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PDBsum entry 2dga

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Hydrolase PDB id
2dga
Jmol
Contents
Protein chain
491 a.a.
Ligands
SO4
GOL ×3
Waters ×613
HEADER    HYDROLASE                               10-MAR-06   2DGA
TITLE     CRYSTAL STRUCTURE OF HEXAMERIC BETA-GLUCOSIDASE IN WHEAT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-GLUCOSIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 1-520;
COMPND   5 SYNONYM: BETA-D-GLUCOSIDASE;
COMPND   6 EC: 3.2.1.21;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;
SOURCE   3 ORGANISM_COMMON: BREAD WHEAT;
SOURCE   4 ORGANISM_TAXID: 4565;
SOURCE   5 GENE: TAGLU1B;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS    ALPHA/BETA BARREL, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.SUE,K.YAMAZAKI,T.MIYAMOTO,S.YAJIMA
REVDAT   4   13-JUL-11 2DGA    1       VERSN
REVDAT   3   24-FEB-09 2DGA    1       VERSN
REVDAT   2   22-AUG-06 2DGA    1       JRNL
REVDAT   1   04-JUL-06 2DGA    0
JRNL        AUTH   M.SUE,K.YAMAZAKI,S.YAJIMA,T.NOMURA,T.MATSUKAWA,H.IWAMURA,
JRNL        AUTH 2 T.MIYAMOTO
JRNL        TITL   MOLECULAR AND STRUCTURAL CHARACTERIZATION OF HEXAMERIC
JRNL        TITL 2 BETA-D-GLUCOSIDASES IN WHEAT AND RYE.
JRNL        REF    PLANT PHYSIOL.                V. 141  1237 2006
JRNL        REFN                   ISSN 0032-0889
JRNL        PMID   16751439
JRNL        DOI    10.1104/PP.106.077693
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.21
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 6714547.780
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.6
REMARK   3   NUMBER OF REFLECTIONS             : 217826
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.189
REMARK   3   FREE R VALUE                     : 0.202
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 10846
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 34558
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330
REMARK   3   BIN FREE R VALUE                    : 0.2500
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1846
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3969
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 23
REMARK   3   SOLVENT ATOMS            : 613
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) : 0.19
REMARK   3   ESD FROM SIGMAA              (A) : 0.13
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK   4
REMARK   4 2DGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB025383.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-04
REMARK 200  TEMPERATURE           (KELVIN) : 95.0
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-6A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : TRIANGULAR SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 261540
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 19.500
REMARK 200  R MERGE                    (I) : 0.07900
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) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 17.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.56400
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1V03
REMARK 200
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 74.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM HEPES PH 7.2, 1M LISO4, 150MM
REMARK 280  NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290       5555   Z,X,Y
REMARK 290       6555   Z+1/2,-X+1/2,-Y
REMARK 290       7555   -Z+1/2,-X,Y+1/2
REMARK 290       8555   -Z,X+1/2,-Y+1/2
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z+1/2,-X+1/2
REMARK 290      11555   Y+1/2,-Z+1/2,-X
REMARK 290      12555   -Y+1/2,-Z,X+1/2
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4
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       97.32500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.32500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       97.32500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       97.32500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       97.32500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       97.32500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       97.32500
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       97.32500
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       97.32500
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       97.32500
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       97.32500
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       97.32500
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       97.32500
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       97.32500
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       97.32500
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       97.32500
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       97.32500
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       97.32500
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000      145.98750
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       48.66250
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       48.66250
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000      145.98750
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000      145.98750
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      145.98750
