spacer
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PDBsum entry 1l7g

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Hydrolase PDB id
1l7g
Jmol
Contents
Protein chain
388 a.a. *
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN-MAN
NAG-NAG
NAG
BCZ
GOL ×3
Metals
_CA ×2
Waters ×573
* Residue conservation analysis
HEADER    HYDROLASE                               15-MAR-02   1L7G
TITLE     CRYSTAL STRUCTURE OF E119G MUTANT INFLUENZA VIRUS NEURAMINIDASE IN
TITLE    2 COMPLEX WITH BCX-1812
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: INTEGRAL MEMBRANE PROTEIN, MEMBRANE STALK CLEAVED BY
COMPND   5 PRONASE RELEASING FULLY ACTIVE RESIDUES 82-468;
COMPND   6 EC: 3.2.1.18;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 STRAIN: A/NWS/TERN/AUSTRALIA/G70C/75
KEYWDS    NEURAMINIDASE, HYDROLASE, INFLUENZA, GLYCOSYLATED PROTEIN, BCX-1812,
KEYWDS   2 E119G MUTANT
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.J.SMITH,J.L.MCKIMM-BRESHKIN,M.MCDONALD,R.T.FERNLEY,J.N.VARGHESE,
AUTHOR   2 P.M.COLMAN
REVDAT   4   13-JUL-11 1L7G    1       VERSN
REVDAT   3   24-FEB-09 1L7G    1       VERSN
REVDAT   2   01-APR-03 1L7G    1       JRNL
REVDAT   1   29-MAY-02 1L7G    0
JRNL        AUTH   B.J.SMITH,J.L.MCKIMM-BRESHKIN,M.MCDONALD,R.T.FERNLEY,
JRNL        AUTH 2 J.N.VARGHESE,P.M.COLMAN
JRNL        TITL   STRUCTURAL STUDIES OF THE RESISTANCE OF INFLUENZA VIRUS
JRNL        TITL 2 NEURAMINDASE TO INHIBITORS.
JRNL        REF    J.MED.CHEM.                   V.  45  2207 2002
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   12014958
JRNL        DOI    10.1021/JM010528U
REMARK   2
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 41542
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.148
REMARK   3   FREE R VALUE                     : 0.168
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2092
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3062
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 168
REMARK   3   SOLVENT ATOMS            : 573
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.008 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 0.026 ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1L7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-02.
REMARK 100 THE RCSB ID CODE IS RCSB015710.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 113
REMARK 200  PH                             : 5.9
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          : MACSCIENCE
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : ELLIPTICAL GLASS MONOCAPILLARY
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43185
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 26.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.76000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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   (%): 56.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE, PH 5.9, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293K
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       90.37500
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000       90.37500
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       90.37500
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       90.37500
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       90.37500
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       90.37500
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       90.37500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 21780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 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 CA    CA A 998  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1778  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    ASP A 127   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 172   CG  -  CD  -  NE  ANGL. DEV. =  16.4 DEGREES
REMARK 500    ARG A 172   CD  -  NE  -  CZ  ANGL. DEV. =  55.3 DEGREES
REMARK 500    ARG A 172   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG A 209   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG A 327   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES
REMARK 500    GLU A 465   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.0 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    ASP A 111       43.66   -142.43
REMARK 500    SER A 164       -3.56     70.86
REMARK 500    ASN A 200       44.22   -154.45
REMARK 500    ASN A 221       80.83   -155.16
REMARK 500    GLU A 277       62.64     36.90
REMARK 500    TRP A 295      -77.04    -79.73
REMARK 500    GLN A 315     -163.98   -163.88
REMARK 500    ASN A 359       47.50    -84.58
REMARK 500    SER A 404     -138.95   -118.98
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 A1551        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH A1654        DISTANCE =  5.91 ANGSTROMS
REMARK 525    HOH A1709        DISTANCE =  5.94 ANGSTROMS
REMARK 525    HOH A1739        DISTANCE =  6.84 ANGSTROMS
REMARK 525    HOH A1754        DISTANCE =  5.78 ANGSTROMS
REMARK 525    HOH A1767        DISTANCE =  6.52 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 998  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1613   O
REMARK 620 2 HOH A1437   O    93.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 999  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1314   O
REMARK 620 2 GLY A 297   O    93.6
REMARK 620 3 ASN A 347   O    73.5 165.4
REMARK 620 4 HOH A1318   O    82.4  86.4  98.4
REMARK 620 5 ASP A 324   OD1 177.2  86.8 106.4  94.9
REMARK 620 6 ASP A 293   O    89.9  73.8  98.8 158.4  92.8
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 NAG A 1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1086
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1087
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1146
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCZ A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L7F   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF INFLUENZA VIRUS NEURAMINIDASE IN
REMARK 900 COMPLEX WITH BCX-1812
REMARK 900 RELATED ID: 1L7H   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF R292K MUTANT INFLUENZA VIRUS
REMARK 900 NEURAMINIDASE IN COMPLEX WITH BCX-1812
DBREF  1L7G A   82   468  UNP    P03472   NRAM_IATRA      83    470
SEQADV 1L7G GLY A  119  UNP  P03472    GLU   120 ENGINEERED
SEQRES   1 A  388  ARG ASP PHE ASN ASN LEU THR LYS GLY LEU CYS THR ILE
SEQRES   2 A  388  ASN SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL ARG
SEQRES   3 A  388  ILE GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLY PRO
SEQRES   4 A  388  TYR VAL SER CYS ASP PRO ASP GLU CYS ARG PHE TYR ALA
SEQRES   5 A  388  LEU SER GLN GLY THR THR ILE ARG GLY LYS HIS SER ASN
SEQRES   6 A  388  GLY THR ILE HIS ASP ARG SER GLN TYR ARG ALA LEU ILE
SEQRES   7 A  388  SER TRP PRO LEU SER SER PRO PRO THR VAL TYR ASN SER
SEQRES   8 A  388  ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS
SEQRES   9 A  388  ASP GLY LYS THR ARG MET SER ILE CYS ILE SER GLY PRO
SEQRES  10 A  388  ASN ASN ASN ALA SER ALA VAL ILE TRP TYR ASN ARG ARG
SEQRES  11 A  388  PRO VAL THR GLU ILE ASN THR TRP ALA ARG ASN ILE LEU
SEQRES  12 A  388  ARG THR GLN GLU SER GLU CYS VAL CYS HIS ASN GLY VAL
SEQRES  13 A  388  CYS PRO VAL VAL PHE THR ASP GLY SER ALA THR GLY PRO
SEQRES  14 A  388  ALA GLU THR ARG ILE TYR TYR PHE LYS GLU GLY LYS ILE
SEQRES  15 A  388  LEU LYS TRP GLU PRO LEU ALA GLY THR ALA LYS HIS ILE
SEQRES  16 A  388  GLU GLU CYS SER CYS TYR GLY GLU ARG ALA GLU ILE THR
SEQRES  17 A  388  CYS THR CYS ARG ASP ASN TRP GLN GLY SER ASN ARG PRO
SEQRES  18 A  388  VAL ILE ARG ILE ASP PRO VAL ALA MET THR HIS THR SER
SEQRES  19 A  388  GLN TYR ILE CYS SER PRO VAL LEU THR ASP ASN PRO ARG
SEQRES  20 A  388  PRO ASN ASP PRO THR VAL GLY LYS CYS ASN ASP PRO TYR
SEQRES  21 A  388  PRO GLY ASN ASN ASN ASN GLY VAL LYS GLY PHE SER TYR
SEQRES  22 A  388  LEU ASP GLY VAL ASN THR TRP LEU GLY ARG THR ILE SER
SEQRES  23 A  388  ILE ALA SER ARG SER GLY TYR GLU MET LEU LYS VAL PRO
SEQRES  24 A  388  ASN ALA LEU THR ASP ASP LYS SER LYS PRO THR GLN GLY
SEQRES  25 A  388  GLN THR ILE VAL LEU ASN THR ASP TRP SER GLY TYR SER
