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PDBsum entry 1ivc

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Hydrolase (o-glycosyl) PDB id
1ivc
Jmol
Contents
Protein chains
388 a.a.
Ligands
NAG-NAG ×4
NAG-NAG-BMA-FUL
NAG-NAG-BMA-MAN-
MAN-MAN
×2
NAG-NAG-BMA-FUC
ST2 ×2
Metals
_CA ×2
HEADER    HYDROLASE (O-GLYCOSYL)                  12-DEC-94   1IVC
TITLE     STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: INFLUENZA A SUBTYPE N2 NEURAMINIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.2.1.18;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (STRAIN A/TOKYO/3/1967 H2N2);
SOURCE   3 ORGANISM_TAXID: 380960;
SOURCE   4 STRAIN: A/TOKYO/3/1967 H2N2
KEYWDS    HYDROLASE (O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.J.JEDRZEJAS,M.LUO
REVDAT   4   13-JUL-11 1IVC    1       VERSN
REVDAT   3   25-AUG-09 1IVC    1       SOURCE
REVDAT   2   24-FEB-09 1IVC    1       VERSN
REVDAT   1   31-MAR-95 1IVC    0
JRNL        AUTH   M.J.JEDRZEJAS,S.SINGH,W.J.BROUILLETTE,W.G.LAVER,G.M.AIR,
JRNL        AUTH 2 M.LUO
JRNL        TITL   STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS
JRNL        TITL 2 NEURAMINIDASE.
JRNL        REF    BIOCHEMISTRY                  V.  34  3144 1995
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   7880809
JRNL        DOI    10.1021/BI00010A003
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.SINGH,M.J.JEDRZEJAS,G.M.AIR,M.LUO,W.G.LAVER,
REMARK   1  AUTH 2 W.J.BROUILLETTE
REMARK   1  TITL   STRUCTURE-BASED INHIBITORS OF INFLUENZA VIRAL NEURAMINIDASE.
REMARK   1  TITL 2 A BENZOIC ACID LEAD WITH NOVEL INTERACTION
REMARK   1  REF    TO BE PUBLISHED
REMARK   1  REFN
REMARK   1 REFERENCE 2
REMARK   1  AUTH   M.LUO,M.J.JEDRZEJAS,S.SINGH,C.L.WHITE,W.J.BROUILLETTE,
REMARK   1  AUTH 2 G.M.AIR,W.G.LAVER
REMARK   1  TITL   BENZOIC ACID INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE
REMARK   1  REF    TO BE PUBLISHED
REMARK   1  REFN
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.N.VARGHESE,P.M.COLMAN
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE NEURAMINIDASE OF
REMARK   1  TITL 2 INFLUENZA VIRUS A(SLASH)TOKYO(SLASH)3(SLASH)67 AT 2.2
REMARK   1  TITL 3 ANGSTROMS RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 221   473 1991
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.40 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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000
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             : 26168
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) : 0.204
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            : 6044
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 386
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) : 2.02
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  ONLY HALF OF THE ASYMMETRIC UNIT WAS REFINED; THE
REMARK   3  REMAINING HALF WAS GENERATED USING A NONCRYSTALLOGRAPHIC
REMARK   3  TWO-FOLD AXIS.  THE TOPOLOGY AND PARAMETER VALUES GENERATED
REMARK   3  FOR THE BANA106 RESIDUES WERE EITHER TAKEN DIRECTLY FROM
REMARK   3  THE LITERATURE OR BY COMPARISON TO OTHER SIMILAR STRUCTURES
REMARK   3  IN THE X-PLOR TOPOLOGY AND PARAMETER LIBRARY FILES.  MORE
REMARK   3  INFORMATION CONCERNING THE REFINEMENT PROTOCOLS AND BANA106
REMARK   3  FILES IS PRESENTED IN THE ORIGINATING PAPER.
REMARK   4
REMARK   4 1IVC 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        : 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   : 28488
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
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   (%): 63.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NATIVE CRYSTALS SOAKED IN 5MM BANA106
REMARK 280  SOLUTION, PH 6.8.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
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       70.11500
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       70.11500
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  1.000000  0.000000  0.000000       60.17500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.86000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.17500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.86000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.11500
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.17500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.86000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.11500
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.17500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       69.86000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
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 300 REMARK: MTRIX
REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE
REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300  SECOND.
