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PDBsum entry 1xih

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Isomerase(intramolecular oxidoreductase) PDB id
1xih
Jmol
Contents
Protein chain
385 a.a.
Ligands
SOR
Metals
_MN
Waters ×375
HEADER    ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)07-MAR-94   1XIH
TITLE     MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE
TITLE    2 ISOMERASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-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    H.L.CARRELL,J.P.GLUSKER
REVDAT   3   13-JUL-11 1XIH    1       VERSN
REVDAT   2   24-FEB-09 1XIH    1       VERSN
REVDAT   1   22-JUN-94 1XIH    0
JRNL        AUTH   H.L.CARRELL,H.HOIER,J.P.GLUSKER
JRNL        TITL   MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE
JRNL        TITL 2 ENZYME D-XYLOSE ISOMERASE.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  50   113 1994
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   15299449
JRNL        DOI    10.1107/S0907444993009345
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   H.L.CARRELL,J.P.GLUSKER,V.BURGER,F.MANFRE,
REMARK   1  AUTH 2 D.TRITSCH J.-F.BIELLMANN
REMARK   1  TITL   X-RAY ANALYSIS OF D-XYLOSE ISOMERASE AT 1.9 ANGSTROMS:
REMARK   1  TITL 2 NATIVE ENZYME IN COMPLEX WITH SUBSTRATE AND WITH A
REMARK   1  TITL 3 MECHANISM-DESIGNED INACTIVATOR
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  86  4440 1989
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   H.L.CARRELL,B.H.RUBIN,T.J.HURLEY,J.P.GLUSKER
REMARK   1  TITL   X-RAY CRYSTAL STRUCTURE OF D-XYLOSE ISOMERASE AT 4-ANGSTROMS
REMARK   1  TITL 2 RESOLUTION
REMARK   1  REF    J.BIOL.CHEM.                  V. 259  3230 1984
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    1.70 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) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 52652
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) : 0.158
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            : 3031
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 13
REMARK   3   SOLVENT ATOMS            : 375
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) : 0.013 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; 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 1XIH 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   (%): 55.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
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       46.83000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.01000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.35000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.83000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.01000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.35000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.83000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.01000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.35000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.83000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.01000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       51.35000
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: 32590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 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       93.66000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      100.02000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       93.66000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      102.70000
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      100.02000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      102.70000
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     MET A     1
REMARK 465     ASN A     2
REMARK 465     GLY A   388
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH A   509     O    HOH A   540              1.22
