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PDBsum entry 1a4g

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Hydrolase PDB id
1a4g
Jmol
Contents
Protein chains
390 a.a. *
Ligands
NAG ×2
ZMR ×2
Metals
_CA ×3
Waters ×492
* Residue conservation analysis
HEADER    HYDROLASE                               29-JAN-98   1A4G
TITLE     INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH ZANAMIVIR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: RESIDUES 76-465;
COMPND   5 SYNONYM: SIALIDASE;
COMPND   6 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA B VIRUS (STRAIN B/BEIJING/1/87);
SOURCE   3 ORGANISM_TAXID: 11525;
SOURCE   4 STRAIN: B/BEIJING/1/87
KEYWDS    HYDROLASE, GLYCOSIDASE, GLYCOSYLATED PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.CLEASBY,O.SINGH,T.SKARZYNSKI,A.J.WONACOTT
REVDAT   4   13-JUL-11 1A4G    1       VERSN
REVDAT   3   24-FEB-09 1A4G    1       VERSN
REVDAT   2   20-APR-99 1A4G    3       ATOM   HET    SOURCE COMPND
REVDAT   2 2                   3       REMARK HETATM KEYWDS HEADER
REVDAT   2 3                   3       MODRES TER    CONECT
REVDAT   1   02-MAR-99 1A4G    0
JRNL        AUTH   N.R.TAYLOR,A.CLEASBY,O.SINGH,T.SKARZYNSKI,A.J.WONACOTT,
JRNL        AUTH 2 P.W.SMITH,S.L.SOLLIS,P.D.HOWES,P.C.CHERRY,R.BETHELL,
JRNL        AUTH 3 P.COLMAN,J.VARGHESE
JRNL        TITL   DIHYDROPYRANCARBOXAMIDES RELATED TO ZANAMIVIR: A NEW SERIES
JRNL        TITL 2 OF INHIBITORS OF INFLUENZA VIRUS SIALIDASES. 2.
JRNL        TITL 3 CRYSTALLOGRAPHIC AND MOLECULAR MODELING STUDY OF COMPLEXES
JRNL        TITL 4 OF 4-AMINO-4H-PYRAN-6-CARBOXAMIDES AND SIALIDASE FROM
JRNL        TITL 5 INFLUENZA VIRUS TYPES A AND B.
JRNL        REF    J.MED.CHEM.                   V.  41   798 1998
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   9526556
JRNL        DOI    10.1021/JM9703754
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   W.P.BURMEISTER,R.W.RUIGROK,S.CUSACK
REMARK   1  TITL   THE 2.2 A RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA B
REMARK   1  TITL 2 NEURAMINIDASE AND ITS COMPLEX WITH SIALIC ACID
REMARK   1  REF    EMBO J.                       V.  11    49 1992
REMARK   1  REFN                   ISSN 0261-4189
REMARK   1 REFERENCE 2
REMARK   1  AUTH   W.P.BURMEISTER,R.S.DANIELS,S.DAYAN,J.GAGNON,S.CUSACK,
REMARK   1  AUTH 2 R.W.RUIGROK
REMARK   1  TITL   SEQUENCE AND CRYSTALLIZATION OF INFLUENZA VIRUS
REMARK   1  TITL 2 B/BEIJING/1/87 NEURAMINIDASE
REMARK   1  REF    VIROLOGY                      V. 180   266 1991
REMARK   1  REFN                   ISSN 0042-6822
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.8
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.00
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             : 50283
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) : 0.198
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6274
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360
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            : 6072
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 77
REMARK   3   SOLVENT ATOMS            : 492
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) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 2.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.80
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.00
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) : 2.000 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.000 ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.700 ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.000 ; 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  : ENGH.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPENGH.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: THE TWO MONOMERS IN THE
REMARK   3  CRYSTALLOGRAPHIC ASYMMETRIC UNIT HAVE BEEN REFINED INDEPENDENTLY.
