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PDBsum entry 1f8b

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Hydrolase/hydrolase inhibitor PDB id
1f8b
Jmol
Contents
Protein chain
388 a.a. *
Ligands
NAG-NAG-MAN-MAN-
MAN-MAN-MAN
NAG-NAG
NAG
DAN
Metals
_CA ×2
Waters ×346
* Residue conservation analysis
HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-JUN-00   1F8B
TITLE     NATIVE INFLUENZA VIRUS NEURAMINIDASE IN COMPLEX WITH NEU5AC2EN
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 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS
SOURCE   3 (A/TERN/AUSTRALIA/G70C/1975(H11N9));
SOURCE   4 ORGANISM_TAXID: 384509;
SOURCE   5 STRAIN: A/TERN/AUSTRALIA/G70C/75;
SOURCE   6 EXPRESSION_SYSTEM: INFLUENZA A VIRUS;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 11320;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: RECOMBINANT (NWS/G70C) N9
KEYWDS    NEURAMINIDASE, HYDROLASE, INFLUENZA PROTEIN, GLYCOSYLATED PROTEIN,
KEYWDS   2 DANA, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.J.SMITH,P.M.COLMAN,M.VON ITZSTEIN,B.DANYLEC,J.N.VARGHESE
REVDAT   4   16-NOV-11 1F8B    1       HETATM
REVDAT   3   13-JUL-11 1F8B    1       VERSN
REVDAT   2   24-FEB-09 1F8B    1       VERSN
REVDAT   1   11-APR-01 1F8B    0
JRNL        AUTH   B.J.SMITH,P.M.COLMAN,M.VON ITZSTEIN,B.DANYLEC,J.N.VARGHESE
JRNL        TITL   ANALYSIS OF INHIBITOR BINDING IN INFLUENZA VIRUS
JRNL        TITL 2 NEURAMINIDASE.
JRNL        REF    PROTEIN SCI.                  V.  10   689 2001
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   11274459
JRNL        DOI    10.1110/PS.41801
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 34793
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 SET) : 0.166
REMARK   3   FREE R VALUE                     : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1726
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3067
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 145
REMARK   3   SOLVENT ATOMS            : 346
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.012
REMARK   3   BOND ANGLES            (DEGREES) : 1.80
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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  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: NULL
REMARK   4
REMARK   4 1F8B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-00.
REMARK 100 THE RCSB ID CODE IS RCSB011366.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-96
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                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30479
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 75.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.07100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE, PH 5.9, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293.0 K
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       90.51500
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000       90.51500
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       90.51500
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       90.51500
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       90.51500
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       90.51500
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       90.51500
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 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 A1490  LIES ON A SPECIAL POSITION.
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ASP A  127   OD1
REMARK 480     LYS A  261   CE   NZ
REMARK 480     GLU A  416   OE1  OE2
REMARK 480     LYS A  463   NZ
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  96     -176.69   -174.53
REMARK 500    ASP A 111       48.28   -146.06
REMARK 500    ARG A 118      169.67    179.28
REMARK 500    THR A 148       10.59    -66.07
REMARK 500    ASN A 200       38.34   -153.60
REMARK 500    ILE A 222       71.12     48.73
REMARK 500    THR A 225     -152.62   -131.55
