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PDBsum entry 1xld

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Top Page protein ligands metals Protein-protein interface(s) links
Isomerase(intramolecular oxidoreductase) PDB id
1xld
Jmol
Contents
Protein chains
393 a.a. *
Ligands
XYL ×2
Metals
_MN ×4
Waters ×500
* Residue conservation analysis
HEADER    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)09-OCT-91   1XLD
TITLE     MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE
TITLE    2 INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-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: ARTHROBACTER SP.;
SOURCE   3 ORGANISM_TAXID: 1669;
SOURCE   4 STRAIN: NRRL B3728
KEYWDS    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.A.COLLYER,K.HENRICK,D.M.BLOW
REVDAT   3   13-JUL-11 1XLD    1       VERSN
REVDAT   2   24-FEB-09 1XLD    1       VERSN
REVDAT   1   15-JUL-93 1XLD    0
JRNL        AUTH   C.A.COLLYER,K.HENRICK,D.M.BLOW
JRNL        TITL   MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE
JRNL        TITL 2 ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE
JRNL        TITL 3 SHIFT.
JRNL        REF    J.MOL.BIOL.                   V. 212   211 1990
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   2319597
JRNL        DOI    10.1016/0022-2836(90)90316-E
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   C.A.COLLYER,D.M.BLOW
REMARK   1  TITL   OBSERVATIONS OF REACTION INTERMEDIATES AND THE MECHANISM OF
REMARK   1  TITL 2 ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  87  1362 1990
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1 REFERENCE 2
REMARK   1  AUTH   K.HENRICK,D.M.BLOW,H.L.CARRELL,J.P.GLUSKER
REMARK   1  TITL   COMPARISON OF BACKBONE STRUCTURES OF GLUCOSE ISOMERASE FROM
REMARK   1  TITL 2 STREPTOMYCES AND ARTHROBACTER
REMARK   1  REF    PROTEIN ENG.                  V.   1   467 1987
REMARK   1  REFN                   ISSN 0269-2139
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.AKINS,P.BRICK,H.B.JONES,N.HIRAYAMA,P.-C.SHAW,D.M.BLOW
REMARK   1  TITL   THE CRYSTALLIZATION OF GLUCOSE ISOMERASE FROM ARTHROBACTER
REMARK   1  TITL 2 B3728
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V. 874   375 1986
REMARK   1  REFN                   ISSN 0006-3002
REMARK   2
REMARK   2 RESOLUTION.    2.50 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) : 2.50
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             : 31814
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) : 0.148
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            : 6054
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 24
REMARK   3   SOLVENT ATOMS            : 500
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) : 0.018 ; 0.025
REMARK   3    ANGLE DISTANCE                  (A) : 0.044 ; 0.040
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.049 ; 0.050
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.014 ; 0.020
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.160 ; 0.150
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.160 ; 0.200
REMARK   3    MULTIPLE TORSION                (A) : 0.220 ; 0.200
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) : 16.500; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.900 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.400 ; 2.000
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.800 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 2.700 ; 3.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  THIS IS MODEL(15) AS DESCRIBED IN THE JRNL RECORDS ABOVE.
REMARK   3  EACH OF THE TWO MONOMERS OF THE TETRAMER IN THE ASYMMETRIC
REMARK   3  UNIT HAS TWO BOUND MN++ AND ONE BOUND D-XYLOSE AT PH 8.
REMARK   3
REMARK   3  THE B-FACTORS QUOTED FOR MN IN THE JRNL REFERENCE ARE
REMARK   3  INCORRECT.