REMARK 500   O    HOH A   641     O    HOH A   771              1.85
REMARK 500   O    HOH A   559     O    HOH A   765              2.09
REMARK 500   O    HOH A   619     O    HOH A   662              2.17
REMARK 500   O    HOH A   555     O    HOH A   556              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    PRO A   7   C     GLU A   8   N       0.220
REMARK 500    THR A  17   C     VAL A  18   N       0.156
REMARK 500    ASP A  28   C     ALA A  29   N       0.146
REMARK 500    ASP A  35   C     PRO A  36   N       0.145
REMARK 500    PRO A  36   C     VAL A  37   N       0.212
REMARK 500    GLY A  50   C     VAL A  51   N      -0.140
REMARK 500    SER A  63   C     SER A  64   N       0.163
REMARK 500    VAL A  72   C     LYS A  73   N       0.140
REMARK 500    VAL A  98   C     PHE A  99   N       0.194
REMARK 500    THR A 119   C     ILE A 120   N       0.185
REMARK 500    TYR A 134   C     VAL A 135   N       0.152
REMARK 500    ALA A 143   C     GLU A 144   N       0.152
REMARK 500    ASP A 175   C     ILE A 176   N      -0.281
REMARK 500    ASP A 255   C     GLN A 256   N       0.187
REMARK 500    ALA A 278   C     GLY A 279   N       0.143
REMARK 500    ALA A 386   C     ARG A 387   N      -0.176
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   5   CA  -  C   -  N   ANGL. DEV. = -13.3 DEGREES
REMARK 500    PRO A   7   C   -  N   -  CD  ANGL. DEV. = -13.7 DEGREES
REMARK 500    PRO A   7   O   -  C   -  N   ANGL. DEV. = -21.6 DEGREES
REMARK 500    GLU A   8   C   -  N   -  CA  ANGL. DEV. =  20.6 DEGREES
REMARK 500    GLU A   8   O   -  C   -  N   ANGL. DEV. = -11.8 DEGREES
REMARK 500    ASP A  56   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    GLU A  69   O   -  C   -  N   ANGL. DEV. = -10.6 DEGREES
REMARK 500    ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A  76   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ARG A 117   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ARG A 157   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ASP A 163   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ASP A 163   O   -  C   -  N   ANGL. DEV. =  -9.8 DEGREES
REMARK 500    SER A 171   O   -  C   -  N   ANGL. DEV. =  -9.7 DEGREES
REMARK 500    TYR A 174   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    GLY A 173   O   -  C   -  N   ANGL. DEV. = -12.7 DEGREES
REMARK 500    ARG A 177   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG A 188   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ASP A 245   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 259   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG A 266   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG A 284   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ASP A 295   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    GLU A 315   O   -  C   -  N   ANGL. DEV. = -10.6 DEGREES
REMARK 500    ARG A 331   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 340   CD  -  NE  -  CZ  ANGL. DEV. =  40.0 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ALA A 343   C   -  N   -  CA  ANGL. DEV. = -15.1 DEGREES
REMARK 500    GLU A 359   O   -  C   -  N   ANGL. DEV. =  12.2 DEGREES
REMARK 500    ARG A 368   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES
REMARK 500    ASP A 381   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG A 387   CD  -  NE  -  CZ  ANGL. DEV. =  17.6 DEGREES
REMARK 500    ARG A 387   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A 387   CA  -  C   -  O   ANGL. DEV. =  19.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLU A 186       92.54     84.29
REMARK 500    LEU A 193       70.26     45.98
REMARK 500    ASN A 215       74.37   -113.04
REMARK 500    ASN A 247     -169.59   -168.98
REMARK 500    TYR A 254      154.72    -44.80
REMARK 500    ALA A 343       72.30   -155.79
REMARK 500    PHE A 357      -69.79   -150.73
