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PDBsum entry 3xis

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Isomerase(intramolecular oxidoreductase) PDB id
3xis
Jmol
Contents
Protein chain
386 a.a.
Ligands
XYS
XLS
Metals
_MG ×2
Waters ×362
HEADER    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)25-MAR-91   3XIS
TITLE     A METAL-MEDIATED HYDRIDE SHIFT MECHANISM FOR XYLOSE ISOMERASE BASED ON
TITLE    2 THE 1.6 ANGSTROMS STREPTOMYCES RUBIGINOSUS STRUCTURES WITH XYLITOL
TITLE    3 AND D-XYLOSE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: XYLOSE ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 5.3.1.5;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES RUBIGINOSUS;
SOURCE   3 ORGANISM_TAXID: 1929
KEYWDS    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.WHITLOW,A.J.HOWARD
REVDAT   4   13-JUL-11 3XIS    1       VERSN
REVDAT   3   24-FEB-09 3XIS    1       VERSN
REVDAT   2   01-APR-03 3XIS    1       JRNL
REVDAT   1   15-JUL-92 3XIS    0
JRNL        AUTH   M.WHITLOW,A.J.HOWARD,B.C.FINZEL,T.L.POULOS,E.WINBORNE,
JRNL        AUTH 2 G.L.GILLILAND
JRNL        TITL   A METAL-MEDIATED HYDRIDE SHIFT MECHANISM FOR XYLOSE
JRNL        TITL 2 ISOMERASE BASED ON THE 1.6 A STREPTOMYCES RUBIGINOSUS
JRNL        TITL 3 STRUCTURES WITH XYLITOL AND D-XYLOSE.
JRNL        REF    PROTEINS                      V.   9   153 1991
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   2006134
JRNL        DOI    10.1002/PROT.340090302
REMARK   2
REMARK   2 RESOLUTION.    1.60 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) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 43624
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) : 0.151
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            : 3027
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 22
REMARK   3   SOLVENT ATOMS            : 362
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) : 0.022 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 0.032 ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
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 3XIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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   (%): 56.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
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       47.32000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.98500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.98500
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.32000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.98500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.98500
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       47.32000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.98500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.98500
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       47.32000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.98500
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       51.98500
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 34260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -183.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       99.97000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      103.97000
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       99.97000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      103.97000
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     ASN A     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     GLU A  69    CD   OE1  OE2
REMARK 470     GLU A  70    CG   CD   OE1  OE2
REMARK 470     GLY A 388    CA   C    O
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    GLU A 132   CG    GLU A 132   CD     -0.105
REMARK 500    GLU A 373   CD    GLU A 373   OE1    -0.072
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  10   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A  23   CG  -  CD  -  NE  ANGL. DEV. =  18.9 DEGREES
REMARK 500    ARG A  23   CD  -  NE  -  CZ  ANGL. DEV. =  15.0 DEGREES
REMARK 500    ARG A  23   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A  41   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    GLU A  45   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES
REMARK 500    ASP A  56   CB  -  CG  -  OD1 ANGL. DEV. =   8.3 DEGREES
REMARK 500    ARG A  74   CD  -  NE  -  CZ  ANGL. DEV. =  12.7 DEGREES
REMARK 500    ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A  76   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A  76   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A 113   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ASP A 124   CB  -  CG  -  OD1 ANGL. DEV. =   9.2 DEGREES
