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PDBsum entry 2c4a

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Hydrolase PDB id
2c4a
Jmol
Contents
Protein chain
388 a.a.
Ligands
SIA ×2
NAG-NAG ×2
NAG
BMA-MAN-MAN-MAN-
MAN-MAN-MAN
Metals
_CA
Waters ×259
HEADER    HYDROLASE                               17-OCT-05   2C4A
TITLE     STRUCTURE OF NEURAMINIDASE SUBTYPE N9 COMPLEXED WITH 30 MM
TITLE    2 SIALIC ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 3 HOURS AT
TITLE    3 291 K.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE SUBTYPE N9;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 83-470;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_COMMON: AVIAN INFLUENZA VIRUS A;
SOURCE   4 ORGANISM_TAXID: 11320;
SOURCE   5 STRAIN: A/TERN/STERNA ALBIFRONS/N9;
SOURCE   6 EXPRESSION_SYSTEM: GALLUS GALLUS;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9031
KEYWDS    HYDROLASE, INFLUENZA TYPE A, NEURAMINIDASE, SIALIC ACID,
KEYWDS   2 SUBTYPE N9, GLYCOPROTEIN, GLYCOSIDASE, TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.RUDINO-PINERA,P.TUNNAH,S.J.CRENNELL,R.G.WEBSTER,W.G.LAVER,
AUTHOR   2 E.F.GARMAN
REVDAT   2   24-FEB-09 2C4A    1       VERSN
REVDAT   1   27-MAR-07 2C4A    0
JRNL        AUTH   E.RUDINO-PINERA,S.J.CRENNELL,R.G.WEBSTER,W.G.LAVER,
JRNL        AUTH 2 E.F.GARMAN
JRNL        TITL   THE CRYSTAL STRUCTURE OF INFLUENZA TYPE A VIRUS
JRNL        TITL 2 NEURAMINIDASE OF THE N6 SUBTYPE AT 1.85 A
JRNL        TITL 3 RESOLUTION
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.10
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 26444
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.160
REMARK   3   R VALUE            (WORKING SET) : 0.158
REMARK   3   FREE R VALUE                     : 0.205
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1401
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1891
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1510
REMARK   3   BIN FREE R VALUE SET COUNT          : 100
REMARK   3   BIN FREE R VALUE                    : 0.2250
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3067
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 190
REMARK   3   SOLVENT ATOMS            : 259
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.57
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.20
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.184
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.164
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.660
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3338 ; 0.017 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4556 ; 1.602 ; 1.989
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   385 ; 7.647 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   147 ;33.305 ;23.469
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   492 ;13.154 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;18.688 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   514 ; 0.111 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2484 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1586 ; 0.287 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2217 ; 0.310 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   285 ; 0.141 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    89 ; 0.190 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.092 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1993 ; 0.689 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3134 ; 1.057 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1578 ; 1.980 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1422 ; 2.911 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2C4A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-05.
