HEADER HYDROLASE 30-OCT-03 1V3D TITLE STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE FROM HUMAN TITLE 2 PARAINFLUENZA VIRUS TYPE III: COMPLEX WITH NEU5AC2EN 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+NEU5AC2EN, 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 1V3D 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. 2.28 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) : 2.28 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.39 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 353924.470 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.7 REMARK 3 NUMBER OF REFLECTIONS : 58597 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) : 0.213 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 5935 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 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) : 2.28 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 16.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1951 REMARK 3 BIN R VALUE (WORKING SET) : 0.3650 REMARK 3 BIN FREE R VALUE : 0.3760 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 230 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025 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 : 164 REMARK 3 SOLVENT ATOMS : 717 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.18000 REMARK 3 B22 (A**2) : 4.18000 REMARK 3 B33 (A**2) : -8.37000 REMARK 3 B12 (A**2) : 5.44000 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) : 0.32 REMARK 3 ESD FROM SIGMAA (A) : 0.44 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) : 0.40 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.50 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.10 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.94 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 : 0.42 REMARK 3 BSOL : 84.85 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 : DAN.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 : DAN.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 1V3D 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 RCSB006154. 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 REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 14-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : DIAMOND 111 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : MAR CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58597 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280 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 (%) : 92.0 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36 REMARK 200 COMPLETENESS FOR SHELL (%) : 65.1 REMARK 200 DATA REDUNDANCY IN SHELL : 2.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: 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 (%): 65.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55 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 73.20933 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 36.60467 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 73.20933 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 36.60467 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 73.20933 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 36.60467 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 73.20933 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 36.60467 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 695 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 O HOH 101 O HOH 688 2.15 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 0.065 REMARK 500 MET A 401 SD MET A 401 CE -0.054 REMARK 500 MET B 183 SD MET B 183 CE 0.071 REMARK 500 VAL B 197 CB VAL B 197 CG1 -0.054 REMARK 500 ILE B 299 CG1 ILE B 299 CD1 -0.069 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 GLN A 222 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 LEU A 261 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 ILE A 292 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 PRO A 324 N - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 ILE A 332 N - CA - C ANGL. DEV. = -9.8 DEGREES REMARK 500 LEU A 335 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 ILE A 381 N - CA - C ANGL. DEV. =-11.9 DEGREES REMARK 500 SER A 430 N - CA - C ANGL. DEV. = 11.6 DEGREES REMARK 500 LEU A 496 N - CA - C ANGL. DEV. =-13.2 DEGREES REMARK 500 TYR A 509 N - CA - C ANGL. DEV. =-11.5 DEGREES REMARK 500 PHE A 545 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 GLN B 222 N - CA - C ANGL. DEV. =-10.0 DEGREES REMARK 500 ASP B 312 N - CA - C ANGL. DEV. =-10.9 DEGREES REMARK 500 PRO B 320 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 PRO B 324 N - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 LEU B 496 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 TYR B 509 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 