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PDBsum entry 4duo

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Isomerase/isomerase inhibitor PDB id
4duo
Jmol
Contents
Protein chain
388 a.a.
Ligands
XYL
Metals
_MG ×2
Waters ×228
HEADER    ISOMERASE/ISOMERASE INHIBITOR           22-FEB-12   4DUO
TITLE     ROOM-TEMPERATURE X-RAY STRUCTURE OF D-XYLOSE ISOMERASE IN COMPLEX WITH
TITLE    2 2MG2+ IONS AND XYLITOL AT PH 7.7
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    TIM-BARREL, ISOMERASE, ISOMERASE-ISOMERASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.Y.KOVALEVSKY,L.HANSON,P.LANGAN
REVDAT   2   03-OCT-12 4DUO    1       JRNL
REVDAT   1   29-AUG-12 4DUO    0
JRNL        AUTH   A.KOVALEVSKY,B.L.HANSON,S.A.MASON,V.T.FORSYTH,Z.FISHER,
JRNL        AUTH 2 M.MUSTYAKIMOV,M.P.BLAKELEY,D.A.KEEN,P.LANGAN
JRNL        TITL   INHIBITION OF D-XYLOSE ISOMERASE BY POLYOLS: ATOMIC DETAILS
JRNL        TITL 2 BY JOINT X-RAY/NEUTRON CRYSTALLOGRAPHY.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68  1201 2012
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   22948921
JRNL        DOI    10.1107/S0907444912024808
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.148
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.145
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1580
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 31224
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.144
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.141
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.193
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1472
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 29332
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 3053
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 12
REMARK   3   SOLVENT ATOMS      : 228
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3284.00
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 1
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 12529
REMARK   3   NUMBER OF RESTRAINTS                     : 12625
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.007
REMARK   3   ANGLE DISTANCES                      (A) : 0.023
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.023
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.035
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.044
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.010
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.079
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4DUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB070804.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-09
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.7
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 FR-E DW
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29332
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0
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) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: APO-XI CRYSTALS WERE GROWN WITH AMSO4
REMARK 280  BY BATCH; TO OBTAIN THE COMPLEX MG2+ WAS INJECTED INTO DROPS
REMARK 280  CONTAINING CRYSTALS UP TO CONCENTRATION 5 MM; SUBSEQUENTLY,
REMARK 280  XYLITOL WAS INJECTED UP TO CONCENTRATION OF 100 MM, PH 7.7,
REMARK 280  TEMPERATURE 290K
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       46.89500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.81000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.41500
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.89500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.81000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.41500
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.89500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.81000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.41500
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.89500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.81000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       51.41500
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
REMARK 350 TOTAL BURIED SURFACE AREA: 32980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -181.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000     -102.83000
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000     -102.83000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A1122  LIES ON A SPECIAL POSITION.
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  41   CD  -  NE  -  CZ  ANGL. DEV. =  11.3 DEGREES
REMARK 500    ARG A  41   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 208   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A 266   CD  -  NE  -  CZ  ANGL. DEV. =  17.2 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    ARG A 292   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 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      104.26     80.15
REMARK 500    ASN A 247     -165.33   -164.87
REMARK 500    LYS A 253     -169.09   -171.03
REMARK 500    ALA A 343       62.29   -150.99
REMARK 500    PHE A 357      -67.72   -155.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 255   OD2
REMARK 620 2 HOH A1001   O   132.2
REMARK 620 3 GLU A 217   OE2 148.0  71.7
REMARK 620 4 ASP A 257   OD1  86.7  72.7  81.1
REMARK 620 5 ASP A 255   OD1  50.2 130.8  98.8  58.1
REMARK 620 6 XYL A 403   O1   91.5  85.9 114.0 148.8 138.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 402  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 217   OE1
REMARK 620 2 ASP A 245   OD2  93.5
REMARK 620 3 ASP A 287   OD2  97.6  94.9
REMARK 620 4 GLU A 181   OE2  93.8  95.7 163.9
REMARK 620 5 XYL A 403   O4  171.0  95.6  81.2  85.7
REMARK 620 6 XYL A 403   O2   86.3 178.1  83.3  86.3  84.7
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYL A 403
DBREF  4DUO A    1   388  UNP    P24300   XYLA_STRRU       1    388
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 ARG 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     MG  A 401       1
HET     MG  A 402       1
HET    XYL  A 403      10
HETNAM      MG MAGNESIUM ION
HETNAM     XYL D-XYLITOL
FORMUL   2   MG    2(MG 2+)
FORMUL   4  XYL    C5 H12 O5
FORMUL   5  HOH   *228(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 SER A  145  LYS A  149  5                                   5
HELIX    9   9 ASP A  150  GLY A  173  1                                  24
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  GLY A  279  1                                  16
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 ASP A  345  ASP A  353  1                                   9
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   A 8 TYR A 212  VAL A 214  0
SHEET    2   A 8 ARG A 177  ILE A 180  1  N  ILE A 180   O  GLY A 213
SHEET    3   A 8 THR A 133  ALA A 136  1  N  TYR A 134   O  ARG A 177
SHEET    4   A 8 MET A  88  THR A  90  1  N  ALA A  89   O  VAL A 135
SHEET    5   A 8 GLY A  50  HIS A  54  1  N  PHE A  53   O  THR A  90
SHEET    6   A 8 PHE A  11  GLY A  14  1  N  PHE A  13   O  THR A  52
SHEET    7   A 8 ARG A 284  PHE A 286  1  O  PHE A 286   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         OD2BASP A 255                MG    MG A 401     1555   1555  1.78
LINK         OE1 GLU A 217                MG    MG A 402     1555   1555  1.98
LINK         OD2 ASP A 245                MG    MG A 402     1555   1555  1.98
LINK         OD2 ASP A 287                MG    MG A 402     1555   1555  2.02
LINK         OE2 GLU A 181                MG    MG A 402     1555   1555  2.08
LINK        MG    MG A 401                 O   HOH A1001     1555   1555  2.50
LINK         OE2 GLU A 217                MG    MG A 401     1555   1555  2.67
LINK         OD1 ASP A 257                MG    MG A 401     1555   1555  2.69
LINK         OD1BASP A 255                MG    MG A 401     1555   1555  2.86
LINK        MG    MG A 402                 O4  XYL A 403     1555   1555  2.15
LINK        MG    MG A 402                 O2  XYL A 403     1555   1555  2.18
LINK        MG    MG A 401                 O1  XYL A 403     1555   1555  2.79
CISPEP   1 GLU A  186    PRO A  187          0        15.55
SITE     1 AC1  6 GLU A 217  HIS A 220  ASP A 255  ASP A 257
SITE     2 AC1  6 XYL A 403  HOH A1001
SITE     1 AC2  5 GLU A 181  GLU A 217  ASP A 245  ASP A 287
SITE     2 AC2  5 XYL A 403
SITE     1 AC3 16 TRP A  16  PHE A  26  HIS A  54  GLU A 181
SITE     2 AC3 16 LYS A 183  GLU A 217  HIS A 220  ASP A 245
SITE     3 AC3 16 ASP A 255  ASP A 287   MG A 401   MG A 402
SITE     4 AC3 16 HOH A1001  HOH A1022  HOH A1037  HOH A1136
CRYST1   93.790   99.620  102.830  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      0.010662  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010038  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009725        0.00000
      
PROCHECK
Go to PROCHECK summary
 References