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PDBsum entry 1nnb

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Hydrolase(o-glycosyl) PDB id
1nnb
Jmol
Contents
Protein chain
387 a.a.
Ligands
DAN
Metals
_CA
HEADER    HYDROLASE(O-GLYCOSYL)                   08-MAR-93   1NNB
TITLE     THREE-DIMENSIONAL STRUCTURE OF INFLUENZA A N9 NEURAMINIDASE AND ITS
TITLE    2 COMPLEX WITH THE INHIBITOR 2-DEOXY 2,3-DEHYDRO-N-ACETYL NEURAMINIC
TITLE    3 ACID
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.18;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 STRAIN: A/TERN/AUSTRALIA/G70C/75 H11N9;
SOURCE   5 CELL_LINE: S2
KEYWDS    HYDROLASE(O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.BOSSART-WHITAKER,M.CARSON,Y.S.BABU,C.D.SMITH,W.G.LAVER,G.M.AIR
REVDAT   3   13-JUL-11 1NNB    1       VERSN
REVDAT   2   24-FEB-09 1NNB    1       VERSN
REVDAT   1   30-APR-94 1NNB    0
JRNL        AUTH   P.BOSSART-WHITAKER,M.CARSON,Y.S.BABU,C.D.SMITH,W.G.LAVER,
JRNL        AUTH 2 G.M.AIR
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF INFLUENZA A N9 NEURAMINIDASE
JRNL        TITL 2 AND ITS COMPLEX WITH THE INHIBITOR 2-DEOXY
JRNL        TITL 3 2,3-DEHYDRO-N-ACETYL NEURAMINIC ACID.
JRNL        REF    J.MOL.BIOL.                   V. 232  1069 1993
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   8371267
JRNL        DOI    10.1006/JMBI.1993.1461
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   P.J.BOSSART-WHITAKER
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF INFLUENZA
REMARK   1  TITL 2 A(SLASH)TERN(SLASH)AUSTRALIA(SLASH)G70C(SLASH)75 N9
REMARK   1  TITL 3 NEURAMINIDASE AND ITS COMPLEX WITH THE INHIBITOR
REMARK   1  TITL 4 2-DEOXY-2,3-DEHYDRO N-ACETYL NEURAMINIC ACID
REMARK   1  REF    THESIS                                     1992
REMARK   1  REFN                   ISSN 0049-3848
REMARK   1 REFERENCE 2
REMARK   1  AUTH   J.M.NUSS,G.M.AIR
REMARK   1  TITL   TRANSFER OF THE HEMAGGLUTININ ACTIVITY OF INFLUENZA VIRUS
REMARK   1  TITL 2 NEURAMINIDASE SUBTYPE N9 INTO AN N2 BACKGROUND
REMARK   1  REF    VIROLOGY                      V. 183   496 1991
REMARK   1  REFN                   ISSN 0042-6822
REMARK   1 REFERENCE 3
REMARK   1  AUTH   W.R.TULIP,J.N.VARGHESE,A.T.BAKER,A.VAN DONKELAAR,W.G.LAVER,
REMARK   1  AUTH 2 R.G.WEBSTER,P.M.COLMAN
REMARK   1  TITL   REFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA VIRUS
REMARK   1  TITL 2 NEURAMINIDASE AND ESCAPE MUTANTS
REMARK   1  REF    J.MOL.BIOL.                   V. 221   487 1991
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 4
REMARK   1  AUTH   A.T.BAKER,J.N.VARGHESE,W.G.LAVER,G.M.AIR,P.M.COLMAN
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF NEURAMINIDASE OF SUBTYPE N9
REMARK   1  TITL 2 FROM AN AVIAN INFLUENZA VIRUS
REMARK   1  REF    PROTEINS                      V.   2   111 1987
REMARK   1  REFN                   ISSN 0887-3585
REMARK   1 REFERENCE 5
REMARK   1  AUTH   G.M.AIR,L.R.RITCHIE,W.G.LAVER,P.M.COLMAN
REMARK   1  TITL   GENE AND PROTEIN SEQUENCE OF AN INFLUENZA NEURAMINIDASE WITH
REMARK   1  TITL 2 HEMAGGLUTININ ACTIVITY
