O  PHE B  11   N  GLY B  50
SHEET    3   D 4 ARG B 289  PHE B 291  1  O  ARG B 289   N  SER B  12
SHEET    4   D 4 ASP B 245  LEU B 246  1  N  LEU B 246   O  HIS B 290
SHEET    1   E 4 MET B  88  THR B  90  0
SHEET    2   E 4 THR B 133  TRP B 137  1  O  THR B 133   N  VAL B  89
SHEET    3   E 4 ARG B 177  GLU B 181  1  O  ARG B 177   N  LEU B 134
SHEET    4   E 4 PHE B 212  ILE B 214  1  N  GLY B 213   O  PHE B 178
SHEET    1   F 2 GLY B 142  ALA B 143  0
SHEET    2   F 2 ASP B 190  ILE B 191 -1  O  ASP B 190   N  ALA B 143
SHEET    1   G 4 GLY C  50  THR C  52  0
SHEET    2   G 4 PHE C  11  GLY C  14  1  O  PHE C  11   N  GLY C  50
SHEET    3   G 4 ARG C 289  PHE C 291  1  O  ARG C 289   N  SER C  12
SHEET    4   G 4 ASP C 245  LEU C 246  1  N  LEU C 246   O  HIS C 290
SHEET    1   H 4 MET C  88  THR C  90  0
SHEET    2   H 4 THR C 133  TRP C 137  1  O  THR C 133   N  VAL C  89
SHEET    3   H 4 ARG C 177  GLU C 181  1  O  ARG C 177   N  LEU C 134
SHEET    4   H 4 PHE C 212  ILE C 214  1  N  GLY C 213   O  PHE C 178
SHEET    1   I 2 GLY C 142  ALA C 143  0
SHEET    2   I 2 ASP C 190  ILE C 191 -1  O  ASP C 190   N  ALA C 143
SHEET    1   J 4 GLY D  50  THR D  52  0
SHEET    2   J 4 PHE D  11  GLY D  14  1  O  PHE D  11   N  GLY D  50
SHEET    3   J 4 ARG D 289  PHE D 291  1  O  ARG D 289   N  SER D  12
SHEET    4   J 4 ASP D 245  LEU D 246  1  N  LEU D 246   O  HIS D 290
SHEET    1   K 4 MET D  88  THR D  90  0
SHEET    2   K 4 THR D 133  LEU D 136  1  O  THR D 133   N  VAL D  89
SHEET    3   K 4 ARG D 177  ILE D 180  1  O  ARG D 177   N  LEU D 134
SHEET    4   K 4 PHE D 212  ILE D 214  1  N  GLY D 213   O  PHE D 178
SHEET    1   L 2 GLY D 142  ALA D 143  0
SHEET    2   L 2 ASP D 190  ILE D 191 -1  O  ASP D 190   N  ALA D 143
LINK        MG    MG A 395                 OD2 ASP A 292     1555   1555  2.11
LINK        MG    MG A 395                 OE1 GLU A 217     1555   1555  2.10
LINK        MG    MG A 395                 O2  XLS A 397     1555   1555  2.25
LINK        MG    MG A 395                 O4  XLS A 397     1555   1555  2.22
LINK        MG    MG A 395                 OE1 GLU A 181     1555   1555  3.08
LINK        MG    MG A 395                 OE2 GLU A 181     1555   1555  2.05
LINK        MG    MG A 395                 OD2 ASP A 245     1555   1555  1.95
LINK        MG    MG B 395                 O4  XLS B 397     1555   1555  2.19
LINK        MG    MG B 395                 OE2 GLU B 181     1555   1555  2.21
LINK        MG    MG B 395                 OD2 ASP B 245     1555   1555  2.07
LINK        MG    MG B 395                 O2  XLS B 397     1555   1555  2.19
LINK        MG    MG B 395                 OD2 ASP B 292     1555   1555  2.02
LINK        MG    MG B 395                 OE1 GLU B 217     1555   1555  2.01
