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PDBsum entry 1xyb

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Isomerase(intramolecular oxidoreductase) PDB id
1xyb
Jmol
Contents
Protein chains
386 a.a. *
Ligands
GLO ×2
Metals
_MG ×4
Waters ×481
* Residue conservation analysis
HEADER    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)03-JAN-94   1XYB
TITLE     X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE
TITLE    2 COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL
TITLE    3 MOVEMENT DURING CATALYSIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: XYLOSE ISOMERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 5.3.1.5;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES OLIVOCHROMOGENES;
SOURCE   3 ORGANISM_TAXID: 1963
KEYWDS    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.LAVIE,K.N.ALLEN,G.A.PETSKO,D.RINGE
REVDAT   3   13-JUL-11 1XYB    1       VERSN
REVDAT   2   24-FEB-09 1XYB    1       VERSN
REVDAT   1   31-MAY-94 1XYB    0
JRNL        AUTH   A.LAVIE,K.N.ALLEN,G.A.PETSKO,D.RINGE
JRNL        TITL   X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE
JRNL        TITL 2 ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND
JRNL        TITL 3 PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS.
JRNL        REF    BIOCHEMISTRY                  V.  33  5469 1994
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   8180169
JRNL        DOI    10.1021/BI00184A016
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.N.ALLEN,A.LAVIE,G.K.FARBER,A.GLASFELD,G.A.PETSKO,D.RINGE
REMARK   1  TITL   ISOTOPIC EXCHANGE PLUS SUBSTRATE AND INHIBITION KINETICS OF
REMARK   1  TITL 2 D-XYLOSE ISOMERASE DO NOT SUPPORT A PROTON-TRANSFER
REMARK   1  TITL 3 MECHANISM
REMARK   1  REF    BIOCHEMISTRY                  V.  33  1481 1994
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 2
REMARK   1  AUTH   K.N.ALLEN,A.LAVIE,A.GLASFELD,T.N.TANADA,D.P.GERRITY,
REMARK   1  AUTH 2 S.C.CARLSON,G.K.FARBER,G.A.PETSKO,D.RINGE
REMARK   1  TITL   THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING
REMARK   1  TITL 2 OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE:
REMARK   1  TITL 3 REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID
REMARK   1  REF    BIOCHEMISTRY                  V.  33  1488 1994
REMARK   1  REFN                   ISSN 0006-2960
REMARK   2
REMARK   2 RESOLUTION.    1.96 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) : 1.96
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
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             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.166
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6048
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 481
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 2.60
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.10
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 1XYB 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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
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       43.85000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.70000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.85000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.70000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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: 33100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -187.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
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  48   NE2   HIS A  48   CD2    -0.068
REMARK 500    HIS A  53   NE2   HIS A  53   CD2    -0.070
REMARK 500    HIS A  95   NE2   HIS A  95   CD2    -0.073
REMARK 500    HIS A 197   NE2   HIS A 197   CD2    -0.068
REMARK 500    HIS B 548   NE2   HIS B 548   CD2    -0.071
REMARK 500    HIS B 553   NE2   HIS B 553   CD2    -0.066
REMARK 500    HIS B 570   NE2   HIS B 570   CD2    -0.072
REMARK 500    HIS B 881   NE2   HIS B 881   CD2    -0.069
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    TRP A  15   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES
REMARK 500    TRP A  15   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500    TRP A  19   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    TRP A  19   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES
REMARK 500    ARG A  41   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A  73   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A  75   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    MET A  83   CG  -  SD  -  CE  ANGL. DEV. = -13.0 DEGREES
REMARK 500    ARG A 112   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 112   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 116   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 116   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    TRP A 136   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    TRP A 136   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A 156   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 176   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES
REMARK 500    ARG A 176   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    VAL A 195   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.7 DEGREES
REMARK 500    TRP A 236   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    TRP A 236   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES
REMARK 500    ASP A 254   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES
