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HEADER HYDROLASE 16-OCT-03 1V2I TITLE STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE FROM HUMAN TITLE 2 PARAINFLUENZA VIRUS TYPE III 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, ORTHORHOMBIC 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 1V2I 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. 2.20 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.30 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1977203.140 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5 REMARK 3 NUMBER OF REFLECTIONS : 40213 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) : 0.185 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4018 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) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6035 REMARK 3 BIN R VALUE (WORKING SET) : 0.2640 REMARK 3 BIN FREE R VALUE : 0.3430 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 674 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6758 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 171 REMARK 3 SOLVENT ATOMS : 372 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.78000 REMARK 3 B22 (A**2) : 7.49000 REMARK 3 B33 (A**2) : -5.71000 REMARK 3 B12 (A**2) : 0.00000 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) : 0.24 REMARK 3 ESD FROM SIGMAA (A) : 0.26 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) : 0.34 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.011 REMARK 3 BOND ANGLES (DEGREES) : 1.80 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.98 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 : 45.54 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 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1V2I 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 RCSB006124. 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 : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU HR3 HB REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : AXCO MICROCAPILLARY FOCUSING REMARK 200 OPTICS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MAR 180 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40213 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.198 REMARK 200 RESOLUTION RANGE LOW (A) : 70.711 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : 0.14900 REMARK 200 R SYM (I) : 0.14900 REMARK 200 FOR THE DATA SET : 10.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2 REMARK 200 DATA REDUNDANCY IN SHELL : 5.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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: HOMOLOGY MODEL OF HPIV3-HN FROM NDV-HN PDB REMARK 200 ENTRY 1E8T REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, POTASSIUM PHOSPHATE, MES, REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 -1.000000 0.000000 0.000000 41.75000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.60000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.89000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.60000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.75000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.89000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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, E 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 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 