REMARK 500    ALA A 386       41.56   -109.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 PHE A   53     HIS A   54                  148.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    PRO A   5        -10.84
REMARK 500    THR A   6        -11.68
REMARK 500    PRO A   7        -21.62
REMARK 500    ASP A  65        -12.88
REMARK 500    ARG A  68        -10.38
REMARK 500    GLU A  69         11.89
REMARK 500    LYS A  85        -11.71
REMARK 500    GLU A 132         11.48
REMARK 500    THR A 170        -17.54
REMARK 500    ARG A 177        -12.45
REMARK 500    MET A 223         11.98
REMARK 500    GLN A 249         10.26
REMARK 500    PHE A 260         10.09
REMARK 500    SER A 277        -11.96
REMARK 500    PHE A 286         13.53
REMARK 500    ASP A 287         10.19
REMARK 500    VAL A 299         10.35
REMARK 500    GLU A 358        -11.76
REMARK 500    GLY A 385         10.56
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    VAL A  37        20.9      L          L   OUTSIDE RANGE
REMARK 500    ARG A 387        20.0      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 763        DISTANCE =  5.27 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 391  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 181   OE2
REMARK 620 2 ASP A 245   OD2  96.8
REMARK 620 3 SOR A 389   O4   80.7  96.4
REMARK 620 4 SOR A 389   O2   81.4 175.2  79.0
REMARK 620 5 GLU A 217   OE1 101.2  95.8 167.3  88.8
REMARK 620 6 ASP A 287   OD2 159.9  95.5  82.1  85.1  93.3
REMARK 620 N                    1     2     3     4     5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE STRUCTURE OF THE MONOMER IS AN EIGHT-FOLD ALPHA-BETA
REMARK 700 BARREL WITH AN EXTENDED C-TERMINAL LOOP WHICH FACILITATES
REMARK 700 AGGREGATION OF MONOMERS TO TETRAMERS.  TETRAMERS ARE
REMARK 700 POSITIONED ON THE 222 SYMMETRY SITE AT THE ORIGIN OF THE
REMARK 700 CELL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SOR A 389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 391
DBREF  1XIH A    2   388  UNP    P24300   XYLA_STRRU       1    387
SEQADV 1XIH GLN A   41  UNP  P24300    ARG    40 CONFLICT
SEQRES   1 A  388  MET ASN TYR GLN PRO THR PRO GLU ASP ARG PHE THR PHE
SEQRES   2 A  388  GLY LEU TRP THR VAL GLY TRP GLN GLY ARG ASP PRO PHE
SEQRES   3 A  388  GLY ASP ALA THR ARG ARG ALA LEU ASP PRO VAL GLU SER
SEQRES   4 A  388  VAL GLN ARG LEU ALA GLU LEU GLY ALA HIS GLY VAL THR
SEQRES   5 A  388  PHE HIS ASP ASP ASP LEU ILE PRO PHE GLY SER SER ASP
SEQRES   6 A  388  SER GLU ARG GLU GLU HIS VAL LYS ARG PHE ARG GLN ALA
SEQRES   7 A  388  LEU ASP ASP THR GLY MET LYS VAL PRO MET ALA THR THR
SEQRES   8 A  388  ASN LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE
SEQRES   9 A  388  THR ALA ASN ASP ARG ASP VAL ARG ARG TYR ALA LEU ARG
SEQRES  10 A  388  LYS THR ILE ARG ASN ILE ASP LEU ALA VAL GLU LEU GLY
SEQRES  11 A  388  ALA GLU THR TYR VAL ALA TRP GLY GLY ARG GLU GLY ALA
SEQRES  12 A  388  GLU SER GLY GLY ALA LYS ASP VAL ARG ASP ALA LEU ASP
SEQRES  13 A  388  ARG MET LYS GLU ALA PHE ASP LEU LEU GLY GLU TYR VAL
SEQRES  14 A  388  THR SER GLN GLY TYR ASP ILE ARG PHE ALA ILE GLU PRO
SEQRES  15 A  388  LYS PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR
SEQRES  16 A  388  VAL GLY HIS ALA LEU ALA PHE ILE GLU ARG LEU GLU ARG
SEQRES  17 A  388  PRO GLU LEU TYR GLY VAL ASN PRO GLU VAL GLY HIS GLU
SEQRES  18 A  388  GLN MET ALA GLY LEU ASN PHE PRO HIS GLY ILE ALA GLN
SEQRES  19 A  388  ALA LEU TRP ALA GLY LYS LEU PHE HIS ILE ASP LEU ASN
SEQRES  20 A  388  GLY GLN ASN GLY ILE LYS TYR ASP GLN ASP LEU ARG PHE
SEQRES  21 A  388  GLY ALA GLY ASP LEU ARG ALA ALA PHE TRP LEU VAL ASP
SEQRES  22 A  388  LEU LEU GLU SER ALA GLY TYR SER GLY PRO ARG HIS PHE
SEQRES  23 A  388  ASP PHE LYS PRO PRO ARG THR GLU ASP PHE ASP GLY VAL
SEQRES  24 A  388  TRP ALA SER ALA ALA GLY CYS MET ARG ASN TYR LEU ILE
SEQRES  25 A  388  LEU LYS GLU ARG ALA ALA ALA PHE ARG ALA ASP PRO GLU