REMARK 300
REMARK 300            APPLIED TO           TRANSFORMED TO
REMARK 300  MTRIX      RESIDUES               RESIDUES         RMSD
REMARK 300    M1       82  ..     469             ..
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, B
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 450
REMARK 450 SOURCE
REMARK 450 MOLECULE_NAME: BANA106 SYNTHETIC. SEE SINGH ET AL.
REMARK 450   (SUBMITTED TO J. MED CHEM.) AND JEDRZEJAS ET AL.
REMARK 450   (ACCEPTED BY BIOCHEMISTRY, 1994) FOR SYNTHESIS
REMARK 450   INFORMATION.
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   HG1  THR B   455     H1   NAG A   478              1.31
REMARK 500   CG2  THR B   455     H61  NAG A   478              1.42
REMARK 500   H    GLN A   273     HH   TYR A   316              1.53
REMARK 500   H    GLN B   273     HH   TYR B   316              1.53
REMARK 500   HG   SER A   228     HZ2  LYS A   350              1.59
REMARK 500   HG   SER B   228     HZ2  LYS B   350              1.59
REMARK 500   ND2  ASN A   146     O5   NAG A   474              2.15
REMARK 500   ND2  ASN B   146     O5   NAG B   474              2.15
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   H4   FUL A   477     H1   MAN A   481     3654     0.90
REMARK 500   H1   FUL A   477     O3   MAN A   481     3654     0.96
REMARK 500   H5   FUL A   477     O5   MAN A   481     3654     1.26
REMARK 500   HG1  THR A   455     H1   NAG B   478     4555     1.31
REMARK 500  HH21  ARG A   338     HG   SER B   315     7554     1.34
REMARK 500   CG2  THR A   455     H61  NAG B   478     4555     1.42
REMARK 500   HG   SER A   315    HH21  ARG B   338     7554     1.53
REMARK 500   C4   FUL A   477     H1   MAN A   481     3654     1.59
REMARK 500   O5   FUL A   477     H4   MAN A   481     3654     1.60
REMARK 500   O5   FUL A   477     O5   MAN A   481     3654     2.05
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    ARG A 118      173.54    171.45
REMARK 500    TYR A 121      166.79    177.03
REMARK 500    ALA A 133      145.90    179.24
REMARK 500    ALA A 177      134.65   -172.74
REMARK 500    ASP A 208       19.89     58.70
REMARK 500    GLN A 220       19.66     54.99
REMARK 500    ILE A 222       85.45     52.61
REMARK 500    ALA A 246      -75.14    -64.57
REMARK 500    HIS A 264      139.64    167.00
REMARK 500    HIS A 274      114.21   -171.39
REMARK 500    TYR A 284      135.10    -39.99
REMARK 500    CYS A 291     -159.33   -103.30
REMARK 500    VAL A 322      132.25     63.68
REMARK 500    ASN A 328      -73.12    -72.66
REMARK 500    ASP A 329      125.71    151.98
REMARK 500    ASP A 330      -49.67    -18.64
REMARK 500    SER A 332       48.74    -96.41
REMARK 500    SER A 335      127.68   -172.10
REMARK 500    CYS A 337       -1.49     65.55
REMARK 500    ARG A 344       13.31     56.51
REMARK 500    THR A 346     -118.41    -36.57
REMARK 500    GLN A 347      179.64    -38.03
REMARK 500    PRO A 386      151.48    -49.17
REMARK 500    ASN A 387       32.24     38.69
REMARK 500    SER A 404     -125.08   -126.87
REMARK 500    ARG A 430      150.30    -37.45
REMARK 500    LYS A 431      -69.92     85.18
REMARK 500    SER A 440     -156.68   -152.19
REMARK 500    SER A 457      121.70   -171.77
REMARK 500    ILE A 464      -18.73    -46.43
REMARK 500    ARG B 118      173.54    171.45
REMARK 500    TYR B 121      166.79    177.03
REMARK 500    ALA B 133      145.90    179.24
REMARK 500    ALA B 177      134.65   -172.74
REMARK 500    ASP B 208       19.89     58.70
REMARK 500    GLN B 220       19.66     54.99
REMARK 500    ILE B 222       85.45     52.61
REMARK 500    ALA B 246      -75.14    -64.57
REMARK 500    HIS B 264      139.64    167.00
REMARK 500    HIS B 274      114.21   -171.39
REMARK 500    TYR B 284      135.10    -39.99
REMARK 500    CYS B 291     -159.33   -103.30
REMARK 500    VAL B 322      132.25     63.68
REMARK 500    ASN B 328      -73.12    -72.66
REMARK 500    ASP B 329      125.71    151.98
REMARK 500    ASP B 330      -49.67    -18.64
REMARK 500    SER B 332       48.74    -96.41
REMARK 500    SER B 335      127.68   -172.10
REMARK 500    CYS B 337       -1.49     65.55
REMARK 500    ARG B 344       13.31     56.51
REMARK 500
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.
