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HEADER SIALIDASE 01-OCT-00 1E8T TITLE STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS TITLE 2 HEMAGGLUTININ-NEURAMINIDASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: HEAD DOMAIN; COMPND 5 SYNONYM: HN; COMPND 6 EC: 3.2.1.18 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NEWCASTLE DISEASE VIRUS; SOURCE 3 STRAIN: KANSAS KEYWDS SIALIDASE, NEURAMINIDASE, HEMAGGLUTININ-NEURAMINIDASE, KEYWDS 2 HEMAGGLUTININ EXPDTA X-RAY DIFFRACTION AUTHOR S.CRENNELL,T.TAKIMOTO,A.PORTNER,G.TAYLOR REVDAT 2 18-JUL-03 1E8T 1 REMARK REVDAT 1 03-APR-01 1E8T 0 JRNL AUTH S.CRENNELL,T.TAKIMOTO,A.PORTNER,G.TAYLOR JRNL TITL CRYSTAL STRUCTURE OF THE MULTIFUNCTIONAL JRNL TITL 2 PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE. JRNL REF NAT.STRUCT.BIOL. V. 7 1068 2000 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.TAKIMOTO,G.L.TAYLOR,S.J.CRENNELL,R.A.SCROGGS, REMARK 1 AUTH 2 A.PORTNER REMARK 1 TITL CRYSTALLIZATION OF NEWCASTLE DISEASE VIRUS REMARK 1 TITL 2 HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN REMARK 1 REF VIROLOGY V. 270 208 2000 REMARK 1 REFN ASTM VIRLAX US ISSN 0042-6822 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 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) (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 38111 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) : 0.222 REMARK 3 FREE R VALUE : 0.276 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3848 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 : 6914 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 89 REMARK 3 SOLVENT ATOMS : NULL 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) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.38 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 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 1E8T 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 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-5407 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.60 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.992 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38168 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : 11.000 REMARK 200 R MERGE (I) : 0.03100 REMARK 200 R SYM (I) : 0.03100 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: MIR REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.6 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 35.85500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 99.08000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.95500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 99.08000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.85500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.95500 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, Y, Z 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 570 REMARK 465 VAL A 571 REMARK 465 ARG A 572 REMARK 465 GLU A 573 