HEADER HYDROLASE 09-JUN-04 1W0O
TITLE VIBRIO CHOLERAE SIALIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NEURAMINIDASE, NANASE;
COMPND 5 EC: 3.2.1.18
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666
KEYWDS VIBRIO CHOLERAE, SIALIDASE, GLYCOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.MOUSTAFA,H.CONNARIS,M.TAYLOR,V.ZAITSEV,J.C.WILSON,M.J.KIEFEL,M.VON-
AUTHOR 2 ITZSTEIN,G.TAYLOR
REVDAT 5 29-JUL-20 1W0O 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 25-MAR-15 1W0O 1 JRNL REMARK VERSN FORMUL
REVDAT 3 24-FEB-09 1W0O 1 VERSN
REVDAT 2 24-SEP-04 1W0O 1 JRNL
REVDAT 1 08-JUL-04 1W0O 0
JRNL AUTH I.MOUSTAFA,H.CONNARIS,M.TAYLOR,V.ZAITSEV,J.C.WILSONM,
JRNL AUTH 2 J.KIEFEL,M.VON-ITZSTEIN,G.TAYLOR
JRNL TITL SIALIC ACID RECOGNITION BY VIBRIO CHOLERAE NEURAMINIDASE
JRNL REF J.BIOL.CHEM. V. 279 40819 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15226294
JRNL DOI 10.1074/JBC.M404965200
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 58159
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) : 0.179
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.300
REMARK 3 FREE R VALUE TEST SET COUNT : 5918
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 : 45
REMARK 3 SOLVENT ATOMS : 920
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) : 0.71700
REMARK 3 B22 (A**2) : 0.48400
REMARK 3 B33 (A**2) : -1.20100
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) : 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) : 1.316
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 : 0.38
REMARK 3 BSOL : 57.08
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 : DANA.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 : DANA.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 1W0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1290020132.
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 : 63699
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 91.0
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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 (%): 47.21
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 51 -124.62 45.81
REMARK 500 ALA A 60 -16.15 -49.52
REMARK 500 MET A 190 159.11 174.25
REMARK 500 ILE A 225 72.29 62.47
REMARK 500 ASN A 283 44.54 -144.73
REMARK 500 ASP A 292 73.29 48.13
REMARK 500 ALA A 316 -157.73 -145.72
REMARK 500 PRO A 327 25.82 -62.64
REMARK 500 SER A 402 -40.86 -131.74
REMARK 500 PRO A 516 -9.24 -58.41
REMARK 500 ARG A 577 -58.29 -152.69
REMARK 500 SER A 610 -31.23 -154.60
REMARK 500 SER A 618 -98.82 -133.52
REMARK 500 PHE A 638 -134.59 57.78
REMARK 500 SER A 648 -179.63 71.11
REMARK 500 ALA A 667 12.89 58.70
REMARK 500 ASN A 668 78.27 -110.35
REMARK 500 ASN A 669 -147.23 -129.71
REMARK 500 ASN A 714 80.32 43.01
REMARK 500 ALA A 739 -117.11 -116.07
REMARK 500 THR A 757 -127.79 -127.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2036 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A2081 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH A2086 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A2101 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A2157 DISTANCE = 6.30 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1779 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 253 O
REMARK 620 2 ASN A 256 OD1 79.6
REMARK 620 3 ASN A 256 O 89.4 72.6
REMARK 620 4 ASP A 289 OD1 167.2 87.7 85.1
REMARK 620 5 ASP A 289 OD2 129.1 94.0 137.1 53.1
REMARK 620 6 THR A 313 OG1 107.2 150.1 78.3 83.0 102.7
REMARK 620 7 THR A 313 O 72.1 136.5 137.3 119.4 79.9 71.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1782 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 286 OD1
