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HEADER HYDROLASE 30-OCT-03 1V3E TITLE STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE FROM HUMAN TITLE 2 PARAINFLUENZA VIRUS TYPE III: COMPLEX WITH ZANAMAVIR COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RESIDUES 142-572; COMPND 5 SYNONYM: HEMAGGLUTININ-NEURAMINIDASE, HN; COMPND 6 EC: 3.2.1.18; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN PARAINFLUENZA VIRUS 3; SOURCE 3 ORGANISM_COMMON: VIRUSES; SOURCE 4 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 5 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS PIV3 HN, NATIVE+ZANAMAVIR, HEXAGONAL EXPDTA X-RAY DIFFRACTION AUTHOR M.C.LAWRENCE,N.A.BORG,V.A.STRELTSOV,P.A.PILLING,V.C.EPA, AUTHOR 2 J.N.VARGHESE,J.L.MCKIMM-BRESCHKIN,P.M.COLMAN REVDAT 1 03-FEB-04 1V3E 0 JRNL AUTH M.C.LAWRENCE,N.A.BORG,V.A.STRELTSOV,P.A.PILLING, JRNL AUTH 2 V.C.EPA,J.N.VARGHESE,J.L.MCKIMM-BRESCHKIN, JRNL AUTH 3 P.M.COLMAN JRNL TITL STRUCTURE OF THE HAEMAGGLUTININ-NEURAMINIDASE FROM JRNL TITL 2 HUMAN PARAINFLUENZA VIRUS TYPE III JRNL REF J.MOL.BIOL. V. 335 1343 2004 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.89 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4827515.570 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 120373 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 SET) : 0.184 REMARK 3 FREE R VALUE : 0.219 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300 REMARK 3 FREE R VALUE TEST SET COUNT : 6391 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.89 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 16960 REMARK 3 BIN R VALUE (WORKING SET) : 0.2650 REMARK 3 BIN FREE R VALUE : 0.2950 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.70 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1225 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6766 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 156 REMARK 3 SOLVENT ATOMS : 999 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.14000 REMARK 3 B22 (A**2) : 2.14000 REMARK 3 B33 (A**2) : -4.29000 REMARK 3 B12 (A**2) : 1.55000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21 REMARK 3 ESD FROM SIGMAA (A) : 0.20 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.019 REMARK 3 BOND ANGLES (DEGREES) : 2.00 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.21 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.36 REMARK 3 BSOL : 62.60 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : ZAN.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : ION.PARAM REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM REMARK 3 PARAMETER FILE 6 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : ZAN.TOP REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : ION.TOP REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP REMARK 3 TOPOLOGY FILE 6 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1V3E 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB006155. 