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HEADER HYDROLASE 03-OCT-98 2SLI TITLE LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7- TITLE 2 ANHYDRO-NEU5AC, THE REACTION PRODUCT COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTRAMOLECULAR TRANS-SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DEVOID OF N-TERMINAL 28 RESIDUES; COMPND 5 EC: 3.2.1.18; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACROBDELLA DECORA; SOURCE 3 ORGANISM_COMMON: NORTH AMERICAN LEECH; SOURCE 4 GENE: T7; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 7 EXPRESSION_SYSTEM_VARIANT: DE3; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET 15B; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: E2-M10; SOURCE 11 EXPRESSION_SYSTEM_GENE: T7 KEYWDS HYDROLASE, INTRAMOLECULAR TRANS-SIALIDASE, NEURAMINIDASE EXPDTA X-RAY DIFFRACTION AUTHOR Y.LUO,S.C.LI,Y.T.LI,M.LUO REVDAT 1 27-APR-99 2SLI 0 JRNL AUTH Y.LUO,S.C.LI,Y.T.LI,M.LUO JRNL TITL THE 1.8 A STRUCTURES OF LEECH INTRAMOLECULAR JRNL TITL 2 TRANS-SIALIDASE COMPLEXES: EVIDENCE OF ITS JRNL TITL 3 ENZYMATIC MECHANISM. JRNL REF J.MOL.BIOL. V. 285 323 1999 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.85 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.2 REMARK 3 NUMBER OF REFLECTIONS : 63348 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 : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 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 : 5257 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 20 REMARK 3 SOLVENT ATOMS : 593 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 11.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.90 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) : 1.63 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 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 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : PARAM19.SOL REMARK 3 PARAMETER FILE 3 : PARAM3.CHO REMARK 3 PARAMETER FILE 4 : SKD.PAR REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PARHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL REMARK 3 TOPOLOGY FILE 3 : SKD.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2SLI 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 (2007-03-18) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-MAY-1997 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.90 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/MSC RU-H2R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE(002) REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63696 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04900 REMARK 200 FOR THE DATA SET : 12.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 67.6 REMARK 200 DATA REDUNDANCY IN SHELL : 1.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.17300 REMARK 200 FOR SHELL : 6.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR 3.85 REMARK 200 STARTING MODEL: NATIVE STRUCTURE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 40.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.9 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,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 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 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 VAL A 539 CA VAL A 539 CB 0.044 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 LEU A 121 CA - CB - CG ANGL. DEV. = 11.0 DEGREES REMARK 500 ILE A 151 N - CA - C ANGL. DEV. =-10.4 DEGREES REMARK 500 VAL A 233 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 ALA A 311 N - CA - C ANGL. DEV. =-12.2 DEGREES REMARK 500 LYS A 320 N - CA - C ANGL. DEV. =-24.9 DEGREES REMARK 500 TYR A 373 N - CA - C ANGL. DEV. =-10.1 DEGREES REMARK 500 ASP A 381 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 LEU A 393 CA - CB - CG ANGL. DEV. = 10.8 DEGREES REMARK 500 ASN A 442 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 SER A 476 N - CA - C ANGL. DEV. =-11.6 DEGREES REMARK 500 LEU A 537 