HIS B 538 N - CA - C ANGL. DEV. =-11.8 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 -114.61 55.19 REMARK 500 VAL A 322 -52.91 68.01 REMARK 500 LEU A 522 -107.54 -160.86 REMARK 500 ASN A 540 -45.57 81.87 REMARK 500 ASN B 262 -102.12 62.73 REMARK 500 VAL B 322 -62.71 74.30 REMARK 500 LEU B 522 -105.17 -166.04 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 205 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH 377 DISTANCE = 7.58 ANGSTROMS REMARK 525 HOH 479 DISTANCE = 5.59 ANGSTROMS REMARK 525 HOH 492 DISTANCE = 5.06 ANGSTROMS REMARK 525 HOH 555 DISTANCE = 5.46 ANGSTROMS REMARK 525 HOH 568 DISTANCE = 5.27 ANGSTROMS REMARK 525 HOH 574 DISTANCE = 5.66 ANGSTROMS REMARK 525 HOH 579 DISTANCE = 5.49 ANGSTROMS REMARK 525 HOH 602 DISTANCE = 5.70 ANGSTROMS REMARK 525 HOH 603 DISTANCE = 6.95 ANGSTROMS REMARK 525 HOH 605 DISTANCE = 7.47 ANGSTROMS REMARK 525 HOH 611 DISTANCE = 5.40 ANGSTROMS REMARK 525 HOH 662 DISTANCE = 6.66 ANGSTROMS REMARK 525 HOH 691 DISTANCE = 5.47 ANGSTROMS REMARK 525 HOH 695 DISTANCE = 5.63 ANGSTROMS REMARK 525 HOH 697 DISTANCE = 5.46 ANGSTROMS REMARK 525 HOH 700 DISTANCE = 5.14 ANGSTROMS REMARK 525 HOH 702 DISTANCE = 5.68 ANGSTROMS REMARK 525 HOH 703 DISTANCE = 7.63 ANGSTROMS REMARK 525 HOH 704 DISTANCE = 6.54 ANGSTROMS REMARK 525 HOH 706 DISTANCE = 6.19 ANGSTROMS REMARK 525 HOH 708 DISTANCE = 7.42 ANGSTROMS REMARK 525 HOH 709 DISTANCE = 5.80 ANGSTROMS REMARK 525 HOH 710 DISTANCE = 6.13 ANGSTROMS REMARK 525 HOH 714 DISTANCE = 8.33 ANGSTROMS REMARK 525 HOH 716 DISTANCE = 5.57 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: 1V3E RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEX WITH ZANAMAVIR DBREF 1V3D A 142 572 GB 37958139 AAP35240 142 572 DBREF 1V3D 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 1V3D ASN A 308 ASN GLYCOSYLATION SITE MODRES 1V3D ASN A 351 ASN GLYCOSYLATION SITE MODRES 1V3D ASN A 523 ASN GLYCOSYLATION SITE MODRES 1V3D ASN B 308 ASN GLYCOSYLATION SITE MODRES 1V3D ASN B 351 ASN GLYCOSYLATION SITE MODRES 1V3D ASN B 523 ASN GLYCOSYLATION SITE HET NAG A3081 14 HET NAG C3511 14 HET NAG C3512 14 HET NAG A5231 14 HET NAG B3081 14 HET NDG D3511 14 HET NAG D3512 14 HET NAG B5231 14 HET CA 1001 1 HET CA 2001 1 HET SO4 3001 5 HET SO4 3002 5 HET DAN 1191 20 HET DAN 2191 20 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE HETNAM CA CALCIUM ION HETNAM SO4 SULFATE ION HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID HETSYN NAG NAG FORMUL 3 NAG 7(C8 H15 N O6) FORMUL 7 NDG C8 H15 N O6 FORMUL 9 CA 2(CA 2+) FORMUL 11 SO4 2(O4 S 2-) FORMUL 13 DAN 2(C11 H17 N O8) FORMUL 15 HOH *717(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 SER A 369 SER A 373 5 5 HELIX 6 6 ASP A 441 ILE A 445 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 THR B 359 SER B 367 1 9 HELIX 10 10 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 ASN A 551 -1 O PHE A 545 N SER A 534 SHEET 4 A 4 LEU A 558 GLU A 566 -1 O GLN A 559 N ILE A 550 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 ILE A 210 N CYS A 190 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 HIS A 245 N LEU A 224 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 THR A 302 N LEU A 290 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 ASP A 385 O LYS A 393 SHEET 4 E 5 LYS A 331 LEU A 340 -1 N PHE A 334 O ILE A 382 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 ASP A 385 O LYS A 393 SHEET 4 F 5 LYS A 331 LEU A 340 -1 N PHE A 334 O ILE A 382 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 ASN A 517 N TYR A 509 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 ALA B 204 N VAL B 197 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 ASN B 294 -1 O VAL B 293 N VAL B 265 SHEET 4 L 4 ILE B 299 PHE B 304 -1 O PHE B 304 N ILE B 288 SHEET 1 M 3 TYR B 315 PRO B 320 0 SHEET 2 M 3 LYS B 331 LEU B 340 -1 O TYR B 337 N TYR B 319 SHEET 3 M 3 ILE B 326 TYR B 328 -1 N ILE B 326 O ILE B 333 SHEET 1 N 4 TYR B 315 PRO B 320 0 SHEET 2 N 4 LYS B 331 LEU B 340 -1 O TYR B 337 N TYR B 319 SHEET 3 N 4 ARG B 376 ASP B 385 -1 O SER B 380 N GLY B 336 SHEET 4 N 4 LYS B 393 THR B 398 -1 O LYS B 395 N VAL B 383 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 LYS B 448 N ILE B 436 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 SER B 510 N VAL B 491 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 A 523 C1 NAG A5231 LINK ND2 ASN B 308 C1 NAG B3081 LINK ND2 ASN B 351 C1 NDG D3511 LINK ND2 ASN B 523 C1 NAG B5231 LINK O4 NAG C3511 C1 NAG C3512 LINK O4 NDG D3511 C1 NAG D3512 CISPEP 1 THR A 169 PRO A 170 0 0.00 CISPEP 2 THR B 169 PRO B 170 0 -0.07 CRYST1 219.005 219.005 109.814 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 0.004566 0.002636 0.000000 0.00000 SCALE2 0.000000 0.005272 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009106 0.00000