REMARK   4
REMARK   4 1XLD 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   (%): 56.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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       51.16667
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      102.33333
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      102.33333
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       51.16667
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: 34290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 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 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     1
REMARK 465     SER B     1
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   3    CG   CD   OE1  NE2
REMARK 470     LYS A  31    CG   CD   CE   NZ
REMARK 470     GLU A  64    CG   CD   OE1  OE2
REMARK 470     LYS A  79    CG   CD   CE   NZ
REMARK 470     GLN B   3    CG   CD   OE1  NE2
REMARK 470     LYS B  31    CG   CD   CE   NZ
REMARK 470     GLU B  64    CG   CD   OE1  OE2
REMARK 470     LYS B  79    CG   CD   CE   NZ
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 B 238   CB    GLU B 238   CG      0.124
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    PRO A   6   O   -  C   -  N   ANGL. DEV. = -10.8 DEGREES
REMARK 500    ALA A   7   C   -  N   -  CA  ANGL. DEV. =  21.7 DEGREES
REMARK 500    ASP A   8   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ASP A   8   CB  -  CG  -  OD2 ANGL. DEV. =   8.9 DEGREES
REMARK 500    THR A  20   N   -  CA  -  CB  ANGL. DEV. = -11.6 DEGREES
REMARK 500    ASP A  23   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES
REMARK 500    ASP A  23   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ASP A  34   CB  -  CG  -  OD1 ANGL. DEV. =   9.1 DEGREES
REMARK 500    THR A  51   CA  -  CB  -  CG2 ANGL. DEV. =  11.6 DEGREES
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =  23.0 DEGREES
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG A  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    GLU A  68   OE1 -  CD  -  OE2 ANGL. DEV. =   9.3 DEGREES
REMARK 500    ASP A  73   CB  -  CG  -  OD2 ANGL. DEV. =  -7.8 DEGREES
REMARK 500    ARG A 108   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 DEGREES
REMARK 500    ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG A 112   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES
REMARK 500    PHE A 113   CB  -  CG  -  CD2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    LEU A 115   CB  -  CA  -  C   ANGL. DEV. =  12.5 DEGREES
REMARK 500    ARG A 139   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    TYR A 144   CB  -  CG  -  CD2 ANGL. DEV. =   4.5 DEGREES
REMARK 500    TYR A 144   CB  -  CG  -  CD1 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    ASP A 145   CB  -  CG  -  OD1 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ASP A 149   N   -  CA  -  CB  ANGL. DEV. =  14.5 DEGREES
REMARK 500    ASP A 149   CB  -  CG  -  OD1 ANGL. DEV. =   9.4 DEGREES
REMARK 500    ASP A 149   N   -  CA  -  C   ANGL. DEV. = -17.0 DEGREES
REMARK 500    ASP A 170   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TYR A 173   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    TYR A 173   CB  -  CG  -  CD1 ANGL. DEV. =   5.3 DEGREES
REMARK 500    ARG A 176   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH1 ANGL. DEV. =   7.6 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.2 DEGREES
REMARK 500    VAL A 211   CA  -  CB  -  CG2 ANGL. DEV. =   9.8 DEGREES
REMARK 500    PHE A 241   CB  -  CG  -  CD2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    PHE A 241   CB  -  CG  -  CD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG A 249   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ASP A 256   CB  -  CG  -  OD1 ANGL. DEV. =   8.5 DEGREES
REMARK 500    GLY A 262   C   -  N   -  CA  ANGL. DEV. =  15.0 DEGREES