ALA A 317 CA ALA A 317 CB 0.072 REMARK 500 PRO A 505 CB PRO A 505 CG 0.084 REMARK 500 PRO B 320 CB PRO B 320 CG 0.076 REMARK 500 MET B 401 SD MET B 401 CE -0.183 REMARK 500 ILE B 421 CG1 ILE B 421 CD1 0.092 REMARK 500 ILE B 436 CG1 ILE B 436 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 GLY A 179 N - CA - C ANGL. DEV. =-11.0 DEGREES REMARK 500 LEU A 261 N - CA - C ANGL. DEV. =-11.3 DEGREES REMARK 500 ILE A 332 N - CA - C ANGL. DEV. =-12.6 DEGREES REMARK 500 LEU A 496 N - CA - C ANGL. DEV. =-11.3 DEGREES REMARK 500 TYR A 509 N - CA - C ANGL. DEV. =-13.7 DEGREES REMARK 500 LYS A 541 N - CA - C ANGL. DEV. =-17.8 DEGREES REMARK 500 LEU B 261 N - CA - C ANGL. DEV. =-11.3 DEGREES REMARK 500 PRO B 324 N - CA - C ANGL. DEV. = 10.9 DEGREES REMARK 500 GLY B 387 N - CA - C ANGL. DEV. = 11.2 DEGREES REMARK 500 TYR B 509 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 ARG B 515 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 HIS B 538 N - CA - C ANGL. DEV. =-11.9 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 -112.93 58.59 REMARK 500 VAL A 322 -60.03 75.96 REMARK 500 LEU A 522 -108.27 -153.58 REMARK 500 ASN B 262 -114.54 62.17 REMARK 500 VAL B 322 -57.80 77.99 REMARK 500 LYS B 386 -110.03 -172.87 REMARK 500 TYR B 539 -102.43 64.81 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 304 DISTANCE = 5.01 ANGSTROMS REMARK 525 HOH 331 DISTANCE = 7.29 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1V3B RELATED DB: PDB REMARK 900 THE SAME PROTEIN, ANOTHER CRYSTAL SYSTEM-HEXAGONAL REMARK 900 RELATED ID: 1V3C RELATED DB: PDB REMARK 900 THE SAME PROTEIN, ANOTHER CRYSTAL SYSTEM-HEXAGONAL, COMPLEX REMARK 900 WITH NEU5AC REMARK 900 RELATED ID: 1V3D RELATED DB: PDB REMARK 900 THE SAME PROTEIN, ANOTHER CRYSTAL SYSTEM-HEXAGONAL, COMPLEX REMARK 900 WITH NEU5AC2EN REMARK 900 RELATED ID: 1V3E RELATED DB: PDB REMARK 900 THE SAME PROTEIN, ANOTHER CRYSTAL SYSTEM-HEXAGONAL, COMPLEX REMARK 900 WITH ZANAMAVIR DBREF 1V2I A 142 572 GB 37958139 AAP35240 142 572 DBREF 1V2I 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 1V2I ASN A 308 ASN GLYCOSYLATION SITE MODRES 1V2I ASN A 351 ASN GLYCOSYLATION SITE MODRES 1V2I ASN A 523 ASN GLYCOSYLATION SITE MODRES 1V2I ASN B 308 ASN GLYCOSYLATION SITE MODRES 1V2I ASN B 351 ASN GLYCOSYLATION SITE MODRES 1V2I ASN B 523 ASN GLYCOSYLATION SITE HET NDG A3081 14 HET NAG C3511 14 HET NAG C3512 14 HET BMA C3513 11 HET MAN C3514 11 HET MAN C3515 11 HET NAG A5231 14 HET NAG B3081 14 HET NAG D3511 14 HET NAG D3512 14 HET NAG E5231 14 HET NAG E5232 14 HET CA 1001 1 HET CA 1002 1 HET PO4 2001 5 HET PO4 2002 5 HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM CA CALCIUM ION HETNAM PO4 PHOSPHATE ION HETSYN NAG NAG FORMUL 3 NDG C8 H15 N O6 FORMUL 4 NAG 8(C8 H15 N O6) FORMUL 4 BMA C6 H12 O6 FORMUL 4 MAN 2(C6 H12 O6) FORMUL 9 CA 2(CA 2+) FORMUL 11 PO4 2(O4 P 3-) FORMUL 13 HOH *372(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 GLY A 542 HIS A 552 -1 O PHE A 545 N SER A 534 SHEET 4 A 4 THR A 557 GLU A 566 -1 O GLN A 559 N ILE A 550 SHEET 1 B 2 LEU A 163 LEU A 166 0 SHEET 2 B 2 LYS A 569 SER A 572 -1 O SER A 570 N SER A 165 SHEET 1 C 2 PRO A 178 GLY A 179 0 SHEET 2 C 2 MET B 183 PRO B 184 -1 O MET B 183 N GLY A 179 SHEET 1 D 4 CYS A 190 ILE A 198 0 SHEET 2 D 4 TYR A 203 ILE A 210 -1 O ASN A 208 N ARG A 192 SHEET 3 D 4 TYR A 221 VAL A 231 -1 O GLN