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        24.5      L          L   OUTSIDE RANGE
REMARK 500    VAL A 231        24.2      L          L   OUTSIDE RANGE
REMARK 500    ARG A 430        20.6      L          L   OUTSIDE RANGE
REMARK 500    GLN B 226        24.5      L          L   OUTSIDE RANGE
REMARK 500    VAL B 231        24.2      L          L   OUTSIDE RANGE
REMARK 500    ARG B 430        20.6      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE CALCIUM, CA 470, STABILIZES A LOOP NEAR THE
REMARK 600 NEURAMINIDASE ACTIVE SITE.
REMARK 600
REMARK 600 THE BANA106 INHIBITOR IS RESIDUE ST2 471.  ST2 IS
REMARK 600 4-(ACETYLAMINO)-3-AMINO-5-HYDROXY BENZOIC ACID.
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 470  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 293   O
REMARK 620 2 GLY A 297   O    76.7
REMARK 620 3 GLN A 347   O   128.4 154.1
REMARK 620 4 THR A 346   O    88.7 124.8  68.7
REMARK 620 5 GLY A 345   O   104.2  64.4 108.8  68.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 470  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 293   O
REMARK 620 2 GLY B 345   O   104.2
REMARK 620 3 THR B 346   O    88.7  68.5
REMARK 620 4 GLN B 347   O   128.4 108.8  68.7
REMARK 620 5 GLY B 297   O    76.7  64.4 124.8 154.1
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN
REMARK 800  CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CT2
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 NAG A 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 484
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ST2 A 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ST2 B 471
DBREF  1IVC A   82   469  UNP    P06820   NRAM_IATOK      82    469
DBREF  1IVC B   82   469  UNP    P06820   NRAM_IATOK      82    469
SEQADV 1IVC ASP A  339  UNP  P06820    ASN   339 CONFLICT
SEQADV 1IVC ASP B  339  UNP  P06820    ASN   339 CONFLICT
SEQRES   1 A  388  VAL GLU TYR ARG ASN TRP SER LYS PRO GLN CYS GLN ILE
SEQRES   2 A  388  THR GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE ARG
SEQRES   3 A  388  LEU SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU PRO
SEQRES   4 A  388  TYR VAL SER CYS ASP PRO VAL LYS CYS TYR GLN PHE ALA
SEQRES   5 A  388  LEU GLY GLN GLY THR THR LEU ASP ASN LYS HIS SER ASN
SEQRES   6 A  388  ASP THR VAL HIS ASP ARG ILE PRO HIS ARG THR LEU LEU
SEQRES   7 A  388  MET ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR ARG
SEQRES   8 A  388  GLN VAL CYS ILE ALA TRP SER SER SER SER CYS HIS ASP
SEQRES   9 A  388  GLY LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASP ASP
SEQRES  10 A  388  LYS ASN ALA THR ALA SER PHE ILE TYR ASP GLY ARG LEU
SEQRES  11 A  388  VAL ASP SER ILE GLY SER TRP SER GLN ASN ILE LEU ARG
SEQRES  12 A  388  THR GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR CYS
SEQRES  13 A  388  THR VAL VAL MET THR ASP GLY SER ALA SER GLY ARG ALA
SEQRES  14 A  388  ASP THR ARG ILE LEU PHE ILE GLU GLU GLY LYS ILE VAL
SEQRES  15 A  388  HIS ILE SER PRO LEU ALA GLY SER ALA GLN HIS VAL GLU
SEQRES  16 A  388  GLU CYS SER CYS TYR PRO ARG TYR PRO GLY VAL ARG CYS
SEQRES  17 A  388  ILE CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO VAL
SEQRES  18 A  388  VAL ASP ILE ASN MET GLU ASP TYR SER ILE ASP SER SER
