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PDBsum entry 1xoe

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Hydrolase PDB id
1xoe
Jmol
Contents
Protein chain
387 a.a.
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN
MAN
NAG ×2
ABX
Waters ×338
HEADER    HYDROLASE                               06-OCT-04   1XOE
TITLE     N9 TERN INFLUENZA NEURAMINIDASE COMPLEXED WITH (2R,4R,5R)-5-(1-
TITLE    2 ACETYLAMINO-3-METHYL-BUTYL-PYRROLIDINE-2, 4-DICAROBYXYLIC ACID 4-
TITLE    3 METHYL ESTERDASE COMPLEXED WITH
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: N9 TERN INFLUENZA NEURAMINIDASE;
COMPND   5 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 STRAIN: STRAIN A/TERN/AUSTRALIA/G70C/75
KEYWDS    NEURAMINIDASE, PYRROLIDINE INHIBITORS, INFLUENZA, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.T.WANG,S.WANG,R.GENTLES,T.SOWIN,C.J.MARING,D.J.KEMPF,W.M.KATI,
AUTHOR   2 V.STOLL,K.D.STEWART,G.LAVER
REVDAT   3   13-JUL-11 1XOE    1       VERSN
REVDAT   2   24-FEB-09 1XOE    1       VERSN
REVDAT   1   11-JAN-05 1XOE    0
JRNL        AUTH   G.T.WANG,S.WANG,R.GENTLES,T.SOWIN,C.J.MARING,D.J.KEMPF,
JRNL        AUTH 2 W.M.KATI,V.STOLL,K.D.STEWART,G.LAVER
JRNL        TITL   DESIGN, SYNTHESIS, AND STRUCTURAL ANALYSIS OF INHIBITORS OF
JRNL        TITL 2 INFLUENZA NEURAMINIDASE CONTAINING A 2,3-DISUBSTITUTED
JRNL        TITL 3 TETRAHYDROFURAN-5-CARBOXYLIC ACID CORE.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  15   125 2005
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   15582424
JRNL        DOI    10.1016/J.BMCL.2004.10.022
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNX 2000
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK   3               : YIP,DZAKULA)
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.99
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 259786.250
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.3
REMARK   3   NUMBER OF REFLECTIONS             : 22351
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 + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.265
REMARK   3   FREE R VALUE                     : 0.315
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 1522
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008
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   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 23873
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) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3462
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990
REMARK   3   BIN FREE R VALUE                    : 0.3370
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.10
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 264
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3055
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 132
REMARK   3   SOLVENT ATOMS            : 338
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33
REMARK   3   ESD FROM SIGMAA              (A) : 0.28
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) : 0.43
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.95
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL
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 : FLAT MODEL
REMARK   3   KSOL        : 0.33
REMARK   3   BSOL        : 10.26
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : NA2.PAR
REMARK   3  PARAMETER FILE  3  : NAG.PAR
REMARK   3  PARAMETER FILE  4  : MUL.PAR
REMARK   3  PARAMETER FILE  5  : &_1_PARAMETER_INFILE_5
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NA2.TOP
REMARK   3  TOPOLOGY FILE  3   : NAG.TOP
REMARK   3  TOPOLOGY FILE  4   : MUL.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1XOE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030576.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
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) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22351
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2