REMARK 500    LEU A 273   CA  -  CB  -  CG  ANGL. DEV. =  16.9 DEGREES
REMARK 500    ARG A 297   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ASP A 299   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES
REMARK 500    TYR A 301   CB  -  CG  -  CD2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ARG A 321   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 326   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    GLU A 342   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES
REMARK 500    GLU A 342   N   -  CA  -  CB  ANGL. DEV. =  15.3 DEGREES
REMARK 500    GLU A 342   CA  -  CB  -  CG  ANGL. DEV. =  24.6 DEGREES
REMARK 500    GLU A 342   OE1 -  CD  -  OE2 ANGL. DEV. =   7.9 DEGREES
REMARK 500    ASN A 359   CA  -  CB  -  CG  ANGL. DEV. =  27.7 DEGREES
REMARK 500    ALA A 372   O   -  C   -  N   ANGL. DEV. = -11.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     111 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    HIS A   9       44.52     71.65
REMARK 500    THR A  16      -71.60    -70.46
REMARK 500    GLU A 185      110.98     70.75
REMARK 500    HIS A 207       45.86   -106.35
REMARK 500    ARG A 249       69.55   -110.72
REMARK 500    LYS A 252     -162.95   -169.61
REMARK 500    PHE A 364      -79.89   -139.15
REMARK 500    GLN B   3       96.63     78.06
REMARK 500    ASP B  23     -166.28   -120.39
REMARK 500    ALA B  62      137.15    -34.63
REMARK 500    PHE B  93      -22.95   -147.45
REMARK 500    GLU B 185      111.19     70.19
REMARK 500    LEU B 192       61.63     60.27
REMARK 500    ASN B 246     -168.09   -166.88
REMARK 500    LYS B 252     -162.95   -165.64
REMARK 500    PHE B 364      -77.58   -138.31
REMARK 500    ARG B 375      125.16    -36.22
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    GLU A 342        24.9      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 567A       DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH A 664A       DISTANCE =  6.96 ANGSTROMS
REMARK 525    HOH A 679A       DISTANCE =  5.61 ANGSTROMS
REMARK 525    HOH A 725A       DISTANCE =  6.17 ANGSTROMS
REMARK 525    HOH A 727A       DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH B 647B       DISTANCE =  6.75 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                              MN A 398  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 254   OD2
REMARK 620 2 HOH A 519A  O    88.5
REMARK 620 3 HIS A 219   NE2  97.1 110.9
REMARK 620 4 ASP A 254   OD1  55.7 137.5  96.9
REMARK 620 5 GLU A 216   OE2 155.3 114.1  84.3  99.6
REMARK 620 6 ASP A 256   OD1  90.2  78.0 168.5  79.8  85.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A 399  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 180   OE2
REMARK 620 2 GLU A 216   OE1  94.6
REMARK 620 3 ASP A 244   OD2  96.7 111.5
REMARK 620 4 ASP A 292   OD2 160.9  84.8 101.4
REMARK 620 5 XYL A 400   O2   84.9  80.6 167.5  76.1
REMARK 620 6 XYL A 400   O4   86.5 153.3  94.8  85.6  72.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 398  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 254   OD1
REMARK 620 2 ASP B 254   OD2  55.9
REMARK 620 3 HOH B 519B  O   145.0  93.7
REMARK 620 4 GLU B 216   OE2 101.1 155.3 110.9
REMARK 620 5 ASP B 256   OD1  82.1  98.9  86.7  85.1
REMARK 620 6 HIS B 219   NE2  93.9  95.6 107.3  75.5 159.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 399  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 XYL B 400   O2
REMARK 620 2 XYL B 400   O4   75.2
REMARK 620 3 GLU B 216   OE1  84.1 157.7
REMARK 620 4 ASP B 244   OD2 164.0  89.2 110.6
REMARK 620 5 ASP B 292   OD2  76.0  86.8  80.1  99.6
REMARK 620 6 GLU B 180   OE2  79.9  85.7  99.0 103.2 155.8
REMARK 620 N                    1     2     3     4     5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE TWO SHEETS PRESENTED AS *BAA* AND *BAB* ON SHEET
REMARK 700 RECORDS BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS.