REMARK 620 2 HOH A2367 O 81.8
REMARK 620 3 HOH A2426 O 87.8 74.5
REMARK 620 4 HOH A2433 O 88.4 84.9 159.4
REMARK 620 5 HOH A2434 O 77.8 142.6 134.9 63.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1781 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 320 OD2
REMARK 620 2 ASP A 320 OD1 50.7
REMARK 620 3 PHE A 578 O 102.4 87.8
REMARK 620 4 HOH A2466 O 95.9 107.2 161.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1780 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 548 O
REMARK 620 2 ASP A 621 OD1 111.0
REMARK 620 3 ASP A 621 OD2 89.9 52.9
REMARK 620 4 ASP A 682 OD1 94.0 87.9 138.8
REMARK 620 5 ASP A 682 OD2 87.9 139.8 166.6 54.6
REMARK 620 6 ALA A 683 O 174.2 74.5 92.3 87.8 88.7
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KIT RELATED DB: PDB
REMARK 900 VIBRIO CHOLERAE NEURAMINIDASE
REMARK 900 RELATED ID: 1W0P RELATED DB: PDB
REMARK 900 VIBRIO CHOLERAE SIALIDASE
DBREF 1W0O 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 DAN A1778 20
HET CA A1779 1
HET CA A1780 1
HET CA A1781 1
HET CA A1782 1
HET SIA A1783 21
HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
HETNAM CA CALCIUM ION
HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID
FORMUL 2 DAN C11 H17 N O8
FORMUL 3 CA 4(CA 2+)
FORMUL 7 SIA C11 H19 N O9
FORMUL 8 HOH *920(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 ALA A 508 GLN A 513 1 6
HELIX 10 10 SER A 608 SER A 610 5 3
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 ALA A 65 GLY A 70 -1 O TRP A 66 N TYR A 206
SHEET 4 AA 4 SER A 54 THR A 58 -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 ASN A 189 ASN A 195 -1 O ILE A 191 N TYR A 79
SHEET 4 AC 6 TYR A 111 ASN A 114 -1 O TYR A 111 N VAL A 192
SHEET 5 AC 6 GLN A 117 VAL A 119 -1 O GLN A 117 N ASN A 114
SHEET 6 AC 6 THR A 184 ALA A 185 -1 O THR A 184 N ARG A 118
SHEET 1 AD 4 ILE A 108 THR A 109 0
SHEET 2 AD 4 PRO A 121 LEU A 125 -1 O ILE A 123 N ILE A 108
SHEET 3 AD 4 LEU A 131 PHE A 135 -1 O VAL A 132 N SER A 124
SHEET 4 AD 4 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 ASP A 507 -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 599 0
SHEET 6 AL 7 LEU A 580 SER A 587 -1 O SER A 584 N GLY A 597
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 LYS A 607 0
SHEET 2 AM 2 ILE A 611 THR A 614 -1 O ILE A 611 N LYS A 607
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 O ALA A 253 CA CA A1779 1555 1555 2.26
LINK OD1 ASN A 256 CA CA A1779 1555 1555 2.31
LINK O ASN A 256 CA CA A1779 1555 1555 2.28
LINK OD1 ASP A 286 CA CA A1782 1555 1555 2.35
LINK OD1 ASP A 289 CA CA A1779 1555 1555 2.61
LINK OD2 ASP A 289 CA CA A1779 1555 1555 2.26
LINK OG1 THR A 313 CA CA A1779 1555 1555 2.35
LINK O THR A 313 CA CA A1779 1555 1555 2.52
LINK OD2 ASP A 320 CA CA A1781 1555 1555 2.41
LINK OD1 ASP A 320 CA CA A1781 1555 1555 2.67
LINK O PRO A 548 CA CA A1780 1555 1555 2.37
LINK O PHE A 578 CA CA A1781 1555 1555 2.32
LINK OD1 ASP A 621 CA CA A1780 1555 1555 2.50
LINK OD2 ASP A 621 CA CA A1780 1555 1555 2.41
LINK OD1 ASP A 682 CA CA A1780 1555 1555 2.36
LINK OD2 ASP A 682 CA CA A1780 1555 1555 2.43
LINK O ALA A 683 CA CA A1780 1555 1555 2.34
LINK CA CA A1781 O HOH A2466 1555 1555 2.32
LINK CA CA A1782 O HOH A2367 1555 1555 2.43
LINK CA CA A1782 O HOH A2426 1555 1555 2.28
LINK CA CA A1782 O HOH A2433 1555 1555 2.55
LINK CA CA A1782 O HOH A2434 1555 1555 2.70
CISPEP 1 GLY A 221 PRO A 222 0 0.36
CISPEP 2 ASN A 705 PRO A 706 0 -0.20
CISPEP 3 GLY A 729 PRO A 730 0 0.33
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
(ATOM LINES ARE NOT SHOWN.)
END
