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HEADER HYDROLASE 09-JUN-04 1W0P TITLE VIBRIO CHOLERAE SIALIDASE WITH ALPHA-2,6-SIALYLLACTOSE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE KEYWDS VIBRIO CHOLERAE, SIALIDASE, NEURAMINIDASE, LECTIN EXPDTA X-RAY DIFFRACTION AUTHOR I.MOUSTAFA,H.CONNARIS,M.TAYLOR,V.ZAITSEV,J.C.WILSON, AUTHOR 2 M.J.KIEFEL,M.VON-ITZSTEIN,G.TAYLOR REVDAT 2 24-SEP-04 1W0P 1 JRNL REVDAT 1 08-JUL-04 1W0P 0 JRNL AUTH I.MOUSTAFA,H.CONNARIS,M.TAYLOR,V.ZAITSEV, JRNL AUTH 2 J.C.WILSON,M.J.KIEFEL,M.VON ITZSTEIN,G.TAYLOR JRNL TITL SIALIC ACID RECOGNITION BY VIBRIO CHOLERAE JRNL TITL 2 NEURAMINIDASE. JRNL REF J.BIOL.CHEM. V. 279 40819 2004 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 106040 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) : 0.214 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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 : 5827 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 39 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) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.32 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 : GOLTRS.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 : CARBOHYDRATE.TOP REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1W0P 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-20133 . 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 : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 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 : 106040 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 8.000 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL 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: MOLECULAR REPLACEMENT 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 (%): 47.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 35.15500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.80750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.45500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.80750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.15500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.45500 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 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 1 REMARK 465 ARG A 2 REMARK 465 PHE A 3 REMARK 465 LYS A 4 REMARK 465 ASN A 5 REMARK 465 VAL A 6 REMARK 465 LYS A 7 REMARK 465 LYS A 8 REMARK 465 THR A 9 REMARK 465 ALA A 10 REMARK 465 LEU A 11 REMARK 465 MET A 12 REMARK 465 LEU A 13 REMARK 465 ALA A 14 REMARK 465 MET A 15 REMARK 465 PHE A 16 REMARK 465 GLY A 17 REMARK 465 MET A 18 REMARK 465 ALA A 19 REMARK 465 THR A 20 REMARK 465 SER A 21 REMARK 465 SER A 22 REMARK 465 ASN A 23 REMARK 465 ALA A 24 REMARK 465 LEU A 778 REMARK 465 SER A 779 REMARK 465 GLN A 780 REMARK 465 ASN A 781 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 100 SD MET A 100 CE 0.034 REMARK 500 MET A 622 CG MET A 622 SD 0.031 REMARK 500 MET A 767 SD MET A 767 CE -0.038 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 PHE A 27 