REMARK 500    GLU A 277       64.49     37.88
REMARK 500    CYS A 291     -163.37   -114.15
REMARK 500    GLN A 315     -163.54   -162.34
REMARK 500    ASN A 359       43.53    -78.76
REMARK 500    SER A 404     -140.38   -118.85
REMARK 500    SER A 440     -159.57   -150.30
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 A1381        DISTANCE =  6.47 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     NAG A 1087
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 999  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 297   O
REMARK 620 2 HOH A1154   O    93.1
REMARK 620 3 ASP A 293   O    77.7  88.3
REMARK 620 4 HOH A1236   O    82.8  80.3 156.9
REMARK 620 5 ASN A 347   O   165.8  73.3 105.3  90.8
REMARK 620 6 ASP A 324   OD1  84.1 175.4  94.6  95.7 109.2
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 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 475
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 DAN A 0
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7NN9   RELATED DB: PDB
REMARK 900 THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX OF 4-GUANIDINO-
REMARK 900 NEU5AC2EN AND INFLUENZA VIRUS NEURAMINIDASE PROTEIN
REMARK 900 SCIENCE(1995),4:1081-1087 J.N.VARGHESE, V.C.EPA, P.M.COLMAN
REMARK 900 RELATED ID: 1F8C   RELATED DB: PDB
REMARK 900 RELATED ID: 1F8D   RELATED DB: PDB
REMARK 900 RELATED ID: 1F8E   RELATED DB: PDB
DBREF  1F8B A   82   468  GB     324880   AAA43574        83    470
SEQADV 1F8B MET A  376  GB   324880    ILE   377 CONFLICT
SEQADV 1F8B ASP A  386  GB   324880    GLU   387 CONFLICT
SEQADV 1F8B LYS A  387  GB   324880    ARG   388 CONFLICT
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 GLU 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 1F8B ASN A   86  ASN  GLYCOSYLATION SITE
MODRES 1F8B ASN A  200  ASN  GLYCOSYLATION SITE
MODRES 1F8B ASN A  146  ASN  GLYCOSYLATION SITE
HET    NAG  A 469      14
HET    NAG  A 470      14
HET    MAN  A 471      11
HET    MAN  A 472      11
HET    MAN  A 473      11
HET    MAN  A 474      11
HET    MAN  A 475      11
HET    NAG  A1086      14
HET    NAG  A1087      12
HET    NAG  A1146      14
HET     CA  A 999       1
HET     CA  A 998       1
HET    DAN  A   0      20
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM      CA CALCIUM ION
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   2  NAG    5(C8 H15 N O6)
FORMUL   2  MAN    5(C6 H12 O6)
FORMUL   6   CA    2(CA 2+)
FORMUL   8  DAN    C11 H17 N O8
FORMUL   9  HOH   *346(H2 O)
HELIX    1   1 ASN A  104  GLY A  109  1                                   6
HELIX    2   2 GLU A  110  SER A  112  5                                   3
HELIX    3   3 GLY A  142  ASN A  146  5                                   5
HELIX    4   4 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  SER A 445   N  TYR A 100
SHEET    3   A 4 CYS A 421  GLY A 429 -1  N  PHE A 422   O  MET A 446
SHEET    4   A 4 SER A 407  PHE A 410 -1  O  GLY A 408   N  TYR A 423
SHEET    1   B 4 TYR A 121  CYS A 124  0
SHEET    2   B 4 CYS A 129  SER A 135 -1  N  ARG A 130   O  SER A 123
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  N  ARG A 172   O  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  N  MET A 190   O  CYS A 183
SHEET    3   C 4 SER A 202  TYR A 207 -1  N  SER A 202   O  SER A 195
SHEET    4   C 4 ARG A 210  ASN A 216 -1  O  ARG A 210   N  TYR A 207
SHEET    1   D 3 VAL A 236  GLY A 244  0
SHEET    2   D 3 ALA A 250  LYS A 258 -1  N  GLU A 251   O  ASP A 243
SHEET    3   D 3 LYS A 261  PRO A 267 -1  O  LYS A 261   N  LYS A 258
SHEET    1   E 4 GLU A 276  GLU A 283  0
SHEET    2   E 4 GLU A 286  ARG A 292 -1  O  GLU A 286   N  GLU A 283
SHEET    3   E 4 PRO A 301  ASP A 306 -1  O  PRO A 301   N  CYS A 291
SHEET    4   E 4 THR A 311  TYR A 316 -1  O  THR A 311   N  ASP A 306
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  N  GLU A 375   O  ARG A 364
SHEET    4   F 4 GLN A 392  TRP A 403 -1  O  GLN A 392   N  LYS A 378
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.03
