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HEADER HYDROLASE/HYDROLASE INHIBITOR 30-JUN-00 1F8C TITLE NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH 4-AMINO-2- TITLE 2 DEOXY-2,3-DEHYDRO-N-NEURAMINIC ACID 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 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_COMMON: VIRUS; SOURCE 4 STRAIN: A/TERN/AUSTRALIA/G70C/75; SOURCE 5 EXPRESSION_SYSTEM: INFLUENZA A VIRUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: VIRUS; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: RECOMBINANT (NWS/G70C) N9 KEYWDS NEURAMINIDASE, HYDROLASE, INFLUENZA PROTEIN, GLYCOSYLATED KEYWDS 2 PROTEIN, 4-AMINO-DANA EXPDTA X-RAY DIFFRACTION AUTHOR B.J.SMITH,P.M.COLMAN,M.VON ITZSTEIN,B.DANYLEC,J.N.VARGHESE REVDAT 1 11-APR-01 1F8C 0 JRNL AUTH B.J.SMITH,P.M.COLMAN,M.VON ITZSTEIN,B.DANYLEC, JRNL AUTH 2 J.N.VARGHESE JRNL TITL ANALYSIS OF INHIBITOR BINDING IN INFLUENZA VIRUS JRNL TITL 2 NEURAMINIDASE. JRNL REF PROTEIN SCI. V. 10 689 2001 JRNL REFN ASTM PRCIEI US ISSN 0961-8368 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 46543 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 SET) : 0.178 REMARK 3 FREE R VALUE : 0.216 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2328 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3069 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 147 REMARK 3 SOLVENT ATOMS : 368 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) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.78 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1F8C 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 RCSB011367. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-1996 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 : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47677 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 100.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 86.1 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.09600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 REMARK 200 COMPLETENESS FOR SHELL (%) : 33.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.55000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.43 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 20K 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 90.49000 REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 90.49000 REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 90.49000 REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 90.49000 REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 90.49000 REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 90.49000 REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 90.49000 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, X, Y 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 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 THR A 225 CA THR A 225 CB 0.062 REMARK 500 MET A 446 SD MET A 446 CE -0.067 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 ASP A 125 N - CA - C ANGL. DEV. =-12.8 DEGREES REMARK 500 ASP A 151 N - CA - C ANGL. DEV. = 10.9 DEGREES REMARK 500 GLN A 226 N - CA - C ANGL. DEV. = 12.4 DEGREES REMARK 500 GLY A 297 N - CA - C ANGL. DEV. = 10.5 DEGREES REMARK 500 ASN A 299 N - CA - C ANGL. DEV. =-12.2 DEGREES REMARK 500 THR A 323 N - CA - C ANGL. DEV. = 10.2 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 8119 DISTANCE = 6.45 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7NN9 RELATED DB: PDB REMARK 900 THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX OF 4-GUANIDINO- REMARK 900 NEU5AC2EN AND INFLUENZA VIRUS NEURAMINIDASE PROTEIN REMARK 900 SCIENCE(1995),4:1081-1087 J.N. VARGHESE, V.C. EPA, P.M. REMARK 900 COLMAN DBREF 1F8C A 82 468 GB 324880 AAA43574 83 470 SEQADV 1F8C MET A 376 GB 324880 ILE 377 CONFLICT SEQADV 1F8C ASP A 386 GB 324880 GLU 387 CONFLICT SEQADV 1F8C LYS A 387 GB 324880 ARG 388 CONFLICT 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 MODRES 1F8C ASN A 86 ASN GLYCOSYLATION SITE MODRES 1F8C ASN A 200 ASN GLYCOSYLATION SITE MODRES 1F8C ASN A 146 ASN GLYCOSYLATION SITE HET NAG X 201 14 HET NAG X 202 14 HET MAN X 203 11 HET MAN X 204 11 HET MAN X 205 11 HET MAN X 206 11 HET MAN X 207 11 HET NAG Y 86 14 HET NAG Y 87 14 HET NAG A1146 14 HET CA 999 1 HET CA 998 1 HET 4AM 4 20 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MAN ALPHA-D-MANNOSE HETNAM CA CALCIUM ION HETNAM 4AM 4-AMINO-2-DEOXY-2,3-DEHYDRO-N-NEURAMINIC ACID HETSYN NAG NAG FORMUL 2 NAG 5(C8 H15 N O6) FORMUL 2 MAN 5(C6 H12 O6) FORMUL 6 CA 2(CA 2+) FORMUL 8 4AM C11 H18 N2 O7 FORMUL 9 HOH *367(H2 O) HELIX 1 1 ASN A 104 GLY A 109 1 6 HELIX 2 2 GLU A 110 SER A 112 5 3 HELIX 3 3 GLY A 142 ASN A 146 5 5 HELIX 4 4 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 SER A 445 N TYR A 100 SHEET 3 A 4 CYS A 421 GLY A 429 -1 N PHE A 422 O MET A 446 SHEET 4 A 4 SER A 407 PHE A 410 -1 O GLY A 408 N TYR A 423 SHEET 1 B 4 TYR A 121 ASP A 125 0 SHEET 2 B 4 GLU A 128 SER A 135 -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 N ARG A 172 O 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 N MET A 190 O CYS A 183 SHEET 3 C 4 SER A 202 TYR A 207 -1 N SER A 202 O SER A 195 SHEET 4 C 4 ARG A 210 ASN A 216 -1 O ARG A 210 N TYR A 207 SHEET 1 D 3 VAL A 236 GLY A 244 0 SHEET 2 D 3 ALA A 250 LYS A 258 -1 N GLU A 251 O ASP A 243 SHEET 3 D 3 LYS A 261 PRO A 267 -1 O LYS A 261 N LYS A 258 SHEET 1 E 4 GLU A 276 GLU A 283 0 SHEET 2 E 4 GLU A 286 ARG A 292 -1 O GLU A 286 N GLU A 283 SHEET 3 E 4 PRO A 301 ASP A 306 -1 O PRO A 301 N CYS A 291 SHEET 4 E 4 THR A 311 TYR A 316 -1 O THR A 311 N ASP A 306 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 N GLU A 375 O ARG A 364 SHEET 4 F 4 GLN A 392 TRP A 403 -1 O GLN A 392 N LYS A 378 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 C1 MAN X 204 O3 MAN X 203 LINK O4 NAG X 202 C1 MAN X 203 LINK C1 MAN X 205 O2 MAN X 204 LINK O2 MAN X 205 C1 MAN X 206 LINK ND2 ASN A 86 C1 NAG Y 86 LINK ND2 ASN A 200 C1 NAG X 201 LINK O4 NAG X 201 C1 NAG X 202 LINK ND2 ASN A 146 C1 NAG A1146 LINK C1 MAN X 207 O6 MAN X 203 CISPEP 1 ASN A 325 PRO A 326 0 -0.58 CISPEP 2 ARG A 430 PRO A 431 0 0.37 CRYST1 180.980 180.980 180.980 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 0.005525 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005525 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005525 0.00000