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 ILE A 108 N - CA - C ANGL. DEV. =-10.7 DEGREES REMARK 500 VAL A 119 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 LEU A 120 N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 LEU A 125 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 ILE A 191 N - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 GLY A 215 N - CA - C ANGL. DEV. = 10.3 DEGREES REMARK 500 LYS A 244 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 THR A 257 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 ASP A 289 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 PRO A 312 N - CA - C ANGL. DEV. =-12.0 DEGREES REMARK 500 PRO A 327 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 PHE A 357 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 GLN A 395 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 ILE A 396 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 ILE A 476 N - CA - C ANGL. DEV. = -9.6 DEGREES REMARK 500 ALA A 481 N - CA - C ANGL. DEV. = 11.9 DEGREES REMARK 500 ILE A 585 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 SER A 610 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 ILE A 731 N - CA - C ANGL. DEV. =-11.7 DEGREES REMARK 500 ILE A 754 N - CA - C ANGL. DEV. = -8.4 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 51 -119.06 45.23 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: SIA BINDING SITE FOR CHAIN A DBREF 1W0P A 1 781 UNP P37060 NANH_VIBCH 1 781 SEQRES 1 A 781 MET ARG PHE LYS ASN VAL LYS LYS THR ALA LEU MET LEU SEQRES 2 A 781 ALA MET PHE GLY MET ALA THR SER SER ASN ALA ALA LEU SEQRES 3 A 781 PHE ASP TYR ASN ALA THR GLY ASP THR GLU PHE ASP SER SEQRES 4 A 781 PRO ALA LYS GLN GLY TRP MET GLN ASP ASN THR ASN ASN SEQRES 5 A 781 GLY SER GLY VAL LEU THR ASN ALA ASP GLY MET PRO ALA SEQRES 6 A 781 TRP LEU VAL GLN GLY ILE GLY GLY ARG ALA GLN TRP THR SEQRES 7 A 781 TYR SER LEU SER THR ASN GLN HIS ALA GLN ALA SER SER SEQRES 8 A 781 PHE GLY TRP ARG MET THR THR GLU MET LYS VAL LEU SER SEQRES 9 A 781 GLY GLY MET ILE THR ASN TYR TYR ALA ASN GLY THR GLN SEQRES 10 A 781 ARG VAL LEU PRO ILE ILE SER LEU ASP SER SER GLY ASN SEQRES 11 A 781 LEU VAL VAL GLU PHE GLU GLY GLN THR GLY ARG THR VAL SEQRES 12 A 781 LEU ALA THR GLY THR ALA ALA THR GLU TYR HIS LYS PHE SEQRES 13 A 781 GLU LEU VAL PHE LEU PRO GLY SER ASN PRO SER ALA SER SEQRES 14 A 781 PHE TYR PHE ASP GLY LYS LEU ILE ARG ASP ASN ILE GLN SEQRES 15 A 781 PRO THR ALA SER LYS GLN ASN MET ILE VAL TRP GLY ASN SEQRES 16 A 781 GLY SER SER ASN THR ASP GLY VAL ALA ALA TYR ARG ASP SEQRES 17 A 781 ILE LYS PHE GLU ILE GLN GLY ASP VAL ILE PHE ARG GLY SEQRES 18 A 781 PRO ASP ARG ILE PRO SER ILE VAL ALA SER SER VAL THR SEQRES 19 A 781 PRO GLY VAL VAL THR ALA PHE ALA GLU LYS ARG VAL GLY SEQRES 20 A 781 GLY GLY ASP PRO GLY ALA LEU SER ASN THR ASN ASP ILE SEQRES 21 A 781 ILE THR ARG THR SER ARG ASP GLY GLY ILE THR TRP ASP SEQRES 22 A 781 THR GLU LEU ASN LEU THR GLU GLN ILE ASN VAL SER ASP SEQRES 23 A 781 GLU PHE ASP PHE SER ASP PRO ARG PRO ILE TYR ASP PRO