REMARK   1  REF    VIROLOGY                      V. 145   117 1985
REMARK   1  REFN                   ISSN 0042-6822
REMARK   1 REFERENCE 6
REMARK   1  AUTH   W.G.LAVER,P.M.COLMAN,R.G.WEBSTER,V.S.HINSHAW
REMARK   1  TITL   INFLUENZA VIRUS NEURAMINIDASE WITH HEMAGGLUTININ ACTIVITY
REMARK   1  REF    VIROLOGY                      V. 137   314 1984
REMARK   1  REFN                   ISSN 0042-6822
REMARK   1 REFERENCE 7
REMARK   1  TITL   MEMORANDUM: A REVISION OF THE SYSTEM OF NOMENCLATURE FOR
REMARK   1  TITL 2 INFLUENZA VIRUSES
REMARK   1  REF    BULL.WHO.                     V.  58   585 1980
REMARK   1  REFN                   ISSN 0366-4996
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
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             : 10389
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) : 0.179
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           : 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            : 3056
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 21
REMARK   3   SOLVENT ATOMS            : 0
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) : 0.013
REMARK   3   BOND ANGLES            (DEGREES) : 1.60
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:
REMARK   3  RESIDUE 336 IS GLY.  IT WAS REFINED AS ASN AND THE AUTHORS
REMARK   3  NOTED THAT THE SIDE CHAIN OF THIS RESIDUE NEVER DISPLAYED
REMARK   3  DENSITY (SEE FIGURE 3A OF THE PAPER CITED ON *JRNL* RECORDS
REMARK   3  ABOVE).  THE AUTHORS BELIEVE THAT CHANGING IT TO GLY WILL
REMARK   3  HAVE A NEGLIGIBLE EFFECT ON THE REST OF THE STRUCTURE.
REMARK   4
REMARK   4 1NNB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 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: NULL
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   (%): 58.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   Z,X,Y
REMARK 290       6555   Z,-X,-Y
REMARK 290       7555   -Z,-X,Y
REMARK 290       8555   -Z,X,-Y
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z,-X
REMARK 290      11555   Y,-Z,-X
REMARK 290      12555   -Y,-Z,X
REMARK 290      13555   Y,X,-Z
REMARK 290      14555   -Y,-X,-Z
REMARK 290      15555   Y,-X,Z
REMARK 290      16555   -Y,X,Z
REMARK 290      17555   X,Z,-Y
REMARK 290      18555   -X,Z,Y
REMARK 290      19555   -X,-Z,-Y
REMARK 290      20555   X,-Z,Y
REMARK 290      21555   Z,Y,-X
REMARK 290      22555   Z,-Y,X
REMARK 290      23555   -Z,Y,X
REMARK 290      24555   -Z,-Y,-X
REMARK 290      25555   X+1/2,Y+1/2,Z+1/2
REMARK 290      26555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      27555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      28555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      29555   Z+1/2,X+1/2,Y+1/2
REMARK 290      30555   Z+1/2,-X+1/2,-Y+1/2
REMARK 290      31555   -Z+1/2,-X+1/2,Y+1/2
REMARK 290      32555   -Z+1/2,X+1/2,-Y+1/2
REMARK 290      33555   Y+1/2,Z+1/2,X+1/2
REMARK 290      34555   -Y+1/2,Z+1/2,-X+1/2
REMARK 290      35555   Y+1/2,-Z+1/2,-X+1/2
REMARK 290      36555   -Y+1/2,-Z+1/2,X+1/2
REMARK 290      37555   Y+1/2,X+1/2,-Z+1/2
REMARK 290      38555   -Y+1/2,-X+1/2,-Z+1/2