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       48.66250
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       48.66250
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      145.98750
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       48.66250
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000      145.98750
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       48.66250
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000      145.98750
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       48.66250
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       48.66250
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       48.66250
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000      145.98750
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       48.66250
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000      145.98750
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000      145.98750
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000      145.98750
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       48.66250
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       48.66250
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000      145.98750
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000      145.98750
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       48.66250
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       48.66250
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       48.66250
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       48.66250
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000      145.98750
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       48.66250
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000      145.98750
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       48.66250
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000      145.98750
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000      145.98750
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000      145.98750
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 23090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 95740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -187.0 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  0.000000  0.000000  1.000000      -97.32500
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      -97.32500
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      -97.32500
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000       97.32500
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000      -48.66250
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000       48.66250
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       48.66250
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000     -145.98750
REMARK 350   BIOMT2   5  0.000000  0.000000  1.000000      -48.66250
REMARK 350   BIOMT3   5  0.000000  1.000000  0.000000       48.66250
REMARK 350   BIOMT1   6  0.000000  0.000000 -1.000000      -48.66250
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000      -48.66250
REMARK 350   BIOMT3   6 -1.000000  0.000000  0.000000      -48.66250
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   -44
REMARK 465     HIS A   -43
REMARK 465     HIS A   -42
REMARK 465     HIS A   -41
REMARK 465     HIS A   -40
REMARK 465     HIS A   -39
REMARK 465     HIS A   -38
REMARK 465     SER A   -37
REMARK 465     SER A   -36
REMARK 465     GLY A   -35
REMARK 465     LEU A   -34
REMARK 465     VAL A   -33
REMARK 465     PRO A   -32
REMARK 465     ARG A   -31
REMARK 465     GLY A   -30
REMARK 465     SER A   -29
REMARK 465     GLY A   -28
REMARK 465     MET A   -27
REMARK 465     LYS A   -26
REMARK 465     GLU A   -25
REMARK 465     THR A   -24
REMARK 465     ALA A   -23
REMARK 465     ALA A   -22
REMARK 465     ALA A   -21
REMARK 465     LYS A   -20
REMARK 465     PHE A   -19
REMARK 465     GLU A   -18
REMARK 465     ARG A   -17
REMARK 465     GLN A   -16
REMARK 465     HIS A   -15
REMARK 465     MET A   -14
REMARK 465     ASP A   -13
REMARK 465     SER A   -12
REMARK 465     PRO A   -11
REMARK 465     ASP A   -10
REMARK 465     LEU A    -9
REMARK 465     GLY A    -8
REMARK 465     THR A    -7
REMARK 465     ASP A    -6
REMARK 465     ASP A    -5
REMARK 465     ASP A    -4
REMARK 465     ASP A    -3
REMARK 465     LYS A    -2
REMARK 465     ALA A    -1
REMARK 465     MET A     0
REMARK 465     ALA A     1
REMARK 465     GLY A     2
REMARK 465     THR A     3
REMARK 465     PRO A     4
REMARK 465     SER A     5
REMARK 465     LYS A     6
REMARK 465     PRO A     7
REMARK 465     ALA A     8
REMARK 465     GLU A     9
REMARK 465     PRO A    10
REMARK 465     ILE A    11
REMARK 465     LEU A   503
REMARK 465     LEU A   504
REMARK 465     LYS A   505
REMARK 465     THR A   506
REMARK 465     THR A   507
REMARK 465     ASN A   508
REMARK 465     ASN A   509
REMARK 465     ASN A   510
REMARK 465     ALA A   511
REMARK 465     THR A   512
REMARK 465     MET A   513
REMARK 465     THR A   514
REMARK 465     ALA A   515
REMARK 465     ALA A   516
REMARK 465     SER A   517
REMARK 465     VAL A   518
REMARK 465     SER A   519
REMARK 465     VAL A   520
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    ALA A  78     -128.28     53.74