SEQRES 24 A 781 SER SER ASN THR VAL LEU VAL SER TYR ALA ARG TRP PRO SEQRES 25 A 781 THR ASP ALA ALA GLN ASN GLY ASP ARG ILE LYS PRO TRP SEQRES 26 A 781 MET PRO ASN GLY ILE PHE TYR SER VAL TYR ASP VAL ALA SEQRES 27 A 781 SER GLY ASN TRP GLN ALA PRO ILE ASP VAL THR ASP GLN SEQRES 28 A 781 VAL LYS GLU ARG SER PHE GLN ILE ALA GLY TRP GLY GLY SEQRES 29 A 781 SER GLU LEU TYR ARG ARG ASN THR SER LEU ASN SER GLN SEQRES 30 A 781 GLN ASP TRP GLN SER ASN ALA LYS ILE ARG ILE VAL ASP SEQRES 31 A 781 GLY ALA ALA ASN GLN ILE GLN VAL ALA ASP GLY SER ARG SEQRES 32 A 781 LYS TYR VAL VAL THR LEU SER ILE ASP GLU SER GLY GLY SEQRES 33 A 781 LEU VAL ALA ASN LEU ASN GLY VAL SER ALA PRO ILE ILE SEQRES 34 A 781 LEU GLN SER GLU HIS ALA LYS VAL HIS SER PHE HIS ASP SEQRES 35 A 781 TYR GLU LEU GLN TYR SER ALA LEU ASN HIS THR THR THR SEQRES 36 A 781 LEU PHE VAL ASP GLY GLN GLN ILE THR THR TRP ALA GLY SEQRES 37 A 781 GLU VAL SER GLN GLU ASN ASN ILE GLN PHE GLY ASN ALA SEQRES 38 A 781 ASP ALA GLN ILE ASP GLY ARG LEU HIS VAL GLN LYS ILE SEQRES 39 A 781 VAL LEU THR GLN GLN GLY HIS ASN LEU VAL GLU PHE ASP SEQRES 40 A 781 ALA PHE TYR LEU ALA GLN GLN THR PRO GLU VAL GLU LYS SEQRES 41 A 781 ASP LEU GLU LYS LEU GLY TRP THR LYS ILE LYS THR GLY SEQRES 42 A 781 ASN THR MET SER LEU TYR GLY ASN ALA SER VAL ASN PRO SEQRES 43 A 781 GLY PRO GLY HIS GLY ILE THR LEU THR ARG GLN GLN ASN SEQRES 44 A 781 ILE SER GLY SER GLN ASN GLY ARG LEU ILE TYR PRO ALA SEQRES 45 A 781 ILE VAL LEU ASP ARG PHE PHE LEU ASN VAL MET SER ILE SEQRES 46 A 781 TYR SER ASP ASP GLY GLY SER ASN TRP GLN THR GLY SER SEQRES 47 A 781 THR LEU PRO ILE PRO PHE ARG TRP LYS SER SER SER ILE SEQRES 48 A 781 LEU GLU THR LEU GLU PRO SER GLU ALA ASP MET VAL GLU SEQRES 49 A 781 LEU GLN ASN GLY ASP LEU LEU LEU THR ALA ARG LEU ASP SEQRES 50 A 781 PHE ASN GLN ILE VAL ASN GLY VAL ASN TYR SER PRO ARG SEQRES 51 A 781 GLN GLN PHE LEU SER LYS ASP GLY GLY ILE THR TRP SER SEQRES 52 A 781 LEU LEU GLU ALA ASN ASN ALA ASN VAL PHE SER ASN ILE SEQRES 53 A 781 SER THR GLY THR VAL ASP ALA SER ILE THR ARG PHE GLU SEQRES 54 A 781 GLN SER ASP GLY SER HIS PHE LEU LEU PHE THR ASN PRO SEQRES 55 A 781 GLN GLY ASN PRO ALA GLY THR ASN GLY ARG GLN ASN LEU SEQRES 56 A 781 GLY LEU TRP PHE SER PHE ASP GLU GLY VAL THR TRP LYS SEQRES 57 A 781 GLY PRO ILE GLN LEU VAL ASN GLY ALA SER ALA TYR SER SEQRES 58 A 781 ASP ILE TYR GLN LEU ASP SER GLU ASN ALA ILE VAL ILE SEQRES 59 A 781 VAL GLU THR ASP ASN SER ASN MET ARG ILE LEU ARG MET SEQRES 60 A 781 PRO ILE THR LEU LEU LYS GLN LYS LEU THR LEU SER GLN SEQRES 61 A 781 ASN HET SIA A1784 21 HET CA A1779 1 HET CA A1780 1 HET CA A1781 1 HET CA A1782 1 HET TRS A1783 8 HET GOL A1778 6 HETNAM SIA O-SIALIC ACID HETNAM CA CALCIUM ION HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL HETNAM GOL GLYCEROL HETSYN TRS TRIS BUFFER FORMUL 2 SIA C11 H19 N O9 FORMUL 3 CA 4(CA 2+) FORMUL 7 TRS C4 H12 N O3 1+ FORMUL 8 GOL C3 H8 O3 FORMUL 9 HOH *586(H2 O) HELIX 1 1 ASP A 34 ASP A 38 5 5 HELIX 2 2 SER A 39 GLY A 44 5 6 HELIX 3 3 SER A 82 GLY A 93 1 12 HELIX 