REMARK 290      39555   Y+1/2,-X+1/2,Z+1/2
REMARK 290      40555   -Y+1/2,X+1/2,Z+1/2
REMARK 290      41555   X+1/2,Z+1/2,-Y+1/2
REMARK 290      42555   -X+1/2,Z+1/2,Y+1/2
REMARK 290      43555   -X+1/2,-Z+1/2,-Y+1/2
REMARK 290      44555   X+1/2,-Z+1/2,Y+1/2
REMARK 290      45555   Z+1/2,Y+1/2,-X+1/2
REMARK 290      46555   Z+1/2,-Y+1/2,X+1/2
REMARK 290      47555   -Z+1/2,Y+1/2,X+1/2
REMARK 290      48555   -Z+1/2,-Y+1/2,-X+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  25  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000       91.89000
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       91.89000
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       91.89000
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       91.89000
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       91.89000
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       91.89000
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: 15680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   3 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   HE   ARG A   294    HD21  ASN A   296              1.40
REMARK 500   HD1  HIS A   186     H    GLY A   188              1.48
REMARK 500   H    LEU A    88     HD1  HIS A   235              1.57
REMARK 500
REMARK 500 REMARK: NULL
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   HE2  HIS A   145     H    LYS A   465    15555     1.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  97     -173.44   -172.77
REMARK 500    LYS A 103      134.16   -178.12
REMARK 500    ASP A 112       25.81   -143.48
REMARK 500    THR A 149       15.45    -69.59
REMARK 500    ASN A 202       36.59   -163.10
REMARK 500    ARG A 211       16.98     49.37
REMARK 500    ILE A 224       71.06     34.80
REMARK 500    THR A 227     -156.68   -119.79
REMARK 500    LYS A 266      153.55    177.40
REMARK 500    CYS A 293     -154.54   -114.77
REMARK 500    GLN A 298      -43.79   -139.24
REMARK 500    THR A 325       22.21   -141.56
REMARK 500    ASP A 326     -166.61   -100.99
REMARK 500    ASN A 327      118.98   -173.54
REMARK 500    ASP A 357       44.87   -143.16
REMARK 500    ASN A 360       51.87   -100.06
REMARK 500    GLN A 393      158.56    178.93
REMARK 500    SER A 404     -140.10   -121.33
REMARK 500    SER A 442     -163.39   -126.30
REMARK 500    PHE A 454       69.65   -109.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A 142         0.07    SIDE CHAIN
REMARK 500    ARG A 153         0.12    SIDE CHAIN
REMARK 500    ARG A 212         0.07    SIDE CHAIN
REMARK 500    TYR A 257         0.06    SIDE CHAIN
REMARK 500    TYR A 258         0.07    SIDE CHAIN
REMARK 500    ARG A 302         0.10    SIDE CHAIN
REMARK 500    ARG A 365         0.07    SIDE CHAIN
REMARK 500    ARG A 421         0.09    SIDE CHAIN
REMARK 500    TYR A 425         0.12    SIDE CHAIN
REMARK 500    TYR A 468         0.08    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    VAL A 323         10.32
REMARK 500
REMARK 500 REMARK: NULL
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 471  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 326   OD2