REMARK 500    ARG A 265   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 265   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    TRP A 269   CD1 -  CG  -  CD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    TRP A 269   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES
REMARK 500    TRP A 299   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP A 299   CB  -  CG  -  CD1 ANGL. DEV. =  -8.0 DEGREES
REMARK 500    TRP A 299   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A 299   CG  -  CD2 -  CE3 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A 367   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 367   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    TRP B 515   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    TRP B 515   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TRP B 519   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TRP B 519   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES
REMARK 500    GLY B 518   CA  -  C   -  N   ANGL. DEV. =  13.5 DEGREES
REMARK 500    ARG B 522   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    MET B 583   CG  -  SD  -  CE  ANGL. DEV. = -12.4 DEGREES
REMARK 500    ARG B 612   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG B 616   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG B 616   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    TRP B 636   CD1 -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES
REMARK 500    TRP B 636   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES
REMARK 500    ARG B 656   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    TRP B 736   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ASP B 754   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES
REMARK 500    ARG B 758   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG B 765   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES
REMARK 500    ARG B 765   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      58 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  16      -72.38    -84.66
REMARK 500    PHE A  93      -33.12   -135.38
REMARK 500    GLU A 185      106.41     69.70
REMARK 500    ASN A 246     -160.31   -169.35
REMARK 500    SER A 249       67.63   -110.76
REMARK 500    LYS A 252     -169.37   -168.50
REMARK 500    ALA A 342       75.55   -152.07
REMARK 500    PHE A 356      -67.01   -160.55
REMARK 500    THR B 516      -77.77    -85.43
REMARK 500    GLU B 685      110.54     69.99
REMARK 500    ARG B 707       71.51   -119.72
REMARK 500    ASN B 746     -160.86   -166.36
REMARK 500    SER B 749       68.22   -106.74
REMARK 500    LYS B 752     -170.79   -172.65
REMARK 500    ALA B 842       70.35   -150.06
REMARK 500    PHE B 856      -76.37   -151.05
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 B1340        DISTANCE =  5.14 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THERE IS ONE GLUCOSE MOLECULE IN THE OPEN FORM BOUND TO THE
REMARK 600 ENZYME IN EACH ACTIVE SITE LABELED GLO A 950 IN MONOMER 1
REMARK 600 AND GLO B 960 IN MONOMER 2.
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 400  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 180   OE1
REMARK 620 2 GLU A 180   OE2  45.1
REMARK 620 3 GLO A 950   O2   93.5  65.7
REMARK 620 4 GLU A 216   OE1 149.9 109.9  87.3
REMARK 620 5 ASP A 244   OD2  74.0 107.0 166.3 106.3
REMARK 620 6 ASP A 286   OD2 128.0 146.7  84.6  82.0  98.5
REMARK 620 7 GLO A 950   O4   64.0  83.3  63.0 139.6 105.5  69.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLO A 950   O1
REMARK 620 2 GLO A 950   O2   70.1
REMARK 620 3 GLU A 216   OE1 152.3  82.7
REMARK 620 4 GLU A 216   OE2 156.3 123.9  44.0
REMARK 620 5 HOH A1700   O    88.1  84.5  94.4 111.0
REMARK 620 6 HIS A 219   NE2  88.1  96.6  90.1  72.1 175.4
REMARK 620 7 ASP A 254   OD1  92.3 159.3 113.2  69.4 106.3  71.3
REMARK 620 8 ASP A 254   OD2  62.5 132.4 144.8 102.1  90.2  85.8  33.1
REMARK 620 9 ASP A 256   OD1 120.6 147.4  85.2  59.7  66.4 113.5  51.3  64.9
REMARK 620 N                    1     2     3     4     5     6     7     8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 900  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 680   OE2
REMARK 620 2 ASP B 744   OD2 105.2
REMARK 620 3 GLU B 716   OE1 109.5 111.0
REMARK 620 4 GLO B 960   O2   75.1 167.2  80.4
REMARK 620 5 ASP B 786   OD2 143.6 103.2  80.5  72.3
REMARK 620 6 GLO B 960   O4   84.2 105.6 135.2  61.7  66.5
REMARK 620 7 GLU B 680   OE1  45.6  70.2 150.1 103.0 129.1  67.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 901  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 719   NE2
REMARK 620 2 ASP B 754   OD1 100.6
REMARK 620 3 ASP B 756   OD1 156.1  91.7
REMARK 620 4 ASP B 754   OD2 101.7  54.4 102.1
REMARK 620 5 GLU B 716   OE1  68.3 146.4  90.2 156.4
REMARK 620 6 GLU B 716   OE2  70.0 113.7  86.3 165.1  33.0
REMARK 620 7 GLO B 960   O2   62.1 154.5 111.5 108.2  48.2  79.4
REMARK 620 8 GLO B 960   O1   64.2 114.7 128.3  66.8  89.7 117.4  42.3
REMARK 620 9 HOH B1800   O   102.5 145.0  77.2  95.1  67.7  98.8  40.9  55.4
REMARK 620 N                    1     2     3     4     5     6     7     8
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEETS PRESENTED AS *SA1*, *SA2*, *SB1*, AND *SB2* ON
REMARK 700 SHEET RECORDS BELOW ARE ACTUALLY EIGHT-STRANDED
REMARK 700 BETA-BARRELS.  THESE ARE REPRESENTED AS NINE-STRANDED
REMARK 700 SHEETS IN WHICH THE FIRST AND LAST STRANDS OF EACH SHEET
REMARK 700 ARE IDENTICAL.