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 : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; N REMARK 200 RADIATION SOURCE : APS; ROTATING ANODE REMARK 200 BEAMLINE : 14-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU-MSC REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00; 1.5418 REMARK 200 MONOCHROMATOR : DIAMOND 111; NI FILTER REMARK 200 OPTICS : AXCO MICROCAPILLARY FOCUSING REMARK 200 OPTICS REMARK 200 REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; RIGAKU RAXIS IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120414 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890 REMARK 200 RESOLUTION RANGE LOW (A) : 190.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 14.600 REMARK 200 R MERGE (I) : 0.14600 REMARK 200 R SYM (I) : 0.14600 REMARK 200 FOR THE DATA SET : 26.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 8.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: PIV3 HN MONOMER FROM HEXAGONAL STRUCTURE ENTRY REMARK 200 1V3B REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM AND LITHIUM PHOSPHATE, REMARK 280 HEPES, PH 7.50, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,2/3+Z REMARK 290 3555 -X+Y,-X,1/3+Z REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,2/3+Z REMARK 290 6555 X-Y,X,1/3+Z REMARK 290 7555 Y,X,2/3-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,1/3-Z REMARK 290 10555 -Y,-X,2/3-Z REMARK 290 11555 -X+Y,Y,-Z REMARK 290 12555 X,X-Y,1/3-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.26933 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.63467 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 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 73.26933 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.63467 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 73.26933 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 36.63467 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 73.26933 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.63467 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 2 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, D 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 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 HOH 280 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 REMARK 500 OG SER A 195 O HOH 436 1.73 REMARK 500 O HOH 76 O HOH 993 1.86 REMARK 500 O HOH 974 O HOH 999 1.86 REMARK 500 O HOH 981 O HOH 986 1.89 REMARK 500 O HOH 262 O HOH 986 1.90 REMARK 500 O HOH 973 O HOH 999 1.90 REMARK 500 O HOH 797 O HOH 988 1.91 REMARK 500 O HOH 974 O HOH 983 1.96 REMARK 500 O HOH 800 O HOH 995 1.97 REMARK 500 O HOH 888 O HOH 988 2.00 REMARK 500 OE1 GLU A 462 O HOH 992 2.02 REMARK 500 O HOH 32 O HOH 988 2.05 REMARK 500 O HOH 461 O HOH 999 2.05 REMARK 500 O HOH 76 O HOH 992 2.09 REMARK 500 O HOH 980 O HOH 986 2.11 REMARK 500 O HOH 984 O HOH 989 2.11 REMARK 500 O HOH 797 O HOH 984 2.13 REMARK 500 O HOH 262 O HOH 981 2.14 REMARK 500 ND2 ASN A 556 O HOH 950 2.15 