REMARK 100 THE PDBE ID CODE IS EBI-25840.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-04
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.80
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200H
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : CONFOCAL OSMIC BLUE
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE (MAR345)
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27874
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.660
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 9.900
REMARK 200  R MERGE                    (I) : 0.12000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.27000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 7NN9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLISED FROM
REMARK 280  1.9M POTASSIUM PHOSPHATE PH 6.8, THEN SOAKED FOR 3 HOURS
REMARK 280  IN 30 MM NEU5AC
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   Z,X,Y
REMARK 290       6555   Z,-X,-Y
REMARK 290       7555   -Z,-X,Y
REMARK 290       8555   -Z,X,-Y
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z,-X
REMARK 290      11555   Y,-Z,-X
REMARK 290      12555   -Y,-Z,X
REMARK 290      13555   Y,X,-Z
REMARK 290      14555   -Y,-X,-Z
REMARK 290      15555   Y,-X,Z
REMARK 290      16555   -Y,X,Z
REMARK 290      17555   X,Z,-Y
REMARK 290      18555   -X,Z,Y
REMARK 290      19555   -X,-Z,-Y
REMARK 290      20555   X,-Z,Y
REMARK 290      21555   Z,Y,-X
REMARK 290      22555   Z,-Y,X
REMARK 290      23555   -Z,Y,X
REMARK 290      24555   -Z,-Y,-X
REMARK 290      25555   X+1/2,Y+1/2,Z+1/2
REMARK 290      26555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      27555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      28555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      29555   Z+1/2,X+1/2,Y+1/2
REMARK 290      30555   Z+1/2,-X+1/2,-Y+1/2
REMARK 290      31555   -Z+1/2,-X+1/2,Y+1/2
REMARK 290      32555   -Z+1/2,X+1/2,-Y+1/2
REMARK 290      33555   Y+1/2,Z+1/2,X+1/2
REMARK 290      34555   -Y+1/2,Z+1/2,-X+1/2
REMARK 290      35555   Y+1/2,-Z+1/2,-X+1/2
REMARK 290      36555   -Y+1/2,-Z+1/2,X+1/2
REMARK 290      37555   Y+1/2,X+1/2,-Z+1/2
REMARK 290      38555   -Y+1/2,-X+1/2,-Z+1/2
REMARK 290      39555   Y+1/2,-X+1/2,Z+1/2
REMARK 290      40555   -Y+1/2,X+1/2,Z+1/2
REMARK 290      41555   X+1/2,Z+1/2,-Y+1/2
REMARK 290      42555   -X+1/2,Z+1/2,Y+1/2
REMARK 290      43555   -X+1/2,-Z+1/2,-Y+1/2
REMARK 290      44555   X+1/2,-Z+1/2,Y+1/2
REMARK 290      45555   Z+1/2,Y+1/2,-X+1/2
REMARK 290      46555   Z+1/2,-Y+1/2,X+1/2
REMARK 290      47555   -Z+1/2,Y+1/2,X+1/2
REMARK 290      48555   -Z+1/2,-Y+1/2,-X+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  25  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000       90.66800
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       90.66800
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000       90.66800
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       90.66800
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       90.66800
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       90.66800
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 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375      HOH A2163  LIES ON A SPECIAL POSITION.
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   ND2  ASN A    86  -  O5   NAG A  1473              2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    VAL A 333   C     GLY A 335   N       0.234
REMARK 500    ASP A 385   C     ASP A 386   N       0.149
