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PDBsum entry 1gw9

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Isomerase PDB id
1gw9
Jmol
Contents
Protein chain
385 a.a. *
Ligands
LXC ×2
Metals
IOD ×29
_CA ×2
Waters ×347
* Residue conservation analysis
HEADER    ISOMERASE                               13-MAR-02   1GW9
TITLE     TRI-IODIDE DERIVATIVE OF XYLOSE ISOMERASE FROM STREPTOMYCES
TITLE    2 RUBIGINOSUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: XYLOSE ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 5.3.1.5
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES RUBIGINOSUS;
SOURCE   3 ORGANISM_TAXID: 1929
KEYWDS    ISOMERASE, PENTOSE SHUNT, XYLOSE METABOLISM, MAGNESIUM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.EVANS,G.BRICOGNE
REVDAT   2   24-FEB-09 1GW9    1       VERSN
REVDAT   1   06-JUN-02 1GW9    0
JRNL        AUTH   G.EVANS,G.BRICOGNE
JRNL        TITL   TRIIODIDE DERIVATIZATION AND COMBINATORIAL
JRNL        TITL 2 COUNTER-ION REPLACEMENT: TWO METHODS FOR ENHANCING
JRNL        TITL 3 PHASING SIGNAL USING LABORATORY CU KALPHA X-RAY
JRNL        TITL 4 EQUIPMENT
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  58   976 2002
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   12037300
JRNL        DOI    10.1107/S0907444902005486
REMARK   2
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : BUSTER/TNT
REMARK   3   AUTHORS     : BLANC,ROVERSI,VONRHEIN,BRICOGNE,TRONRUD,
REMARK   3               : TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.05
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6
REMARK   3   NUMBER OF REFLECTIONS             : 66821
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165
REMARK   3   R VALUE            (WORKING SET) : 0.164
REMARK   3   FREE R VALUE                     : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 3400
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED               : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 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 FREE R VALUE         : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3060
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 51
REMARK   3   SOLVENT ATOMS            : 347
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
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        RMS   WEIGHT   COUNT
REMARK   3   BOND LENGTHS                 (A) : NULL   ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL   ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL   ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL   ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL   ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL   ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL   ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL   ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION APPLIED
REMARK   4
REMARK   4 1GW9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-02.
REMARK 100 THE PDBE ID CODE IS EBI-8640.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-00
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : OSMIC MULTILAYER
REMARK 200  OPTICS                         : OSMIC MULTILAYER
REMARK 200
REMARK 200  DETECTOR TYPE                  : MAR-345 (IP)
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 1257016
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.050
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : 18.800
REMARK 200  R MERGE                    (I) : 0.06500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.26400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
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
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULPHATE,
REMARK 280  10MM TRIS-HCL AT PH7.5 AND THEN SOAKED IN AN EQUIVALENT
REMARK 280  SOLUTION WITH 50MM KI/50MM I2 AND 1.9M L-XYLOSE
REMARK 280  ADDED AS CRYO-PROTECTANT.
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       46.17700
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.27000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.25350
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.17700
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.27000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.25350
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.17700
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.27000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.25350
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.17700
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.27000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       51.25350
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 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       98.54000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      102.50700
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       92.35400
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      102.50700
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       92.35400
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       98.54000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375      HOH A2250  LIES ON A SPECIAL POSITION.