REMARK 500 O HOH 983 O HOH 999 2.16 REMARK 500 O HOH 461 O HOH 974 2.18 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD2 ASP B 296 OD2 ASP B 296 10665 1.51 REMARK 500 O HOH 904 O HOH 904 10665 1.86 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 MET A 183 SD MET A 183 CE 0.177 REMARK 500 ILE A 226 CG1 ILE A 226 CD1 0.143 REMARK 500 MET A 377 SD MET A 377 CE 0.136 REMARK 500 MET B 175 SD MET B 175 CE -0.376 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 LEU A 261 N - CA - C ANGL. DEV. =-12.0 DEGREES REMARK 500 LEU A 496 N - CA - C ANGL. DEV. =-12.5 DEGREES REMARK 500 TYR A 509 N - CA - C ANGL. DEV. =-12.1 DEGREES REMARK 500 ARG A 515 CB - CG - CD ANGL. DEV. =-12.5 DEGREES REMARK 500 HIS A 552 N - CA - C ANGL. DEV. =-13.7 DEGREES REMARK 500 ASN B 347 N - CA - C ANGL. DEV. =-12.9 DEGREES REMARK 500 LEU B 496 N - CA - C ANGL. DEV. =-15.1 DEGREES REMARK 500 HIS B 538 N - CA - C ANGL. DEV. =-14.6 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 262 -114.89 51.86 REMARK 500 VAL A 322 -53.24 76.55 REMARK 500 ASN A 540 -32.32 85.18 REMARK 500 ASN B 262 -113.82 59.30 REMARK 500 VAL B 322 -56.20 76.93 REMARK 500 LEU B 522 -101.54 -152.33 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 960 DISTANCE = 5.42 ANGSTROMS REMARK 525 HOH 971 DISTANCE = 5.24 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1V2I RELATED DB: PDB REMARK 900 THE SAME PROTEIN, ANOTHER CRYSTAL SYSTEM-ORTHORHOMBIC REMARK 900 RELATED ID: 1V3B RELATED DB: PDB REMARK 900 THE SAME PROTEIN REMARK 900 RELATED ID: 1V3C RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEX WITH NEU5AC REMARK 900 RELATED ID: 1V3D RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEX WITH NEU5AC2EN DBREF 1V3E A 142 572 GB 37958139 AAP35240 142 572 DBREF 1V3E B 142 572 GB 37958139 AAP35240 142 572 SEQRES 1 A 431 ILE THR HIS ASP VAL GLY ILE LYS PRO LEU ASN PRO ASP SEQRES 2 A 431 ASP PHE TRP ARG CYS THR SER GLY LEU PRO SER LEU MET SEQRES 3 A 431 LYS THR PRO LYS ILE ARG LEU MET PRO GLY PRO GLY LEU SEQRES 4 A 431 LEU ALA MET PRO THR THR VAL ASP GLY CYS ILE ARG THR SEQRES 5 A 431 PRO SER LEU VAL ILE ASN ASP LEU ILE TYR ALA TYR THR SEQRES 6 A 431 SER ASN LEU ILE THR ARG GLY CYS GLN ASP ILE GLY LYS SEQRES 7 A 431 SER TYR GLN VAL LEU GLN ILE GLY ILE ILE THR VAL ASN SEQRES 8 A 431 SER ASP LEU VAL PRO ASP LEU ASN PRO ARG ILE SER HIS SEQRES 9 A 431 THR PHE ASN ILE ASN ASP ASN ARG LYS SER CYS SER LEU SEQRES 10 A 431 ALA LEU LEU ASN THR ASP VAL TYR GLN LEU CYS SER THR SEQRES 11 A 431 PRO LYS VAL ASP GLU ARG SER ASP TYR ALA SER PRO GLY SEQRES 12 A 431 ILE GLU ASP ILE VAL LEU ASP ILE VAL ASN TYR ASP GLY SEQRES 13 A 431 SER ILE SER THR THR ARG PHE LYS ASN ASN ASN ILE SER SEQRES 14 A 431 PHE ASP GLN PRO TYR ALA ALA LEU TYR PRO SER VAL GLY SEQRES 15 A 431 PRO GLY ILE TYR TYR LYS GLY LYS ILE ILE PHE LEU GLY SEQRES 16 A 431 TYR GLY GLY LEU GLU HIS PRO ILE ASN GLU ASN VAL ILE SEQRES 17 A 431 CYS ASN THR THR GLY CYS PRO GLY LYS THR GLN ARG ASP SEQRES 18 