SEQRES  19 A  388  TYR VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG ASN
SEQRES  20 A  388  ASP ASP ARG SER SER ASN SER ASN CYS ARG ASP PRO ASN
SEQRES  21 A  388  ASN GLU ARG GLY THR GLN GLY VAL LYS GLY TRP ALA PHE
SEQRES  22 A  388  ASP ASN GLY ASN ASP LEU TRP MET GLY ARG THR ILE SER
SEQRES  23 A  388  LYS ASP LEU ARG SER GLY TYR GLU THR PHE LYS VAL ILE
SEQRES  24 A  388  GLY GLY TRP SER THR PRO ASN SER LYS SER GLN ILE ASN
SEQRES  25 A  388  ARG GLN VAL ILE VAL ASP SER ASP ASN ARG SER GLY TYR
SEQRES  26 A  388  SER GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE ASN
SEQRES  27 A  388  ARG CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS GLN
SEQRES  28 A  388  GLU THR ARG VAL TRP TRP THR SER ASN SER ILE VAL VAL
SEQRES  29 A  388  PHE CYS GLY THR SER GLY THR TYR GLY THR GLY SER TRP
SEQRES  30 A  388  PRO ASP GLY ALA ASN ILE ASN PHE MET PRO ILE
SEQRES   1 B  388  VAL GLU TYR ARG ASN TRP SER LYS PRO GLN CYS GLN ILE
SEQRES   2 B  388  THR GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE ARG
SEQRES   3 B  388  LEU SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU PRO
SEQRES   4 B  388  TYR VAL SER CYS ASP PRO VAL LYS CYS TYR GLN PHE ALA
SEQRES   5 B  388  LEU GLY GLN GLY THR THR LEU ASP ASN LYS HIS SER ASN
SEQRES   6 B  388  ASP THR VAL HIS ASP ARG ILE PRO HIS ARG THR LEU LEU
SEQRES   7 B  388  MET ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR ARG
SEQRES   8 B  388  GLN VAL CYS ILE ALA TRP SER SER SER SER CYS HIS ASP
SEQRES   9 B  388  GLY LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASP ASP
SEQRES  10 B  388  LYS ASN ALA THR ALA SER PHE ILE TYR ASP GLY ARG LEU
SEQRES  11 B  388  VAL ASP SER ILE GLY SER TRP SER GLN ASN ILE LEU ARG
SEQRES  12 B  388  THR GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR CYS
SEQRES  13 B  388  THR VAL VAL MET THR ASP GLY SER ALA SER GLY ARG ALA
SEQRES  14 B  388  ASP THR ARG ILE LEU PHE ILE GLU GLU GLY LYS ILE VAL
SEQRES  15 B  388  HIS ILE SER PRO LEU ALA GLY SER ALA GLN HIS VAL GLU
SEQRES  16 B  388  GLU CYS SER CYS TYR PRO ARG TYR PRO GLY VAL ARG CYS
SEQRES  17 B  388  ILE CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO VAL
SEQRES  18 B  388  VAL ASP ILE ASN MET GLU ASP TYR SER ILE ASP SER SER
SEQRES  19 B  388  TYR VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG ASN
SEQRES  20 B  388  ASP ASP ARG SER SER ASN SER ASN CYS ARG ASP PRO ASN
SEQRES  21 B  388  ASN GLU ARG GLY THR GLN GLY VAL LYS GLY TRP ALA PHE
SEQRES  22 B  388  ASP ASN GLY ASN ASP LEU TRP MET GLY ARG THR ILE SER
SEQRES  23 B  388  LYS ASP LEU ARG SER GLY TYR GLU THR PHE LYS VAL ILE
SEQRES  24 B  388  GLY GLY TRP SER THR PRO ASN SER LYS SER GLN ILE ASN
SEQRES  25 B  388  ARG GLN VAL ILE VAL ASP SER ASP ASN ARG SER GLY TYR
SEQRES  26 B  388  SER GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE ASN
SEQRES  27 B  388  ARG CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS GLN
SEQRES  28 B  388  GLU THR ARG VAL TRP TRP THR SER ASN SER ILE VAL VAL
SEQRES  29 B  388  PHE CYS GLY THR SER GLY THR TYR GLY THR GLY SER TRP
SEQRES  30 B  388  PRO ASP GLY ALA ASN ILE ASN PHE MET PRO ILE
MODRES 1IVC ASN A   86  ASN  GLYCOSYLATION SITE
MODRES 1IVC ASN A  146  ASN  GLYCOSYLATION SITE
MODRES 1IVC ASN A  200  ASN  GLYCOSYLATION SITE