REMARK 620 2 ASP A 295   O    90.3
REMARK 620 3 GLY A 299   O    94.6  82.8
REMARK 620 4 ASN A 348   O   100.3 106.8 162.1
REMARK 620 N                    1     2     3
REMARK 700
REMARK 700 SHEET
REMARK 700 STRAND 1 OF SHEET S3 (LEU 225 - HIS 235) IS NOT REALLY PART
REMARK 700 OF THE SHEET BY H-BONDING CRITERIA BECAUSE IT IS IN AN
REMARK 700 EXTENDED CONFORMATION.  OTHERS HAVE BEEN INCLUDED IN THE
REMARK 700 SHEET MOSTLY FOR THE SAKE OF SYMMETRY; I.E., THE STRUCTURE
REMARK 700 THEN CONSISTS OF SIX SHEETS OF FOUR ANTIPARALLEL STRANDS
REMARK 700 EACH.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: SUB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAL
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A 500
DBREF  1NNB A   84   470  UNP    P03472   NRAM_IATRA      84    470
SEQRES   1 A  387  ASP PHE ASN ASN LEU THR LYS GLY LEU CYS THR ILE ASN
SEQRES   2 A  387  SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL ARG ILE
SEQRES   3 A  387  GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLU PRO TYR
SEQRES   4 A  387  VAL SER CYS ASP PRO ASP GLU CYS ARG PHE TYR ALA LEU
SEQRES   5 A  387  SER GLN GLY THR THR ILE ARG GLY LYS HIS SER ASN GLY
SEQRES   6 A  387  THR ILE HIS ASP ARG SER GLN TYR ARG ALA LEU ILE SER
SEQRES   7 A  387  TRP PRO LEU SER SER PRO PRO THR VAL TYR ASN SER ARG
SEQRES   8 A  387  VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS ASP
SEQRES   9 A  387  GLY LYS THR ARG MET SER ILE CYS ILE SER GLY PRO ASN
SEQRES  10 A  387  ASN ASN ALA SER ALA VAL ILE TRP TYR ASN ARG ARG PRO
SEQRES  11 A  387  VAL THR GLU ILE ASN THR TRP ALA ARG ASN ILE LEU ARG
SEQRES  12 A  387  THR GLN GLU SER GLU CYS VAL CYS HIS ASN GLY VAL CYS
SEQRES  13 A  387  PRO VAL VAL PHE THR ASP GLY SER ALA THR GLY PRO ALA
SEQRES  14 A  387  GLU THR ARG ILE TYR TYR PHE LYS GLU GLY LYS ILE LEU
SEQRES  15 A  387  LYS TRP GLU PRO LEU ALA GLY THR ALA LYS HIS ILE GLU
SEQRES  16 A  387  GLU CYS SER CYS TYR GLY GLU ARG ALA GLU ILE THR CYS
SEQRES  17 A  387  THR CYS ARG ASP ASN TRP GLN GLY SER ASN ARG PRO VAL
SEQRES  18 A  387  ILE ARG ILE ASP PRO VAL ALA MET THR HIS THR SER GLN
SEQRES  19 A  387  TYR ILE CYS SER PRO VAL LEU THR ASP ASN PRO ARG PRO
SEQRES  20 A  387  ASN ASP PRO THR VAL GLY LYS CYS ASN ASP PRO TYR PRO
SEQRES  21 A  387  GLY ASN ASN ASN ASN GLY VAL LYS GLY PHE SER TYR LEU
SEQRES  22 A  387  ASP GLY VAL ASN THR TRP LEU GLY ARG THR ILE SER ILE
SEQRES  23 A  387  ALA SER ARG SER GLY TYR GLU MET LEU LYS VAL PRO ASN
SEQRES  24 A  387  ALA LEU THR ASP ASP LYS SER LYS PRO THR GLN GLY GLN
SEQRES  25 A  387  THR ILE VAL LEU ASN THR ASP TRP SER GLY TYR SER GLY
SEQRES  26 A  387  SER PHE MET ASP TYR TRP ALA GLU GLY GLU CYS TYR ARG
SEQRES  27 A  387  ALA CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG PRO LYS
SEQRES  28 A  387  GLU ASP LYS VAL TRP TRP THR SER ASN SER ILE VAL SER
SEQRES  29 A  387  MET CYS SER SER THR GLU PHE LEU GLY GLN TRP ASP TRP
SEQRES  30 A  387  PRO ASP GLY ALA LYS ILE GLU TYR PHE LEU
HET     CA  A 471       1
HET    DAN  A 500      33
HETNAM      CA CALCIUM ION
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   2   CA    CA 2+