SEQRES  26 A  388  GLY SER PHE MET ASP TYR TRP ALA GLU GLY GLU CYS TYR
SEQRES  27 A  388  ARG ALA CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG PRO
SEQRES  28 A  388  LYS GLU ASP LYS VAL TRP TRP THR SER ASN SER ILE VAL
SEQRES  29 A  388  SER MET CYS SER SER THR GLU PHE LEU GLY GLN TRP ASP
SEQRES  30 A  388  TRP PRO ASP GLY ALA LYS ILE GLU TYR PHE LEU
MODRES 1L7G ASN A   86  ASN  GLYCOSYLATION SITE
MODRES 1L7G ASN A  146  ASN  GLYCOSYLATION SITE
MODRES 1L7G ASN A  200  ASN  GLYCOSYLATION SITE
HET    NAG  A1200      14
HET    NAG  A1201      14
HET    BMA  A1202      11
HET    MAN  A1203      11
HET    MAN  A1204      11
HET    MAN  A1205      11
HET    MAN  A1206      11
HET    NAG  A1086      14
HET    NAG  A1087      14
HET    NAG  A1146      14
HET     CA  A 999       1
HET     CA  A 998       1
HET    BCZ  A 801      23
HET    GOL  A 701       6
HET    GOL  A 702       6
HET    GOL  A 703       6
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM      CA CALCIUM ION
HETNAM     BCZ 3-(1-ACETYLAMINO-2-ETHYL-BUTYL)-4-GUANIDINO-2-HYDROXY-
HETNAM   2 BCZ  CYCLOPENTANECARBOXYLIC ACID
HETNAM     GOL GLYCEROL
HETSYN     BCZ BCX-1812
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  NAG    5(C8 H15 N O6)
FORMUL   2  BMA    C6 H12 O6
FORMUL   2  MAN    4(C6 H12 O6)
FORMUL   5   CA    2(CA 2+)
FORMUL   7  BCZ    C15 H28 N4 O4
FORMUL   8  GOL    3(C3 H8 O3)
FORMUL  11  HOH   *573(H2 O)
HELIX    1   1 ASN A  104  GLU A  110  1                                   7
HELIX    2   2 GLY A  142  ASN A  146  5                                   5
HELIX    3   3 LYS A  463  LEU A  468  5                                   6
SHEET    1   A 4 SER A  96  LYS A 102  0
SHEET    2   A 4 THR A 439  SER A 449 -1  O  CYS A 447   N  HIS A  98
SHEET    3   A 4 CYS A 421  GLY A 429 -1  N  VAL A 424   O  VAL A 444
SHEET    4   A 4 SER A 407  PHE A 410 -1  N  GLY A 408   O  TYR A 423
SHEET    1   B 4 LEU A 115  ASP A 125  0
SHEET    2   B 4 GLU A 128  THR A 139 -1  O  GLU A 128   N  ASP A 125
SHEET    3   B 4 ALA A 157  PRO A 162 -1  O  ALA A 157   N  SER A 135
SHEET    4   B 4 ARG A 172  ILE A 176 -1  O  ARG A 172   N  SER A 160
SHEET    1   C 4 SER A 179  HIS A 184  0
SHEET    2   C 4 ARG A 189  SER A 195 -1  O  MET A 190   N  CYS A 183
SHEET    3   C 4 SER A 202  TYR A 207 -1  O  TRP A 206   N  SER A 191
SHEET    4   C 4 ARG A 210  ASN A 216 -1  O  THR A 213   N  ILE A 205
SHEET    1   D 4 ARG A 224  THR A 225  0
SHEET    2   D 4 CYS A 237  GLY A 244 -1  O  THR A 242   N  ARG A 224
SHEET    3   D 4 ALA A 250  LYS A 258 -1  O  PHE A 257   N  CYS A 237
SHEET    4   D 4 LYS A 261  PRO A 267 -1  O  GLU A 266   N  ILE A 254
SHEET    1   E 4 SER A 279  GLU A 283  0
SHEET    2   E 4 GLU A 286  THR A 290 -1  O  THR A 290   N  SER A 279
SHEET    3   E 4 PRO A 301  ASP A 306 -1  O  ILE A 305   N  ILE A 287
SHEET    4   E 4 THR A 311  TYR A 316 -1  O  GLN A 315   N  VAL A 302
SHEET    1   F 4 SER A 353  TYR A 354  0
SHEET    2   F 4 TRP A 361  ARG A 364 -1  O  TRP A 361   N  TYR A 354
SHEET    3   F 4 SER A 372  LYS A 378 -1  O  LEU A 377   N  LEU A 362
SHEET    4   F 4 GLN A 392  TRP A 403 -1  O  GLN A 395   N  MET A 376
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.05
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.04
SSBOND   3 CYS A  175    CYS A  193                          1555   1555  2.05
SSBOND   4 CYS A  183    CYS A  230                          1555   1555  2.06
SSBOND   5 CYS A  232    CYS A  237                          1555   1555  2.03
SSBOND   6 CYS A  278    CYS A  291                          1555   1555  2.08
SSBOND   7 CYS A  280    CYS A  289                          1555   1555  2.05
SSBOND   8 CYS A  318    CYS A  337                          1555   1555  2.06
SSBOND   9 CYS A  421    CYS A  447                          1555   1555  2.05
LINK         ND2 ASN A  86                 C1  NAG A1086     1555   1555  1.47
LINK         ND2 ASN A 146                 C1  NAG A1146     1555   1555  1.46
LINK         ND2 ASN A 200                 C1  NAG A1200     1555   1555  1.45
LINK         O4  NAG A1200                 C1  NAG A1201     1555   1555  1.41