MODRES 1IVC ASN A  234  ASN  GLYCOSYLATION SITE
MODRES 1IVC ASN B   86  ASN  GLYCOSYLATION SITE
MODRES 1IVC ASN B  146  ASN  GLYCOSYLATION SITE
MODRES 1IVC ASN B  200  ASN  GLYCOSYLATION SITE
MODRES 1IVC ASN B  234  ASN  GLYCOSYLATION SITE
HET    NAG  A 472      27
HET    NAG  A 473      28
HET    NAG  A 474      26
HET    NAG  A 475      27
HET    BMA  A 476      22
HET    FUL  A 477      21
HET    NAG  A 478      26
HET    NAG  A 479      27
HET    BMA  A 480      21
HET    MAN  A 481      21
HET    MAN  A 482      22
HET    MAN  A 483      22
HET    NAG  A 484      27
HET    NAG  A 485      28
HET    NAG  B 472      27
HET    NAG  B 473      28
HET    NAG  B 474      26
HET    NAG  B 475      27
HET    BMA  B 476      22
HET    FUC  B 477      21
HET    NAG  B 478      26
HET    NAG  B 479      27
HET    BMA  B 480      21
HET    MAN  B 481      21
HET    MAN  B 482      22
HET    MAN  B 483      22
HET    NAG  B 484      27
HET    NAG  B 485      28
HET     CA  A 470       1
HET     CA  B 470       1
HET    ST2  A 471      19
HET    ST2  B 471      19
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     FUL BETA-L-FUCOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM      CA CALCIUM ION
HETNAM     ST2 4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC ACID
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL   3  NAG    16(C8 H15 N O6)
FORMUL   4  BMA    4(C6 H12 O6)
FORMUL   4  FUL    C6 H12 O5
FORMUL   5  MAN    6(C6 H12 O6)
FORMUL   8  FUC    C6 H12 O5
FORMUL  11   CA    2(CA 2+)
FORMUL  13  ST2    2(C9 H10 N2 O4)
HELIX    1   1 SER A  105  ALA A  110  1                                   6
HELIX    2   2 LYS A  143  SER A  145  5                                   3
HELIX    3   3 ASP A  330  SER A  332  5                                   3
HELIX    4   4 SER B  105  ALA B  110  1                                   6
HELIX    5   5 LYS B  143  SER B  145  5                                   3
HELIX    6   6 ASP B  330  SER B  332  5                                   3
SHEET    1   A 4 TYR A 121  CYS A 124  0
SHEET    2   A 4 CYS A 129  LEU A 134 -1  N  PHE A 132   O  TYR A 121
SHEET    3   A 4 THR A 157  GLU A 162 -1  N  ASN A 161   O  GLN 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 TRP A 189  GLY A 196 -1  N  ILE A 194   O  SER A 179
SHEET    3   B 4 ALA A 201  TYR A 207 -1  N  ILE A 206   O  HIS A 191
SHEET    4   B 4 ARG A 210  GLY A 216 -1  N  ILE A 215   O  ALA A 203
SHEET    1   C 4 VAL A 231  ILE A 233  0
SHEET    2   C 4 THR A 236  GLY A 244 -1  N  THR A 238   O  VAL A 231
SHEET    3   C 4 ALA A 250  GLU A 258 -1  N  ILE A 257   O  CYS A 237
SHEET    4   C 4 LYS A 261  PRO A 267 -1  N  SER A 266   O  ILE A 254
SHEET    1   D 4 SER A 279  ARG A 283  0
SHEET    2   D 4 GLY A 286  ILE A 290 -1  N  ILE A 290   O  SER A 279
SHEET    3   D 4 PRO A 301  ASN A 306 -1  N  ILE A 305   O  VAL A 287
SHEET    4   D 4 ILE A 312  TYR A 316 -1  N  SER A 315   O  VAL A 302
SHEET    1   E 4 ALA A 353  ASN A 356  0
SHEET    2   E 4 ASP A 359  ARG A 364 -1  N  TRP A 361   O  PHE A 354
SHEET    3   E 4 GLU A 375  ILE A 380 -1  N  VAL A 379   O  LEU A 360
SHEET    4   E 4 SER A 390  ILE A 392 -1  N  ILE A 392   O  LYS A 378
SHEET    1   F 4 SER A 407  GLU A 413  0