LINK        MG    MG C 395                 OE1 GLU C 217     1555   1555  2.04
LINK        MG    MG C 395                 OD2 ASP C 245     1555   1555  2.00
LINK        MG    MG C 395                 O2  XLS C 397     1555   1555  2.16
LINK        MG    MG C 395                 O4  XLS C 397     1555   1555  2.23
LINK        MG    MG C 395                 OD2 ASP C 292     1555   1555  2.03
LINK        MG    MG C 395                 OE2 GLU C 181     1555   1555  2.17
LINK        MG    MG D 395                 OE2 GLU D 181     1555   1555  2.15
LINK        MG    MG D 395                 OD2 ASP D 245     1555   1555  2.07
LINK        MG    MG D 395                 O4  XLS D 397     1555   1555  2.21
LINK        MG    MG D 395                 OD2 ASP D 292     1555   1555  1.92
LINK        MG    MG D 395                 O2  XLS D 397     1555   1555  2.35
LINK        MG    MG D 395                 OE1 GLU D 217     1555   1555  2.03
CISPEP   1 GLN A  186    PRO A  187          0         3.86
CISPEP   2 GLN B  186    PRO B  187          0         3.60
CISPEP   3 GLN C  186    PRO C  187          0         4.25
CISPEP   4 GLN D  186    PRO D  187          0         4.65
SITE     1 AC1 16 TRP A  16  HIS A  54  TRP A 137  GLU A 181
SITE     2 AC1 16 LYS A 183  GLU A 217  HIS A 220  ASP A 245
SITE     3 AC1 16 ASP A 292   MG A 395  HOH A 398  HOH A 455
SITE     4 AC1 16 HOH A 456  HOH A 530  HOH A 564  PHE B  26
SITE     1 AC2 16 PHE A  26  TRP B  16  HIS B  54  TRP B 137
SITE     2 AC2 16 GLU B 181  LYS B 183  GLU B 217  HIS B 220
SITE     3 AC2 16 ASP B 245  ASP B 292   MG B 395  HOH B 404
SITE     4 AC2 16 HOH B 458  HOH B 459  HOH B 534  HOH B 561
SITE     1 AC3 16 TRP C  16  HIS C  54  TRP C 137  GLU C 181
SITE     2 AC3 16 LYS C 183  GLU C 217  HIS C 220  ASP C 245
SITE     3 AC3 16 ASP C 292   MG C 395  HOH C 416  HOH C 470
SITE     4 AC3 16 HOH C 471  HOH C 576  HOH C 581  PHE D  26
SITE     1 AC4 16 PHE C  26  TRP D  16  HIS D  54  TRP D 137
SITE     2 AC4 16 GLU D 181  LYS D 183  GLU D 217  HIS D 220
SITE     3 AC4 16 ASP D 245  ASP D 292   MG D 395  HOH D 429
SITE     4 AC4 16 HOH D 483  HOH D 484  HOH D 553  HOH D 589
SITE     1 AC5  5 GLU A 181  GLU A 217  ASP A 245  ASP A 292
SITE     2 AC5  5 XLS A 397
SITE     1 AC6  5 GLU B 181  GLU B 217  ASP B 245  ASP B 292
SITE     2 AC6  5 XLS B 397
SITE     1 AC7  5 GLU C 181  GLU C 217  ASP C 245  ASP C 292
SITE     2 AC7  5 XLS C 397
SITE     1 AC8  5 GLU D 181  GLU D 217  ASP D 245  ASP D 292
SITE     2 AC8  5 XLS D 397
CRYST1  143.450  143.450  231.500  90.00  90.00 120.00 P 32 2 1     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      0.006971  0.004025  0.000000        0.00000
SCALE2      0.000000  0.008049  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004320        0.00000
      
PROCHECK
Go to PROCHECK summary
 References