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) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.3
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 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   Z,X,Y
REMARK 290       6555   Z,-X,-Y
REMARK 290       7555   -Z,-X,Y
REMARK 290       8555   -Z,X,-Y
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z,-X
REMARK 290      11555   Y,-Z,-X
REMARK 290      12555   -Y,-Z,X
REMARK 290      13555   Y,X,-Z
REMARK 290      14555   -Y,-X,-Z
REMARK 290      15555   Y,-X,Z
REMARK 290      16555   -Y,X,Z
REMARK 290      17555   X,Z,-Y
REMARK 290      18555   -X,Z,Y
REMARK 290      19555   -X,-Z,-Y
REMARK 290      20555   X,-Z,Y
REMARK 290      21555   Z,Y,-X
REMARK 290      22555   Z,-Y,X
REMARK 290      23555   -Z,Y,X
REMARK 290      24555   -Z,-Y,-X
REMARK 290      25555   X+1/2,Y+1/2,Z+1/2
REMARK 290      26555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      27555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      28555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      29555   Z+1/2,X+1/2,Y+1/2
REMARK 290      30555   Z+1/2,-X+1/2,-Y+1/2
REMARK 290      31555   -Z+1/2,-X+1/2,Y+1/2
REMARK 290      32555   -Z+1/2,X+1/2,-Y+1/2
REMARK 290      33555   Y+1/2,Z+1/2,X+1/2
REMARK 290      34555   -Y+1/2,Z+1/2,-X+1/2
REMARK 290      35555   Y+1/2,-Z+1/2,-X+1/2
REMARK 290      36555   -Y+1/2,-Z+1/2,X+1/2
REMARK 290      37555   Y+1/2,X+1/2,-Z+1/2
REMARK 290      38555   -Y+1/2,-X+1/2,-Z+1/2
REMARK 290      39555   Y+1/2,-X+1/2,Z+1/2
REMARK 290      40555   -Y+1/2,X+1/2,Z+1/2
REMARK 290      41555   X+1/2,Z+1/2,-Y+1/2
REMARK 290      42555   -X+1/2,Z+1/2,Y+1/2
REMARK 290      43555   -X+1/2,-Z+1/2,-Y+1/2
REMARK 290      44555   X+1/2,-Z+1/2,Y+1/2
REMARK 290      45555   Z+1/2,Y+1/2,-X+1/2
REMARK 290      46555   Z+1/2,-Y+1/2,X+1/2
REMARK 290      47555   -Z+1/2,Y+1/2,X+1/2
REMARK 290      48555   -Z+1/2,-Y+1/2,-X+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  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        0.00000
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000
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        0.00000
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  25  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000       90.18200
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       90.18200
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       90.18200
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       90.18200
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       90.18200
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       90.18200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 26960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 103.0 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  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   3 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
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    CYS A 320   CA  -  CB  -  SG  ANGL. DEV. =   7.8 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    SER A  97     -174.06   -179.93
REMARK 500    ASP A 112       37.47   -141.37
REMARK 500    THR A 139      159.04    175.34
REMARK 500    THR A 149       10.05    -67.98
REMARK 500    SER A 165       -2.65     70.49
REMARK 500    ASN A 202       39.46   -168.00
REMARK 500    ASN A 223       86.59   -157.28
REMARK 500    ILE A 224       70.32     50.72
REMARK 500    GLU A 279       71.86     35.92
REMARK 500    CYS A 293     -162.69   -118.67
REMARK 500    ASN A 327      132.44   -174.11
REMARK 500    ASN A 360       45.88    -86.09
REMARK 500    SER A 404     -132.45   -119.61
REMARK 500    TYR A 413        2.05    -61.59
REMARK 500    PHE A 454       78.48   -102.30
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 562        DISTANCE =  6.29 ANGSTROMS
REMARK 525    HOH A 612        DISTANCE =  6.81 ANGSTROMS