REMARK 700 EACH IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE
REMARK 700 FIRST 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 XYL A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYL B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 399
DBREF  1XLD A    1   394  UNP    P12070   XYLA_ARTS7       1    394
DBREF  1XLD B    1   394  UNP    P12070   XYLA_ARTS7       1    394
SEQRES   1 A  394  SER VAL GLN PRO THR PRO ALA ASP HIS PHE THR PHE GLY
SEQRES   2 A  394  LEU TRP THR VAL GLY TRP THR GLY ALA ASP PRO PHE GLY
SEQRES   3 A  394  VAL ALA THR ARG LYS ASN LEU ASP PRO VAL GLU ALA VAL
SEQRES   4 A  394  HIS LYS LEU ALA GLU LEU GLY ALA TYR GLY ILE THR PHE
SEQRES   5 A  394  HIS ASP ASN ASP LEU ILE PRO PHE ASP ALA THR GLU ALA
SEQRES   6 A  394  GLU ARG GLU LYS ILE LEU GLY ASP PHE ASN GLN ALA LEU
SEQRES   7 A  394  LYS ASP THR GLY LEU LYS VAL PRO MET VAL THR THR ASN
SEQRES   8 A  394  LEU PHE SER HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 A  394  SER ASN ASP ARG SER ILE ARG ARG PHE ALA LEU ALA LYS
SEQRES  10 A  394  VAL LEU HIS ASN ILE ASP LEU ALA ALA GLU MET GLY ALA
SEQRES  11 A  394  GLU THR PHE VAL MET TRP GLY GLY ARG GLU GLY SER GLU
SEQRES  12 A  394  TYR ASP GLY SER LYS ASP LEU ALA ALA ALA LEU ASP ARG
SEQRES  13 A  394  MET ARG GLU GLY VAL ASP THR ALA ALA GLY TYR ILE LYS
SEQRES  14 A  394  ASP LYS GLY TYR ASN LEU ARG ILE ALA LEU GLU PRO LYS
SEQRES  15 A  394  PRO ASN GLU PRO ARG GLY ASP ILE PHE LEU PRO THR VAL
SEQRES  16 A  394  GLY HIS GLY LEU ALA PHE ILE GLU GLN LEU GLU HIS GLY
SEQRES  17 A  394  ASP ILE VAL GLY LEU ASN PRO GLU THR GLY HIS GLU GLN
SEQRES  18 A  394  MET ALA GLY LEU ASN PHE THR HIS GLY ILE ALA GLN ALA
SEQRES  19 A  394  LEU TRP ALA GLU LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 A  394  GLN ARG GLY ILE LYS TYR ASP GLN ASP LEU VAL PHE GLY
SEQRES  21 A  394  HIS GLY ASP LEU THR SER ALA PHE PHE THR VAL ASP LEU
SEQRES  22 A  394  LEU GLU ASN GLY PHE PRO ASN GLY GLY PRO LYS TYR THR
SEQRES  23 A  394  GLY PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR ASP
SEQRES  24 A  394  GLY TYR ASP GLY VAL TRP ASP SER ALA LYS ALA ASN MET
SEQRES  25 A  394  SER MET TYR LEU LEU LEU LYS GLU ARG ALA LEU ALA PHE
SEQRES  26 A  394  ARG ALA ASP PRO GLU VAL GLN GLU ALA MET LYS THR SER
SEQRES  27 A  394  GLY VAL PHE GLU LEU GLY GLU THR THR LEU ASN ALA GLY
SEQRES  28 A  394  GLU SER ALA ALA ASP LEU MET ASN ASP SER ALA SER PHE
SEQRES  29 A  394  ALA GLY PHE ASP ALA GLU ALA ALA ALA GLU ARG ASN PHE
SEQRES  30 A  394  ALA PHE ILE ARG LEU ASN GLN LEU ALA ILE GLU HIS LEU
SEQRES  31 A  394  LEU GLY SER ARG
SEQRES   1 B  394  SER VAL GLN PRO THR PRO ALA ASP HIS PHE THR PHE GLY
SEQRES   2 B  394  LEU TRP THR VAL GLY TRP THR GLY ALA ASP PRO PHE GLY
SEQRES   3 B  394  VAL ALA THR ARG LYS ASN LEU ASP PRO VAL GLU ALA VAL
SEQRES   4 B  394  HIS LYS LEU ALA GLU LEU GLY ALA TYR GLY ILE THR PHE
SEQRES   5 B  394  HIS ASP ASN ASP LEU ILE PRO PHE ASP ALA THR GLU ALA