REMARK   4
REMARK   4 1A4G 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        : FEB-95
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX9.6
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 140043
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 2.700
REMARK 200  R MERGE                    (I) : 0.12800
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: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: 1NSC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.70000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      147.40000
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      147.40000
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       73.70000
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: 20100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
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 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    TYR A 295   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG B 153   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG B 153   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG B 222   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    VAL B 270   N   -  CA  -  CB  ANGL. DEV. = -13.9 DEGREES
REMARK 500    ARG B 355   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG B 355   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ALA A 175      132.55   -171.84
REMARK 500    ASN A 198       65.01   -162.87
REMARK 500    ALA A 217       10.54   -141.27
REMARK 500    ASN A 218       51.27     32.49
REMARK 500    ASN A 219       83.13   -154.82
REMARK 500    ILE A 220       77.06     52.39
REMARK 500    GLU A 225       32.35     70.40
REMARK 500    ASP A 383     -163.48     55.80
REMARK 500    TRP A 407     -121.06   -111.10
REMARK 500    ALA B  94      -61.23   -103.51
REMARK 500    ASP B 148      -62.62    -92.50
REMARK 500    ASN B 198       51.87   -145.33
REMARK 500    ASN B 219       84.30   -160.71
REMARK 500    ILE B 220       78.38     48.62
REMARK 500    HIS B 272      108.71   -165.43
REMARK 500    SER B 282     -169.97   -170.93
REMARK 500    CYS B 336      -36.06    -39.67
REMARK 500    ASP B 383     -160.96     59.86
REMARK 500    TRP B 407     -128.40   -104.97
REMARK 500    SER B 439     -163.96   -172.65
REMARK 500    MET B 448      108.59   -161.57
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    TYR B 321         0.08    SIDE CHAIN
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   2  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 292   O
REMARK 620 2 THR A 296   O    85.1
REMARK 620 3 ASP A 323   OD2  90.3  92.2
REMARK 620 4 GLY A 343   O    96.5  83.2 171.4
REMARK 620 5 GLY A 345   O    90.4 167.5  99.5  85.7
REMARK 620 6 HOH A 594   O   174.4  91.1  93.9  79.0  92.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B   2  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 323   OD2
REMARK 620 2 HOH B 551   O    78.6
REMARK 620 3 ASP B 292   O    92.2 169.9
REMARK 620 4 GLY B 343   O   164.8  87.2 102.4
REMARK 620 5 GLY B 345   O    94.0  84.0  92.6  89.6
REMARK 620 6 THR B 296   O    94.2  98.2  86.5  82.6 171.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B   3  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 109   OG
REMARK 620 2 HOH B 480   O    94.4
REMARK 620 3 ASN B 108   O    79.8 104.3