REMARK 525    HOH A 641        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A 674        DISTANCE =  5.88 ANGSTROMS
REMARK 525    HOH A 739        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH A 756        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH A 812        DISTANCE =  5.15 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     MAN A  507
REMARK 610     NAG A  508
REMARK 610     NAG A  509
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABX A 500
DBREF  1XOE A   84   470  UNP    P03472   NRAM_IATRA      84    470
SEQRES   1 A  387  ASP PHE ASN ASN LEU THR LYS GLY LEU CYS THR ILE ASN
SEQRES   2 A  387  SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL ARG ILE
SEQRES   3 A  387  GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLU PRO TYR
SEQRES   4 A  387  VAL SER CYS ASP PRO ASP GLU CYS ARG PHE TYR ALA LEU
SEQRES   5 A  387  SER GLN GLY THR THR ILE ARG GLY LYS HIS SER ASN GLY
SEQRES   6 A  387  THR ILE HIS ASP ARG SER GLN TYR ARG ALA LEU ILE SER
SEQRES   7 A  387  TRP PRO LEU SER SER PRO PRO THR VAL TYR ASN SER ARG
SEQRES   8 A  387  VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS ASP
SEQRES   9 A  387  GLY LYS THR ARG MET SER ILE CYS ILE SER GLY PRO ASN
SEQRES  10 A  387  ASN ASN ALA SER ALA VAL ILE TRP TYR ASN ARG ARG PRO
SEQRES  11 A  387  VAL THR GLU ILE ASN THR TRP ALA ARG ASN ILE LEU ARG
SEQRES  12 A  387  THR GLN GLU SER GLU CYS VAL CYS HIS ASN GLY VAL CYS
SEQRES  13 A  387  PRO VAL VAL PHE THR ASP GLY SER ALA THR GLY PRO ALA
SEQRES  14 A  387  GLU THR ARG ILE TYR TYR PHE LYS GLU GLY LYS ILE LEU
SEQRES  15 A  387  LYS TRP GLU PRO LEU ALA GLY THR ALA LYS HIS ILE GLU
SEQRES  16 A  387  GLU CYS SER CYS TYR GLY GLU ARG ALA GLU ILE THR CYS
SEQRES  17 A  387  THR CYS ARG ASP ASN TRP GLN GLY SER ASN ARG PRO VAL
SEQRES  18 A  387  ILE ARG ILE ASP PRO VAL ALA MET THR HIS THR SER GLN
SEQRES  19 A  387  TYR ILE CYS SER PRO VAL LEU THR ASP ASN PRO ARG PRO
SEQRES  20 A  387  ASN ASP PRO THR VAL GLY LYS CYS ASN ASP PRO TYR PRO
SEQRES  21 A  387  GLY ASN ASN ASN ASN GLY VAL LYS GLY PHE SER TYR LEU
SEQRES  22 A  387  ASP GLY VAL ASN THR TRP LEU GLY ARG THR ILE SER ILE
SEQRES  23 A  387  ALA SER ARG SER GLY TYR GLU MET LEU LYS VAL PRO ASN
SEQRES  24 A  387  ALA LEU THR ASP ASP LYS SER LYS PRO THR GLN GLY GLN
SEQRES  25 A  387  THR ILE VAL LEU ASN THR ASP TRP SER GLY TYR SER GLY
SEQRES  26 A  387  SER PHE MET ASP TYR TRP ALA GLU GLY GLU CYS TYR ARG
SEQRES  27 A  387  ALA CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG PRO LYS
SEQRES  28 A  387  GLU ASP LYS VAL TRP TRP THR SER ASN SER ILE VAL SER
SEQRES  29 A  387  MET CYS SER SER THR GLU PHE LEU GLY GLN TRP ASP TRP
SEQRES  30 A  387  PRO ASP GLY ALA LYS ILE GLU TYR PHE LEU
HET    NAG  A 501      14
HET    NAG  A 502      14
HET    BMA  A 503      11
HET    MAN  A 504      11
HET    MAN  A 505      11
HET    MAN  A 506      11
HET    MAN  A 507      11
HET    NAG  A 508      14
HET    NAG  A 509      14
HET    ABX  A 500      21
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     ABX 5-[1-(ACETYLAMINO)-3-METHYLBUTYL]-4-(METHOXYCARBONYL)
HETNAM   2 ABX  PROLINE
FORMUL   2  NAG    4(C8 H15 N O6)
FORMUL   2  BMA    C6 H12 O6
FORMUL   2  MAN    4(C6 H12 O6)
FORMUL   6  ABX    C14 H24 N2 O5
FORMUL   7  HOH   *338(H2 O)
HELIX    1   1 ASN A  105  GLU A  111  1                                   7
HELIX    2   2 GLY A  143  ASN A  147  5                                   5
HELIX    3   3 LYS A  465  LEU A  470  5                                   6
SHEET    1   A 4 SER A  97  LYS A 103  0
SHEET    2   A 4 THR A 441  SER A 451 -1  O  SER A 447   N  TYR A 101
SHEET    3   A 4 CYS A 423  GLY A 431 -1  N  PHE A 424   O  MET A 448
SHEET    4   A 4 SER A 407  PHE A 410 -1  N  GLY A 408   O  TYR A 425
SHEET    1   B 4 TYR A 122  CYS A 125  0
SHEET    2   B 4 CYS A 130  SER A 136 -1  O  TYR A 133   N  TYR A 122
SHEET    3   B 4 ALA A 158  PRO A 163 -1  O  ILE A 160   N  ALA A 134