REMARK 500    ASP A 147       31.68    -73.00
REMARK 500    TYR A 156       14.24   -144.04
REMARK 500    ARG A 225      -46.70   -130.79
REMARK 500    ASN A 250       40.40   -145.02
REMARK 500    TYR A 334      -37.98   -130.04
REMARK 500    TYR A 383       75.68   -153.34
REMARK 500    ASN A 408      131.01   -172.66
REMARK 500    TRP A 463     -120.90     40.92
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 A1813        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH A1816        DISTANCE =  5.35 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1316
DBREF  2DGA A    1   520  UNP    Q1XH05   Q1XH05_WHEAT    50    569
SEQADV 2DGA MET A  -44  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA HIS A  -43  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA HIS A  -42  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA HIS A  -41  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA HIS A  -40  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA HIS A  -39  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA HIS A  -38  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA SER A  -37  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA SER A  -36  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA GLY A  -35  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA LEU A  -34  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA VAL A  -33  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA PRO A  -32  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ARG A  -31  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA GLY A  -30  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA SER A  -29  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA GLY A  -28  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA MET A  -27  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA LYS A  -26  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA GLU A  -25  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA THR A  -24  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ALA A  -23  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ALA A  -22  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ALA A  -21  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA LYS A  -20  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA PHE A  -19  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA GLU A  -18  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ARG A  -17  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA GLN A  -16  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA HIS A  -15  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA MET A  -14  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ASP A  -13  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA SER A  -12  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA PRO A  -11  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ASP A  -10  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA LEU A   -9  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA GLY A   -8  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA THR A   -7  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ASP A   -6  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ASP A   -5  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ASP A   -4  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ASP A   -3  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA LYS A   -2  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA ALA A   -1  UNP  Q1XH05              CLONING ARTIFACT
SEQADV 2DGA MET A    0  UNP  Q1XH05              CLONING ARTIFACT
SEQRES   1 A  565  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES   2 A  565  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE
SEQRES   3 A  565  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP
SEQRES   4 A  565  ASP ASP ASP LYS ALA MET ALA GLY THR PRO SER LYS PRO
SEQRES   5 A  565  ALA GLU PRO ILE GLY PRO VAL PHE THR LYS LEU LYS PRO
SEQRES   6 A  565  TRP GLN ILE PRO LYS ARG ASP TRP PHE ASP LYS ASP PHE
SEQRES   7 A  565  LEU PHE GLY ALA SER THR SER ALA TYR GLN ILE GLU GLY
SEQRES   8 A  565  ALA TRP ASN GLU ASP GLY LYS GLY PRO SER THR TRP ASP
SEQRES   9 A  565  HIS PHE CYS HIS THR TYR PRO GLU ARG ILE SER ASP MET
SEQRES  10 A  565  THR ASN GLY ASP VAL ALA ALA ASN SER TYR HIS LEU TYR
SEQRES  11 A  565  GLU GLU ASP VAL LYS ALA LEU LYS ASP MET GLY MET LYS
SEQRES  12 A  565  VAL TYR ARG PHE SER ILE SER TRP SER ARG ILE LEU PRO
SEQRES  13 A  565  ASP GLY THR GLY LYS VAL ASN GLN ALA GLY ILE ASP TYR
SEQRES  14 A  565  TYR ASN LYS LEU ILE ASN SER LEU ILE ASP ASN ASP ILE
SEQRES  15 A  565  VAL PRO TYR VAL THR ILE TRP HIS TRP ASP THR PRO GLN
SEQRES  16 A  565  ALA LEU GLU ASP LYS TYR GLY GLY PHE LEU ASN ARG GLN
SEQRES  17 A  565  ILE VAL ASP ASP TYR LYS GLN PHE ALA GLU VAL CYS PHE
SEQRES  18 A  565  LYS ASN PHE GLY ASP ARG VAL LYS ASN TRP PHE THR PHE
SEQRES  19 A  565  ASN GLU PRO HIS THR TYR CYS CYS PHE SER TYR GLY GLU
SEQRES  20 A  565  GLY ILE HIS ALA PRO GLY ARG CYS SER PRO GLY MET ASP
SEQRES  21 A  565  CYS ALA VAL PRO GLU GLY ASP SER LEU ARG GLU PRO TYR
SEQRES  22 A  565  THR ALA GLY HIS HIS ILE LEU LEU ALA HIS ALA GLU ALA
SEQRES  23 A  565  VAL GLN LEU PHE LYS ALA ARG TYR ASN MET HIS GLY ASP
SEQRES  24 A  565  SER LYS ILE GLY MET ALA PHE ASP VAL MET GLY TYR GLU