REMARK 700 THERE ARE SEVERAL BIFURCATED SHEETS IN THIS STRUCTURE.
REMARK 700 THESE ARE REPRESENTED BY TWO SHEETS WHICH HAVE ONE OR MORE
REMARK 700 IDENTICAL STRANDS.  SHEETS *SA1* AND *SB1* REPRESENT ONE
REMARK 700 BIFURCATED SHEET.  SHEETS *SA2* AND *SB2* REPRESENT
REMARK 700 ANOTHER BIFURCATED SHEET.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: M1A
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: METAL BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: M2A
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: METAL BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: M1B
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: METAL BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: M2B
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: METAL BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLO A 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLO B 960
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 901
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE REPORTED HERE DISAGREES WITH THAT ORIGINALLY
REMARK 999 REPORTED (FARBER ET AL., BIOCHEMISTRY V. 28, P. 7289,
REMARK 999 1989) AND FOUND AS SWISS-PROT: XYLA_STROL AND PIR: S28986.
REMARK 999 A TOTAL OF 13 AMINO ACIDS WERE CHANGED, OF WHICH 5 WERE IN
REMARK 999 THE C-TERMINAL DOMAIN.  THE AUTHORS STATE THAT THIS
REMARK 999 CORRECTED SEQUENCE WILL BE INCLUDED IN THE SPRING 1994
REMARK 999 RELEASES OF THE SEQUENCE DATA BASES.  SEE THE JRNL
REMARK 999 REFERENCE ABOVE FOR MORE INFORMATION.
DBREF  1XYB A    1   386  UNP    P15587   XYLA_STROL       1    386
DBREF  1XYB B  501   886  UNP    P15587   XYLA_STROL       1    386
SEQRES   1 A  386  SER TYR GLN PRO THR PRO GLU ASP ARG PHE THR PHE GLY
SEQRES   2 A  386  LEU TRP THR VAL GLY TRP GLN GLY ARG ASP PRO PHE GLY
SEQRES   3 A  386  ASP ALA THR ARG PRO ALA LEU ASP PRO VAL GLU THR VAL
SEQRES   4 A  386  GLN ARG LEU ALA GLU LEU GLY ALA HIS GLY VAL THR PHE
SEQRES   5 A  386  HIS ASP ASP ASP LEU ILE PRO PHE GLY SER SER ASP THR
SEQRES   6 A  386  GLU ARG GLU SER HIS ILE LYS ARG PHE ARG GLN ALA LEU
SEQRES   7 A  386  ASP ALA THR GLY MET THR VAL PRO MET ALA THR THR ASN
SEQRES   8 A  386  LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 A  386  ALA ASN ASP ARG ASP VAL ARG ARG TYR ALA LEU ARG LYS
SEQRES  10 A  386  THR ILE ARG ASN ILE ASP LEU ALA VAL GLU LEU GLY ALA
SEQRES  11 A  386  LYS THR TYR VAL ALA TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES  12 A  386  SER GLY ALA ALA LYS ASP VAL ARG VAL ALA LEU ASP ARG
SEQRES  13 A  386  MET LYS GLU ALA PHE ASP LEU LEU GLY GLU TYR VAL THR
SEQRES  14 A  386  SER GLN GLY TYR ASP THR ARG PHE ALA ILE GLU PRO LYS
SEQRES  15 A  386  PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR VAL
SEQRES  16 A  386  GLY HIS ALA LEU ALA PHE ILE GLU ARG LEU GLU ARG PRO
SEQRES  17 A  386  GLU LEU TYR GLY VAL ASN PRO GLU VAL GLY HIS GLU GLN
SEQRES  18 A  386  MET ALA GLY LEU ASN PHE PRO HIS GLY ILE ALA GLN ALA