A 431 CYS ASN GLN ALA SER HIS SER PRO TRP PHE SER ASP ARG SEQRES 19 A 431 ARG MET VAL ASN SER ILE ILE VAL VAL ASP LYS GLY LEU SEQRES 20 A 431 ASN SER ILE PRO LYS LEU LYS VAL TRP THR ILE SER MET SEQRES 21 A 431 ARG GLN ASN TYR TRP GLY SER GLU GLY ARG LEU LEU LEU SEQRES 22 A 431 LEU GLY ASN LYS ILE TYR ILE TYR THR ARG SER THR SER SEQRES 23 A 431 TRP HIS SER LYS LEU GLN LEU GLY ILE ILE ASP ILE THR SEQRES 24 A 431 ASP TYR SER ASP ILE ARG ILE LYS TRP THR TRP HIS ASN SEQRES 25 A 431 VAL LEU SER ARG PRO GLY ASN ASN GLU CYS PRO TRP GLY SEQRES 26 A 431 HIS SER CYS PRO ASP GLY CYS ILE THR GLY VAL TYR THR SEQRES 27 A 431 ASP ALA TYR PRO LEU ASN PRO THR GLY SER ILE VAL SER SEQRES 28 A 431 SER VAL ILE LEU ASP SER GLN LYS SER ARG VAL ASN PRO SEQRES 29 A 431 VAL ILE THR TYR SER THR ALA THR GLU ARG VAL ASN GLU SEQRES 30 A 431 LEU ALA ILE LEU ASN ARG THR LEU SER ALA GLY TYR THR SEQRES 31 A 431 THR THR SER CYS ILE THR HIS TYR ASN LYS GLY TYR CYS SEQRES 32 A 431 PHE HIS ILE VAL GLU ILE ASN HIS LYS SER LEU ASN THR SEQRES 33 A 431 LEU GLN PRO MET LEU PHE LYS THR GLU ILE PRO LYS SER SEQRES 34 A 431 CYS SER SEQRES 1 B 431 ILE THR HIS ASP VAL GLY ILE LYS PRO LEU ASN PRO ASP SEQRES 2 B 431 ASP PHE TRP ARG CYS THR SER GLY LEU PRO SER LEU MET SEQRES 3 B 431 LYS THR PRO LYS ILE ARG LEU MET PRO GLY PRO GLY LEU SEQRES 4 B 431 LEU ALA MET PRO THR THR VAL ASP GLY CYS ILE ARG THR SEQRES 5 B 431 PRO SER LEU VAL ILE ASN ASP LEU ILE TYR ALA TYR THR SEQRES 6 B 431 SER ASN LEU ILE THR ARG GLY CYS GLN ASP ILE GLY LYS SEQRES 7 B 431 SER TYR GLN VAL LEU GLN ILE GLY ILE ILE THR VAL ASN SEQRES 8 B 431 SER ASP LEU VAL PRO ASP LEU ASN PRO ARG ILE SER HIS SEQRES 9 B 431 THR PHE ASN ILE ASN ASP ASN ARG LYS SER CYS SER LEU SEQRES 10 B 431 ALA LEU LEU ASN THR ASP VAL TYR GLN LEU CYS SER THR SEQRES 11 B 431 PRO LYS VAL ASP GLU ARG SER ASP TYR ALA SER PRO GLY SEQRES 12 B 431 ILE GLU ASP ILE VAL LEU ASP ILE VAL ASN TYR ASP GLY SEQRES 13 B 431 SER ILE SER THR THR ARG PHE LYS ASN ASN ASN ILE SER SEQRES 14 B 431 PHE ASP GLN PRO TYR ALA ALA LEU TYR PRO SER VAL GLY SEQRES 15 B 431 PRO GLY ILE TYR TYR LYS GLY LYS ILE ILE PHE LEU GLY SEQRES 16 B 431 TYR GLY GLY LEU GLU HIS PRO ILE ASN GLU ASN VAL ILE SEQRES 17 B 431 CYS ASN THR THR GLY CYS PRO GLY LYS THR GLN ARG ASP SEQRES 18 B 431 CYS ASN GLN ALA SER HIS SER PRO TRP PHE SER ASP ARG SEQRES 19 B 431 ARG MET VAL ASN SER ILE ILE VAL VAL ASP LYS GLY LEU SEQRES 20 B 431 ASN SER ILE PRO LYS LEU LYS VAL TRP THR ILE SER MET SEQRES 21 B 431 ARG GLN ASN TYR TRP GLY SER GLU GLY ARG LEU LEU LEU SEQRES 22 B 431 LEU GLY ASN LYS ILE TYR ILE TYR THR ARG SER THR SER SEQRES 23 B 431 TRP HIS SER LYS LEU GLN LEU GLY ILE ILE ASP ILE THR SEQRES 24 B 431 ASP TYR SER ASP ILE ARG ILE LYS TRP THR TRP HIS ASN SEQRES 25 B 431 VAL LEU SER ARG PRO GLY ASN ASN GLU CYS PRO TRP GLY SEQRES 26 B 431 HIS SER CYS PRO ASP GLY CYS ILE THR GLY VAL TYR THR SEQRES 27 B 431 ASP ALA TYR PRO LEU ASN PRO THR GLY SER ILE VAL SER SEQRES 28 B 431 SER VAL ILE