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CHA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HIGH AFFINITY CALCIUM BINDING SITE IN CHAIN A.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CLA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: LOW AFFINITY CALCIUM BINDING SITE IN CHAIN A.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZAA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR ZANAMIVIR IN CHAIN A.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CHB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HIGH AFFINITY CALCIUM BINDING SITE IN CHAIN B.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CLB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: N/LOW AFFINITY CALCIUM BINDING SITE IN CHAIN B.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZAB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR ZANAMIVIR IN CHAIN B.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR A 466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR B 466
DBREF  1A4G A   76   465  UNP    P27907   NRAM_INBBE      76    465
DBREF  1A4G B   76   465  UNP    P27907   NRAM_INBBE      76    465
SEQRES   1 A  390  GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY
SEQRES   2 A  390  SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG
SEQRES   3 A  390  PHE GLY GLU ALA ARG GLY ASN SER ALA PRO LEU ILE ILE
SEQRES   4 A  390  ARG GLU PRO PHE ILE ALA CYS GLY PRO LYS GLU CYS LYS
SEQRES   5 A  390  HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY
SEQRES   6 A  390  TYR TYR ASN GLY THR ARG GLU ASP ARG ASN LYS LEU ARG
SEQRES   7 A  390  HIS LEU ILE SER VAL LYS LEU GLY LYS ILE PRO THR VAL
SEQRES   8 A  390  GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER
SEQRES   9 A  390  ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL
SEQRES  10 A  390  ASP GLY PRO ASP SER ASN ALA LEU ILE LYS ILE LYS TYR
SEQRES  11 A  390  GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA ASN
SEQRES  12 A  390  ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE
SEQRES  13 A  390  GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA
SEQRES  14 A  390  SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU
SEQRES  15 A  390  GLY ARG ILE ILE LYS GLU ILE PHE PRO THR GLY ARG VAL
SEQRES  16 A  390  GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN
SEQRES  17 A  390  LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR
SEQRES  18 A  390  ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP
SEQRES  19 A  390  THR ALA GLU ILE ARG LEU MET CYS THR GLU THR TYR LEU
SEQRES  20 A  390  ASP THR PRO ARG PRO ASP ASP GLY SER ILE THR GLY PRO
SEQRES  21 A  390  CYS GLU SER ASN GLY ASP LYS GLY ARG GLY GLY ILE LYS
SEQRES  22 A  390  GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY
SEQRES  23 A  390  ARG TRP TYR SER ARG THR MET SER LYS THR GLU ARG MET
SEQRES  24 A  390  GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP
SEQRES  25 A  390  THR ASP SER ASP ALA LEU ALA HIS SER GLY VAL MET VAL
SEQRES  26 A  390  SER MET LYS GLU PRO GLY TRP TYR SER PHE GLY PHE GLU
SEQRES  27 A  390  ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE
SEQRES  28 A  390  GLU MET VAL HIS ASP GLY GLY LYS LYS THR TRP HIS SER
SEQRES  29 A  390  ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN
SEQRES  30 A  390  LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU
SEQRES   1 B  390  GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY
SEQRES   2 B  390  SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG
SEQRES   3 B  390  PHE GLY GLU ALA ARG GLY ASN SER ALA PRO LEU ILE ILE
SEQRES   4 B  390  ARG GLU PRO PHE ILE ALA CYS GLY PRO LYS GLU CYS LYS
SEQRES   5 B  390  HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY
SEQRES   6 B  390  TYR TYR ASN GLY THR ARG GLU ASP ARG ASN LYS LEU ARG
SEQRES   7 B  390  HIS LEU ILE SER VAL LYS LEU GLY LYS ILE PRO THR VAL