SEQRES  19 A  386  LEU TRP ALA GLY LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 A  386  GLN SER GLY ILE LYS TYR ASP GLN ASP LEU ARG PHE GLY
SEQRES  21 A  386  ALA GLY ASP LEU ARG ALA ALA PHE TRP LEU VAL ASP LEU
SEQRES  22 A  386  LEU GLU SER ALA GLY TYR GLU GLY PRO ARG HIS PHE ASP
SEQRES  23 A  386  PHE LYS PRO PRO ARG THR GLU ASP ILE ASP GLY VAL TRP
SEQRES  24 A  386  ALA SER ALA ALA GLY CYS MET ARG ASN TYR LEU ILE LEU
SEQRES  25 A  386  LYS GLU ARG ALA ALA ALA PHE ARG ALA ASP PRO GLU VAL
SEQRES  26 A  386  GLN GLU ALA LEU ARG ALA SER ARG LEU ASP GLU LEU ALA
SEQRES  27 A  386  GLN PRO THR ALA ALA ASP GLY VAL GLN GLU LEU LEU ALA
SEQRES  28 A  386  ASP ARG THR ALA PHE GLU ASP PHE ASP VAL ASP ALA ALA
SEQRES  29 A  386  ALA ALA ARG GLY MET ALA PHE GLU ARG LEU ASP GLN LEU
SEQRES  30 A  386  ALA MET ASP HIS LEU LEU GLY ALA ARG
SEQRES   1 B  386  SER TYR GLN PRO THR PRO GLU ASP ARG PHE THR PHE GLY
SEQRES   2 B  386  LEU TRP THR VAL GLY TRP GLN GLY ARG ASP PRO PHE GLY
SEQRES   3 B  386  ASP ALA THR ARG PRO ALA LEU ASP PRO VAL GLU THR VAL
SEQRES   4 B  386  GLN ARG LEU ALA GLU LEU GLY ALA HIS GLY VAL THR PHE
SEQRES   5 B  386  HIS ASP ASP ASP LEU ILE PRO PHE GLY SER SER ASP THR
SEQRES   6 B  386  GLU ARG GLU SER HIS ILE LYS ARG PHE ARG GLN ALA LEU
SEQRES   7 B  386  ASP ALA THR GLY MET THR VAL PRO MET ALA THR THR ASN
SEQRES   8 B  386  LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 B  386  ALA ASN ASP ARG ASP VAL ARG ARG TYR ALA LEU ARG LYS
SEQRES  10 B  386  THR ILE ARG ASN ILE ASP LEU ALA VAL GLU LEU GLY ALA
SEQRES  11 B  386  LYS THR TYR VAL ALA TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES  12 B  386  SER GLY ALA ALA LYS ASP VAL ARG VAL ALA LEU ASP ARG
SEQRES  13 B  386  MET LYS GLU ALA PHE ASP LEU LEU GLY GLU TYR VAL THR
SEQRES  14 B  386  SER GLN GLY TYR ASP THR ARG PHE ALA ILE GLU PRO LYS
SEQRES  15 B  386  PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR VAL
SEQRES  16 B  386  GLY HIS ALA LEU ALA PHE ILE GLU ARG LEU GLU ARG PRO
SEQRES  17 B  386  GLU LEU TYR GLY VAL ASN PRO GLU VAL GLY HIS GLU GLN
SEQRES  18 B  386  MET ALA GLY LEU ASN PHE PRO HIS GLY ILE ALA GLN ALA
SEQRES  19 B  386  LEU TRP ALA GLY LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 B  386  GLN SER GLY ILE LYS TYR ASP GLN ASP LEU ARG PHE GLY
SEQRES  21 B  386  ALA GLY ASP LEU ARG ALA ALA PHE TRP LEU VAL ASP LEU
SEQRES  22 B  386  LEU GLU SER ALA GLY TYR GLU GLY PRO ARG HIS PHE ASP
SEQRES  23 B  386  PHE LYS PRO PRO ARG THR GLU ASP ILE ASP GLY VAL TRP
SEQRES  24 B  386  ALA SER ALA ALA GLY CYS MET ARG ASN TYR LEU ILE LEU
SEQRES  25 B  386  LYS GLU ARG ALA ALA ALA PHE ARG ALA ASP PRO GLU VAL
SEQRES  26 B  386  GLN GLU ALA LEU ARG ALA SER ARG LEU ASP GLU LEU ALA
SEQRES  27 B  386  GLN PRO THR ALA ALA ASP GLY VAL GLN GLU LEU LEU ALA
SEQRES  28 B  386  ASP ARG THR ALA PHE GLU ASP PHE ASP VAL ASP ALA ALA
SEQRES  29 B  386  ALA ALA ARG GLY MET ALA PHE GLU ARG LEU ASP GLN LEU
SEQRES  30 B  386  ALA MET ASP HIS LEU LEU GLY ALA ARG