REMARK 500    GLN A 392   C     GLY A 394   N       0.244
REMARK 500    GLU A 416   CD    GLU A 416   OE1    -0.237
REMARK 500
REMARK 500 REMARK: NULL
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    ASP A 127   CB  -  CG  -  OD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500    ARG A 172   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 364   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG A 364   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    GLU A 416   CG  -  CD  -  OE2 ANGL. DEV. = -18.8 DEGREES
REMARK 500    GLU A 416   OE1 -  CD  -  OE2 ANGL. DEV. =  19.5 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 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    ASP A 111       39.64   -148.71
REMARK 500    THR A 138      149.76   -172.47
REMARK 500    SER A 164       -1.93     69.57
REMARK 500    ASN A 200       37.90   -156.43
REMARK 500    THR A 217      132.08    -39.10
REMARK 500    ASN A 221       83.88   -152.40
REMARK 500    THR A 225     -154.62   -141.37
REMARK 500    ARG A 284       54.90     38.93
REMARK 500    CYS A 291     -167.97   -121.77
REMARK 500    ASN A 359       46.92    -84.95
REMARK 500    PHE A 452       78.53   -102.46
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 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    VAL A 204        24.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 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 A1483  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 324   OD2
REMARK 620 2 HOH A2157   O    94.5
REMARK 620 3 ASP A 293   O    94.6 152.5
REMARK 620 4 ASN A 347   O   111.6  92.5 108.0
REMARK 620 5 HOH A2168   O   176.0  82.3  87.2  71.0
REMARK 620 6 GLY A 297   O    82.3  81.1  74.5 165.2  94.7
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1483
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A14   RELATED DB: PDB
REMARK 900  COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5
REMARK 900   RESIDUE LINKER AND INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 1BJI   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF TERN
REMARK 900   N9 INFLUENZA VIRUS NEURAMINIDASE COMPLEXED
REMARK 900  WITH THE GLAXO 6-CARBOXAMIDE SIALIC ACID
REMARK 900  ANALOGUE GR217029
REMARK 900 RELATED ID: 1F8B   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA VIRUS NEURAMINIDASE IN
REMARK 900  COMPLEX WITHNEU5AC2EN
REMARK 900 RELATED ID: 1F8C   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH
REMARK 900   4-AMINO-2-DEOXY-2,3-DEHYDRO-N-
REMARK 900  NEURAMINIC ACID
REMARK 900 RELATED ID: 1F8D   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH
REMARK 900   9-AMINO-2-DEOXY-2,3-DEHYDRO-N-
REMARK 900  NEURAMINIC ACID
REMARK 900 RELATED ID: 1F8E   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH
REMARK 900   4,9-DIAMINO-2-DEOXY-2,3-DEHYDRO-N-
REMARK 900  ACETYL-NEURAMINIC ACID
REMARK 900 RELATED ID: 1INY   RELATED DB: PDB
REMARK 900  INFLUENZA A SUBTYPE N9 NEURAMINIDASE (
REMARK 900  SIALIDASE) COMPLEXED WITH EPANA INHIBITOR (4-
REMARK 900  ACETAMIDO- 2,4-DIDEOXY-D-GLYCERO-ALPHA-D-
REMARK 900  GALACTO-1-OCTOPYRANOSYL) PHOSPHONIC ACID
REMARK 900 RELATED ID: 1L7F   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE INCOMPLEX WITH BCX-1812
REMARK 900 RELATED ID: 1L7G   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF E119G MUTANT INFLUENZA
REMARK 900  VIRUSNEURAMINIDASE IN COMPLEX WITH BCX-1812
REMARK 900 RELATED ID: 1L7H   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF R292K MUTANT INFLUENZA