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     2
REMARK 465     ARG A   388
REMARK 465     GLY A   389
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     ASN A   2    N    CA   O    CB   CG   OD1  ND2
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  2036  -  O    HOH A  2092              2.02
REMARK 500   O    HOH A  2104  -  O    HOH A  2161              1.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ASP A 264   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG A 331   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A 368   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG A 368   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    THR A  17      -74.41    -84.14
REMARK 500    GLU A 186       99.84     78.75
REMARK 500    LYS A 253     -173.04   -172.61
REMARK 500    ALA A 343       64.23   -152.25
REMARK 500    PHE A 357      -78.88   -156.27
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 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                              CA A1387  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 287   OD2
REMARK 620 2 LXC A1390   O2   80.5
REMARK 620 3 LXC A1390   O3   91.2  75.5
REMARK 620 4 GLU A 181   OE2 161.3  81.1  80.9
REMARK 620 5 GLU A 217   OE1  84.4  96.7 171.6 101.1
REMARK 620 6 ASP A 245   OD2  98.5 164.3  88.8  98.3  98.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1388  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2245   O
REMARK 620 2 HIS A 220   NE2 108.1
REMARK 620 3 ASP A 255   OD2 104.1  95.4
REMARK 620 4 GLU A 217   OE2  89.4  74.0 165.1
REMARK 620 5 ASP A 255   OD1 150.4  98.0  58.7 111.6
REMARK 620 6 ASP A 257   OD1  78.6 166.2  94.5  94.4  79.1
REMARK 620 7 HOH A2243   O   140.0  87.5 111.0  59.1  52.7  80.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LXC A1389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LXC A1390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1387
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1388
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1395
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1396
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1397
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1398
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1399
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1405
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1406
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1407
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1409
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1411
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1412
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1413
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1414
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1415
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1416
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1417
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1419
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XIB   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE (PH 7.4)
REMARK 900 RELATED ID: 1XIC   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEXED WITH D-XYLOSE
REMARK 900   (PH 9.0)
REMARK 900 RELATED ID: 1XID   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEXED WITH L-ASCORBIC
REMARK 900   ACID, MN, AND MG (PH 7.4)
REMARK 900 RELATED ID: 1XIE   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEXED WITH 1,5-
REMARK 900  DIANHYDROSORBITOL (PH 7.4)
REMARK 900 RELATED ID: 1XIF   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEXED WITH GLUCOSE,
REMARK 900  MN, AND MG (PH 8.0)
REMARK 900 RELATED ID: 1XIG   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEXED WITH XYLITOL,
REMARK 900  MG, AND MN (PH 7.4)