SEQRES   6 B  394  GLU ARG GLU LYS ILE LEU GLY ASP PHE ASN GLN ALA LEU
SEQRES   7 B  394  LYS ASP THR GLY LEU LYS VAL PRO MET VAL THR THR ASN
SEQRES   8 B  394  LEU PHE SER HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES   9 B  394  SER ASN ASP ARG SER ILE ARG ARG PHE ALA LEU ALA LYS
SEQRES  10 B  394  VAL LEU HIS ASN ILE ASP LEU ALA ALA GLU MET GLY ALA
SEQRES  11 B  394  GLU THR PHE VAL MET TRP GLY GLY ARG GLU GLY SER GLU
SEQRES  12 B  394  TYR ASP GLY SER LYS ASP LEU ALA ALA ALA LEU ASP ARG
SEQRES  13 B  394  MET ARG GLU GLY VAL ASP THR ALA ALA GLY TYR ILE LYS
SEQRES  14 B  394  ASP LYS GLY TYR ASN LEU ARG ILE ALA LEU GLU PRO LYS
SEQRES  15 B  394  PRO ASN GLU PRO ARG GLY ASP ILE PHE LEU PRO THR VAL
SEQRES  16 B  394  GLY HIS GLY LEU ALA PHE ILE GLU GLN LEU GLU HIS GLY
SEQRES  17 B  394  ASP ILE VAL GLY LEU ASN PRO GLU THR GLY HIS GLU GLN
SEQRES  18 B  394  MET ALA GLY LEU ASN PHE THR HIS GLY ILE ALA GLN ALA
SEQRES  19 B  394  LEU TRP ALA GLU LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES  20 B  394  GLN ARG GLY ILE LYS TYR ASP GLN ASP LEU VAL PHE GLY
SEQRES  21 B  394  HIS GLY ASP LEU THR SER ALA PHE PHE THR VAL ASP LEU
SEQRES  22 B  394  LEU GLU ASN GLY PHE PRO ASN GLY GLY PRO LYS TYR THR
SEQRES  23 B  394  GLY PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR ASP
SEQRES  24 B  394  GLY TYR ASP GLY VAL TRP ASP SER ALA LYS ALA ASN MET
SEQRES  25 B  394  SER MET TYR LEU LEU LEU LYS GLU ARG ALA LEU ALA PHE
SEQRES  26 B  394  ARG ALA ASP PRO GLU VAL GLN GLU ALA MET LYS THR SER
SEQRES  27 B  394  GLY VAL PHE GLU LEU GLY GLU THR THR LEU ASN ALA GLY
SEQRES  28 B  394  GLU SER ALA ALA ASP LEU MET ASN ASP SER ALA SER PHE
SEQRES  29 B  394  ALA GLY PHE ASP ALA GLU ALA ALA ALA GLU ARG ASN PHE
SEQRES  30 B  394  ALA PHE ILE ARG LEU ASN GLN LEU ALA ILE GLU HIS LEU
SEQRES  31 B  394  LEU GLY SER ARG
HET    XYL  A 400      10
HET    XYL  B 400      10
HET     MN  A 398       1
HET     MN  A 399       1
HET     MN  B 398       1
HET     MN  B 399       1
HETNAM     XYL D-XYLITOL
HETNAM      MN MANGANESE (II) ION
FORMUL   3  XYL    2(C5 H12 O5)
FORMUL   5   MN    4(MN 2+)
FORMUL   9  HOH   *500(H2 O)
HELIX    1  A0 LEU A   14  VAL A   17  5                                   4
HELIX    2  A1 PRO A   35  LEU A   45  1                                  11
HELIX    3 A2A ASP A   54  ILE A   58  5                                   5
HELIX    4  A2 GLU A   64  THR A   81  1KINKED                            18
HELIX    5  A3 ARG A  108  MET A  128  1KINKED                            21
HELIX    6  A4 LEU A  150  LYS A  171  1                                  22
HELIX    7  A5 VAL A  195  GLN A  204  1                                  10
HELIX    8 A6A THR A  217  GLU A  220  1TURN                               4
HELIX    9 A6B HIS A  219  GLY A  224  5                                   6
HELIX   10  A6 PHE A  227  TRP A  236  1                                  10