REMARK 465 ALA A 574 REMARK 465 ARG A 575 REMARK 465 SER A 576 REMARK 465 GLY A 577 REMARK 465 GLU B 573 REMARK 465 ALA B 574 REMARK 465 ARG B 575 REMARK 465 SER B 576 REMARK 465 GLY B 577 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 354 SD MET A 354 CE -0.066 REMARK 500 ARG A 557 CB ARG A 557 CG -0.044 REMARK 500 MET B 249 SD MET B 249 CE -0.157 REMARK 500 MET B 491 SD MET B 491 CE -0.092 REMARK 500 ILE B 558 CG1 ILE B 558 CD1 -0.043 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 THR A 173 N - CA - C ANGL. DEV. =-13.4 DEGREES REMARK 500 LEU A 208 CA - CB - CG ANGL. DEV. = 8.8 DEGREES REMARK 500 SER A 252 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 LEU A 275 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 GLY A 365 N - CA - C ANGL. DEV. = 8.7 DEGREES REMARK 500 PRO A 441 N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 TYR A 442 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 ASN A 445 N - CA - C ANGL. DEV. = 9.1 DEGREES REMARK 500 LEU A 492 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 VAL A 534 N - CA - C ANGL. DEV. =-10.4 DEGREES REMARK 500 THR B 173 N - CA - C ANGL. DEV. =-11.0 DEGREES REMARK 500 LEU B 275 N - CA - C ANGL. DEV. =-10.4 DEGREES REMARK 500 TYR B 442 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 LEU B 492 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 VAL B 534 N - CA - C ANGL. DEV. = -9.6 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 ILE A 127 136.19 64.84 REMARK 500 VAL A 302 -41.91 71.75 REMARK 500 VAL B 302 -38.05 74.98 DBREF 1E8T A 124 577 UNP Q9Q2W5 Q9Q2W5 124 577 DBREF 1E8T B 124 577 UNP Q9Q2W5 Q9Q2W5 124 577 SEQRES 1 A 454 GLY ALA PRO ILE HIS ASP PRO ASP PHE ILE GLY GLY ILE SEQRES 2 A 454 GLY LYS GLU LEU ILE VAL ASP ASN ALA SER ASP VAL THR SEQRES 3 A 454 SER PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE SEQRES 4 A 454 ILE PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE SEQRES 5 A 454 PRO SER PHE ASP MET SER ALA THR HIS TYR CYS TYR THR SEQRES 6 A 454 HIS ASN VAL ILE LEU SER GLY CYS ARG ASP HIS SER HIS SEQRES 7 A 454 SER HIS GLN TYR LEU ALA LEU GLY VAL LEU ARG THR THR SEQRES 8 A 454 ALA THR GLY ARG ILE PHE PHE SER THR LEU ARG SER ILE SEQRES 9 A 454 SER LEU ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SEQRES 10 A 454 SER ALA THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS SEQRES 11 A 454 VAL THR GLU THR GLU GLU GLU ASP TYR ASN SER ALA VAL SEQRES 12 A 454 PRO THR LEU MET ALA HIS GLY ARG LEU GLY PHE ASP GLY SEQRES 13 A 454 GLN TYR HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE SEQRES 14 A 454 GLU ASP TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SEQRES 15 A 454 SER PHE ILE ASP GLY ARG VAL TRP PHE SER VAL TYR GLY SEQRES 16 A 454 GLY LEU LYS PRO ASN SER PRO SER ASP THR VAL GLN GLU SEQRES 17 A 454 GLY LYS TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS SEQRES 18 A 454 PRO ASP GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SEQRES 