SHEET    2   F 4 ILE A 418  GLY A 429 -1  N  TYR A 423   O  GLY A 408
SHEET    3   F 4 THR A 439  THR A 449 -1  N  PHE A 446   O  PHE A 422
SHEET    4   F 4 GLY A  96  LYS A 102 -1  N  SER A 101   O  VAL A 445
SHEET    1   G 2 TYR A 374  THR A 376  0
SHEET    2   G 2 GLN A 395  VAL A 398 -1  N  VAL A 398   O  TYR A 374
SHEET    1   H 4 TYR B 121  CYS B 124  0
SHEET    2   H 4 CYS B 129  LEU B 134 -1
SHEET    3   H 4 THR B 157  GLU B 162 -1
SHEET    4   H 4 ARG B 172  ILE B 176 -1
SHEET    1   I 4 SER B 179  HIS B 184  0
SHEET    2   I 4 TRP B 189  GLY B 196 -1
SHEET    3   I 4 ALA B 201  TYR B 207 -1
SHEET    4   I 4 ARG B 210  GLY B 216 -1
SHEET    1   J 4 VAL B 231  ILE B 233  0
SHEET    2   J 4 THR B 236  GLY B 244 -1
SHEET    3   J 4 ALA B 250  GLU B 258 -1
SHEET    4   J 4 LYS B 261  PRO B 267 -1
SHEET    1   K 4 SER B 279  ARG B 283  0
SHEET    2   K 4 GLY B 286  ILE B 290 -1
SHEET    3   K 4 PRO B 301  ASN B 306 -1
SHEET    4   K 4 ILE B 312  TYR B 316 -1
SHEET    1   L 4 ALA B 353  ASN B 356  0
SHEET    2   L 4 ASP B 359  ARG B 364 -1
SHEET    3   L 4 GLU B 375  ILE B 380 -1
SHEET    4   L 4 SER B 390  ILE B 392 -1
SHEET    1   M 4 SER B 407  GLU B 413  0
SHEET    2   M 4 ILE B 418  GLY B 429 -1
SHEET    3   M 4 THR B 439  THR B 449 -1
SHEET    4   M 4 GLY B  96  LYS B 102 -1
SHEET    1   N 2 TYR B 374  THR B 376  0
SHEET    2   N 2 GLN B 395  VAL B 398 -1
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.02
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.03
SSBOND   3 CYS A  175    CYS A  193                          1555   1555  2.01
SSBOND   4 CYS A  183    CYS A  230                          1555   1555  2.02
SSBOND   5 CYS A  232    CYS A  237                          1555   1555  2.01
SSBOND   6 CYS A  278    CYS A  291                          1555   1555  2.03
SSBOND   7 CYS A  280    CYS A  289                          1555   1555  2.03
SSBOND   8 CYS A  318    CYS A  337                          1555   1555  2.03
SSBOND   9 CYS A  421    CYS A  447                          1555   1555  2.00
SSBOND  10 CYS B   92    CYS B  417                          1555   1555  2.02
SSBOND  11 CYS B  124    CYS B  129                          1555   1555  2.03
SSBOND  12 CYS B  175    CYS B  193                          1555   1555  2.01
SSBOND  13 CYS B  183    CYS B  230                          1555   1555  2.02
SSBOND  14 CYS B  232    CYS B  237                          1555   1555  2.01
SSBOND  15 CYS B  278    CYS B  291                          1555   1555  2.03
SSBOND  16 CYS B  280    CYS B  289                          1555   1555  2.03
SSBOND  17 CYS B  318    CYS B  337                          1555   1555  2.03
SSBOND  18 CYS B  421    CYS B  447                          1555   1555  2.00
LINK         ND2 ASN A  86                 C1  NAG A 472     1555   1555  1.49
LINK         ND2 ASN A 146                 C1  NAG A 474     1555   1555  1.47
LINK         ND2 ASN A 200                 C1  NAG A 478     1555   1555  1.43
LINK         ND2 ASN A 234                 C1  NAG A 484     1555   1555  1.53
LINK         ND2 ASN B  86                 C1  NAG B 472     1555   1555  1.49
LINK         ND2 ASN B 146                 C1  NAG B 474     1555   1555  1.47