SEQRES   8 B  390  GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER
SEQRES   9 B  390  ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL
SEQRES  10 B  390  ASP GLY PRO ASP SER ASN ALA LEU ILE LYS ILE LYS TYR
SEQRES  11 B  390  GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA ASN
SEQRES  12 B  390  ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE
SEQRES  13 B  390  GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA
SEQRES  14 B  390  SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU
SEQRES  15 B  390  GLY ARG ILE ILE LYS GLU ILE PHE PRO THR GLY ARG VAL
SEQRES  16 B  390  GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN
SEQRES  17 B  390  LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR
SEQRES  18 B  390  ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP
SEQRES  19 B  390  THR ALA GLU ILE ARG LEU MET CYS THR GLU THR TYR LEU
SEQRES  20 B  390  ASP THR PRO ARG PRO ASP ASP GLY SER ILE THR GLY PRO
SEQRES  21 B  390  CYS GLU SER ASN GLY ASP LYS GLY ARG GLY GLY ILE LYS
SEQRES  22 B  390  GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY
SEQRES  23 B  390  ARG TRP TYR SER ARG THR MET SER LYS THR GLU ARG MET
SEQRES  24 B  390  GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP
SEQRES  25 B  390  THR ASP SER ASP ALA LEU ALA HIS SER GLY VAL MET VAL
SEQRES  26 B  390  SER MET LYS GLU PRO GLY TRP TYR SER PHE GLY PHE GLU
SEQRES  27 B  390  ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE
SEQRES  28 B  390  GLU MET VAL HIS ASP GLY GLY LYS LYS THR TRP HIS SER
SEQRES  29 B  390  ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN
SEQRES  30 B  390  LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU
MODRES 1A4G ASN A  283  ASN  GLYCOSYLATION SITE
MODRES 1A4G ASN B  283  ASN  GLYCOSYLATION SITE
HET    NAG  A   1      14
HET    NAG  B   1      14
HET     CA  A   2       1
HET     CA  B   2       1
HET     CA  B   3       1
HET    ZMR  A 466      23
HET    ZMR  B 466      23
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      CA CALCIUM ION
HETNAM     ZMR ZANAMIVIR
HETSYN     ZMR MODIFIED SIALIC ACID
FORMUL   3  NAG    2(C8 H15 N O6)
FORMUL   5   CA    3(CA 2+)
FORMUL   8  ZMR    2(C12 H20 N4 O7)
FORMUL  10  HOH   *492(H2 O)
HELIX    1   1 PRO A   99  PHE A  102  5                                   4
HELIX    2   2 PRO B   99  PHE B  102  5                                   4
HELIX    3   3 ASP B  196  ASN B  198  5                                   3
SHEET    1  1A 4 ILE A 113  CYS A 121  0
SHEET    2  1A 4 CYS A 126  THR A 132 -1  N  LEU A 131   O  ARG A 115
SHEET    3  1A 4 HIS A 154  LYS A 159 -1  O  VAL A 158   N  HIS A 128
SHEET    4  1A 4 ILE A 170  ALA A 174 -1  O  ILE A 170   N  SER A 157
SHEET    1  2A 4 SER A 177  HIS A 182  0
SHEET    2  2A 4 TRP A 187  ASP A 193 -1  N  VAL A 192   O  SER A 177
SHEET    3  2A 4 LEU A 200  TYR A 205 -1  N  LYS A 202   O  GLY A 191
SHEET    4  2A 4 ALA A 208  HIS A 214 -1  N  TYR A 213   O  ILE A 201
SHEET    1 3AA 4 ARG A 222  THR A 223  0
SHEET    2 3AA 4 ASP A 234  GLY A 242 -1  O  THR A 240   N  ARG A 222
SHEET    3 3AA 4 SER A 248  ARG A 256 -1  N  LEU A 253   O  LEU A 237
SHEET    4 3AA 4 ARG A 259  ILE A 264 -1  N  ARG A 259   O  ARG A 256
SHEET    1 3BA 4 ASN A 229  ILE A 231  0
SHEET    2 3BA 4 ASP A 234  GLY A 242 -1  O  TYR A 236   N  ASN A 229
SHEET    3 3BA 4 SER A 248  ARG A 256 -1  N  LEU A 253   O  LEU A 237
SHEET    4 3BA 4 ARG A 259  ILE A 264 -1  N  ARG A 259   O  ARG A 256
SHEET    1  4A 4 GLU A 274  PHE A 280  0
SHEET    2  4A 4 THR A 285  ARG A 291 -1  O  ARG A 291   N  GLU A 274
SHEET    3  4A 4 PRO A 300  ASN A 305 -1  O  PRO A 300   N  CYS A 290