4 4 THR A 146 GLU A 152 5 7 HELIX 5 5 THR A 279 ASN A 283 5 5 HELIX 6 6 GLN A 317 ARG A 321 5 5 HELIX 7 7 VAL A 348 LYS A 353 1 6 HELIX 8 8 GLU A 433 HIS A 438 1 6 HELIX 9 9 ASP A 507 GLN A 513 1 7 HELIX 10 10 ASP A 521 LEU A 525 5 5 HELIX 11 11 ASN A 671 PHE A 673 5 3 HELIX 12 12 ASP A 758 SER A 760 5 3 HELIX 13 13 ILE A 769 LYS A 773 1 5 HELIX 14 14 GLN A 774 LEU A 776 5 3 SHEET 1 AA 4 LEU A 26 ASN A 30 0 SHEET 2 AA 4 GLY A 202 ILE A 213 -1 O ILE A 209 N TYR A 29 SHEET 3 AA 4 PRO A 64 GLY A 70 -1 O TRP A 66 N TYR A 206 SHEET 4 AA 4 SER A 54 ASN A 59 -1 O SER A 54 N GLN A 69 SHEET 1 AB 6 LEU A 26 ASN A 30 0 SHEET 2 AB 6 GLY A 202 ILE A 213 -1 O ILE A 209 N TYR A 29 SHEET 3 AB 6 TRP A 94 GLY A 105 -1 O ARG A 95 N GLU A 212 SHEET 4 AB 6 HIS A 154 LEU A 161 -1 O HIS A 154 N MET A 100 SHEET 5 AB 6 SER A 167 PHE A 172 -1 O SER A 167 N LEU A 161 SHEET 6 AB 6 LYS A 175 ILE A 181 -1 O LYS A 175 N PHE A 172 SHEET 1 AC 6 MET A 46 GLN A 47 0 SHEET 2 AC 6 ALA A 75 TYR A 79 -1 O THR A 78 N MET A 46 SHEET 3 AC 6 MET A 190 ASN A 195 -1 O ILE A 191 N TYR A 79 SHEET 4 AC 6 TYR A 111 ALA A 113 -1 O TYR A 111 N VAL A 192 SHEET 5 AC 6 GLN A 117 VAL A 119 -1 O VAL A 119 N TYR A 112 SHEET 6 AC 6 THR A 184 ALA A 185 -1 O THR A 184 N ARG A 118 SHEET 1 AD 3 PRO A 121 LEU A 125 0 SHEET 2 AD 3 LEU A 131 PHE A 135 -1 O VAL A 132 N SER A 124 SHEET 3 AD 3 THR A 142 ALA A 145 -1 O THR A 142 N VAL A 133 SHEET 1 AE 4 ASP A 216 PHE A 219 0 SHEET 2 AE 4 MET A 762 PRO A 768 -1 O MET A 762 N ILE A 218 SHEET 3 AE 4 ASN A 750 GLU A 756 -1 O ALA A 751 N MET A 767 SHEET 4 AE 4 SER A 741 GLN A 745 -1 O ASP A 742 N ILE A 754 SHEET 1 AF 4 ARG A 224 ALA A 230 0 SHEET 2 AF 4 VAL A 238 VAL A 246 -1 O THR A 239 N VAL A 229 SHEET 3 AF 4 THR A 257 SER A 265 -1 O THR A 257 N VAL A 246 SHEET 4 AF 4 LEU A 276 ASN A 277 -1 O LEU A 276 N THR A 262 SHEET 1 AG 4 PHE A 288 ASP A 298 0 SHEET 2 AG 4 THR A 303 PRO A 312 -1 O THR A 303 N ASP A 298 SHEET 3 AG 4 GLY A 329 ASP A 336 -1 O GLY A 329 N ARG A 310 SHEET 4 AG 4 ILE A 346 ASP A 347 -1 O ILE A 346 N TYR A 332 SHEET 1 AH 4 PHE A 288 ASP A 298 0 SHEET 2 AH 4 THR A 303 PRO A 312 -1 O THR A 303 N ASP A 298 SHEET 3 AH 4 GLY A 329 ASP A 336 -1 O GLY A 329 N ARG A 310 SHEET 4 AH 4 ASN A 341 TRP A 342 -1 O ASN A 341 N ASP A 336 SHEET 1 AI 7 GLN A 461 TRP A 466 0 SHEET 2 AI 7 THR A 453 VAL A 458 -1 O THR A 454 N TRP A 466 SHEET 3 AI 7 HIS A 441 SER A 448 -1 O GLU A 444 N PHE A 457 SHEET 4 AI 7 TRP A 380 GLY A 391 -1 O TRP A 380 N TYR A 447 SHEET 5 AI 7 GLY A 487 GLN A 498 -1 O ARG A 488 N VAL A 389 SHEET 6 AI 7 PHE A 357 GLY A 361 -1 O PHE A 357 N VAL A 491 SHEET 7 AI 7 MET A 536 TYR A 539 -1 O MET A 536 N ALA A 360 SHEET 1 AJ 6 GLN A 461 TRP A 466 0 SHEET 2 AJ 6 THR A 453 VAL A 458 -1 O THR A 454 N TRP A 466 SHEET 3 AJ 6 HIS A 441 SER A 448 -1 O GLU A 444 N PHE A 457 SHEET 4 AJ 6 TRP A 380 GLY A 391 -1 O TRP A 380 N TYR A 447 SHEET 5 AJ 6 GLY A 487 GLN A 498 -1 O ARG A 488 N VAL A 389 SHEET 6 AJ 6 HIS A 501 PHE A 506 -1 O HIS A 501 N GLN A 498 SHEET 1 AK10 ILE A 428 GLN