A 225 N TYR A 205 SHEET 4 D 4 PRO A 237 THR A 246 -1 O ARG A 242 N ILE A 226 SHEET 1 E 4 LYS A 254 LEU A 261 0 SHEET 2 E 4 ASP A 264 SER A 270 -1 O TYR A 266 N ALA A 259 SHEET 3 E 4 ILE A 288 VAL A 293 -1 O VAL A 289 N CYS A 269 SHEET 4 E 4 ILE A 299 PHE A 304 -1 O PHE A 304 N ILE A 288 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 PHE A 334 O ILE A 382 SHEET 5 F 5 TYR A 315 PRO A 320 -1 N TYR A 319 O TYR A 337 SHEET 1 G 5 SER A 310 PHE A 311 0 SHEET 2 G 5 PRO A 392 THR A 398 1 O VAL A 396 N SER A 310 SHEET 3 G 5 MET A 377 LYS A 386 -1 N VAL A 383 O LYS A 395 SHEET 4 G 5 LYS A 331 LEU A 340 -1 N PHE A 334 O ILE A 382 SHEET 5 G 5 ILE A 326 TYR A 328 -1 N ILE A 326 O ILE A 333 SHEET 1 H 4 GLY A 410 LEU A 415 0 SHEET 2 H 4 LYS A 418 THR A 423 -1 O TYR A 422 N ARG A 411 SHEET 3 H 4 GLN A 433 ASP A 438 -1 O GLY A 435 N ILE A 421 SHEET 4 H 4 ARG A 446 TRP A 449 -1 O ARG A 446 N ASP A 438 SHEET 1 I 4 ALA A 481 PRO A 483 0 SHEET 2 I 4 ILE A 490 LEU A 496 -1 O SER A 492 N TYR A 482 SHEET 3 I 4 PRO A 505 THR A 511 -1 O VAL A 506 N ILE A 495 SHEET 4 I 4 ARG A 515 ALA A 520 -1 O LEU A 519 N ILE A 507 SHEET 1 J 4 ILE B 148 PRO B 150 0 SHEET 2 J 4 ALA B 528 HIS B 538 -1 O THR B 537 N LYS B 149 SHEET 3 J 4 LYS B 541 ASN B 551 -1 O PHE B 545 N SER B 534 SHEET 4 J 4 LEU B 558 GLU B 566 -1 O THR B 565 N CYS B 544 SHEET 1 K 2 PRO B 164 LEU B 166 0 SHEET 2 K 2 LYS B 569 CYS B 571 -1 O SER B 570 N SER B 165 SHEET 1 L 4 CYS B 190 ILE B 198 0 SHEET 2 L 4 TYR B 203 ILE B 210 -1 O ASN B 208 N ARG B 192 SHEET 3 L 4 TYR B 221 VAL B 231 -1 O GLN B 225 N TYR B 205 SHEET 4 L 4 PRO B 237 PHE B 247 -1 O HIS B 245 N LEU B 224 SHEET 1 M 4 LYS B 254 LEU B 261 0 SHEET 2 M 4 ASP B 264 SER B 270 -1 O TYR B 266 N ALA B 259 SHEET 3 M 4 ILE B 288 VAL B 293 -1 O VAL B 289 N CYS B 269 SHEET 4 M 4 ILE B 299 PHE B 304 -1 O PHE B 304 N ILE B 288 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 ILE B 381 O TRP B 397 SHEET 4 N 5 LYS B 331 LEU B 340 -1 N PHE B 334 O ILE B 382 SHEET 5 N 5 TYR B 315 PRO B 320 -1 N TYR B 319 O TYR B 337 SHEET 1 O 5 SER B 310 PHE B 311 0 SHEET 2 O 5 LYS B 393 THR B 398 1 O VAL B 396 N SER B 310 SHEET 3 O 5 MET B 377 ASP B 385 -1 N ILE B 381 O TRP B 397 SHEET 4 O 5 LYS B 331 LEU B 340 -1 N PHE B 334 O ILE B 382 SHEET 5 O 5 ILE B 326 TYR B 328 -1 N ILE B 326 O ILE B 333 SHEET 1 P 4 GLY B 410 LEU B 415 0 SHEET 2 P 4 LYS B 418 THR B 423 -1 O TYR B 420 N LEU B 413 SHEET 3 P 4 LEU B 434 ASP B 438 -1 O GLY B 435 N ILE B 421 SHEET 4 P 4 ARG B 446 THR B 450 -1 O ARG B 446 N ASP B 438 SHEET 1 Q 4 ALA B 481 PRO B 483 0 SHEET 2 Q 4 VAL B 491 LEU B 496 -1 O SER B 492 N TYR B 482 SHEET 3 Q 4 PRO B 505 SER B 510 -1 O THR B 508 N SER B 493 SHEET 4 Q 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 NDG 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 NAG D3511 LINK ND2 ASN B 523 C1 NAG E5231 LINK O4 NAG C3511 C1 NAG C3512 LINK O4 NAG C3512 C1 BMA C3513 LINK O3 BMA C3513 C1 MAN C3514 LINK O6 BMA C3513 C1 MAN C3515 LINK O4 NAG D3511 C1 NAG D3512 LINK O4 NAG E5231 C1 NAG E5232 CISPEP 1 THR A 169 PRO A 170 0 -0.30 CISPEP 2 THR B 169 PRO B 170 0 -0.36 CRYST1 83.500 93.780 105.200 90.00 90.00 90.00 P 21 21 21 8 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 0.011976 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010663 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009506 0.00000