REMARK 900  VIRUSNEURAMINIDASE IN COMPLEX WITH BCX-1812
REMARK 900 RELATED ID: 1MWE   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF TERN
REMARK 900   N9 INFLUENZA VIRUS NEURAMINIDASE COMPLEXED
REMARK 900  WITH SIALIC ACID AT 4 DEGREES C REVEALING
REMARK 900   A SECOND SIALIC ACID BINDING SITE
REMARK 900 RELATED ID: 1NCA   RELATED DB: PDB
REMARK 900  N9 NEURAMINIDASE-NC41 COMPLEX WITH FAB
REMARK 900 RELATED ID: 1NCB   RELATED DB: PDB
REMARK 900  N9 NEURAMINIDASE-NC41 MUTANT WITH ASN 329
REMARK 900  REPLACED BY ASP (N329D) COMPLEX WITH FAB
REMARK 900 RELATED ID: 1NCC   RELATED DB: PDB
REMARK 900  N9 NEURAMINIDASE-NC41 MUTANT WITH ILE 368
REMARK 900  REPLACED BY ARG (I368R) COMPLEX WITH FAB
REMARK 900 RELATED ID: 1NMC   RELATED DB: PDB
REMARK 900  COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A
REMARK 900  15 RESIDUE LINKER AND INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 1NNA   RELATED DB: PDB
REMARK 900  NEURAMINIDASE (SIALIDASE)
REMARK 900 RELATED ID: 1NNB   RELATED DB: PDB
REMARK 900  NEURAMINIDASE (SIALIDASE) COMPLEXED WITH 2-
REMARK 900  DEOXY-2,3-DEHYDRO-N-ACETYL NEURAMINIC ACID
REMARK 900 RELATED ID: 1NNC   RELATED DB: PDB
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN)
REMARK 900   COMPLEXED WITH 4-GUANIDINO-NEU5AC2EN
REMARK 900  INHIBITOR
REMARK 900 RELATED ID: 1XOE   RELATED DB: PDB
REMARK 900  N9 TERN INFLUENZA NEURAMINIDASE COMPLEXED WITH
REMARK 900   (2R,4R,5R)-5-(1-ACETYLAMINO-3-METHYL-
REMARK 900  BUTYL-PYRROLIDINE-2, 4-DICAROBYXYLIC ACID 4
REMARK 900  -METHYL ESTERDASE COMPLEXED WITH
REMARK 900 RELATED ID: 1XOG   RELATED DB: PDB
REMARK 900  N9 TERN INFLUENZA NEURAMINIDASE COMPLEXED WITH
REMARK 900   A 2,5-DISUBSTITUTED TETRAHYDROFURAN-5-
REMARK 900  CARBOXYLIC ACID
REMARK 900 RELATED ID: 2QWA   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A DRUG RESISTANT
REMARK 900  VARIANT R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWB   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF
REMARK 900  SIALIC ACID AND A DRUG RESISTANT VARIANT
REMARK 900  R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWC   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF
REMARK 900  NEU5AC2EN AND A DRUG RESISTANT VARIANT R292K
REMARK 900   OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWD   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 4-
REMARK 900  AMINO-NEU5AC2EN AND A DRUG RESISTANT VARIANT
REMARK 900   R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWE   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 4-
REMARK 900  GUANIDINO-NEU5AC2EN AND A DRUG RESISTANT
REMARK 900  VARIANT R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWF   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF N-
REMARK 900  ACETYL-4-GUANIDINO-6- METHYL(PROPYL)
REMARK 900  CARBOXAMIDE-4,5-DIHYDRO-2H-PYRAN-2-
REMARK 900  CARBOXYLIC ACID AND A DRUG RESISTANT VARIANT
REMARK 900   R292K OF TERN N9 INFLUENZA VIRUS
REMARK 900  NEURAMINIDASE
REMARK 900 RELATED ID: 2QWG   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 5-
REMARK 900  N-ACETYL-4-AMINO-6- DIETHYLCARBOXAMIDE-4,5
REMARK 900  -DIHYDRO-2H-PYRAN-2-CARBOXYLIC ACID AND A
REMARK 900   DRUG RESISTANT VARIANT R292K OF TERN N9
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWH   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 5-
REMARK 900  N-ACETYL-5-AMINO-3- (1-ETHYLPROPOXY)-1-
REMARK 900  CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND A
REMARK 900   DRUG RESISTANT VARIANT R292K OF TERN N9