A 431 0 SHEET 2 AK10 LEU A 417 LEU A 421 -1 O LEU A 417 N LEU A 430 SHEET 3 AK10 ARG A 403 ILE A 411 -1 O THR A 408 N ASN A 420 SHEET 4 AK10 GLU A 469 VAL A 470 -1 O GLU A 469 N LYS A 404 SHEET 5 AK10 ARG A 403 ILE A 411 -1 O LYS A 404 N GLU A 469 SHEET 6 AK10 THR A 528 GLY A 533 0 SHEET 7 AK10 GLY A 364 ASN A 371 -1 O SER A 365 N THR A 532 SHEET 8 AK10 ASN A 474 ASN A 480 -1 O ILE A 476 N ARG A 370 SHEET 9 AK10 ASN A 394 ASP A 400 -1 O GLN A 395 N GLY A 479 SHEET 10 AK10 ARG A 403 ILE A 411 -1 O ARG A 403 N ASP A 400 SHEET 1 AL 7 SER A 543 ASN A 545 0 SHEET 2 AL 7 LEU A 568 LEU A 575 -1 O ILE A 573 N ASN A 545 SHEET 3 AL 7 ILE A 552 THR A 553 -1 O ILE A 552 N ILE A 569 SHEET 4 AL 7 LEU A 568 LEU A 575 -1 O ILE A 569 N ILE A 552 SHEET 5 AL 7 GLN A 595 THR A 596 0 SHEET 6 AL 7 LEU A 580 SER A 587 -1 O TYR A 586 N GLN A 595 SHEET 7 AL 7 LEU A 568 LEU A 575 -1 O LEU A 568 N SER A 587 SHEET 1 AM 2 PHE A 604 TRP A 606 0 SHEET 2 AM 2 LEU A 612 THR A 614 -1 O GLU A 613 N ARG A 605 SHEET 1 AN 4 GLU A 616 GLU A 624 0 SHEET 2 AN 4 LEU A 630 ASP A 637 -1 O LEU A 631 N VAL A 623 SHEET 3 AN 4 ARG A 650 SER A 655 -1 O GLN A 651 N ALA A 634 SHEET 4 AN 4 SER A 663 ASN A 669 -1 O SER A 663 N LEU A 654 SHEET 1 AO 2 ILE A 641 VAL A 642 0 SHEET 2 AO 2 VAL A 645 ASN A 646 -1 O VAL A 645 N VAL A 642 SHEET 1 AP 4 SER A 684 GLU A 689 0 SHEET 2 AP 4 HIS A 695 PRO A 702 -1 O PHE A 696 N PHE A 688 SHEET 3 AP 4 LEU A 715 SER A 720 -1 O GLY A 716 N ASN A 701 SHEET 4 AP 4 LYS A 728 GLN A 732 -1 O LYS A 728 N PHE A 719 LINK CA CA A1779 OD1 ASN A 256 LINK CA CA A1779 OD1 ASP A 289 LINK CA CA A1779 OD2 ASP A 289 LINK CA CA A1779 O THR A 313 LINK CA CA A1779 OG1 THR A 313 LINK CA CA A1779 O ASN A 256 LINK CA CA A1779 O ALA A 253 LINK CA CA A1780 O PRO A 548 LINK CA CA A1780 OD2 ASP A 621 LINK CA CA A1780 OD1 ASP A 621 LINK CA CA A1780 OD1 ASP A 682 LINK CA CA A1780 OD2 ASP A 682 LINK CA CA A1780 O ALA A 683 LINK CA CA A1781 O PHE A 578 LINK CA CA A1781 OD1 ASP A 320 LINK CA CA A1781 C TRS A1783 LINK CA CA A1781 C1 TRS A1783 LINK CA CA A1781 N TRS A1783 LINK CA CA A1781 O1 TRS A1783 LINK CA CA A1781 O2 TRS A1783 LINK CA CA A1781 OD2 ASP A 320 LINK CA CA A1782 O HOH Z 201 LINK CA CA A1782 OD1 ASP A 286 CISPEP 1 GLY A 221 PRO A 222 0 -0.89 CISPEP 2 ASN A 705 PRO A 706 0 0.50 SITE 1 AC1 5 GLN A 317 ASN A 318 GLU A 619 ASP A 637 SITE 2 AC1 5 HOH Z 228 SITE 1 AC2 4 ALA A 253 ASN A 256 ASP A 289 THR A 313 SITE 1 AC3 4 PRO A 548 ASP A 621 ASP A 682 ALA A 683 SITE 1 AC4 2 ASP A 320 PHE A 578 SITE 1 AC5 2 ASP A 286 HOH Z 201 SITE 1 AC6 10 ASP A 320 GLN A 343 ILE A 346 PHE A 578 SITE 2 AC6 10 GLU A 616 PHE A 638 HOH Z 235 HOH Z 240 SITE 3 AC6 10 HOH Z 250 HOH Z 251 SITE 1 AC7 9 ARG A 74 MET A 107 ARG A 118 GLN A 188 SITE 2 AC7 9 GLY A 196 SER A 197 SER A 198 HOH Z 44 SITE 3 AC7 9 HOH Z 586 CRYST1 70.310 74.910 151.615 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 0.014223 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013349 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006596 0.00000