LINK         ND2 ASN B 200                 C1  NAG B 478     1555   1555  1.43
LINK         ND2 ASN B 234                 C1  NAG B 484     1555   1555  1.53
LINK         O4  NAG A 472                 C1  NAG A 473     1555   1555  1.47
LINK         O4  NAG A 474                 C1  NAG A 475     1555   1555  1.45
LINK         O6  NAG A 474                 C1  FUL A 477     1555   1555  1.48
LINK         O4  NAG A 475                 C1  BMA A 476     1555   1555  1.51
LINK         O4  NAG A 478                 C1  NAG A 479     1555   1555  1.50
LINK         O6  NAG A 478                 C1  MAN A 483     1555   1555  1.45
LINK         O4  NAG A 479                 C1  BMA A 480     1555   1555  1.52
LINK         O3  BMA A 480                 C1  MAN A 481     1555   1555  1.54
LINK         O2  MAN A 481                 C1  MAN A 482     1555   1555  1.52
LINK         O4  NAG A 484                 C1  NAG A 485     1555   1555  1.44
LINK         O4  NAG B 472                 C1  NAG B 473     1555   1555  1.47
LINK         O4  NAG B 474                 C1  NAG B 475     1555   1555  1.45
LINK         O6  NAG B 474                 C1  FUC B 477     1555   1555  1.48
LINK         O4  NAG B 475                 C1  BMA B 476     1555   1555  1.51
LINK         O4  NAG B 478                 C1  NAG B 479     1555   1555  1.50
LINK         O6  NAG B 478                 C1  MAN B 483     1555   1555  1.45
LINK         O4  NAG B 479                 C1  BMA B 480     1555   1555  1.52
LINK         O3  BMA B 480                 C1  MAN B 481     1555   1555  1.54
LINK         O2  MAN B 481                 C1  MAN B 482     1555   1555  1.52
LINK         O4  NAG B 484                 C1  NAG B 485     1555   1555  1.44
LINK        CA    CA A 470                 O   ASP A 293     1555   1555  2.14
LINK        CA    CA A 470                 O   GLY A 297     1555   1555  2.66
LINK        CA    CA A 470                 O   GLN A 347     1555   1555  1.87
LINK        CA    CA A 470                 O   THR A 346     1555   1555  2.07
LINK        CA    CA A 470                 O   GLY A 345     1555   1555  2.15
LINK         C1  FUL A 477                 O3  MAN A 481     1555   3654  1.93
LINK         C5  FUL A 477                 O5  MAN A 481     3654   1555  1.94
LINK         C1  FUL A 477                 O3  MAN A 481     3654   1555  1.93
LINK         C5  FUL A 477                 O5  MAN A 481     1555   3654  1.94
LINK         O5  FUL A 477                 C4  MAN A 481     3654   1555  2.05
LINK         O5  FUL A 477                 C4  MAN A 481     1555   3654  2.05
LINK        CA    CA B 470                 O   ASP B 293     1555   1555  2.14
LINK        CA    CA B 470                 O   GLY B 345     1555   1555  2.15
LINK        CA    CA B 470                 O   THR B 346     1555   1555  2.07
LINK        CA    CA B 470                 O   GLN B 347     1555   1555  1.87
LINK        CA    CA B 470                 O   GLY B 297     1555   1555  2.66
CISPEP   1 TYR A  284    PRO A  285          0        -0.25
CISPEP   2 THR A  325    PRO A  326          0         0.48
CISPEP   3 TYR B  284    PRO B  285          0        -0.25
CISPEP   4 THR B  325    PRO B  326          0         0.48