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWI   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF N-
REMARK 900  ACETYL-4-GUANIDINO-6- METHYL(PROPYL)
REMARK 900  CARBOXAMIDE-4,5-DIHYDRO-2H-PYRAN-2-
REMARK 900  CARBOXYLIC ACID AND WILDTYPE TERN N9
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWJ   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 5-
REMARK 900  N-ACETYL-4-AMINO-6- DIETHYLCARBOXAMIDE-4,5
REMARK 900  -DIHYDRO-2H-PYRAN-2-CARBOXYLIC ACID AND A
REMARK 900   DRUG RESISTANT VARIANT R292K OF TERN N9
REMARK 900  INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 2QWK   RELATED DB: PDB
REMARK 900  THE X-RAY STRUCTURE OF A COMPLEX OF 5-
REMARK 900  N-ACETYL-5-AMINO-3- (1-ETHYLPROPOXY)-1-
REMARK 900  CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND
REMARK 900  WILDTYPE TERN N9 INFLUENZA VIRUS NEURAMINIDASE
REMARK 900 RELATED ID: 3NN9   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ASN
REMARK 900   329 REPLACED BY ASP) (N329D)
REMARK 900 RELATED ID: 4NN9   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ILE
REMARK 900   368 REPLACED BY ARG) (I368R)
REMARK 900 RELATED ID: 5NN9   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ALA
REMARK 900   369 REPLACED BY ASP) (A369D)
REMARK 900 RELATED ID: 6NN9   RELATED DB: PDB
REMARK 900  NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH LYS
REMARK 900   432 REPLACED BY ASN) (K432N)
REMARK 900 RELATED ID: 7NN9   RELATED DB: PDB
REMARK 900  NATIVE INFLUENZA VIRUS NEURAMINIDASE SUBTYPE
REMARK 900  N9 (TERN)
DBREF  2C4A A   82   468  UNP    P03472   NRAM_IATRA      83    470
SEQRES   1 A  388  ARG ASP PHE ASN ASN LEU THR LYS GLY LEU CYS THR ILE
SEQRES   2 A  388  ASN SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL ARG
SEQRES   3 A  388  ILE GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLU PRO
SEQRES   4 A  388  TYR VAL SER CYS ASP PRO ASP GLU CYS ARG PHE TYR ALA
SEQRES   5 A  388  LEU SER GLN GLY THR THR ILE ARG GLY LYS HIS SER ASN
SEQRES   6 A  388  GLY THR ILE HIS ASP ARG SER GLN TYR ARG ALA LEU ILE
SEQRES   7 A  388  SER TRP PRO LEU SER SER PRO PRO THR VAL TYR ASN SER
SEQRES   8 A  388  ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS
SEQRES   9 A  388  ASP GLY LYS THR ARG MET SER ILE CYS ILE SER GLY PRO
SEQRES  10 A  388  ASN ASN ASN ALA SER ALA VAL ILE TRP TYR ASN ARG ARG
SEQRES  11 A  388  PRO VAL THR GLU ILE ASN THR TRP ALA ARG ASN ILE LEU
SEQRES  12 A  388  ARG THR GLN GLU SER GLU CYS VAL CYS HIS ASN GLY VAL
SEQRES  13 A  388  CYS PRO VAL VAL PHE THR ASP GLY SER ALA THR GLY PRO
SEQRES  14 A  388  ALA GLU THR ARG ILE TYR TYR PHE LYS GLU GLY LYS ILE
SEQRES  15 A  388  LEU LYS TRP GLU PRO LEU ALA GLY THR ALA LYS HIS ILE
SEQRES  16 A  388  GLU GLU CYS SER CYS TYR GLY GLU ARG ALA GLU ILE THR
SEQRES  17 A  388  CYS THR CYS ARG ASP ASN TRP GLN GLY SER ASN ARG PRO
SEQRES  18 A  388  VAL ILE ARG ILE ASP PRO VAL ALA MET THR HIS THR SER
SEQRES  19 A  388  GLN TYR ILE CYS SER PRO VAL LEU THR ASP ASN PRO ARG
SEQRES  20 A  388  PRO ASN ASP PRO THR VAL GLY LYS CYS ASN ASP PRO TYR
SEQRES  21 A  388  PRO GLY ASN ASN ASN ASN GLY VAL LYS GLY PHE SER TYR
SEQRES  22 A  388  LEU ASP GLY VAL ASN THR TRP LEU GLY ARG THR ILE SER
SEQRES  23 A  388  ILE ALA SER ARG SER GLY TYR GLU MET LEU LYS VAL PRO
SEQRES  24 A  388  ASN ALA LEU THR ASP ASP LYS SER LYS PRO THR GLN GLY
SEQRES  25 A  388  GLN THR ILE VAL LEU ASN THR ASP TRP SER GLY TYR SER
SEQRES  26 A  388  GLY SER PHE MET ASP TYR TRP ALA GLU GLY GLU CYS TYR
SEQRES  27 A  388  ARG ALA CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG PRO