HET    GLO  A 950      12
HET    GLO  B 960      12
HET     MG  A 400       1
HET     MG  A 401       2
HET     MG  B 900       1
HET     MG  B 901       2
HETNAM     GLO D-GLUCOSE IN LINEAR FORM
HETNAM      MG MAGNESIUM ION
FORMUL   3  GLO    2(C6 H12 O6)
FORMUL   5   MG    4(MG 2+)
FORMUL   9  HOH   *481(H2 O)
HELIX    1  H1 LEU A   14  TRP A   19  1IN ALPHA/BETA BARREL               6
HELIX    2  H2 PRO A   35  LEU A   45  1IN ALPHA/BETA BARREL              11
HELIX    3  H3 ASP A   64  THR A   81  1IN ALPHA/BETA BARREL              18
HELIX    4  H4 ARG A  108  LEU A  128  1IN ALPHA/BETA BARREL              21
HELIX    5  H5 VAL A  150  GLN A  171  1IN ALPHA/BETA BARREL              22
HELIX    6  H6 VAL A  195  ARG A  204  1IN ALPHA/BETA BARREL              10
HELIX    7  H7 VAL A  217  ALA A  223  1IN ALPHA/BETA BARREL               7
HELIX    8  H8 PHE A  227  ALA A  237  1IN ALPHA/BETA BARREL              11
HELIX    9  H9 ARG A  265  SER A  276  1IN ALPHA/BETA BARREL              12
HELIX   10 H10 ILE A  295  ALA A  321  1IN ALPHA/BETA BARREL              27
HELIX   11 H11 GLU A  324  ALA A  331  1IN ALPHA/BETA BARREL               8
HELIX   12 H12 LEU A  334  ALA A  338  1IN ALPHA/BETA BARREL               5
HELIX   13 H13 VAL A  346  ASP A  352  1IN ALPHA/BETA BARREL               7
HELIX   14 H14 VAL A  361  ALA A  366  1IN ALPHA/BETA BARREL               6
HELIX   15 H15 PHE A  371  LEU A  382  1IN ALPHA/BETA BARREL              12
HELIX   16 H16 LEU B  514  TRP B  519  1IN ALPHA/BETA BARREL               6
HELIX   17 H17 PRO B  535  LEU B  545  1IN ALPHA/BETA BARREL              11
HELIX   18 H18 ASP B  564  THR B  581  1IN ALPHA/BETA BARREL              18
HELIX   19 H19 ARG B  608  LEU B  628  1IN ALPHA/BETA BARREL              21
HELIX   20 H20 VAL B  650  GLN B  671  1IN ALPHA/BETA BARREL              22
HELIX   21 H21 VAL B  695  ARG B  704  1IN ALPHA/BETA BARREL              10
HELIX   22 H22 VAL B  717  ALA B  723  1IN ALPHA/BETA BARREL               7
HELIX   23 H23 PHE B  727  ALA B  737  1IN ALPHA/BETA BARREL              11
HELIX   24 H24 ARG B  765  SER B  776  1IN ALPHA/BETA BARREL              12
HELIX   25 H25 ILE B  795  ALA B  821  1IN ALPHA/BETA BARREL              27
HELIX   26 H26 GLU B  824  ALA B  831  1IN C-TERMINAL DOMAIN               8
HELIX   27 H27 LEU B  834  ALA B  838  1IN C-TERMINAL DOMAIN               5
HELIX   28 H28 VAL B  846  ASP B  852  1IN C-TERMINAL DOMAIN               7
HELIX   29 H29 VAL B  861  ALA B  866  1IN C-TERMINAL DOMAIN               6
HELIX   30 H30 PHE B  871  LEU B  882  1IN C-TERMINAL DOMAIN              12
SHEET    1 SA1 9 PHE A  10  GLY A  13  0
SHEET    2 SA1 9 GLY A  49  HIS A  53  1
SHEET    3 SA1 9 THR A  84  THR A  90  1
SHEET    4 SA1 9 THR A 132  GLY A 138  1
SHEET    5 SA1 9 ARG A 176  PRO A 183  1
SHEET    6 SA1 9 TYR A 211  GLU A 216  1
SHEET    7 SA1 9 PHE A 241  ASN A 246  1
SHEET    8 SA1 9 ARG A 283  ASP A 286  1
SHEET    9 SA1 9 PHE A  10  GLY A  13  1