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.04
SSBOND   3 CYS A  175    CYS A  193                          1555   1555  2.03
SSBOND   4 CYS A  183    CYS A  230                          1555   1555  2.04
SSBOND   5 CYS A  232    CYS A  237                          1555   1555  2.03
SSBOND   6 CYS A  278    CYS A  291                          1555   1555  2.05
SSBOND   7 CYS A  280    CYS A  289                          1555   1555  2.04
SSBOND   8 CYS A  318    CYS A  337                          1555   1555  2.03
SSBOND   9 CYS A  421    CYS A  447                          1555   1555  2.05
LINK         O4  NAG A 470                 C1  MAN A 471     1555   1555  1.40
LINK         O2  MAN A 473                 C1  MAN A 474     1555   1555  1.41
LINK         O3  MAN A 471                 C1  MAN A 472     1555   1555  1.41
LINK         C1  MAN A 475                 O6  MAN A 471     1555   1555  1.42
LINK         C1  NAG A 470                 O4  NAG A 469     1555   1555  1.44
LINK         ND2 ASN A  86                 C1  NAG A1086     1555   1555  1.44
LINK         C1  MAN A 473                 O2  MAN A 472     1555   1555  1.45
LINK         C1  NAG A 469                 ND2 ASN A 200     1555   1555  1.45
LINK         ND2 ASN A 146                 C1  NAG A1146     1555   1555  1.46
LINK         O4  NAG A1086                 C1  NAG A1087     1555   1555  2.38
LINK        CA    CA A 998                 O   HOH A1449     1555   1555  2.90
LINK        CA    CA A 999                 O   GLY A 297     1555   1555  2.61
LINK        CA    CA A 999                 O   HOH A1154     1555   1555  2.79
LINK        CA    CA A 999                 O   ASP A 293     1555   1555  2.61
LINK        CA    CA A 999                 O   HOH A1236     1555   1555  2.77
LINK        CA    CA A 999                 O   ASN A 347     1555   1555  2.57
LINK        CA    CA A 999                 OD1 ASP A 324     1555   1555  2.76
LINK        CA    CA A 998                 O   HOH A1449     1555  15555  2.90
LINK        CA    CA A 998                 O   HOH A1449     1555   2555  2.90
LINK        CA    CA A 998                 O   HOH A1449     1555  16555  2.90
CISPEP   1 ASN A  325    PRO A  326          0        -0.58
CISPEP   2 ARG A  430    PRO A  431          0         0.43
SITE     1 AC1  9 ASN A 199  ASN A 200  ARG A 220  LEU A 453
SITE     2 AC1  9 GLY A 454  GLN A 455  NAG A 470  HOH A1226
SITE     3 AC1  9 HOH A1376
SITE     1 AC2  8 GLN A 392  GLY A 394  PHE A 452  NAG A 469
SITE     2 AC2  8 MAN A 471  HOH A1173  HOH A1362  HOH A1438
SITE     1 AC3 10 LEU A 377  THR A 391  GLN A 392  GLY A 394
SITE     2 AC3 10 NAG A 470  MAN A 472  MAN A 475  HOH A1222
SITE     3 AC3 10 HOH A1362  HOH A1452
SITE     1 AC4  6 ARG A 364  GLU A 375  MAN A 471  MAN A 473
SITE     2 AC4  6 MAN A 474  HOH A1296
SITE     1 AC5  7 ASP A 330  ARG A 364  LYS A 389  PRO A 390
SITE     2 AC5  7 MAN A 472  MAN A 474  HOH A1408
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 A 472  MAN A 473
SITE     3 AC6 11 HOH A1221  HOH A1293  HOH A1296
SITE     1 AC7  3 MAN A 471  HOH A1358  HOH A1359
SITE     1 AC8  6 ASP A  83  PHE A  84  ASN A  86  ASN A 234
SITE     2 AC8  6 NAG A1087  HOH A1328
SITE     1 AC9  2 ASP A  83  NAG A1086
SITE     1 BC1  2 ASN A 146  TRP A 437
SITE     1 BC2  6 ASP A 293  GLY A 297  ASP A 324  ASN A 347
SITE     2 BC2  6 HOH A1154  HOH A1236
SITE     1 BC3  1 HOH A1449
SITE     1 BC4 19 ARG A 118  GLU A 119  ASP A 151  ARG A 152
SITE     2 BC4 19 TRP A 178  ILE A 222  ARG A 224  ALA A 246
SITE     3 BC4 19 GLU A 276  GLU A 277  ARG A 292  ARG A 371
SITE     4 BC4 19 TYR A 406  HOH A1234  HOH A1279  HOH A1281
SITE     5 BC4 19 HOH A1472  HOH A1473  HOH A1481
CRYST1  181.030  181.030  181.030  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      0.005524  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005524  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005524        0.00000
      
PROCHECK
Go to PROCHECK summary
 References