REMARK 900 RELATED ID: 1XIH   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEXED WITH D-SORBITOL
REMARK 900   AND NO ADDED MN (PH 9.0)
REMARK 900 RELATED ID: 1XII   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEXED WITH 300MM D-
REMARK 900  XYLULOSE AND MN (PH 8.0)
REMARK 900 RELATED ID: 1XIJ   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEXED WITH THREONATE
REMARK 900  AND MN (PH 9.0)
REMARK 900 RELATED ID: 1XIS   RELATED DB: PDB
REMARK 900  XYLOSE ISOMERASE COMPLEX WITH MNCL2
REMARK 900 RELATED ID: 2XIS   RELATED DB: PDB
REMARK 900  XYLOSE ISOMERASE COMPLEX WITH XYLITOL
REMARK 900 RELATED ID: 3XIS   RELATED DB: PDB
REMARK 900  XYLOSE ISOMERASE COMPLEX WITH XYLOSE
REMARK 900 RELATED ID: 4XIS   RELATED DB: PDB
REMARK 900  XYLOSE ISOMERASE COMPLEX WITH XYLOSE AND
REMARK 900  MNCL2
REMARK 900 RELATED ID: 8XIA   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEX WITH D-XYLOSE
REMARK 900 RELATED ID: 9XIA   RELATED DB: PDB
REMARK 900  D-XYLOSE ISOMERASE COMPLEX WITH INACTIVATOR
DBREF  1GW9 A    2   388  UNP    P24300   XYLA_STRRU       1    387
SEQADV 1GW9 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    LXC  A1389      10
HET    LXC  A1390      10
HET     CA  A1387       1
HET     CA  A1388       1
HET    IOD  A1391       1
HET    IOD  A1392       1
HET    IOD  A1393       1
HET    IOD  A1394       1
HET    IOD  A1395       1
HET    IOD  A1396       1
HET    IOD  A1397       1
HET    IOD  A1398       1
HET    IOD  A1399       1
HET    IOD  A1400       1
HET    IOD  A1401       1
HET    IOD  A1402       1
HET    IOD  A1403       1
HET    IOD  A1404       1
HET    IOD  A1405       1
HET    IOD  A1406       1
HET    IOD  A1407       1
HET    IOD  A1408       1
HET    IOD  A1409       1
HET    IOD  A1410       1
HET    IOD  A1411       1
HET    IOD  A1412       1
HET    IOD  A1413       1
HET    IOD  A1414       1
HET    IOD  A1415       1
HET    IOD  A1416       1
HET    IOD  A1417       1
HET    IOD  A1418       1
HET    IOD  A1419       1
HETNAM     LXC BETA-L-XYLOPYRANOSE
HETNAM      CA CALCIUM ION
HETNAM     IOD IODIDE ION
HETSYN     LXC L-XYLOSE (CYCLIC FORM)
FORMUL   2  LXC    2(C5 H10 O5)
FORMUL   4   CA    2(CA 2+)
FORMUL   6  IOD    29(I 1-)
FORMUL  35  HOH   *347(H2 O1)
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  LEU A  129  1                                  22
HELIX    8   8 SER A  145  LYS A  149  5                                   5
HELIX    9   9 ASP A  150  GLN A  172  1                                  23
HELIX   10  10 THR A  195  GLU A  204  1                                  10
HELIX   11  11 ARG A  208  GLU A  210  5                                   3
HELIX   12  12 GLU A  217  MET A  223  1                                   7
HELIX   13  13 ASN A  227  ALA A  238  1                                  12
HELIX   14  14 ASP A  264  ALA A  278  1                                  15
HELIX   15  15 ASP A  295  ASP A  323  1                                  29
HELIX   16  16 ASP A  323  SER A  333  1                                  11
HELIX   17  17 ARG A  334  ALA A  339  1                                   6
HELIX   18  18 GLY A  346  ASP A  353  1                                   8
HELIX   19  19 ARG A  354  PHE A  357  5                                   4
HELIX   20  20 ASP A  361  ARG A  368  1                                   8
HELIX   21  21 ALA A  371  GLY A  385  1                                  15
SHEET    1  AA 8 TYR A 212  VAL A 214  0
SHEET    2  AA 8 ARG A 177  ILE A 180  1  O  PHE A 178   N  GLY A 213
SHEET    3  AA 8 THR A 133  ALA A 136  1  O  TYR A 134   N  ALA A 179
SHEET    4  AA 8 MET A  88  THR A  90  1  O  ALA A  89   N  VAL A 135
SHEET    5  AA 8 GLY A  50  HIS A  54  1  O  PHE A  53   N  THR A  90