SHEET    1 SA2 9 PHE A  10  GLY A  13  0
SHEET    2 SA2 9 GLY A  49  HIS A  53  1
SHEET    3 SA2 9 THR A  84  THR A  90  1
SHEET    4 SA2 9 GLU A 140  GLU A 143  1
SHEET    5 SA2 9 ARG A 176  PRO A 183  1
SHEET    6 SA2 9 TYR A 211  GLU A 216  1
SHEET    7 SA2 9 PHE A 241  ASN A 246  1
SHEET    8 SA2 9 GLY A 278  GLY A 281  1
SHEET    9 SA2 9 PHE A  10  GLY A  13  1
SHEET    1 SB1 9 PHE B 510  GLY B 513  0
SHEET    2 SB1 9 GLY B 549  HIS B 553  1
SHEET    3 SB1 9 THR B 584  THR B 590  1
SHEET    4 SB1 9 THR B 632  GLY B 638  1
SHEET    5 SB1 9 ARG B 676  PRO B 683  1
SHEET    6 SB1 9 TYR B 711  GLU B 716  1
SHEET    7 SB1 9 PHE B 741  ASN B 746  1
SHEET    8 SB1 9 ARG B 783  ASP B 786  1
SHEET    9 SB1 9 PHE B 510  GLY B 513  1
SHEET    1 SB2 9 PHE B 510  GLY B 513  0
SHEET    2 SB2 9 GLY B 549  HIS B 553  1
SHEET    3 SB2 9 THR B 584  THR B 590  1
SHEET    4 SB2 9 GLU B 640  GLU B 643  1
SHEET    5 SB2 9 ARG B 676  PRO B 683  1
SHEET    6 SB2 9 TYR B 711  GLU B 716  1
SHEET    7 SB2 9 PHE B 741  ASN B 746  1
SHEET    8 SB2 9 GLY B 778  GLY B 781  1
SHEET    9 SB2 9 PHE B 510  GLY B 513  1
LINK        MG    MG A 400                 OE1 GLU A 180     1555   1555  3.01
LINK        MG    MG A 400                 OE2 GLU A 180     1555   1555  2.44
LINK        MG    MG A 400                 O2  GLO A 950     1555   1555  2.70
LINK        MG    MG A 400                 OE1 GLU A 216     1555   1555  2.36
LINK        MG    MG A 400                 OD2 ASP A 244     1555   1555  2.37
LINK        MG    MG A 400                 OD2 ASP A 286     1555   1555  2.41
LINK        MG    MG A 400                 O4  GLO A 950     1555   1555  2.51
LINK        MG  B MG A 401                 O1  GLO A 950     1555   1555  2.32
LINK        MG  B MG A 401                 O2  GLO A 950     1555   1555  2.38
LINK        MG  B MG A 401                 OE1 GLU A 216     1555   1555  2.88
LINK        MG  B MG A 401                 OE2 GLU A 216     1555   1555  2.74
LINK        MG  B MG A 401                 O   HOH A1700     1555   1555  2.36
LINK        MG  A MG A 401                 NE2 HIS A 219     1555   1555  2.86
LINK        MG  A MG A 401                 OD1 ASP A 254     1555   1555  2.38
LINK        MG  A MG A 401                 OD2 ASP A 254     1555   1555  2.45
LINK        MG  A MG A 401                 OE2 GLU A 216     1555   1555  2.51
LINK        MG  A MG A 401                 OD1 ASP A 256     1555   1555  2.41
LINK        MG  A MG A 401                 O   HOH A1700     1555   1555  3.07
LINK        MG  B MG A 401                 NE2 HIS A 219     1555   1555  2.38
LINK        MG    MG B 900                 OE2 GLU B 680     1555   1555  2.40
LINK        MG    MG B 900                 OD2 ASP B 744     1555   1555  2.35
LINK        MG    MG B 900                 OE1 GLU B 716     1555   1555  2.35
LINK        MG    MG B 900                 O2  GLO B 960     1555   1555  2.56