19 A 454 SER TYR LYS PRO GLY ARG PHE GLY GLY LYS ARG ILE GLN SEQRES 20 A 454 GLN ALA ILE LEU SER ILE LYS VAL SER THR SER LEU GLY SEQRES 21 A 454 GLU ASP PRO VAL LEU THR VAL PRO PRO ASN THR VAL THR SEQRES 22 A 454 LEU MET GLY ALA GLU GLY ARG ILE LEU THR VAL GLY THR SEQRES 23 A 454 SER HIS PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER SEQRES 24 A 454 PRO ALA LEU LEU TYR PRO MET THR VAL SER ASN LYS THR SEQRES 25 A 454 ALA THR LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR SEQRES 26 A 454 ARG PRO GLY SER ILE PRO CYS GLN ALA SER ALA ARG CYS SEQRES 27 A 454 PRO ASN SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR SEQRES 28 A 454 PRO LEU ILE PHE TYR ARG ASN HIS THR LEU ARG GLY VAL SEQRES 29 A 454 PHE GLY THR MET LEU ASP SER GLU GLN ALA ARG LEU ASN SEQRES 30 A 454 PRO ALA SER ALA VAL PHE ASP SER THR SER ARG SER ARG SEQRES 31 A 454 ILE THR ARG VAL SER SER SER SER THR LYS ALA ALA TYR SEQRES 32 A 454 THR THR SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS SEQRES 33 A 454 THR TYR CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU SEQRES 34 A 454 PHE GLY GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE SEQRES 35 A 454 LEU LYS ASN ASP GLY VAL ARG GLU ALA ARG SER GLY SEQRES 1 B 454 GLY ALA PRO ILE HIS ASP PRO ASP PHE ILE GLY GLY ILE SEQRES 2 B 454 GLY LYS GLU LEU ILE VAL ASP ASN ALA SER ASP VAL THR SEQRES 3 B 454 SER PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE SEQRES 4 B 454 ILE PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE SEQRES 5 B 454 PRO SER PHE ASP MET SER ALA THR HIS TYR CYS TYR THR SEQRES 6 B 454 HIS ASN VAL ILE LEU SER GLY CYS ARG ASP HIS SER HIS SEQRES 7 B 454 SER HIS GLN TYR LEU ALA LEU GLY VAL LEU ARG THR THR SEQRES 8 B 454 ALA THR GLY ARG ILE PHE PHE SER THR LEU ARG SER ILE SEQRES 9 B 454 SER LEU ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SEQRES 10 B 454 SER ALA THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS SEQRES 11 B 454 VAL THR GLU THR GLU GLU GLU ASP TYR ASN SER ALA VAL SEQRES 12 B 454 PRO THR LEU MET ALA HIS GLY ARG LEU GLY PHE ASP GLY SEQRES 13 B 454 GLN TYR HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE SEQRES 14 B 454 GLU ASP TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SEQRES 15 B 454 SER PHE ILE ASP GLY ARG VAL TRP PHE SER VAL TYR GLY SEQRES 16 B 454 GLY LEU LYS PRO ASN SER PRO SER ASP THR VAL GLN GLU SEQRES 17 B 454 GLY LYS TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS SEQRES 18 B 454 PRO ASP GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SEQRES 19 B 454 SER TYR LYS PRO GLY ARG PHE GLY GLY LYS ARG ILE GLN SEQRES 20 B 454 GLN ALA ILE LEU SER ILE LYS VAL SER THR SER LEU GLY SEQRES 21 B 454 GLU ASP PRO VAL LEU THR VAL PRO PRO ASN THR VAL THR SEQRES 22 B 454 LEU MET GLY ALA GLU GLY ARG ILE LEU THR VAL GLY THR SEQRES 23 B 454 SER HIS PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER SEQRES 24 B 454 PRO ALA LEU LEU TYR PRO MET THR VAL