SHEET    4  4A 4 THR A 310  LEU A 315 -1  O  THR A 310   N  ASN A 305
SHEET    1  5A 4 PHE A 351  ARG A 355  0
SHEET    2  5A 4 ILE A 360  ARG A 366 -1  O  TRP A 363   N  VAL A 352
SHEET    3  5A 4 MET A 376  TYR A 382 -1  N  GLU A 377   O  ARG A 366
SHEET    4  5A 4 ALA A 394  VAL A 400 -1  N  ALA A 394   O  VAL A 380
SHEET    1  6A 4 SER A 409  LYS A 415  0
SHEET    2  6A 4 ASP A 420  HIS A 430 -1  O  GLY A 425   N  PHE A 410
SHEET    3  6A 4 SER A 439  LEU A 447 -1  O  ALA A 443   N  ILE A 426
SHEET    4  6A 4 PHE A  91  ILE A  97 -1  O  ILE A  97   N  THR A 442
SHEET    1  1B 4 ILE B 113  CYS B 121  0
SHEET    2  1B 4 CYS B 126  THR B 132 -1  N  LEU B 131   O  ARG B 115
SHEET    3  1B 4 HIS B 154  LYS B 159 -1  O  VAL B 158   N  HIS B 128
SHEET    4  1B 4 ILE B 170  ALA B 174 -1  O  ILE B 170   N  SER B 157
SHEET    1  2B 4 SER B 177  HIS B 182  0
SHEET    2  2B 4 TRP B 187  ASP B 193 -1  N  VAL B 192   O  SER B 177
SHEET    3  2B 4 LEU B 200  TYR B 205 -1  N  LYS B 202   O  GLY B 191
SHEET    4  2B 4 ALA B 208  HIS B 214 -1  N  TYR B 213   O  ILE B 201
SHEET    1 3AB 4 ARG B 222  THR B 223  0
SHEET    2 3AB 4 ASP B 234  GLY B 242 -1  O  THR B 240   N  ARG B 222
SHEET    3 3AB 4 SER B 248  ARG B 256 -1  N  LEU B 253   O  LEU B 237
SHEET    4 3AB 4 ARG B 259  ILE B 264 -1  N  ARG B 259   O  ARG B 256
SHEET    1 3BB 4 ASN B 229  ILE B 231  0
SHEET    2 3BB 4 ASP B 234  GLY B 242 -1  O  TYR B 236   N  ASN B 229
SHEET    3 3BB 4 SER B 248  ARG B 256 -1  N  LEU B 253   O  LEU B 237
SHEET    4 3BB 4 ARG B 259  ILE B 264 -1  N  ARG B 259   O  ARG B 256
SHEET    1  4B 4 GLU B 274  PHE B 280  0
SHEET    2  4B 4 THR B 285  ARG B 291 -1  O  ARG B 291   N  GLU B 274
SHEET    3  4B 4 PRO B 300  ASN B 305 -1  O  PRO B 300   N  CYS B 290
SHEET    4  4B 4 THR B 310  LEU B 315 -1  O  THR B 310   N  ASN B 305
SHEET    1  5B 4 PHE B 351  ARG B 355  0
SHEET    2  5B 4 ILE B 360  ARG B 366 -1  O  TRP B 363   N  VAL B 352
SHEET    3  5B 4 MET B 376  TYR B 382 -1  N  GLU B 377   O  ARG B 366
SHEET    4  5B 4 ALA B 394  VAL B 400 -1  N  ALA B 394   O  VAL B 380
SHEET    1  6B 4 SER B 409  LYS B 415  0
SHEET    2  6B 4 ASP B 420  HIS B 430 -1  O  GLY B 425   N  PHE B 410
SHEET    3  6B 4 SER B 439  LEU B 447 -1  O  ALA B 443   N  ILE B 426
SHEET    4  6B 4 PHE B  91  ILE B  97 -1  O  ILE B  97   N  THR B 442
SSBOND   1 CYS A   86    CYS A  419                          1555   1555  2.04
SSBOND   2 CYS A  121    CYS A  126                          1555   1555  2.03
SSBOND   3 CYS A  181    CYS A  228                          1555   1555  2.03
SSBOND   4 CYS A  230    CYS A  235                          1555   1555  2.04
SSBOND   5 CYS A  276    CYS A  290                          1555   1555  2.03
SSBOND   6 CYS A  278    CYS A  288                          1555   1555  2.02
SSBOND   7 CYS A  317    CYS A  336                          1555   1555  2.03
SSBOND   8 CYS A  423    CYS A  446                          1555   1555  2.03
SSBOND   9 CYS B   86    CYS B  419                          1555   1555  2.04
SSBOND  10 CYS B  121    CYS B  126                          1555   1555  2.04
SSBOND  11 CYS B  181    CYS B  228                          1555   1555  2.02
SSBOND  12 CYS B  230    CYS B  235                          1555   1555  2.02
SSBOND  13 CYS B  276    CYS B  290                          1555   1555  2.03
SSBOND  14 CYS B  278    CYS B  288                          1555   1555  2.03
SSBOND  15 CYS B  317    CYS B  336                          1555   1555  2.02
SSBOND  16 CYS B  423    CYS B  446                          1555   1555  2.03