SEQRES  28 A  388  LYS GLU ASP LYS VAL TRP TRP THR SER ASN SER ILE VAL
SEQRES  29 A  388  SER MET CYS SER SER THR GLU PHE LEU GLY GLN TRP ASP
SEQRES  30 A  388  TRP PRO ASP GLY ALA LYS ILE GLU TYR PHE LEU
HET    SIA  A1469      21
HET    SIA  A1470      21
HET    NAG  A1471      14
HET    NAG  A1472      14
HET    NAG  A1473      14
HET    NAG  A1474      14
HET    NAG  A1475      14
HET    BMA  A1476      11
HET    MAN  A1477      11
HET    MAN  A1478      11
HET    MAN  A1479      11
HET    MAN  A1480      11
HET    MAN  A1481      11
HET    MAN  A1482      11
HET     CA  A1483       1
HETNAM     SIA O-SIALIC ACID
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM      CA CALCIUM ION
HETSYN     NAG NAG
FORMUL   2  SIA    2(C11 H19 N O9)
FORMUL   4  NAG    5(C8 H15 N O6)
FORMUL   9  BMA    C6 H12 O6
FORMUL  10  MAN    6(C6 H12 O6)
FORMUL  16   CA    CA 2+
FORMUL  17  HOH   *259(H2 O1)
HELIX    1   1 ASN A  104  GLU A  110  1                                   7
HELIX    2   2 GLY A  142  ASN A  146  5                                   5
HELIX    3   3 LYS A  463  LEU A  468  5                                   6
SHEET    1  AA 2 GLY A  90  LEU A  91  0
SHEET    2  AA 2 CYS A 417  TYR A 418  1  N  TYR A 418   O  GLY A  90
SHEET    1  AB 4 SER A  96  LYS A 102  0
SHEET    2  AB 4 THR A 439  SER A 449 -1  O  SER A 445   N  TYR A 100
SHEET    3  AB 4 CYS A 421  GLY A 429 -1  O  PHE A 422   N  MET A 446
SHEET    4  AB 4 SER A 407  PHE A 410 -1  O  GLY A 408   N  TYR A 423
SHEET    1  AC 4 LEU A 115  CYS A 124  0
SHEET    2  AC 4 CYS A 129  THR A 139 -1  O  ARG A 130   N  SER A 123
SHEET    3  AC 4 ALA A 157  PRO A 162 -1  O  ALA A 157   N  SER A 135
SHEET    4  AC 4 ARG A 172  ILE A 176 -1  O  ARG A 172   N  SER A 160
SHEET    1  AD 4 SER A 179  HIS A 184  0
SHEET    2  AD 4 ARG A 189  SER A 195 -1  O  MET A 190   N  CYS A 183
SHEET    3  AD 4 SER A 202  TYR A 207 -1  O  SER A 202   N  SER A 195
SHEET    4  AD 4 ARG A 210  ASN A 216 -1  O  ARG A 210   N  TYR A 207
SHEET    1  AE 3 VAL A 236  GLY A 244  0
SHEET    2  AE 3 ALA A 250  LYS A 258 -1  O  GLU A 251   N  ASP A 243
SHEET    3  AE 3 LYS A 261  PRO A 267 -1  O  LYS A 261   N  LYS A 258
SHEET    1  AF 4 GLU A 276  GLU A 283  0
SHEET    2  AF 4 GLU A 286  ARG A 292 -1  O  GLU A 286   N  GLU A 283
SHEET    3  AF 4 PRO A 301  ASP A 306 -1  O  PRO A 301   N  CYS A 291
SHEET    4  AF 4 THR A 311  TYR A 316 -1  O  THR A 311   N  ASP A 306
SHEET    1  AG 4 SER A 353  TYR A 354  0
SHEET    2  AG 4 TRP A 361  ARG A 364 -1  O  TRP A 361   N  TYR A 354
SHEET    3  AG 4 SER A 372  LYS A 378 -1  O  GLU A 375   N  ARG A 364
SHEET    4  AG 4 GLN A 392  TRP A 403 -1  O  GLN A 392   N  LYS A 378
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.05
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.06
SSBOND   3 CYS A  175    CYS A  193                          1555   1555  2.05
SSBOND   4 CYS A  183    CYS A  230                          1555   1555  2.05
SSBOND   5 CYS A  232    CYS A  237                          1555   1555  2.03
SSBOND   6 CYS A  278    CYS A  291                          1555   1555  2.06
SSBOND   7 CYS A  280    CYS A  289                          1555   1555  2.07
SSBOND   8 CYS A  318    CYS A  337                          1555   1555  2.05
SSBOND   9 CYS A  421    CYS A  447                          1555   1555  2.08
LINK         ND2 ASN A  86                 C1  NAG A1473     1555   1555  1.62
LINK         ND2 ASN A  86                 O5  NAG A1473     1555   1555  2.17