LEU ASP SER GLN LYS SER ARG VAL ASN PRO SEQRES 29 B 431 VAL ILE THR TYR SER THR ALA THR GLU ARG VAL ASN GLU SEQRES 30 B 431 LEU ALA ILE LEU ASN ARG THR LEU SER ALA GLY TYR THR SEQRES 31 B 431 THR THR SER CYS ILE THR HIS TYR ASN LYS GLY TYR CYS SEQRES 32 B 431 PHE HIS ILE VAL GLU ILE ASN HIS LYS SER LEU ASN THR SEQRES 33 B 431 LEU GLN PRO MET LEU PHE LYS THR GLU ILE PRO LYS SER SEQRES 34 B 431 CYS SER MODRES 1V3E ASN A 308 ASN GLYCOSYLATION SITE MODRES 1V3E ASN A 351 ASN GLYCOSYLATION SITE MODRES 1V3E ASN A 523 ASN GLYCOSYLATION SITE MODRES 1V3E ASN B 308 ASN GLYCOSYLATION SITE MODRES 1V3E ASN B 351 ASN GLYCOSYLATION SITE MODRES 1V3E ASN B 523 ASN GLYCOSYLATION SITE HET NAG A3081 14 HET NAG C3511 14 HET NAG C3512 14 HET NAG B3081 14 HET NAG D3511 14 HET NAG D3512 14 HET NAG B5231 14 HET CA 4001 1 HET CA 2001 1 HET SO4 3001 5 HET SO4 3002 5 HET ZMR 1200 23 HET ZMR 2200 23 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM CA CALCIUM ION HETNAM SO4 SULFATE ION HETNAM ZMR ZANAMIVIR HETSYN NAG NAG HETSYN ZMR MODIFIED SIALIC ACID FORMUL 3 NAG 7(C8 H15 N O6) FORMUL 8 CA 2(CA 2+) FORMUL 10 SO4 2(O4 S 2-) FORMUL 12 ZMR 2(C12 H20 N4 O7) FORMUL 14 HOH *999(H2 O) HELIX 1 1 ASN A 152 TRP A 157 1 6 HELIX 2 2 ASP A 275 SER A 282 1 8 HELIX 3 3 LYS A 305 ILE A 309 5 5 HELIX 4 4 THR A 359 SER A 367 1 9 HELIX 5 5 HIS A 368 HIS A 368 5 1 HELIX 6 6 SER A 369 SER A 373 5 5 HELIX 7 7 ASN B 152 TRP B 157 1 6 HELIX 8 8 ASP B 275 SER B 282 1 8 HELIX 9 9 LYS B 305 ILE B 309 5 5 HELIX 10 10 THR B 359 SER B 367 1 9 HELIX 11 11 HIS B 368 HIS B 368 5 1 HELIX 12 12 SER B 369 SER B 373 5 5 SHEET 1 A 4 ILE A 148 PRO A 150 0 SHEET 2 A 4 ALA A 528 HIS A 538 -1 O THR A 537 N LYS A 149 SHEET 3 A 4 LYS A 541 HIS A 552 -1 O ILE A 547 N THR A 532 SHEET 4 A 4 THR A 557 GLU A 566 -1 O THR A 557 N HIS A 552 SHEET 1 B 2 PRO A 164 LEU A 166 0 SHEET 2 B 2 LYS A 569 CYS A 571 -1 O SER A 570 N SER A 165 SHEET 1 C 4 CYS A 190 ILE A 198 0 SHEET 2 C 4 TYR A 203 ILE A 210 -1 O ASN A 208 N ARG A 192 SHEET 3 C 4 TYR A 221 VAL A 231 -1 O GLN A 225 N TYR A 205 SHEET 4 C 4 PRO A 237 PHE A 247 -1 O PHE A 247 N GLN A 222 SHEET 1 D 4 LYS A 254 LEU A 261 0 SHEET 2 D 4 ASP A 264 SER A 270 -1 O ASP A 264 N LEU A 261 SHEET 3 D 4 ILE A 288 VAL A 293 -1 O VAL A 289 N CYS A 269 SHEET 4 D 4 ILE A 299 PHE A 304 -1 O PHE A 304 N ILE A 288 SHEET 1 E 5 SER A 310 PHE A 311 0 SHEET 2 E 5 PRO A 392 THR A 398 1 O VAL A 396 N SER A 310 SHEET 3 E 5 MET A 377 LYS A 386 -1 N VAL A 383 O LYS A 395 SHEET 4 E 5 LYS A 331 LEU A 340 -1 N ILE A 332 O VAL A 384 SHEET 5 E 5 TYR A 315 PRO A 320 -1 N TYR A 319 O TYR A 337 SHEET 1 F 5 SER A 310 PHE A 311 0 SHEET 2 F 5 PRO A 392 THR A 398 1 O VAL A 396 N SER A 310 SHEET 3 F 5 MET A 377 LYS A 386 -1 N VAL A 383 O LYS A 395 SHEET 4 F 5 LYS A 331 LEU A 340 -1 N ILE A 332 O VAL A 384 SHEET 5 F 5 ILE A 326 TYR A 328 -1 N ILE A 326 O ILE A 333 SHEET 1 G 4 GLY A 410 LEU A 415 0 SHEET 2 G 4 LYS A 418 THR A 423 -1 O TYR A 420 N LEU A 413 SHEET 3 G 