SER ASN LYS THR SEQRES 25 B 454 ALA THR LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR SEQRES 26 B 454 ARG PRO GLY SER ILE PRO CYS GLN ALA SER ALA ARG CYS SEQRES 27 B 454 PRO ASN SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR SEQRES 28 B 454 PRO LEU ILE PHE TYR ARG ASN HIS THR LEU ARG GLY VAL SEQRES 29 B 454 PHE GLY THR MET LEU ASP SER GLU GLN ALA ARG LEU ASN SEQRES 30 B 454 PRO ALA SER ALA VAL PHE ASP SER THR SER ARG SER ARG SEQRES 31 B 454 ILE THR ARG VAL SER SER SER SER THR LYS ALA ALA TYR SEQRES 32 B 454 THR THR SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS SEQRES 33 B 454 THR TYR CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU SEQRES 34 B 454 PHE GLY GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE SEQRES 35 B 454 LEU LYS ASN ASP GLY VAL ARG GLU ALA ARG SER GLY MODRES 1E8T ASN A 341 ASN GLYCOSYLATION SITE MODRES 1E8T ASN A 481 ASN GLYCOSYLATION SITE MODRES 1E8T ASN B 481 ASN GLYCOSYLATION SITE HET NAG A1570 14 HET NAG A1571 14 HET NAG A1572 14 HET NAG B1573 14 HET NAG B1574 14 HET CA A1001 1 HET GOL A1002 6 HET GOL A1003 6 HET GOL B1004 6 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM CA CALCIUM ION HETNAM GOL GLYCEROL HETSYN NAG NAG FORMUL 3 NAG 5(C8 H15 N O6) FORMUL 6 CA CA 2+ FORMUL 7 GOL 3(C3 H8 O3) FORMUL 10 HOH *211(H2 O) HELIX 1 1 ASP A 129 ILE A 133 5 5 HELIX 2 2 ASP A 147 THR A 149 5 3 HELIX 3 3 THR A 257 SER A 264 1 8 HELIX 4 4 ASP A 287 PHE A 292 1 6 HELIX 5 5 SER A 324 GLU A 331 1 8 HELIX 6 6 GLU A 347 TYR A 359 1 13 HELIX 7 7 PRO A 361 GLY A 365 5 5 HELIX 8 8 ASN A 550 GLY A 554 5 5 HELIX 9 9 THR B 257 TYR B 262 1 6 HELIX 10 10 ASP B 287 PHE B 292 1 6 HELIX 11 11 SER B 324 GLN B 330 1 7 HELIX 12 12 GLU B 347 TYR B 359 1 13 HELIX 13 13 PRO B 361 GLY B 365 5 5 SHEET 1 A 2 PHE A 151 PRO A 153 0 SHEET 2 A 2 ILE A 565 LYS A 567 -1 N LEU A 566 O TYR A 152 SHEET 1 B 4 CYS A 172 ARG A 174 0 SHEET 2 B 4 TYR A 185 ILE A 192 -1 N ILE A 192 O CYS A 172 SHEET 3 B 4 SER A 202 THR A 213 -1 N GLY A 209 O TYR A 185 SHEET 4 B 4 ILE A 219 LEU A 229 -1 N LEU A 229 O GLN A 204 SHEET 1 C 2 SER A 177 SER A 181 0 SHEET 2 C 2 HIS A 184 THR A 188 -1 N THR A 188 O SER A 177 SHEET 1 D 4 SER A 239 THR A 243 0 SHEET 2 D 4 GLY A 246 LYS A 253 -1 N LEU A 250 O SER A 239 SHEET 3 D 4 LEU A 269 GLY A 276 -1 N LEU A 275 O CYS A 247 SHEET 4 D 4 TYR A 281 ASP A 285 -1 N LYS A 284 O HIS A 272 SHEET 1 E 4 SER A 306 ILE A 308 0 SHEET 2 E 4 ARG A 311 GLY A 319 -1 N TRP A 313 O SER A 306 SHEET 3 E 4 ILE A 369 LYS A 377 -1 N ILE A 376 O VAL A 312 SHEET 4 E 4 VAL A 387 THR A 389 -1 N THR A 389 O ILE A 373 SHEET 1 F 4 GLY A 402 VAL A 407 0 SHEET 2 F 4 SER A 410 GLN A 415 -1 N TYR A 414 O ARG A 403 SHEET 3 F 4 ALA A 424 MET A 429 -1 N MET A 429 O HIS A 411 SHEET 4 F 4 TYR A 442 PHE A 444 -1 N PHE A 444 O ALA A 424 SHEET 1 G 2 MET A 429 SER A 432 0 SHEET 2 G 2 THR A 435 LEU A 438 -1 N THR A 437 O THR A 430 SHEET 1 H 3 PRO A 501 PHE A 506 0 SHEET 2 H 3 GLY