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HEADER HYDROLASE 15-MAR-02 1L7G TITLE CRYSTAL STRUCTURE OF E119G MUTANT INFLUENZA VIRUS TITLE 2 NEURAMINIDASE IN COMPLEX WITH BCX-1812 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: INTEGRAL MEMBRANE PROTEIN, MEMBRANE STALK COMPND 5 CLEAVED BY PRONASE RELEASING FULLY ACTIVE RESIDUES 82-468; COMPND 6 EC: 3.2.1.18; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: AVIAN INFLUENZA VIRUS; SOURCE 3 STRAIN: A/NWS/TERN/AUSTRALIA/G70C/75 KEYWDS NEURAMINIDASE, HYDROLASE, INFLUENZA, GLYCOSYLATED PROTEIN, KEYWDS 2 BCX-1812, E119G MUTANT EXPDTA X-RAY DIFFRACTION AUTHOR B.J.SMITH,J.L.MCKIMM-BRESHKIN,M.MCDONALD,R.T.FERNLEY, AUTHOR 2 J.N.VARGHESE,P.M.COLMAN REVDAT 2 01-APR-03 1L7G 1 JRNL REVDAT 1 29-MAY-02 1L7G 0 JRNL AUTH B.J.SMITH,J.L.MCKIMM-BRESHKIN,M.MCDONALD, JRNL AUTH 2 R.T.FERNLEY,J.N.VARGHESE,P.M.COLMAN JRNL TITL STRUCTURAL STUDIES OF THE RESISTANCE OF INFLUENZA JRNL TITL 2 VIRUS NEURAMINDASE TO INHIBITORS. JRNL REF J.MED.CHEM. V. 45 2207 2002 JRNL REFN ASTM JMCMAR US ISSN 0022-2623 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.85 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 41542 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.148 REMARK 3 FREE R VALUE : 0.168 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2092 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3085 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 150 REMARK 3 SOLVENT ATOMS : 591 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.008 ; NULL REMARK 3 ANGLE DISTANCE (A) : 0.026 ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1L7G COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB015710. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 113.0 REMARK 200 PH : 5.90 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : MACSCIENCE REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : ELLIPTICAL GLASS MONOCAPILLARY REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43185 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 26.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.76000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE, PH 5.9, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K 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 1/2+X,1/2+Y,1/2+Z REMARK 290 26555 1/2-X,1/2-Y,1/2+Z REMARK 290 27555 1/2-X,1/2+Y,1/2-Z REMARK 290 28555 1/2+X,1/2-Y,1/2-Z REMARK 290 29555 1/2+Z,1/2+X,1/2+Y REMARK 290 30555 1/2+Z,1/2-X,1/2-Y REMARK 290 31555 1/2-Z,1/2-X,1/2+Y REMARK 290 32555 1/2-Z,1/2+X,1/2-Y REMARK 290 33555 1/2+Y,1/2+Z,1/2+X REMARK 290 34555 1/2-Y,1/2+Z,1/2-X REMARK 290 35555 1/2+Y,1/2-Z,1/2-X REMARK 290 36555 1/2-Y,1/2-Z,1/2+X REMARK 290 37555 1/2+Y,1/2+X,1/2-Z REMARK 290 38555 1/2-Y,1/2-X,1/2-Z REMARK 290 39555 1/2+Y,1/2-X,1/2+Z REMARK 290 40555 1/2-Y,1/2+X,1/2+Z REMARK 290 41555 1/2+X,1/2+Z,1/2-Y REMARK 290 42555 1/2-X,1/2+Z,1/2+Y REMARK 290 43555 1/2-X,1/2-Z,1/2-Y REMARK 290 44555 1/2+X,1/2-Z,1/2+Y REMARK 290 45555 1/2+Z,1/2+Y,1/2-X REMARK 290 46555 1/2+Z,1/2-Y,1/2+X REMARK 290 47555 1/2-Z,1/2+Y,1/2+X REMARK 290 48555 1/2-Z,1/2-Y,1/2-X 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 90.37500 REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 90.37500 REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 90.37500 REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 90.37500 REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 90.37500 REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 90.37500 REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 90.37500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). 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 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 CA CA 998 LIES ON A SPECIAL POSITION. REMARK 375 HOH 573 LIES ON A SPECIAL POSITION. 