REMARK 500    GLU A 132   CB  -  CG  -  CD  ANGL. DEV. =  45.5 DEGREES
REMARK 500    ARG A 152   CD  -  NE  -  CZ  ANGL. DEV. =  15.5 DEGREES
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG A 157   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    TYR A 174   CA  -  CB  -  CG  ANGL. DEV. =  11.7 DEGREES
REMARK 500    ARG A 177   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 177   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG A 188   NE  -  CZ  -  NH1 ANGL. DEV. =   8.0 DEGREES
REMARK 500    ARG A 188   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A 205   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 205   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A 208   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 259   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A 266   CD  -  NE  -  CZ  ANGL. DEV. =  19.1 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 284   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 284   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ASP A 295   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    GLU A 294   O   -  C   -  N   ANGL. DEV. =  10.7 DEGREES
REMARK 500    ARG A 331   CD  -  NE  -  CZ  ANGL. DEV. =   9.7 DEGREES
REMARK 500    ARG A 331   NE  -  CZ  -  NH1 ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG A 331   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ARG A 340   CG  -  CD  -  NE  ANGL. DEV. =  13.8 DEGREES
REMARK 500    ARG A 340   CD  -  NE  -  CZ  ANGL. DEV. =  20.2 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH1 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    ASP A 345   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 354   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES
REMARK 500    ARG A 368   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      54 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      -73.92    -83.94
REMARK 500    PHE A  94      -30.29   -136.95
REMARK 500    ASP A 175       72.57   -100.85
REMARK 500    GLU A 186      105.09     72.96
REMARK 500    ASN A 247     -166.40   -169.31
REMARK 500    LYS A 253     -170.24   -171.97
REMARK 500    PHE A 357      -70.96   -160.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A  23         0.12    SIDE CHAIN
REMARK 500    ARG A  41         0.19    SIDE CHAIN
REMARK 500    ARG A  76         0.14    SIDE CHAIN
REMARK 500    ARG A 117         0.09    SIDE CHAIN
REMARK 500    ARG A 177         0.10    SIDE CHAIN
REMARK 500    ARG A 208         0.11    SIDE CHAIN
REMARK 500    ARG A 321         0.09    SIDE CHAIN
REMARK 500    ARG A 331         0.08    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE A  94        24.0      L          L   OUTSIDE RANGE
REMARK 500    PHE A 296        23.4      L          L   OUTSIDE RANGE
REMARK 500    GLN A 348        24.6      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 683        DISTANCE =  5.26 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                              MG A 392  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 181   OE2
REMARK 620 2 GLU A 217   OE1 107.9
REMARK 620 3 ASP A 287   OD2 160.7  84.3
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 391  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 255   OD2
REMARK 620 2 HOH A 511   O   129.3
REMARK 620 N                    1
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEET S1 IS ACTUALLY AN EIGHT-STRANDED BETA BARREL.  THIS
REMARK 700 IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST
REMARK 700 AND LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYS A 393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYS A 393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 392
DBREF  3XIS A    2   388  UNP    P24300   XYLA_STRRU       1    387
SEQRES   1 A  387  ASN TYR GLN PRO THR PRO GLU ASP ARG PHE THR PHE GLY
SEQRES   2 A  387  LEU TRP THR VAL GLY TRP GLN GLY ARG ASP PRO PHE GLY
SEQRES   3 A  387  ASP ALA THR ARG ARG ALA LEU ASP PRO VAL GLU SER VAL
SEQRES   4 A  387  ARG ARG LEU ALA GLU LEU GLY ALA HIS GLY VAL THR PHE
SEQRES   5 A  387  HIS ASP ASP ASP LEU ILE PRO PHE GLY SER SER ASP SER
SEQRES   6 A  387  GLU ARG GLU GLU HIS VAL LYS ARG PHE ARG GLN ALA LEU
SEQRES   7 A  387  ASP ASP THR GLY MET LYS VAL PRO MET ALA THR THR ASN
SEQRES   8 A  387  LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 A  387  ALA ASN ASP ARG ASP VAL ARG ARG TYR ALA LEU ARG LYS
SEQRES  10 A  387  THR ILE ARG ASN ILE ASP LEU ALA VAL GLU LEU GLY ALA
SEQRES  11 A  387  GLU THR TYR VAL ALA TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES  12 A  387  SER GLY GLY ALA LYS ASP VAL ARG ASP ALA LEU ASP ARG