LINK         O4  NAG A1201                 C1  BMA A1202     1555   1555  1.41
LINK         O3  BMA A1202                 C1  MAN A1203     1555   1555  1.41
LINK         O6  BMA A1202                 C1  MAN A1206     1555   1555  1.42
LINK         O2  MAN A1203                 C1  MAN A1204     1555   1555  1.39
LINK         O2  MAN A1204                 C1  MAN A1205     1555   1555  1.41
LINK         O4  NAG A1086                 C1  NAG A1087     1555   1555  1.41
LINK        CA    CA A 998                 O   HOH A1613     1555   1555  3.05
LINK        CA    CA A 998                 O   HOH A1437     1555   1555  2.90
LINK        CA    CA A 999                 O   HOH A1314     1555   1555  2.83
LINK        CA    CA A 999                 O   GLY A 297     1555   1555  2.72
LINK        CA    CA A 999                 O   ASN A 347     1555   1555  2.75
LINK        CA    CA A 999                 O   HOH A1318     1555   1555  2.79
LINK        CA    CA A 999                 OD1 ASP A 324     1555   1555  2.75
LINK        CA    CA A 999                 O   ASP A 293     1555   1555  2.66
LINK        CA    CA A 998                 O   HOH A1437     1555  16555  2.90
LINK        CA    CA A 998                 O   HOH A1437     1555   2555  2.90
LINK        CA    CA A 998                 O   HOH A1613     1555  15555  3.05
LINK        CA    CA A 998                 O   HOH A1613     1555   2555  3.05
LINK        CA    CA A 998                 O   HOH A1613     1555  16555  3.05
LINK        CA    CA A 998                 O   HOH A1437     1555  15555  2.90
CISPEP   1 ASN A  325    PRO A  326          0        -4.80
CISPEP   2 ARG A  430    PRO A  431          0         0.84
SITE     1 AC1 11 ASN A 200  ARG A 220  LEU A 453  GLY A 454
SITE     2 AC1 11 GLN A 455  NAG A1201  HOH A1231  HOH A1256
SITE     3 AC1 11 HOH A1546  HOH A1607  HOH A1608
SITE     1 AC2  9 GLN A 392  GLY A 394  NAG A1200  BMA A1202
SITE     2 AC2  9 HOH A1231  HOH A1286  HOH A1339  HOH A1476
SITE     3 AC2  9 HOH A1599
SITE     1 AC3 11 LEU A 377  THR A 391  GLN A 392  GLY A 394
SITE     2 AC3 11 NAG A1201  MAN A1203  MAN A1206  HOH A1339
SITE     3 AC3 11 HOH A1428  HOH A1548  HOH A1618
SITE     1 AC4 10 ARG A 364  GLU A 375  BMA A1202  MAN A1204
SITE     2 AC4 10 MAN A1205  HOH A1377  HOH A1423  HOH A1583
SITE     3 AC4 10 HOH A1612  HOH A1730
SITE     1 AC5 10 ASP A 330  ARG A 364  LYS A 389  PRO A 390
SITE     2 AC5 10 MAN A1203  MAN A1205  HOH A1434  HOH A1630
SITE     3 AC5 10 HOH A1759  HOH A1771
SITE     1 AC6 11 ARG A 327  ASN A 329  ASP A 330  ARG A 364
SITE     2 AC6 11 ILE A 366  ILE A 368  MAN A1203  MAN A1204
SITE     3 AC6 11 HOH A1271  HOH A1292  HOH A1537
SITE     1 AC7  6 BMA A1202  HOH A1518  HOH A1542  HOH A1634
SITE     2 AC7  6 HOH A1646  HOH A1770
SITE     1 AC8  7 ASP A  83  PHE A  84  ASN A  86  ASN A 234
SITE     2 AC8  7 NAG A1087  HOH A1464  HOH A1490
SITE     1 AC9  4 ASP A  83  NAG A1086  HOH A1628  HOH A1763
SITE     1 BC1  6 ASN A 146  TRP A 437  HOH A1517  HOH A1582
SITE     2 BC1  6 HOH A1601  HOH A1605
SITE     1 BC2  6 ASP A 293  GLY A 297  ASP A 324  ASN A 347
SITE     2 BC2  6 HOH A1314  HOH A1318
SITE     1 BC3  2 HOH A1437  HOH A1613
SITE     1 BC4 15 ARG A 118  LEU A 134  ASP A 151  ARG A 152
SITE     2 BC4 15 ARG A 156  TRP A 178  GLU A 227  GLU A 276
SITE     3 BC4 15 GLU A 277  ARG A 292  ARG A 371  TYR A 406
SITE     4 BC4 15 HOH A1241  HOH A1503  HOH A1604
SITE     1 BC5  5 LYS A 336  CYS A 337  ASN A 338  ASP A 339
SITE     2 BC5  5 HOH A1589
SITE     1 BC6  5 ARG A 107  HIS A 144  THR A 148  HOH A1512
SITE     2 BC6  5 HOH A1690
SITE     1 BC7 10 ALA A 413  GLU A 414  CYS A 417  ARG A 419
SITE     2 BC7 10 HOH A1280  HOH A1364  HOH A1365  HOH A1420
SITE     3 BC7 10 HOH A1457  HOH A1485
CRYST1  180.750  180.750  180.750  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      0.005533  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005533  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005533        0.00000
      
PROCHECK
Go to PROCHECK summary
 References