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ARG A 172 CD ARG A 172 NE -0.077 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 172 CG - CD - NE ANGL. DEV. = 16.2 DEGREES REMARK 500 ARG A 172 CD - NE - CZ ANGL. DEV. = 54.7 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1L7F RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF INFLUENZA VIRUS NEURAMINIDASE IN REMARK 900 COMPLEX WITH BCX-1812 REMARK 900 RELATED ID: 1L7H RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF R292K MUTANT INFLUENZA VIRUS REMARK 900 NEURAMINIDASE IN COMPLEX WITH BCX-1812 DBREF 1L7G A 82 468 UNP P03472 NRAM_IATRA 83 470 SEQADV 1L7G GLY A 119 UNP P03472 GLU 120 ENGINEERED SEQRES 1 A 388 ARG ASP PHE ASN ASN LEU THR LYS GLY LEU CYS THR ILE SEQRES 2 A 388 ASN SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL ARG SEQRES 3 A 388 ILE GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLY 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 MODRES 1L7G ASN A 86 ASN GLYCOSYLATION SITE MODRES 1L7G ASN A 146 ASN GLYCOSYLATION SITE MODRES 1L7G ASN A 200 ASN GLYCOSYLATION SITE HET NAG B1200 14 HET NAG B1201 14 HET BMA B1202 11 HET MAN B1203 11 HET MAN B1204 11 HET MAN B1205 11 HET MAN B1206 11 HET NAG C1086 14 HET NAG C1087 14 HET NAG A1146 14 HET CA 999 1 HET CA 998 1 HET BCZ 801 23 HET GOL 701 6 HET GOL 702 6 HET GOL 703 6 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM CA CALCIUM ION HETNAM BCZ 3-(1-ACETYLAMINO-2-ETHYL-BUTYL)-4-GUANIDINO-2-HYDROXY- HETNAM 2 BCZ CYCLOPENTANECARBOXYLIC ACID HETNAM GOL GLYCEROL HETSYN NAG NAG HETSYN BCZ BCX-1812 FORMUL 2 NAG 5(C8 H15 N O6) FORMUL 2 BMA C6 H12 O6 FORMUL 2 MAN 4(C6 H12 O6) FORMUL 5 CA 2(CA 2+) FORMUL 7 BCZ C15 H28 N4 O4 FORMUL 8 GOL 3(C3 H8 O3) FORMUL 11 HOH *573(H2 O) 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 A 4 SER A 96 LYS A 102 0 SHEET 2 A 4 THR A 439 SER A 449 -1 O CYS A 447 N HIS A 98 SHEET 3 A 4 CYS A 421 GLY A 429 -1 N VAL A 424 O VAL A 444 SHEET 4 A 4 SER A 407 PHE A 410 -1 N GLY A 408 O TYR A 423 SHEET 1 B 4 LEU A 115 ASP A 125 0 SHEET 2 B 4 GLU A 128 THR A 139 -1 O GLU A 128 N ASP A 125 SHEET 3 B 4 ALA A 157 PRO A 162 -1 O ALA A 157 N SER A 135 SHEET 4 B 4 ARG A 172 ILE A 176 -1 O ARG A 172 N SER A 160 SHEET 1 C 4 SER A 179 HIS A 184 0 SHEET 2 C 4 ARG A 189 SER A 195 -1 O MET A 190 N CYS A 183 SHEET 3 C 4 SER A 202 TYR A 207 -1 O TRP A 206 N SER A 191 SHEET 4 C 4 ARG A 210 ASN A 216 -1 O THR A 213 N ILE A 205 SHEET 1 D 4 ARG A 224 THR A 225 0 SHEET 2 D 4 CYS A 237 GLY A 244 -1 O THR A 242 N ARG A 224 SHEET 3 D 4 ALA A 250 LYS A 258 -1 O PHE A 257 N CYS A 237 SHEET 4 D 4 LYS A 261 PRO A 267 -1 O GLU A 266 N ILE A 254 SHEET 1 E 4 SER A 279 GLU A 283 0 SHEET 2 E 4 GLU A 286 THR A 290 -1 O THR A 290 N SER A 279 SHEET 3 E 4 PRO A 301 ASP A 306 -1 O ILE A 305 N ILE A 287 SHEET 4 E 4 THR A 311 TYR A 316 -1 O GLN A 315 N VAL A 302 SHEET 1 F 4 SER A 353 TYR A 354 0 SHEET 2 F 4 TRP A 361 ARG A 364 -1 O TRP A 361 N TYR A 354 SHEET 3 F 4 SER A 372 LYS A 378 -1 O LEU A 377 N LEU A 362 SHEET 4 F 4 GLN A 392 TRP A 403 -1 O GLN A 395 N MET A 376 SSBOND 1 CYS A 92 CYS A 417 SSBOND 2 CYS A 124 CYS A 129 SSBOND 3 CYS A 175 CYS A 193 SSBOND 4 CYS A 183 CYS A 230 SSBOND 5 CYS A 232 CYS A 237 SSBOND 6 CYS A 278 CYS A 291 SSBOND 7 CYS A 280 CYS A 289 SSBOND 8 CYS A 318 CYS A 337 SSBOND 9 CYS A 421 CYS A 447 LINK ND2 ASN A 86 C1 NAG C1086 LINK ND2 ASN A 146 C1 NAG A1146 LINK ND2 ASN A 200 C1 NAG B1200 LINK O4 NAG B1200 C1 NAG B1201 LINK O4 NAG B1201 C1 BMA B1202 LINK O3 BMA B1202 C1 MAN B1203 LINK O6 BMA B1202 C1 MAN B1206 LINK O2 MAN B1203 C1 MAN B1204 LINK O2 MAN B1204 C1 MAN B1205 LINK O4 NAG C1086 C1 NAG C1087 CISPEP 1 ASN A 325 PRO A 326 0 -4.80 CISPEP 2 ARG A 430 PRO A 431 0 0.84 CRYST1 180.750 180.750 180.750 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 0.005533 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005533 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005533 0.00000