SEQRES  13 A  387  MET LYS GLU ALA PHE ASP LEU LEU GLY GLU TYR VAL THR
SEQRES  14 A  387  SER GLN GLY TYR ASP ILE ARG PHE ALA ILE GLU PRO LYS
SEQRES  15 A  387  PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR VAL
SEQRES  16 A  387  GLY HIS ALA LEU ALA PHE ILE GLU ARG LEU GLU ARG PRO
SEQRES  17 A  387  GLU LEU TYR GLY VAL ASN PRO GLU VAL GLY HIS GLU GLN
SEQRES  18 A  387  MET ALA GLY LEU ASN PHE PRO HIS GLY ILE ALA GLN ALA
SEQRES  19 A  387  LEU TRP ALA GLY LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 A  387  GLN ASN GLY ILE LYS TYR ASP GLN ASP LEU ARG PHE GLY
SEQRES  21 A  387  ALA GLY ASP LEU ARG ALA ALA PHE TRP LEU VAL ASP LEU
SEQRES  22 A  387  LEU GLU SER ALA GLY TYR SER GLY PRO ARG HIS PHE ASP
SEQRES  23 A  387  PHE LYS PRO PRO ARG THR GLU ASP PHE ASP GLY VAL TRP
SEQRES  24 A  387  ALA SER ALA ALA GLY CYS MET ARG ASN TYR LEU ILE LEU
SEQRES  25 A  387  LYS GLU ARG ALA ALA ALA PHE ARG ALA ASP PRO GLU VAL
SEQRES  26 A  387  GLN GLU ALA LEU ARG ALA SER ARG LEU ASP GLU LEU ALA
SEQRES  27 A  387  ARG PRO THR ALA ALA ASP GLY LEU GLN ALA LEU LEU ASP
SEQRES  28 A  387  ASP ARG SER ALA PHE GLU GLU PHE ASP VAL ASP ALA ALA
SEQRES  29 A  387  ALA ALA ARG GLY MET ALA PHE GLU ARG LEU ASP GLN LEU
SEQRES  30 A  387  ALA MET ASP HIS LEU LEU GLY ALA ARG GLY
HET    XYS  A 393      10
HET    XLS  A 393      10
HET     MG  A 391       1
HET     MG  A 392       1
HETNAM     XYS XYLOPYRANOSE
HETNAM     XLS D-XYLOSE (LINEAR FORM)
HETNAM      MG MAGNESIUM ION
FORMUL   2  XYS    C5 H10 O5
FORMUL   2  XLS    C5 H10 O5
FORMUL   3   MG    2(MG 2+)
FORMUL   5  HOH   *362(H2 O)
HELIX    1  H1 LEU A   34  ALA A   44  1                                  11
HELIX    2  H2 SER A   63  ASP A   80  1                                  18
HELIX    3  H3 ASN A  107  VAL A  127  1                                  21
HELIX    4  H4 ARG A  152  GLN A  172  1                                  21
HELIX    5  H5 PRO A  194  ALA A  201  1                                   8
HELIX    6  H6 PRO A  216  HIS A  220  1                                   5
HELIX    7  H7 LEU A  226  ALA A  235  1                                  10
HELIX    8  H8 GLY A  263  LEU A  275  1                                  13
HELIX    9  H9 GLU A  294  PHE A  320  1                                  27
HELIX   10 H10 ALA A  322  LEU A  330  1                                   9
HELIX   11 H11 ASP A  345  LEU A  350  1                                   6
HELIX   12 H12 ASP A  361  ALA A  365  1                                   5
HELIX   13 H13 MET A  370  HIS A  382  1                                  13
SHEET    1  S1 9 PHE A  11  GLY A  14  0
SHEET    2  S1 9 ALA A  48  THR A  52  1
SHEET    3  S1 9 VAL A  86  MET A  88  1
SHEET    4  S1 9 ALA A 131  TYR A 134  1
SHEET    5  S1 9 ASP A 175  PHE A 178  1
SHEET    6  S1 9 GLU A 210  TYR A 212  1
SHEET    7  S1 9 ASP A 245  LEU A 246  1
SHEET    8  S1 9 GLY A 282  HIS A 285  1
SHEET    9  S1 9 PHE A  11  GLY A  14  1
SHEET    1  S2 2 GLY A 142  ALA A 143  0
SHEET    2  S2 2 ARG A 188  GLY A 189  1
LINK         OE2 GLU A 181                MG    MG A 392     1555   1555  2.34
LINK         OE1 GLU A 217                MG    MG A 392     1555   1555  2.00
LINK         OD2 ASP A 255                MG    MG A 391     1555   1555  2.14
LINK         OD2 ASP A 287                MG    MG A 392     1555   1555  1.99
LINK        MG    MG A 391                 O   HOH A 511     1555   1555  1.84
CISPEP   1 GLU A  186    PRO A  187          0        12.12
SITE     1 AC1 19 TRP A  16  HIS A  54  VAL A 135  TRP A 137
SITE     2 AC1 19 GLU A 181  LYS A 183  GLU A 217  HIS A 220
SITE     3 AC1 19 ASP A 245  ASP A 287   MG A 391   MG A 392
SITE     4 AC1 19 XYS A 393  HOH A 448  HOH A 479  HOH A 511
SITE     5 AC1 19 HOH A 570  HOH A 637  HOH A 721
SITE     1 AC2 19 TRP A  16  HIS A  54  VAL A 135  TRP A 137
SITE     2 AC2 19 GLU A 181  LYS A 183  GLU A 217  HIS A 220
SITE     3 AC2 19 ASP A 245  ASP A 287   MG A 391   MG A 392
SITE     4 AC2 19 XYS A 393  HOH A 448  HOH A 479  HOH A 511
SITE     5 AC2 19 HOH A 570  HOH A 637  HOH A 721
SITE     1 AC3  8 GLU A 217  HIS A 220  ASP A 255  ASP A 257
SITE     2 AC3  8 XYS A 393  HOH A 511  HOH A 513  HOH A 721
SITE     1 AC4  5 GLU A 181  GLU A 217  ASP A 245  ASP A 287
SITE     2 AC4  5 XYS A 393
CRYST1   94.640   99.970  103.970  90.00  90.00  90.00 I 2 2 2       8
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      0.010566  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010003  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009618        0.00000
      
PROCHECK
Go to PROCHECK summary
 References