FORMUL   3  DAN    C11 H17 N O8
HELIX    1   1 ALA A  106  GLY A  110  1                                   5
SHEET    1  S1 4 VAL A 115  CYS A 125  0
SHEET    2  S1 4 CYS A 130  THR A 139 -1
SHEET    3  S1 4 ALA A 158  PRO A 163 -1
SHEET    4  S1 4 ARG A 174  ILE A 178 -1
SHEET    1  S2 4 SER A 181  HIS A 186  0
SHEET    2  S2 4 ARG A 191  SER A 197 -1
SHEET    3  S2 4 SER A 204  TYR A 209 -1
SHEET    4  S2 4 ARG A 212  ASN A 218 -1
SHEET    1  S3 4 LEU A 225  HIS A 235  0
SHEET    2  S3 4 VAL A 238  GLY A 246 -1
SHEET    3  S3 4 ALA A 252  LYS A 260 -1
SHEET    4  S3 4 LYS A 263  PRO A 269 -1
SHEET    1  S4 4 GLU A 278  GLU A 285  0
SHEET    2  S4 4 GLU A 288  CYS A 293 -1
SHEET    3  S4 4 PRO A 303  ASP A 308 -1
SHEET    4  S4 4 THR A 313  TYR A 318 -1
SHEET    1  S5 4 SER A 354  TYR A 355  0
SHEET    2  S5 4 TRP A 362  ARG A 365 -1
SHEET    3  S5 4 SER A 373  LYS A 379 -1
SHEET    4  S5 4 GLN A 393  ASP A 402 -1
SHEET    1  S6 4 SER A 407  PHE A 410  0
SHEET    2  S6 4 CYS A 423  GLY A 431 -1
SHEET    3  S6 4 THR A 441  SER A 451 -1
SHEET    4  S6 4 SER A  97  LYS A 103 -1
SSBOND   1 CYS A   93    CYS A  419                          1555   1555  2.01
SSBOND   2 CYS A  125    CYS A  130                          1555   1555  2.03
SSBOND   3 CYS A  177    CYS A  195                          1555   1555  2.04
SSBOND   4 CYS A  185    CYS A  232                          1555   1555  2.03
SSBOND   5 CYS A  234    CYS A  239                          1555   1555  2.02
SSBOND   6 CYS A  280    CYS A  293                          1555   1555  2.03
SSBOND   7 CYS A  282    CYS A  291                          1555   1555  2.02
SSBOND   8 CYS A  320    CYS A  338                          1555   1555  2.03
SSBOND   9 CYS A  423    CYS A  449                          1555   1555  2.03
LINK        CA    CA A 471                 OD2 ASP A 326     1555   1555  2.79
LINK        CA    CA A 471                 O   ASP A 295     1555   1555  2.65
LINK        CA    CA A 471                 O   GLY A 299     1555   1555  2.67
LINK        CA    CA A 471                 O   ASN A 348     1555   1555  2.30
CISPEP   1 ASN A  327    PRO A  328          0         6.26
CISPEP   2 ARG A  432    PRO A  433          0        -0.06
SITE     1 SUB 18 ARG A 119  GLU A 120  ASP A 152  ARG A 153
SITE     2 SUB 18 TRP A 180  SER A 181  ILE A 224  ARG A 226
SITE     3 SUB 18 GLU A 229  HIS A 276  GLU A 278  GLU A 279
SITE     4 SUB 18 ARG A 294  ASN A 296  GLY A 349  ARG A 372
SITE     5 SUB 18 TYR A 406  GLU A 427
SITE     1 CAL  4 ASP A 295  GLY A 299  ASP A 326  GLY A 349
SITE     1 AC1  4 ASP A 295  GLY A 299  ASP A 326  ASN A 348
SITE     1 AC2 11 ARG A 119  GLU A 120  ASP A 152  ARG A 153
SITE     2 AC2 11 ILE A 224  ALA A 248  GLU A 278  GLU A 279
SITE     3 AC2 11 ARG A 294  ARG A 372  TYR A 406
CRYST1  183.780  183.780  183.780  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      0.005441  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005441  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005441        0.00000
      
PROCHECK
Go to PROCHECK summary
 References