A 486 LEU A 492 -1 N MET A 491 O ALA A 502 SHEET 3 H 3 PRO A 473 ILE A 477 -1 N ILE A 477 O GLY A 486 SHEET 1 I 3 ARG A 557 GLU A 564 0 SHEET 2 I 3 LYS A 539 SER A 549 -1 N ILE A 548 O ARG A 557 SHEET 3 I 3 LYS A 523 VAL A 534 -1 N VAL A 534 O LYS A 539 SHEET 1 J 2 TRP A 295 PRO A 300 0 SHEET 2 J 2 VAL A 316 LEU A 320 -1 N GLY A 319 O VAL A 296 SHEET 1 K 2 PHE B 151 PRO B 153 0 SHEET 2 K 2 ILE B 565 LYS B 567 -1 N LEU B 566 O TYR B 152 SHEET 1 L 4 CYS B 172 ARG B 174 0 SHEET 2 L 4 TYR B 185 ILE B 192 -1 N ILE B 192 O CYS B 172 SHEET 3 L 4 HIS B 203 THR B 213 -1 N GLY B 209 O TYR B 185 SHEET 4 L 4 ILE B 219 LEU B 229 -1 N LEU B 229 O GLN B 204 SHEET 1 M 2 SER B 177 MET B 180 0 SHEET 2 M 2 TYR B 185 THR B 188 -1 N THR B 188 O SER B 177 SHEET 1 N 4 SER B 239 THR B 243 0 SHEET 2 N 4 GLY B 246 LYS B 253 -1 N LEU B 250 O SER B 239 SHEET 3 N 4 LEU B 269 GLY B 276 -1 N LEU B 275 O CYS B 247 SHEET 4 N 4 TYR B 281 ASP B 285 -1 N LYS B 284 O HIS B 272 SHEET 1 O 4 SER B 306 ILE B 308 0 SHEET 2 O 4 ARG B 311 GLY B 319 -1 N TRP B 313 O SER B 306 SHEET 3 O 4 ILE B 369 LYS B 377 -1 N ILE B 376 O VAL B 312 SHEET 4 O 4 VAL B 387 THR B 389 -1 N THR B 389 O ILE B 373 SHEET 1 P 4 GLY B 402 VAL B 407 0 SHEET 2 P 4 SER B 410 GLN B 415 -1 N TYR B 414 O ARG B 403 SHEET 3 P 4 ALA B 424 MET B 429 -1 N MET B 429 O HIS B 411 SHEET 4 P 4 TYR B 442 PHE B 444 -1 N PHE B 444 O ALA B 424 SHEET 1 Q 2 MET B 429 SER B 432 0 SHEET 2 Q 2 THR B 435 LEU B 438 -1 N THR B 437 O THR B 430 SHEET 1 R 3 PRO B 501 PHE B 506 0 SHEET 2 R 3 GLY B 486 LEU B 492 -1 N MET B 491 O ALA B 502 SHEET 3 R 3 TYR B 474 ILE B 477 -1 N ILE B 477 O GLY B 486 SHEET 1 S 3 ARG B 557 GLU B 564 0 SHEET 2 S 3 LYS B 539 SER B 549 -1 N ILE B 548 O ARG B 557 SHEET 3 S 3 LYS B 523 VAL B 534 -1 N VAL B 534 O LYS B 539 SHEET 1 T 2 TRP B 295 PRO B 300 0 SHEET 2 T 2 VAL B 316 LEU B 320 -1 N GLY B 319 O VAL B 296 SSBOND 1 CYS A 172 CYS A 196 SSBOND 2 CYS A 186 CYS A 247 SSBOND 3 CYS A 238 CYS A 251 SSBOND 4 CYS A 344 CYS A 461 SSBOND 5 CYS A 455 CYS A 465 SSBOND 6 CYS A 531 CYS A 542 SSBOND 7 CYS B 172 CYS B 196 SSBOND 8 CYS B 186 CYS B 247 SSBOND 9 CYS B 238 CYS B 251 SSBOND 10 CYS B 344 CYS B 461 SSBOND 11 CYS B 455 CYS B 465 SSBOND 12 CYS B 531 CYS B 542 LINK CA CA A1001 O ASP A 261 LINK CA CA A1001 O VAL A 266 LINK CA CA A1001 O VAL A 296 LINK ND2 ASN A 341 C1 NAG A1570 LINK ND2 ASN A 481 C1 NAG A1571 LINK O4 NAG A1571 C1 NAG A1572 LINK ND2 ASN B 481 C1 NAG B1573 LINK O4 NAG B1573 C1 NAG B1574 CISPEP 1 ILE A 453 PRO A 454 0 0.13 CISPEP 2 ILE B 453 PRO B 454 0 0.58 CRYST1 71.710 77.910 198.160 90.00 90.00 90.00 P 21 21 21 4 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 0.013945 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012835 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005046 0.00000 MTRIX1 1 -0.988300 0.147500 -0.038900 35.58000 1 MTRIX2 1 0.120900 0.913100 0.389400 -12.26000 1 MTRIX3 1 0.093000 0.380200 -0.920200 49.01000 1