LINK         C1  NAG A   1                 ND2 ASN A 283     1555   1555  1.46
LINK         C1  NAG B   1                 ND2 ASN B 283     1555   1555  1.47
LINK        CA    CA A   2                 O   ASP A 292     1555   1555  2.42
LINK        CA    CA A   2                 O   THR A 296     1555   1555  2.47
LINK        CA    CA A   2                 OD2 ASP A 323     1555   1555  2.68
LINK        CA    CA A   2                 O   GLY A 343     1555   1555  2.46
LINK        CA    CA A   2                 O   GLY A 345     1555   1555  2.41
LINK        CA    CA A   2                 O   HOH A 594     1555   1555  2.45
LINK        CA    CA B   2                 OD2 ASP B 323     1555   1555  2.71
LINK        CA    CA B   2                 O   HOH B 551     1555   1555  2.46
LINK        CA    CA B   2                 O   ASP B 292     1555   1555  2.40
LINK        CA    CA B   2                 O   GLY B 343     1555   1555  2.48
LINK        CA    CA B   2                 O   GLY B 345     1555   1555  2.42
LINK        CA    CA B   2                 O   THR B 296     1555   1555  2.43
LINK        CA    CA B   3                 OG  SER B 109     1555   4555  2.45
LINK        CA    CA B   3                 O   HOH B 480     1555   4555  2.65
LINK        CA    CA B   3                 O   ASN B 108     1555   4555  2.77
CISPEP   1 GLN A  137    PRO A  138          0        -3.40
CISPEP   2 THR A  324    PRO A  325          0        -5.82
CISPEP   3 GLN B  137    PRO B  138          0        -5.63
CISPEP   4 THR B  324    PRO B  325          0        -4.45
SITE     1 CHA  5 ASP A 323  GLY A 343  GLY A 345  THR A 296
SITE     2 CHA  5 ASP A 292
SITE     1 CLA  1 GLU A 167
SITE     1 ZAA 10 ASP A 323  ARG A 115  ARG A 291  ARG A 149
SITE     2 ZAA 10 ILE A 220  ARG A 222  TRP A 176  GLU A 274
SITE     3 ZAA 10 ASP A 148  TYR A 408
SITE     1 CHB  5 ASP B 323  GLY B 343  GLY B 345  THR B 296
SITE     2 CHB  5 ASP B 292
SITE     1 CLB  1 GLU B 167
SITE     1 ZAB 10 ASP B 323  ARG B 115  ARG B 291  ARG B 149
SITE     2 ZAB 10 ILE B 220  ARG B 222  TRP B 176  GLU B 274
SITE     3 ZAB 10 ASP B 148  TYR B 408
SITE     1 AC1  7 PRO A  82  ASN A 283  HOH A 538  HOH A 579
SITE     2 AC1  7 HOH A 596  HOH A 609  HOH A 633
SITE     1 AC2  5 PRO B  82  ASN B 283  HOH B 581  HOH B 628
SITE     2 AC2  5 HOH B 702
SITE     1 AC3  6 ASP A 292  THR A 296  ASP A 323  GLY A 343
SITE     2 AC3  6 GLY A 345  HOH A 594
SITE     1 AC4  6 ASP B 292  THR B 296  ASP B 323  GLY B 343
SITE     2 AC4  6 GLY B 345  HOH B 551
SITE     1 AC5  4 ALA A 110  ASN B 108  SER B 109  HOH B 480
SITE     1 AC6 16 ARG A 115  GLU A 116  ASP A 148  ARG A 149
SITE     2 AC6 16 ARG A 153  TRP A 176  ARG A 222  GLU A 225
SITE     3 AC6 16 ALA A 244  GLU A 274  ARG A 291  ARG A 373
SITE     4 AC6 16 TYR A 408  HOH A 701  HOH A 704  HOH A 713
SITE     1 AC7 19 ARG B 115  GLU B 116  ASP B 148  ARG B 149
SITE     2 AC7 19 ARG B 153  TRP B 176  ILE B 220  ARG B 222
SITE     3 AC7 19 GLU B 225  ALA B 244  GLU B 274  GLU B 275
SITE     4 AC7 19 ARG B 291  ASN B 293  ARG B 373  TYR B 408
SITE     5 AC7 19 HOH B 685  HOH B 686  HOH B 694
CRYST1   88.200   88.200  221.100  90.00  90.00 120.00 P 31 2 1     12
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      0.011338  0.006546  0.000000        0.00000
SCALE2      0.000000  0.013092  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004523        0.00000
MTRIX1   1  0.250000  0.433000 -0.866000        0.00000    1
MTRIX2   1  0.433000  0.750000  0.500000        0.00000    1
MTRIX3   1  0.866000 -0.500000  0.000000        0.00000    1
      
PROCHECK
Go to PROCHECK summary
 References