SEQRES  26 A  388  VAL GLN GLU ALA LEU ARG ALA SER ARG LEU ASP GLU LEU
SEQRES  27 A  388  ALA ARG PRO THR ALA ALA ASP GLY LEU GLN ALA LEU LEU
SEQRES  28 A  388  ASP ASP ARG SER ALA PHE GLU GLU PHE ASP VAL ASP ALA
SEQRES  29 A  388  ALA ALA ALA ARG GLY MET ALA PHE GLU ARG LEU ASP GLN
SEQRES  30 A  388  LEU ALA MET ASP HIS LEU LEU GLY ALA ARG GLY
HET    SOR  A 389      12
HET     MN  A 391       1
HETNAM     SOR D-SORBITOL
HETNAM      MN MANGANESE (II) ION
FORMUL   2  SOR    C6 H14 O6
FORMUL   3   MN    MN 2+
FORMUL   4  HOH   *375(H2 O)
HELIX    1   1 THR A    6  ASP A    9  5                                   4
HELIX    2   2 LEU A   15  GLY A   19  1                                   5
HELIX    3   3 ASP A   35  GLY A   47  1                                  13
HELIX    4   4 ASP A   55  ILE A   59  1                                   5
HELIX    5   5 SER A   64  GLY A   83  1                                  20
HELIX    6   6 HIS A   96  LYS A  100  5                                   5
HELIX    7   7 ASP A  108  GLY A  130  1                                  23
HELIX    8   8 ASP A  150  GLN A  172  1                                  23
HELIX    9   9 THR A  195  GLU A  204  1                                  10
HELIX   10  10 ARG A  208  GLU A  210  5                                   3
HELIX   11  11 GLU A  217  MET A  223  1                                   7
HELIX   12  12 ASN A  227  ALA A  238  1                                  12
HELIX   13  13 ASP A  264  ALA A  278  1                                  15
HELIX   14  14 ASP A  295  ASP A  323  1                                  29
HELIX   15  15 ASP A  323  SER A  333  1                                  11
HELIX   16  16 ARG A  334  ALA A  339  1                                   6
HELIX   17  17 GLY A  346  ASP A  353  1                                   8
HELIX   18  18 ARG A  354  PHE A  357  5                                   4
HELIX   19  19 ASP A  361  ALA A  367  1                                   7
HELIX   20  20 ALA A  371  GLY A  385  1                                  15
SHEET    1   A 8 TYR A 212  VAL A 214  0
SHEET    2   A 8 ARG A 177  GLU A 181  1  O  PHE A 178   N  GLY A 213
SHEET    3   A 8 THR A 133  TRP A 137  1  N  TYR A 134   O  ARG A 177
SHEET    4   A 8 MET A  88  THR A  90  1  O  ALA A  89   N  VAL A 135
SHEET    5   A 8 GLY A  50  HIS A  54  1  O  PHE A  53   N  THR A  90
SHEET    6   A 8 PHE A  11  GLY A  14  1  O  PHE A  11   N  GLY A  50
SHEET    7   A 8 ARG A 284  PHE A 286  1  O  ARG A 284   N  THR A  12
SHEET    8   A 8 ASP A 245  LEU A 246  1  N  LEU A 246   O  HIS A 285
SHEET    1   B 2 GLY A 142  ALA A 143  0
SHEET    2   B 2 ASP A 190  ILE A 191 -1  O  ASP A 190   N  ALA A 143
LINK        MN    MN A 391                 OE2 GLU A 181     1555   1555  2.24
LINK        MN    MN A 391                 OD2 ASP A 245     1555   1555  2.23
LINK        MN    MN A 391                 O4  SOR A 389     1555   1555  2.30
LINK        MN    MN A 391                 O2  SOR A 389     1555   1555  2.38
LINK        MN    MN A 391                 OE1 GLU A 217     1555   1555  2.16
LINK        MN    MN A 391                 OD2 ASP A 287     1555   1555  2.22
CISPEP   1 GLU A  186    PRO A  187          0        29.95
SITE     1 AC1 19 TRP A  16  PHE A  26  HIS A  54  THR A  90
SITE     2 AC1 19 PHE A  94  VAL A 135  TRP A 137  GLU A 181
SITE     3 AC1 19 LYS A 183  GLU A 217  HIS A 220  ASP A 245
SITE     4 AC1 19 ASP A 287  HOH A 390   MN A 391  HOH A 408
SITE     5 AC1 19 HOH A 409  HOH A 585  HOH A 692
SITE     1 AC2  5 GLU A 181  GLU A 217  ASP A 245  ASP A 287
SITE     2 AC2  5 SOR A 389
CRYST1   93.660  100.020  102.700  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      0.010677  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009998  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009737        0.00000
      
PROCHECK
Go to PROCHECK summary
 References