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PDBsum entry 2qwd

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Hydrolase PDB id
2qwd
Jmol
Contents
Protein chain
388 a.a.
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN-MAN
NAG-NAG
NAG
4AM
Metals
_CA ×2
Waters ×400
HEADER    HYDROLASE                               07-APR-98   2QWD
TITLE     THE X-RAY STRUCTURE OF A COMPLEX OF 4-AMINO-NEU5AC2EN AND A DRUG
TITLE    2 RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 82 - 468;
COMPND   5 SYNONYM: SIALIDASE;
COMPND   6 EC: 3.2.1.18;
COMPND   7 MUTATION: YES;
COMPND   8 OTHER_DETAILS: INTEGRAL MEMBRANE PROTEIN, MEMBRANE BOUND STALK
COMPND   9 CLEAVED BY PRONASE, RELEASING FULLY ACTIVE HEAD WITH RESIDUES 82 -
COMPND  10 468
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 STRAIN: A/TERN/AUSTRALIA/G70C/75;
SOURCE   5 VARIANT: NEURAMINIDASE R292K MUTATION (N2-TOKYO/3/67 NUMBERING)
KEYWDS    NEURAMINIDASE, INFLUENZA PROTEIN, DRUG RESISTANT VARIANT, SIALIC ACID
KEYWDS   2 ANALOGUES, DANA ANOLOGUES, GLYCOSYLATED PROTEIN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.N.VARGHESE
REVDAT   4   13-JUL-11 2QWD    1       VERSN
REVDAT   3   24-FEB-09 2QWD    1       VERSN
REVDAT   2   01-APR-03 2QWD    1       JRNL
REVDAT   1   11-NOV-98 2QWD    0
JRNL        AUTH   J.N.VARGHESE,P.W.SMITH,S.L.SOLLIS,T.J.BLICK,A.SAHASRABUDHE,
JRNL        AUTH 2 J.L.MCKIMM-BRESCHKIN,P.M.COLMAN
JRNL        TITL   DRUG DESIGN AGAINST A SHIFTING TARGET: A STRUCTURAL BASIS
JRNL        TITL 2 FOR RESISTANCE TO INHIBITORS IN A VARIANT OF INFLUENZA VIRUS
JRNL        TITL 3 NEURAMINIDASE.
JRNL        REF    STRUCTURE                     V.   6   735 1998
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   9655825
JRNL        DOI    10.1016/S0969-2126(98)00075-6
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.L.MCKIMM-BRESCHKIN,A.SAHASRABUDHE,T.J.BLICK,M.MCDONALD,
REMARK   1  AUTH 2 P.M.COLMAN,G.J.HART,R.C.BETHELL,J.N.VARGHESE
REMARK   1  TITL   MUTATIONS IN A CONSERVED RESIDUE IN THE INFLUENZA VIRUS
REMARK   1  TITL 2 NEURAMINIDASE ACTIVE SITE DECREASES SENSITIVITY TO
REMARK   1  TITL 3 NEU5AC2EN-DERIVED INHIBITORS
REMARK   1  REF    J.VIROL.                      V.  72  2456 1998
REMARK   1  REFN                   ISSN 0022-538X
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.0
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.0
REMARK   3   NUMBER OF REFLECTIONS             : 30018
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.165
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.03
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1262
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250
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            : 3065
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 147
REMARK   3   SOLVENT ATOMS            : 400
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.01
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00
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) : 0.013
REMARK   3   BOND ANGLES            (DEGREES) : 1.87
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) : 2.500 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.000 ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.000 ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.500 ; 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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : CHO.PAR
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPCHO.PAR
REMARK   3  TOPOLOGY FILE  3   : 4AMI.TOP
REMARK   3  TOPOLOGY FILE  4   : TOPHPEP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: 2 METAL IONS
REMARK   4
REMARK   4 2QWD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-AUG-96
REMARK 200  TEMPERATURE           (KELVIN) : 107
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 M18X