SHEET    4   B 4 ARG A 174  ILE A 178 -1  O  ARG A 174   N  SER A 161
SHEET    1   C 4 SER A 182  HIS A 186  0
SHEET    2   C 4 ARG A 191  SER A 197 -1  O  MET A 192   N  CYS A 185
SHEET    3   C 4 SER A 204  TYR A 209 -1  O  TRP A 208   N  SER A 193
SHEET    4   C 4 ARG A 212  ASN A 218 -1  O  THR A 215   N  ILE A 207
SHEET    1   D 4 ARG A 226  THR A 227  0
SHEET    2   D 4 VAL A 238  GLY A 246 -1  O  THR A 244   N  ARG A 226
SHEET    3   D 4 ALA A 252  LYS A 260 -1  O  PHE A 259   N  CYS A 239
SHEET    4   D 4 LYS A 263  PRO A 269 -1  O  LYS A 266   N  TYR A 258
SHEET    1   E 4 SER A 281  GLU A 285  0
SHEET    2   E 4 GLU A 288  THR A 292 -1  O  THR A 292   N  SER A 281
SHEET    3   E 4 PRO A 303  ASP A 308 -1  O  ILE A 307   N  ILE A 289
SHEET    4   E 4 THR A 313  TYR A 318 -1  O  THR A 313   N  ASP A 308
SHEET    1   F 4 SER A 354  TYR A 355  0
SHEET    2   F 4 TRP A 362  ARG A 365 -1  O  TRP A 362   N  TYR A 355
SHEET    3   F 4 SER A 373  LYS A 379 -1  O  LEU A 378   N  LEU A 363
SHEET    4   F 4 GLN A 393  TRP A 403 -1  O  GLN A 395   N  MET A 377
SSBOND   1 CYS A   93    CYS A  419                          1555   1555  2.02
SSBOND   2 CYS A  125    CYS A  130                          1555   1555  2.04
SSBOND   3 CYS A  177    CYS A  195                          1555   1555  2.02
SSBOND   4 CYS A  185    CYS A  232                          1555   1555  2.04
SSBOND   5 CYS A  234    CYS A  239                          1555   1555  2.02
SSBOND   6 CYS A  280    CYS A  293                          1555   1555  2.04
SSBOND   7 CYS A  282    CYS A  291                          1555   1555  2.03
SSBOND   8 CYS A  320    CYS A  338                          1555   1555  2.03
SSBOND   9 CYS A  423    CYS A  449                          1555   1555  2.03
LINK         O4  NAG A 501                 C1  NAG A 502     1555   1555  1.42
LINK         O4  NAG A 502                 C1  BMA A 503     1555   1555  1.41
LINK         O3  BMA A 503                 C1  MAN A 504     1555   1555  1.38
LINK         O2  MAN A 504                 C1  MAN A 505     1555   1555  1.42
LINK         O2  MAN A 505                 C1  MAN A 506     1555   1555  1.44
CISPEP   1 ASN A  327    PRO A  328          0        -0.42
CISPEP   2 ARG A  432    PRO A  433          0         0.24
SITE     1 AC1 10 ASN A 201  ASN A 202  LEU A 455  GLY A 456
SITE     2 AC1 10 GLN A 457  NAG A 502  HOH A 512  HOH A 521
SITE     3 AC1 10 HOH A 793  HOH A 845
SITE     1 AC2 11 GLN A 393  GLY A 394  PHE A 454  NAG A 501
SITE     2 AC2 11 BMA A 503  HOH A 521  HOH A 671  HOH A 758
SITE     3 AC2 11 HOH A 781  HOH A 786  HOH A 821
SITE     1 AC3 11 LEU A 378  PRO A 391  THR A 392  GLN A 393
SITE     2 AC3 11 GLY A 394  NAG A 502  MAN A 504  MAN A 507
SITE     3 AC3 11 HOH A 681  HOH A 779  HOH A 781
SITE     1 AC4  7 ARG A 365  GLU A 376  BMA A 503  MAN A 505
SITE     2 AC4  7 MAN A 506  HOH A 769  HOH A 783
SITE     1 AC5  5 ASP A 332  LYS A 390  PRO A 391  MAN A 504
SITE     2 AC5  5 MAN A 506
SITE     1 AC6 10 ARG A 329  ASN A 331  ASP A 332  ARG A 365
SITE     2 AC6 10 ILE A 367  ILE A 369  MAN A 504  MAN A 505
SITE     3 AC6 10 HOH A 636  HOH A 726
SITE     1 AC7  4 THR A 392  BMA A 503  HOH A 628  HOH A 836
SITE     1 AC8  2 ASN A 147  TRP A 439
SITE     1 AC9  5 ASP A  84  PHE A  85  ASN A  87  ASN A 236
SITE     2 AC9  5 HOH A 829
SITE     1 BC1 14 ARG A 119  GLU A 120  ASP A 152  ARG A 153
SITE     2 BC1 14 ARG A 157  TRP A 180  ARG A 226  ALA A 248
SITE     3 BC1 14 GLU A 278  GLU A 279  ARG A 294  ARG A 372
SITE     4 BC1 14 TYR A 406  HOH A 662
CRYST1  180.364  180.364  180.364  90.00  90.00  90.00 I 4 3 2      48
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      0.005544  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005544  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005544        0.00000
      
PROCHECK
Go to PROCHECK summary
 References