HELIX   11  A7 LEU A  264  ASN A  276  1                                  13
HELIX   12  A8 TYR A  301  ALA A  327  1KINKED                            27
HELIX   13  A9 PRO A  329  SER A  338  1                                  10
HELIX   14 A10 VAL A  340  GLY A  344  5                                   5
HELIX   15 A11 ALA A  354  ASN A  359  5                                   6
HELIX   16 A12 ALA A  369  GLU A  374  1TURN                               6
HELIX   17 A13 PHE A  379  LEU A  391  1                                  13
HELIX   18  B0 LEU B   14  VAL B   17  5                                   4
HELIX   19  B1 PRO B   35  LEU B   45  1                                  11
HELIX   20 B2A ASP B   54  ILE B   58  5                                   5
HELIX   21  B2 GLU B   64  THR B   81  1KINKED                            18
HELIX   22  B3 ARG B  108  MET B  128  1KINKED                            21
HELIX   23  B4 LEU B  150  LYS B  171  1                                  22
HELIX   24  B5 VAL B  195  GLN B  204  1                                  10
HELIX   25 B6A THR B  217  GLU B  220  1TURN                               4
HELIX   26 B6B HIS B  219  GLY B  224  5                                   6
HELIX   27  B6 PHE B  227  TRP B  236  1                                  10
HELIX   28  B7 LEU B  264  ASN B  276  1                                  13
HELIX   29  B8 TYR B  301  ALA B  327  1KINKED                            27
HELIX   30  B9 PRO B  329  SER B  338  1                                  10
HELIX   31 B10 VAL B  340  GLY B  344  5                                   5
HELIX   32 B11 ALA B  354  ASN B  359  5                                   6
HELIX   33 B12 ALA B  369  GLU B  374  1TURN                               6
HELIX   34 B13 PHE B  379  LEU B  391  1                                  13
SHEET    1 BAA 9 HIS A   9  LEU A  14  0
SHEET    2 BAA 9 TYR A  48  THR A  51  1
SHEET    3 BAA 9 LYS A  84  VAL A  88  1
SHEET    4 BAA 9 GLU A 131  MET A 135  1
SHEET    5 BAA 9 ARG A 176  GLU A 180  1
SHEET    6 BAA 9 ILE A 210  THR A 217  1
SHEET    7 BAA 9 PHE A 241  LEU A 245  1
SHEET    8 BAA 9 ARG A 289  ASP A 292  1
SHEET    9 BAA 9 HIS A   9  LEU A  14  1
SHEET    1 BAB 9 HIS B   9  LEU B  14  0
SHEET    2 BAB 9 TYR B  48  THR B  51  1
SHEET    3 BAB 9 LYS B  84  VAL B  88  1
SHEET    4 BAB 9 GLU B 131  MET B 135  1
SHEET    5 BAB 9 ARG B 176  GLU B 180  1
SHEET    6 BAB 9 ILE B 210  THR B 217  1
SHEET    7 BAB 9 PHE B 241  LEU B 245  1
SHEET    8 BAB 9 ARG B 289  ASP B 292  1
SHEET    9 BAB 9 HIS B   9  LEU B  14  1
LINK        MN    MN A 398                 OD2 ASP A 254     1555   1555  2.21
LINK        MN    MN A 398                 O   HOH A 519A    1555   1555  1.99
LINK        MN    MN A 398                 NE2 HIS A 219     1555   1555  2.48
LINK        MN    MN A 398                 OD1 ASP A 254     1555   1555  2.45