LINK         ND2 ASN A 146                 C1  NAG A1475     1555   1555  1.90
LINK         ND2 ASN A 200                 C1  NAG A1471     1555   1555  1.73
LINK         O4  NAG A1471                 C1  NAG A1472     1555   1555  1.61
LINK         O4  NAG A1472                 C1  BMA A1476     1555   1555  1.70
LINK         O4  NAG A1473                 C1  NAG A1474     1555   1555  1.88
LINK         O3  BMA A1476                 C1  MAN A1477     1555   1555  1.68
LINK         O6  BMA A1476                 C1  MAN A1480     1555   1555  1.91
LINK         O2  MAN A1477                 C1  MAN A1478     1555   1555  1.59
LINK         O2  MAN A1478                 C1  MAN A1479     1555   1555  1.75
LINK         O6  MAN A1480                 C1  MAN A1481     1555   1555  2.16
LINK         O3  MAN A1480                 C1  MAN A1482     1555   1555  2.24
LINK        CA    CA A1483                 O   HOH A2157     1555   1555  2.88
LINK        CA    CA A1483                 O   ASP A 293     1555   1555  2.58
LINK        CA    CA A1483                 O   ASN A 347     1555   1555  2.66
LINK        CA    CA A1483                 O   HOH A2168     1555   1555  2.84
LINK        CA    CA A1483                 O   GLY A 297     1555   1555  2.61
LINK        CA    CA A1483                 OD2 ASP A 324     1555   1555  2.75
CISPEP   1 ASN A  325    PRO A  326          0        -7.94
CISPEP   2 ARG A  430    PRO A  431          0         0.56
SITE     1 AC1 17 ARG A 118  GLU A 119  ASP A 151  ARG A 152
SITE     2 AC1 17 ILE A 222  ARG A 224  ALA A 246  GLU A 276
SITE     3 AC1 17 GLU A 277  ARG A 292  ARG A 371  TYR A 406
SITE     4 AC1 17 HOH A2064  HOH A2094  HOH A2242  HOH A2243
SITE     5 AC1 17 HOH A2244
SITE     1 AC2 10 SER A 367  SER A 370  SER A 372  ASN A 400
SITE     2 AC2 10 THR A 401  ASP A 402  TRP A 403  LYS A 432
SITE     3 AC2 10 HOH A2245  HOH A2246
SITE     1 AC3  8 ASN A 200  LEU A 453  GLY A 454  GLN A 455
SITE     2 AC3  8 NAG A1472  HOH A2230  HOH A2247  HOH A2248
SITE     1 AC4  9 GLN A 392  GLY A 394  GLN A 455  NAG A1471
SITE     2 AC4  9 BMA A1476  HOH A2191  HOH A2247  HOH A2249
SITE     3 AC4  9 HOH A2259
SITE     1 AC5  6 ASP A  83  PHE A  84  ASN A  86  ASN A 234
SITE     2 AC5  6 NAG A1474  HOH A2102
SITE     1 AC6  4 ASP A  83  NAG A1473  HOH A2250  HOH A2251
SITE     1 AC7  6 ASN A 146  TRP A 437  HOH A2042  HOH A2252
SITE     2 AC7  6 HOH A2253  HOH A2254
SITE     1 AC8  8 LEU A 377  THR A 391  GLN A 392  GLY A 394
SITE     2 AC8  8 NAG A1472  MAN A1477  MAN A1480  HOH A2259
SITE     1 AC9  7 ARG A 364  GLU A 375  BMA A1476  MAN A1478
SITE     2 AC9  7 MAN A1479  HOH A2255  HOH A2256
SITE     1 BC1  7 ASP A 330  ARG A 364  LYS A 389  PRO A 390
SITE     2 BC1  7 MAN A1477  MAN A1479  HOH A2257
SITE     1 BC2 11 ARG A 327  ASN A 329  ASP A 330  ARG A 364
SITE     2 BC2 11 ILE A 366  ILE A 368  MAN A1477  MAN A1478
SITE     3 BC2 11 HOH A2160  HOH A2256  HOH A2258
SITE     1 BC3  4 PRO A 390  BMA A1476  MAN A1481  MAN A1482
SITE     1 BC4  1 MAN A1480
SITE     1 BC5  2 MAN A1480  HOH A2259
SITE     1 BC6  6 ASP A 293  GLY A 297  ASP A 324  ASN A 347
SITE     2 BC6  6 HOH A2157  HOH A2168
CRYST1  181.336  181.336  181.336  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      0.005515  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005515  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005515        0.00000
      
PROCHECK
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 References