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : YALE MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS II
REMARK 200  DATA SCALING SOFTWARE          : PROTEIN V. 4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37126
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 79.1
REMARK 200  DATA REDUNDANCY                : 5.050
REMARK 200  R MERGE                    (I) : 0.08900
REMARK 200  R SYM                      (I) : 0.07700
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 29.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.0
REMARK 200 STARTING MODEL: TERN N9 R292K MUTANT NEURAMINIDASE
REMARK 200
REMARK 200 REMARK: THIS EXPERIMENT WAS CARRIED OUT TO DETERMINE THE STRUCTURE
REMARK 200  OF COMPLEX OF 4-AMINO-NEU5AC2EN AND A DRUG RESISTANT VARIANT OF
REMARK 200  TERN N9 NEURAMINIDASE GROWN IN PRESENCE OF THE ANTI-INFLUENZA
REMARK 200  CARBOXAMIDE DRUG 5-N-ACETYL-4-GUANIDINO-6METHYL(PROPYL)
REMARK 200  CARBOXAMIDE-4,5-DIHYDRO-2HPYRAN-2-CARBOXYLIC ACID. THE VARIANT
REMARK 200  HAS A SINGLE R292K MUTATION.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9M PHOSPHATE (PH 5.9)
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       90.45000
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000       90.45000
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       90.45000
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       90.45000
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       90.45000
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       90.45000
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       90.45000
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  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2 -1.000000  0.000000  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 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        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 989  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1391T LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1323Q 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     ARG A   82   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP A  127   OD2
REMARK 480     ARG A  220   CD   NE   CZ   NH1  NH2
REMARK 480     LYS A  261   CE   NZ
REMARK 480     LYS A  387   NZ
REMARK 480     GLU A  416   OE1  OE2
REMARK 480     LYS A  463   NZ
REMARK 480     GLU A  465   CD   OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  1312Q    O    HOH A  1313Q   48555     0.65
REMARK 500   O    HOH A  1349R    O    HOH A  1352R   31555     0.68
REMARK 500   O    HOH A  1269N    O    HOH A  1269N   48555     0.90
REMARK 500   O    HOH A  1362R    O    HOH A  1365R   48555     1.26
REMARK 500   NZ   LYS A   389     O    HOH A  1362R   48555     2.02
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  96     -176.88   -175.81
REMARK 500    ASP A 111       42.94   -144.57
REMARK 500    THR A 148        5.21    -66.48
REMARK 500    ASN A 200       37.94   -152.13
REMARK 500    ASN A 221       83.36   -152.41
REMARK 500    THR A 225     -154.10   -133.82
REMARK 500    CYS A 291     -151.96   -113.69
REMARK 500    GLN A 315     -167.52   -161.83
REMARK 500    ASN A 359       47.75    -84.78
REMARK 500    SER A 404     -140.61   -116.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    GLN A 226        24.6      L          L   OUTSIDE RANGE
REMARK 500    THR A 323        24.5      L          L   OUTSIDE RANGE
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 A1233L       DISTANCE =  6.24 ANGSTROMS
REMARK 525    HOH A1393T       DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A1394T       DISTANCE =  5.56 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 989  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1392T  O
REMARK 620 2 HOH A1304P  O    53.4