LINK        MN    MN A 398                 OE2 GLU A 216     1555   1555  2.12
LINK        MN    MN A 398                 OD1 ASP A 256     1555   1555  2.16
LINK        MN    MN A 399                 OE2 GLU A 180     1555   1555  2.31
LINK        MN    MN A 399                 OE1 GLU A 216     1555   1555  2.21
LINK        MN    MN A 399                 OD2 ASP A 244     1555   1555  2.03
LINK        MN    MN A 399                 OD2 ASP A 292     1555   1555  2.15
LINK        MN    MN A 399                 O2  XYL A 400     1555   1555  2.39
LINK        MN    MN A 399                 O4  XYL A 400     1555   1555  2.42
LINK        MN    MN B 398                 OD1 ASP B 254     1555   1555  2.33
LINK        MN    MN B 398                 OD2 ASP B 254     1555   1555  2.33
LINK        MN    MN B 398                 O   HOH B 519B    1555   1555  2.09
LINK        MN    MN B 398                 OE2 GLU B 216     1555   1555  2.17
LINK        MN    MN B 398                 OD1 ASP B 256     1555   1555  2.10
LINK        MN    MN B 398                 NE2 HIS B 219     1555   1555  2.65
LINK        MN    MN B 399                 O2  XYL B 400     1555   1555  2.31
LINK        MN    MN B 399                 O4  XYL B 400     1555   1555  2.36
LINK        MN    MN B 399                 OE1 GLU B 216     1555   1555  2.06
LINK        MN    MN B 399                 OD2 ASP B 244     1555   1555  2.02
LINK        MN    MN B 399                 OD2 ASP B 292     1555   1555  2.14
LINK        MN    MN B 399                 OE2 GLU B 180     1555   1555  2.16
CISPEP   1 GLU A  185    PRO A  186          0         6.53
CISPEP   2 GLU B  185    PRO B  186          0         7.12
SITE     1 AC1 16 TRP A  15  HIS A  53  TRP A 136  GLU A 180
SITE     2 AC1 16 LYS A 182  GLU A 216  HIS A 219  ASP A 244
SITE     3 AC1 16 ASP A 254  ASP A 292   MN A 399  HOH A 518A
SITE     4 AC1 16 HOH A 519A HOH A 520A HOH A 521A PHE B  25
SITE     1 AC2 16 PHE A  25  TRP B  15  HIS B  53  TRP B 136
SITE     2 AC2 16 GLU B 180  LYS B 182  GLU B 216  HIS B 219
SITE     3 AC2 16 ASP B 244  ASP B 254  ASP B 292   MN B 398
SITE     4 AC2 16  MN B 399  HOH B 519B HOH B 520B HOH B 521B
SITE     1 AC3  5 GLU A 216  HIS A 219  ASP A 254  ASP A 256
SITE     2 AC3  5 HOH A 519A
SITE     1 AC4  5 GLU A 180  GLU A 216  ASP A 244  ASP A 292
SITE     2 AC4  5 XYL A 400
SITE     1 AC5  6 GLU B 216  HIS B 219  ASP B 254  ASP B 256
SITE     2 AC5  6 XYL B 400  HOH B 519B
SITE     1 AC6  5 GLU B 180  GLU B 216  ASP B 244  ASP B 292
SITE     2 AC6  5 XYL B 400
CRYST1  105.600  105.600  153.500  90.00  90.00 120.00 P 31 2 1     12
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      0.009470  0.005467  0.000000        0.00000
SCALE2      0.000000  0.010935  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006515        0.00000
      
PROCHECK
Go to PROCHECK summary
 References