SEQRES  25 A  565  PRO TYR GLN ASP SER PHE LEU ASP ASP GLN ALA ARG GLU
SEQRES  26 A  565  ARG SER ILE ASP TYR ASN MET GLY TRP PHE LEU GLU PRO
SEQRES  27 A  565  VAL VAL ARG GLY ASP TYR PRO PHE SER MET ARG SER LEU
SEQRES  28 A  565  ILE GLY ASP ARG LEU PRO MET PHE THR LYS GLU GLU GLN
SEQRES  29 A  565  GLU LYS LEU ALA SER SER CYS ASP ILE MET GLY LEU ASN
SEQRES  30 A  565  TYR TYR THR SER ARG PHE SER LYS HIS VAL ASP MET SER
SEQRES  31 A  565  PRO ASP PHE THR PRO THR LEU ASN THR ASP ASP ALA TYR
SEQRES  32 A  565  ALA SER SER GLU THR THR GLY SER ASP GLY ASN ASP ILE
SEQRES  33 A  565  GLY PRO ILE THR GLY THR TYR TRP ILE TYR MET TYR PRO
SEQRES  34 A  565  LYS GLY LEU THR ASP LEU LEU LEU ILE MET LYS GLU LYS
SEQRES  35 A  565  TYR GLY ASN PRO PRO VAL PHE ILE THR GLU ASN GLY ILE
SEQRES  36 A  565  ALA ASP VAL GLU GLY ASP GLU SER MET PRO ASP PRO LEU
SEQRES  37 A  565  ASP ASP TRP LYS ARG LEU ASP TYR LEU GLN ARG HIS ILE
SEQRES  38 A  565  SER ALA VAL LYS ASP ALA ILE ASP GLN GLY ALA ASP VAL
SEQRES  39 A  565  ARG GLY HIS PHE THR TRP GLY LEU ILE ASP ASN PHE GLU
SEQRES  40 A  565  TRP SER LEU GLY TYR SER SER ARG PHE GLY LEU VAL TYR
SEQRES  41 A  565  ILE ASP LYS ASN ASP GLY ASN LYS ARG LYS LEU LYS LYS
SEQRES  42 A  565  SER ALA LYS TRP PHE SER LYS PHE ASN SER VAL PRO LYS
SEQRES  43 A  565  PRO LEU LEU LYS THR THR ASN ASN ASN ALA THR MET THR
SEQRES  44 A  565  ALA ALA SER VAL SER VAL
HET    SO4  A1001       5
HET    GOL  A1314       6
HET    GOL  A1315       6
HET    GOL  A1316       6
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  SO4    O4 S 2-
FORMUL   3  GOL    3(C3 H8 O3)
FORMUL   6  HOH   *613(H2 O)
HELIX    1   1 LYS A   19  ILE A   23  5                                   5
HELIX    2   2 LYS A   25  PHE A   29  5                                   5
HELIX    3   3 SER A   40  GLU A   45  1                                   6
HELIX    4   4 SER A   56  TYR A   65  1                                  10
HELIX    5   5 PRO A   66  ILE A   69  5                                   4
HELIX    6   6 ASN A   80  GLY A   96  1                                  17
HELIX    7   7 SER A  105  LEU A  110  1                                   6
HELIX    8   8 ASN A  118  ASN A  135  1                                  18
HELIX    9   9 PRO A  149  GLY A  157  1                                   9
HELIX   10  10 GLY A  158  ARG A  162  5                                   5
HELIX   11  11 GLN A  163  GLY A  180  1                                  18
HELIX   12  12 GLU A  191  GLY A  201  1                                  11
HELIX   13  13 ARG A  225  TYR A  249  1                                  25
HELIX   14  14 SER A  272  MET A  287  1                                  16
HELIX   15  15 MET A  287  GLY A  297  1                                  11
HELIX   16  16 PRO A  300  GLY A  308  1                                   9
HELIX   17  17 ASP A  309  LEU A  311  5                                   3
HELIX   18  18 THR A  315  ALA A  323  1                                   9
HELIX   19  19 LEU A  352  ALA A  357  5                                   6
HELIX   20  20 TYR A  383  LYS A  397  1                                  15
HELIX   21  21 ASP A  425  GLN A  445  1                                  21
HELIX   22  22 GLU A  462  TYR A  467  5                                   6
HELIX   23  23 LYS A  487  ASN A  497  1                                  11
SHEET    1   A10 ALA A 359  GLU A 362  0
SHEET    2   A10 ILE A 328  HIS A 341 -1  N  PHE A 338   O  GLU A 362
SHEET    3   A10 VAL A 403  GLU A 407  1  O  PHE A 404   N  MET A 329
SHEET    4   A10 VAL A 449  TRP A 455  1  O  PHE A 453   N  ILE A 405
SHEET    5   A10 LEU A  34  SER A  38  1  N  GLY A  36   O  HIS A 452
SHEET    6   A10 VAL A  99  SER A 103  1  O  ARG A 101   N  ALA A  37
SHEET    7   A10 VAL A 138  TRP A 144  1  O  THR A 142   N  PHE A 102
SHEET    8   A10 ASN A 185  ASN A 190  1  O  PHE A 187   N  ILE A 143
SHEET    9   A10 LYS A 256  PRO A 268  1  O  GLY A 258   N  THR A 188
SHEET   10   A10 ILE A 328  HIS A 341  1  O  GLY A 330   N  PHE A 261
SHEET    1   B 2 ASP A 412  VAL A 413  0
SHEET    2   B 2 SER A 469  ARG A 470 -1  O  ARG A 470   N  ASP A 412
SHEET    1   C 2 VAL A 474  ILE A 476  0
SHEET    2   C 2 ARG A 484  LEU A 486 -1  O  LYS A 485   N  TYR A 475
SSBOND   1 CYS A  210    CYS A  216                          1555   1555  2.03
CISPEP   1 GLY A   12    PRO A   13          0        -0.04
CISPEP   2 ALA A  206    PRO A  207          0         0.51
SITE     1 AC1  8 GLN A 270  ASP A 271  SER A 366  ARG A 434
SITE     2 AC1  8 HOH A1465  HOH A1472  HOH A1589  HOH A1820
SITE     1 AC2  7 GLU A 191  ASP A 262  ASN A 332  TYR A 334
SITE     2 AC2  7 TRP A 379  GOL A1315  HOH A1741
SITE     1 AC3 11 GLN A  43  GLU A 191  TYR A 334  TRP A 379
SITE     2 AC3 11 GLU A 407  TRP A 455  GLU A 462  TRP A 463
SITE     3 AC3 11 PHE A 471  GOL A1314  HOH A1415
SITE     1 AC4  5 HIS A 205  GLU A 462  TRP A 463  SER A 464
SITE     2 AC4  5 HOH A1449
CRYST1  194.650  194.650  194.650  90.00  90.00  90.00 P 41 3 2     24
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      0.005137  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005137  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005137        0.00000
      
PROCHECK
Go to PROCHECK summary
 References