LINK        MG    MG B 900                 OD2 ASP B 786     1555   1555  2.43
LINK        MG    MG B 900                 O4  GLO B 960     1555   1555  2.54
LINK        MG    MG B 900                 OE1 GLU B 680     1555   1555  2.99
LINK        MG  A MG B 901                 NE2 HIS B 719     1555   1555  2.72
LINK        MG  A MG B 901                 OD1 ASP B 754     1555   1555  2.41
LINK        MG  A MG B 901                 OD1 ASP B 756     1555   1555  2.43
LINK        MG  A MG B 901                 OD2 ASP B 754     1555   1555  2.45
LINK        MG  B MG B 901                 OE1 GLU B 716     1555   1555  2.73
LINK        MG  B MG B 901                 OE2 GLU B 716     1555   1555  2.60
LINK        MG  B MG B 901                 NE2 HIS B 719     1555   1555  2.44
LINK        MG  B MG B 901                 O2  GLO B 960     1555   1555  2.39
LINK        MG  B MG B 901                 O1  GLO B 960     1555   1555  2.35
LINK        MG  B MG B 901                 O   HOH B1800     1555   1555  2.43
LINK        MG  A MG B 901                 OE2 GLU B 716     1555   1555  2.46
CISPEP   1 GLU A  185    PRO A  186          0        16.78
CISPEP   2 GLU B  685    PRO B  686          0        13.24
SITE     1 M1A  5  MG A 400  GLU A 180  ASP A 244  ASP A 286
SITE     2 M1A  5 GLU A 216
SITE     1 M2A  6  MG A 401  GLU A 216  HIS A 219  ASP A 254
SITE     2 M2A  6 ASP A 256  HOH A1700
SITE     1 M1B  5  MG B 900  GLU B 680  ASP B 744  ASP B 786
SITE     2 M1B  5 GLU B 716
SITE     1 M2B  6  MG B 901  GLU B 716  HIS B 719  ASP B 754
SITE     2 M2B  6 ASP B 756  HOH B1800
SITE     1 AC1 16 HIS A  53  THR A  89  PHE A  93  VAL A 134
SITE     2 AC1 16 TRP A 136  GLU A 180  LYS A 182  GLU A 216
SITE     3 AC1 16 HIS A 219  ASP A 254  ASP A 286   MG A 400
SITE     4 AC1 16  MG A 401  HOH A1292  HOH A1700  PHE B 525
SITE     1 AC2 17 PHE A  25  HIS B 553  THR B 589  PHE B 593
SITE     2 AC2 17 VAL B 634  TRP B 636  GLU B 680  LYS B 682
SITE     3 AC2 17 GLU B 716  HIS B 719  ASP B 754  ASP B 786
SITE     4 AC2 17  MG B 900   MG B 901  HOH B1146  HOH B1149
SITE     5 AC2 17 HOH B1800
SITE     1 AC3  5 GLU A 180  GLU A 216  ASP A 244  ASP A 286
SITE     2 AC3  5 GLO A 950
SITE     1 AC4  6 GLU A 216  HIS A 219  ASP A 254  ASP A 256
SITE     2 AC4  6 GLO A 950  HOH A1700
SITE     1 AC5  5 GLU B 680  GLU B 716  ASP B 744  ASP B 786
SITE     2 AC5  5 GLO B 960
SITE     1 AC6  6 GLU B 716  HIS B 719  ASP B 754  ASP B 756
SITE     2 AC6  6 GLO B 960  HOH B1800
CRYST1   87.700   99.400   94.200  90.00  90.00  90.00 P 21 21 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      0.011403  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010060  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010616        0.00000
MTRIX1   1  0.999270  0.038290 -0.000450       -0.02028    1
MTRIX2   1  0.038290 -0.999270  0.001000        0.02478    1
MTRIX3   1 -0.000410 -0.001020 -1.000000      -47.31872    1
      
PROCHECK
Go to PROCHECK summary
 References