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 A1088G  O
REMARK 620 2 GLY A 297   O    79.1
REMARK 620 3 HOH A1007W  O    86.7  93.3
REMARK 620 4 ASN A 347   O    95.0 166.6  74.3
REMARK 620 5 ASP A 293   O   155.4  77.4  87.4 106.3
REMARK 620 6 ASP A 324   OD2  86.0  84.9 172.7 106.8  99.1
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 469A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 470B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 471C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 472D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 473E
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 474F
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 475G
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 476A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 477B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 478A
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 989
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4AM A 800
DBREF  2QWD A   82   468  UNP    P03472   NRAM_IATRA      83    470
SEQADV 2QWD LYS A  292  UNP  P03472    ARG   294 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 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 LYS 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 2QWD ASN A   86  ASN  GLYCOSYLATION SITE
MODRES 2QWD ASN A  146  ASN  GLYCOSYLATION SITE
MODRES 2QWD ASN A  200  ASN  GLYCOSYLATION SITE
HET    NAG  A 469A     14
HET    NAG  A 470B     14
HET    BMA  A 471C     11
HET    MAN  A 472D     11
HET    MAN  A 473E     11
HET    MAN  A 474F     11
HET    MAN  A 475G     11
HET    NAG  A 476A     14
HET    NAG  A 477B     14
HET    NAG  A 478A     14
HET     CA  A 999       1
HET     CA  A 989       1
HET    4AM  A 800      20
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM      CA CALCIUM ION
HETNAM     4AM 4-AMINO-2-DEOXY-2,3-DEHYDRO-N-NEURAMINIC ACID
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  4AM    C11 H18 N2 O7
FORMUL   8  HOH   *400(H2 O)
HELIX    1   1 ALA A  105  ASP A  111  1                                   7
HELIX    2   2 LYS A  143  SER A  145  5                                   3
HELIX    3   3 ILE A  464  TYR A  466  5                                   3
SHEET    1   A 4 TYR A 121  ASP A 125  0
SHEET    2   A 4 GLU A 128  SER A 135 -1  N  TYR A 132   O  TYR A 121
SHEET    3   A 4 ALA A 157  PRO A 162 -1  N  TRP A 161   O  PHE A 131
SHEET    4   A 4 ARG A 172  ILE A 176 -1  N  CYS A 175   O  LEU A 158
SHEET    1   B 4 SER A 179  HIS A 184  0
SHEET    2   B 4 ARG A 189  SER A 195 -1  N  ILE A 194   O  SER A 179
SHEET    3   B 4 SER A 202  TYR A 207 -1  N  TRP A 206   O  SER A 191
SHEET    4   B 4 ARG A 210  ASN A 216 -1  N  ILE A 215   O  ALA A 203
SHEET    1   C 4 VAL A 231  HIS A 233  0
SHEET    2   C 4 VAL A 236  GLY A 244 -1  N  PRO A 238   O  VAL A 231
SHEET    3   C 4 ALA A 250  LYS A 258 -1  N  PHE A 257   O  CYS A 237
SHEET    4   C 4 LYS A 261  PRO A 267 -1  N  GLU A 266   O  ILE A 254
SHEET    1   D 4 SER A 279  GLU A 283  0
SHEET    2   D 4 GLU A 286  THR A 290 -1  N  THR A 290   O  SER A 279
SHEET    3   D 4 PRO A 301  ASP A 306 -1  N  ILE A 305   O  ILE A 287
SHEET    4   D 4 THR A 311  TYR A 316 -1  N  GLN A 315   O  VAL A 302
SHEET    1   E 3 TRP A 361  ARG A 364  0
SHEET    2   E 3 TYR A 374  LYS A 378 -1  N  LEU A 377   O  LEU A 362
SHEET    3   E 3 GLN A 392  VAL A 398 -1  N  VAL A 398   O  TYR A 374
SHEET    1   F 4 SER A 407  PHE A 410  0
SHEET    2   F 4 CYS A 421  GLY A 429 -1  N  TYR A 423   O  GLY A 408
SHEET    3   F 4 THR A 439  SER A 449 -1  N  MET A 446   O  PHE A 422
SHEET    4   F 4 SER A  96  LYS A 102 -1  N  GLY A 101   O  SER A 445
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.02
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  2.03