SITE     1 CAT 11 ARG A 118  GLU A 119  ASP A 151  ARG A 152
SITE     2 CAT 11 TRP A 178  ILE A 222  ARG A 224  GLU A 276
SITE     3 CAT 11 ARG A 292  ARG A 371  TYR A 406
SITE     1 CT2 11 ARG B 118  GLU B 119  ASP B 151  ARG B 152
SITE     2 CT2 11 TRP B 178  ILE B 222  ARG B 224  GLU B 276
SITE     3 CT2 11 ARG B 292  ARG B 371  TYR B 406
SITE     1 AC1  7 GLU A  83  ASN A  86  SER A  88  TYR A 284
SITE     2 AC1  7 NAG A 473  NAG A 484  NAG A 485
SITE     1 AC2  2 GLU A  83  NAG A 472
SITE     1 AC3  5 ASN A 146  TRP A 437  NAG A 475  FUL A 477
SITE     2 AC3  5 MAN A 481
SITE     1 AC4  3 TRP A 437  NAG A 474  BMA A 476
SITE     1 AC5  1 NAG A 475
SITE     1 AC6  6 ASN A 146  NAG A 474  BMA A 480  MAN A 481
SITE     2 AC6  6 MAN A 482  PHE B 466
SITE     1 AC7  6 ASP A 197  ASN A 200  NAG A 479  MAN A 483
SITE     2 AC7  6 GLY B 454  THR B 455
SITE     1 AC8  4 NAG A 478  BMA A 480  MAN A 481  MAN A 483
SITE     1 AC9  5 FUL A 477  NAG A 479  MAN A 481  MAN A 482
SITE     2 AC9  5 MAN A 483
SITE     1 BC1  5 NAG A 474  FUL A 477  NAG A 479  BMA A 480
SITE     2 BC1  5 MAN A 482
SITE     1 BC2  4 FUL A 477  BMA A 480  MAN A 481  ASN B 463
SITE     1 BC3  6 NAG A 478  NAG A 479  BMA A 480  VAL B 396
SITE     2 BC3  6 THR B 455  GLY B 456
SITE     1 BC4  7 ILE A 233  ASN A 234  TYR A 284  PRO A 285
SITE     2 BC4  7 MET A 307  NAG A 472  NAG A 485
SITE     1 BC5  2 NAG A 472  NAG A 484
SITE     1 BC6  7 GLU B  83  ASN B  86  SER B  88  TYR B 284
SITE     2 BC6  7 NAG B 473  NAG B 484  NAG B 485
SITE     1 BC7  2 GLU B  83  NAG B 472
SITE     1 BC8  4 ASN B 146  TRP B 437  NAG B 475  FUC B 477
SITE     1 BC9  3 TRP B 437  NAG B 474  BMA B 476
SITE     1 CC1  1 NAG B 475
SITE     1 CC2  3 PHE A 466  ASN B 146  NAG B 474
SITE     1 CC3  6 GLY A 454  THR A 455  ASP B 197  ASN B 200
SITE     2 CC3  6 NAG B 479  MAN B 483
SITE     1 CC4  4 NAG B 478  BMA B 480  MAN B 481  MAN B 483
SITE     1 CC5  4 NAG B 479  MAN B 481  MAN B 482  MAN B 483
SITE     1 CC6  3 NAG B 479  BMA B 480  MAN B 482
SITE     1 CC7  2 BMA B 480  MAN B 481
SITE     1 CC8  6 VAL A 396  THR A 455  GLY A 456  NAG B 478
SITE     2 CC8  6 NAG B 479  BMA B 480
SITE     1 CC9  7 ILE B 233  ASN B 234  TYR B 284  PRO B 285
SITE     2 CC9  7 MET B 307  NAG B 472  NAG B 485
SITE     1 DC1  2 NAG B 472  NAG B 484
SITE     1 DC2  6 ASP A 293  GLY A 297  ASP A 324  GLY A 345
SITE     2 DC2  6 THR A 346  GLN A 347
SITE     1 DC3  6 ASP B 293  GLY B 297  ASP B 324  GLY B 345
SITE     2 DC3  6 THR B 346  GLN B 347
SITE     1 DC4  7 ARG A 118  ASP A 151  ARG A 152  GLU A 277
SITE     2 DC4  7 ARG A 292  ARG A 371  TYR A 406
SITE     1 DC5  7 ARG B 118  ASP B 151  ARG B 152  GLU B 277
SITE     2 DC5  7 ARG B 292  ARG B 371  TYR B 406
CRYST1  120.350  139.720  140.230  90.00  90.00  90.00 C 2 2 21     16
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      0.008309  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007157  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007131        0.00000
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1
MTRIX2   1  0.000000  0.000000  1.000000        0.00000    1
MTRIX3   1  0.000000 -1.000000  0.000000        0.00000    1
      
PROCHECK
Go to PROCHECK summary
 References