SHEET    6  AA 8 PHE A  11  GLY A  14  1  O  PHE A  13   N  THR A  52
SHEET    7  AA 8 ARG A 284  PHE A 286  1  O  ARG A 284   N  THR A  12
SHEET    8  AA 8 ASP A 245  LEU A 246  1  N  LEU A 246   O  HIS A 285
SHEET    1  AB 2 GLY A 142  ALA A 143  0
SHEET    2  AB 2 ASP A 190  ILE A 191 -1  O  ASP A 190   N  ALA A 143
LINK        CA    CA A1387                 OD2 ASP A 287     1555   1555  2.07
LINK        CA    CA A1387                 O2  LXC A1390     1555   1555  2.36
LINK        CA    CA A1387                 O3  LXC A1390     1555   1555  2.29
LINK        CA    CA A1387                 OE2 GLU A 181     1555   1555  2.12
LINK        CA    CA A1387                 OE1 GLU A 217     1555   1555  1.96
LINK        CA    CA A1387                 OD2 ASP A 245     1555   1555  2.14
LINK        CA    CA A1388                 NE2 HIS A 220     1555   1555  2.64
LINK        CA    CA A1388                 OD2 ASP A 255     1555   1555  2.04
LINK        CA    CA A1388                 OE2 GLU A 217     1555   1555  2.03
LINK        CA    CA A1388                 OD1 ASP A 255     1555   1555  2.38
LINK        CA    CA A1388                 OD1 ASP A 257     1555   1555  2.28
LINK        CA    CA A1388                 O   HOH A2243     1555   1555  2.58
LINK        CA    CA A1388                 O   HOH A2245     1555   1555  2.43
CISPEP   1 GLU A  186    PRO A  187          0        20.93
SITE     1 AC1 10 ASP A 295  ALA A 332  ARG A 334  ARG A 368
SITE     2 AC1 10 GLY A 369  ALA A 371  HOH A2270  HOH A2275
SITE     3 AC1 10 HOH A2342  HOH A2343
SITE     1 AC2 15 PHE A  26  HIS A  54  TRP A 137  GLU A 181
SITE     2 AC2 15 GLU A 217  HIS A 220  ASP A 245  ASP A 287
SITE     3 AC2 15  CA A1387  HOH A2245  HOH A2265  HOH A2344
SITE     4 AC2 15 HOH A2345  HOH A2346  HOH A2347
SITE     1 AC3  5 GLU A 181  GLU A 217  ASP A 245  ASP A 287
SITE     2 AC3  5 LXC A1390
SITE     1 AC4  6 GLU A 217  HIS A 220  ASP A 255  ASP A 257
SITE     2 AC4  6 HOH A2243  HOH A2245
SITE     1 AC5  2 HIS A  49  IOD A1392
SITE     1 AC6  2 IOD A1391  IOD A1393
SITE     1 AC7  2 IOD A1392  IOD A1394
SITE     1 AC8  2 GLU A 132  IOD A1393
SITE     1 AC9  3 ALA A 201  GLN A 234  IOD A1396
SITE     1 BC1  4 GLU A 204  ALA A 238  IOD A1395  IOD A1397
SITE     1 BC2  5 LEU A 200  GLU A 204  LYS A 240  IOD A1396
SITE     2 BC2  5 IOD A1398
SITE     1 BC3  3 GLU A 204  IOD A1397  IOD A1399
SITE     1 BC4  4 GLU A 204  PRO A 209  LYS A 240  IOD A1398
SITE     1 BC5  3 MET A 158  IOD A1401  HOH A2163
SITE     1 BC6  4 PHE A 104  IOD A1400  IOD A1402  IOD A1404
SITE     1 BC7  6 ALA A 136  TRP A 137  IOD A1401  HOH A2104
SITE     2 BC7  6 HOH A2161  HOH A2162
SITE     1 BC8  3 THR A 119  LEU A 165  HOH A2104
SITE     1 BC9  5 LEU A  93  GLY A 103  PHE A 104  GLU A 141
SITE     2 BC9  5 IOD A1401
SITE     1 CC1  2 PRO A  25  IOD A1406
SITE     1 CC2  5 PRO A  25  GLU A 186  TYR A 254  IOD A1405
SITE     2 CC2  5 HOH A2205
SITE     1 CC3  5 GLY A 239  LYS A 240  LEU A 241  HOH A2229
SITE     2 CC3  5 HOH A2233
SITE     1 CC4  1 IOD A1409
SITE     1 CC5  2 IOD A1408  HOH A2340
SITE     1 CC6  3 GLN A  41  IOD A1412  IOD A1419
SITE     1 CC7  2 GLU A  38  IOD A1411
SITE     1 CC8  3 LEU A 193  GLN A 234  HOH A2093
SITE     1 CC9  5 GLY A 138  MET A 158  LEU A 192  HOH A2163
SITE     2 CC9  5 HOH A2202
SITE     1 DC1  4 GLY A 263  ARG A 266  HOH A2036  HOH A2167
SITE     1 DC2  2 HIS A  71  ARG A  74
SITE     1 DC3  2 ASN A 227  HOH A2094
SITE     1 DC4  2 ALA A 319  HOH A2341
SITE     1 DC5  1 IOD A1411
CRYST1   92.354   98.540  102.507  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      0.010828  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010148  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009755        0.00000
      
PROCHECK
Go to PROCHECK summary
 References