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  2.05
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         ND2 ASN A  86                 C1  NAG A 476A    1555   1555  1.46
LINK         ND2 ASN A 146                 C1  NAG A 478A    1555   1555  1.45
LINK         ND2 ASN A 200                 C1  NAG A 469A    1555   1555  1.46
LINK         O4  NAG A 469A                C1  NAG A 470B    1555   1555  1.44
LINK         O4  NAG A 470B                C1  BMA A 471C    1555   1555  1.41
LINK         O3  BMA A 471C                C1  MAN A 472D    1555   1555  1.42
LINK         O6  BMA A 471C                C1  MAN A 475G    1555   1555  1.48
LINK         O2  MAN A 472D                C1  MAN A 473E    1555   1555  1.44
LINK         O2  MAN A 473E                C1  MAN A 474F    1555   1555  1.42
LINK         O4  NAG A 476A                C1  NAG A 477B    1555   1555  1.40
LINK        CA    CA A 989                 O   HOH A1392T    1555   1555  3.10
LINK        CA    CA A 989                 O   HOH A1304P    1555   1555  2.41
LINK        CA    CA A 999                 O   HOH A1088G    1555   1555  2.64
LINK        CA    CA A 999                 O   GLY A 297     1555   1555  2.40
LINK        CA    CA A 999                 O   HOH A1007W    1555   1555  2.79
LINK        CA    CA A 999                 O   ASN A 347     1555   1555  2.56
LINK        CA    CA A 999                 O   ASP A 293     1555   1555  2.48
LINK        CA    CA A 999                 OD2 ASP A 324     1555   1555  2.73
LINK        CA    CA A 989                 O   HOH A1304P    1555  16555  2.41
LINK        CA    CA A 989                 O   HOH A1392T    1555  16555  3.10
LINK        CA    CA A 989                 O   HOH A1392T    1555   2555  3.10
LINK        CA    CA A 989                 O   HOH A1304P    1555   2555  2.41
LINK        CA    CA A 989                 O   HOH A1304P    1555  15555  2.41
LINK        CA    CA A 989                 O   HOH A1392T    1555  15555  3.10
CISPEP   1 ASN A  325    PRO A  326          0       -10.22
CISPEP   2 ARG A  430    PRO A  431          0         7.23
SITE     1 AC1 10 ASN A 199  ASN A 200  LEU A 453  GLY A 454
SITE     2 AC1 10 GLN A 455  NAG A 470B HOH A1078W HOH A1228K
SITE     3 AC1 10 HOH A1292N HOH A1341R
SITE     1 AC2  8 GLN A 392  GLY A 394  NAG A 469A BMA A 471C
SITE     2 AC2  8 HOH A1026W HOH A1213K HOH A1228K HOH A1292N
SITE     1 AC3  9 LEU A 377  THR A 391  GLN A 392  GLY A 394
SITE     2 AC3  9 NAG A 470B MAN A 472D MAN A 475G HOH A1074W
SITE     3 AC3  9 HOH A1213K
SITE     1 AC4  7 ARG A 364  GLU A 375  BMA A 471C MAN A 473E
SITE     2 AC4  7 MAN A 474F HOH A1147F HOH A1283N
SITE     1 AC5  8 ASP A 330  ARG A 364  LYS A 389  PRO A 390
SITE     2 AC5  8 MAN A 472D MAN A 474F HOH A1260M HOH A1357R
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 472D MAN A 473E
SITE     3 AC6 11 HOH A1073W HOH A1144F HOH A1349R
SITE     1 AC7  4 BMA A 471C HOH A1209K HOH A1210K HOH A1329Q
SITE     1 AC8  6 ASP A  83  PHE A  84  ASN A  86  ASN A 234
SITE     2 AC8  6 NAG A 477B HOH A1179G
SITE     1 AC9  2 ASP A  83  NAG A 476A
SITE     1 BC1  3 ASN A 146  TRP A 437  HOH A1163F
SITE     1 BC2  6 ASP A 293  GLY A 297  ASP A 324  ASN A 347
SITE     2 BC2  6 HOH A1007W HOH A1088G
SITE     1 BC3  2 HOH A1304P HOH A1392T
SITE     1 BC4 14 ARG A 118  GLU A 119  ASP A 151  ARG A 152
SITE     2 BC4 14 ALA A 246  GLU A 276  LYS A 292  ARG A 371
SITE     3 BC4 14 TYR A 406  HOH A1086G HOH A1384T HOH A1385T
SITE     4 BC4 14 HOH A1386T HOH A1396T
CRYST1  180.900  180.900  180.900  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      0.005528  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005528  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005528        0.00000
      
PROCHECK
Go to PROCHECK summary
 References