4 GLN A 433 ASP A 438 -1 O GLY A 435 N ILE A 421 SHEET 4 G 4 ARG A 446 TRP A 449 -1 O ARG A 446 N ASP A 438 SHEET 1 H 4 ALA A 481 PRO A 483 0 SHEET 2 H 4 VAL A 491 LEU A 496 -1 O SER A 492 N TYR A 482 SHEET 3 H 4 PRO A 505 SER A 510 -1 O THR A 508 N SER A 493 SHEET 4 H 4 ARG A 515 ALA A 520 -1 O LEU A 519 N ILE A 507 SHEET 1 I 4 ILE B 148 PRO B 150 0 SHEET 2 I 4 ALA B 528 HIS B 538 -1 O THR B 537 N LYS B 149 SHEET 3 I 4 LYS B 541 HIS B 552 -1 O LYS B 541 N HIS B 538 SHEET 4 I 4 THR B 557 GLU B 566 -1 O PHE B 563 N HIS B 546 SHEET 1 J 2 PRO B 164 LEU B 166 0 SHEET 2 J 2 LYS B 569 CYS B 571 -1 O SER B 570 N SER B 165 SHEET 1 K 4 CYS B 190 ILE B 198 0 SHEET 2 K 4 TYR B 203 ILE B 210 -1 O ASN B 208 N ARG B 192 SHEET 3 K 4 TYR B 221 VAL B 231 -1 O GLN B 225 N TYR B 205 SHEET 4 K 4 PRO B 237 PHE B 247 -1 O HIS B 245 N LEU B 224 SHEET 1 L 4 LYS B 254 LEU B 261 0 SHEET 2 L 4 ASP B 264 SER B 270 -1 O TYR B 266 N ALA B 259 SHEET 3 L 4 ILE B 288 VAL B 293 -1 O ASP B 291 N GLN B 267 SHEET 4 L 4 ILE B 299 PHE B 304 -1 O PHE B 304 N ILE B 288 SHEET 1 M 5 SER B 310 PHE B 311 0 SHEET 2 M 5 LYS B 393 THR B 398 1 O VAL B 396 N SER B 310 SHEET 3 M 5 MET B 377 ASP B 385 -1 N VAL B 383 O LYS B 395 SHEET 4 M 5 LYS B 331 LEU B 340 -1 N PHE B 334 O ILE B 382 SHEET 5 M 5 TYR B 315 PRO B 320 -1 N TYR B 319 O TYR B 337 SHEET 1 N 5 SER B 310 PHE B 311 0 SHEET 2 N 5 LYS B 393 THR B 398 1 O VAL B 396 N SER B 310 SHEET 3 N 5 MET B 377 ASP B 385 -1 N VAL B 383 O LYS B 395 SHEET 4 N 5 LYS B 331 LEU B 340 -1 N PHE B 334 O ILE B 382 SHEET 5 N 5 ILE B 326 TYR B 328 -1 N ILE B 326 O ILE B 333 SHEET 1 O 4 GLY B 410 LEU B 415 0 SHEET 2 O 4 LYS B 418 THR B 423 -1 O TYR B 420 N LEU B 413 SHEET 3 O 4 GLN B 433 ASP B 438 -1 O GLY B 435 N ILE B 421 SHEET 4 O 4 ARG B 446 TRP B 449 -1 O ARG B 446 N ASP B 438 SHEET 1 P 4 ALA B 481 PRO B 483 0 SHEET 2 P 4 VAL B 491 LEU B 496 -1 O SER B 492 N TYR B 482 SHEET 3 P 4 PRO B 505 SER B 510 -1 O THR B 508 N SER B 493 SHEET 4 P 4 ARG B 515 ALA B 520 -1 O LEU B 519 N ILE B 507 SSBOND 1 CYS A 159 CYS A 571 SSBOND 2 CYS A 190 CYS A 214 SSBOND 3 CYS A 256 CYS A 269 SSBOND 4 CYS A 350 CYS A 363 SSBOND 5 CYS A 355 CYS A 469 SSBOND 6 CYS A 463 CYS A 473 SSBOND 7 CYS A 535 CYS A 544 SSBOND 8 CYS B 159 CYS B 571 SSBOND 9 CYS B 190 CYS B 214 SSBOND 10 CYS B 256 CYS B 269 SSBOND 11 CYS B 350 CYS B 363 SSBOND 12 CYS B 355 CYS B 469 SSBOND 13 CYS B 463 CYS B 473 SSBOND 14 CYS B 535 CYS B 544 LINK ND2 ASN A 308 C1 NAG A3081 LINK ND2 ASN A 351 C1 NAG C3511 LINK ND2 ASN B 308 C1 NAG B3081 LINK ND2 ASN B 351 C1 NAG D3511 LINK ND2 ASN B 523 C1 NAG B5231 LINK O4 NAG C3511 C1 NAG C3512 LINK O4 NAG D3511 C1 NAG D3512 CISPEP 1 THR A 169 PRO A 170 0 -0.53 CISPEP 2 THR B 169 PRO B 170 0 -0.25 CRYST1 218.451 218.451 109.904 90.00 90.00 120.00 P 62 2 2 24 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 0.004578 0.002643 0.000000 0.00000 SCALE2 0.000000 0.005286 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009099 0.00000