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 GLY A 540 N - CA - C ANGL. DEV. =-12.5 DEGREES REMARK 500 LEU A 560 CA - CB - CG ANGL. DEV. = 11.2 DEGREES REMARK 500 GLN A 723 N - CA - C ANGL. DEV. = 12.3 DEGREES REMARK 500 LEU A 726 CA - CB - CG ANGL. DEV. = 10.2 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 THR A 166 144.26 76.20 REMARK 500 LYS A 320 74.12 104.56 DBREF 2SLI A 81 759 UNP Q27701 NANL_MACDE 81 759 SEQRES 1 A 679 ILE PRO GLU GLY ILE LEU MET GLU LYS ASN ASN VAL ASP SEQRES 2 A 679 ILE ALA GLU GLY GLN GLY TYR SER LEU ASP GLN GLU ALA SEQRES 3 A 679 GLY ALA LYS TYR VAL LYS ALA MET THR GLN GLY THR ILE SEQRES 4 A 679 ILE LEU SER TYR LYS SER THR SER GLU ASN GLY ILE GLN SEQRES 5 A 679 SER LEU PHE SER VAL GLY ASN SER THR ALA GLY ASN GLN SEQRES 6 A 679 ASP ARG HIS PHE HIS ILE TYR ILE THR ASN SER GLY GLY SEQRES 7 A 679 ILE GLY ILE GLU LEU ARG ASN THR ASP GLY VAL PHE ASN SEQRES 8 A 679 TYR THR LEU ASP ARG PRO ALA SER VAL ARG ALA LEU TYR SEQRES 9 A 679 LYS GLY GLU ARG VAL PHE ASN THR VAL ALA LEU LYS ALA SEQRES 10 A 679 ASP ALA ALA ASN LYS GLN CYS ARG LEU PHE ALA ASN GLY SEQRES 11 A 679 GLU LEU LEU ALA THR LEU ASP LYS ASP ALA PHE LYS PHE SEQRES 12 A 679 ILE SER ASP ILE THR GLY VAL ASP ASN VAL THR LEU GLY SEQRES 13 A 679 GLY THR LYS ARG GLN GLY LYS ILE ALA TYR PRO PHE GLY SEQRES 14 A 679 GLY THR ILE GLY ASP ILE LYS VAL TYR SER ASN ALA LEU SEQRES 15 A 679 SER ASP GLU GLU LEU ILE GLN ALA THR GLY VAL THR THR SEQRES 16 A 679 TYR GLY GLU ASN ILE PHE TYR ALA GLY ASP VAL THR GLU SEQRES 17 A 679 SER ASN TYR PHE ARG ILE PRO SER LEU LEU THR LEU SER SEQRES 18 A 679 THR GLY THR VAL ILE SER ALA ALA ASP ALA ARG TYR GLY SEQRES 19 A 679 GLY THR HIS ASP SER LYS SER LYS ILE ASN ILE ALA PHE SEQRES 20 A 679 ALA LYS SER THR ASP GLY GLY ASN THR TRP SER GLU PRO SEQRES 21 A 679 THR LEU PRO LEU LYS PHE ASP ASP TYR ILE ALA LYS ASN SEQRES 22 A 679 ILE ASP TRP PRO ARG ASP SER VAL GLY LYS ASN VAL GLN SEQRES 23 A 679 ILE GLN GLY SER ALA SER TYR ILE ASP PRO VAL LEU LEU SEQRES 24 A 679 GLU ASP LYS LEU THR LYS ARG ILE PHE LEU PHE ALA ASP SEQRES 25 A 679 LEU MET PRO ALA GLY ILE GLY SER SER ASN ALA SER VAL SEQRES 26 A 679 GLY SER GLY PHE LYS GLU VAL ASN GLY LYS LYS TYR LEU SEQRES 27 A 679 LYS LEU ARG TRP HIS LYS ASP ALA GLY ARG ALA TYR ASP SEQRES 28 A 679 TYR THR ILE ARG GLU LYS GLY VAL ILE TYR ASN ASP ALA SEQRES 29 A 679 THR ASN GLN PRO THR GLU PHE ARG VAL ASP GLY GLU TYR SEQRES 30 A 679 ASN LEU TYR GLN HIS ASP THR ASN LEU THR CYS LYS GLN SEQRES 31 A 679 TYR ASP TYR ASN PHE SER GLY ASN ASN LEU ILE GLU SER SEQRES 32 A 679 LYS THR ASP VAL ASP VAL ASN MET ASN ILE PHE TYR LYS SEQRES 33 A 679 ASN SER VAL PHE LYS ALA PHE PRO THR ASN TYR LEU ALA SEQRES 34 A 679 MET ARG TYR SER ASP ASP GLU GLY ALA SER TRP SER ASP SEQRES 35 A 679 LEU ASP ILE VAL SER SER PHE LYS PRO GLU VAL SER LYS SEQRES 36 A 679 PHE LEU VAL VAL GLY PRO GLY ILE GLY LYS GLN ILE SER SEQRES 37 A 679 THR GLY GLU ASN ALA GLY ARG LEU LEU VAL PRO LEU TYR SEQRES 38 A 679 SER LYS SER SER ALA GLU LEU GLY PHE MET TYR SER ASP SEQRES 39 A 679 ASP HIS GLY ASP ASN TRP THR TYR VAL GLU ALA ASP ASN SEQRES 40 A 679 LEU THR GLY GLY ALA THR ALA GLU ALA GLN ILE VAL GLU SEQRES 41 A 679 MET PRO ASP GLY SER LEU LYS THR TYR LEU ARG THR GLY SEQRES 42 A 679 SER ASN CYS ILE ALA GLU VAL THR SER ILE ASP GLY GLY SEQRES 43 A 679 GLU THR TRP SER ASP ARG VAL PRO LEU GLN GLY ILE SER SEQRES 44 A 679 THR THR SER TYR GLY THR GLN LEU SER VAL ILE ASN TYR SEQRES 45 A 679 SER GLN PRO ILE ASP GLY LYS PRO ALA ILE ILE LEU SER SEQRES 46 A 679 SER PRO ASN ALA THR ASN GLY ARG LYS ASN GLY LYS ILE SEQRES 47 A 679 TRP ILE GLY LEU VAL ASN ASP THR GLY ASN THR GLY ILE SEQRES 48 A 679 ASP LYS TYR SER VAL GLU TRP LYS TYR SER TYR ALA VAL SEQRES 49 A 679 ASP THR PRO GLN MET GLY TYR SER TYR SER CYS LEU ALA SEQRES 50 A 679 GLU LEU PRO ASP GLY GLN VAL GLY LEU LEU TYR GLU LYS SEQRES 51 A 679 TYR ASP SER TRP SER ARG ASN GLU LEU HIS LEU LYS ASP SEQRES 52 A 679 ILE LEU LYS PHE GLU LYS TYR SER ILE SER GLU LEU THR SEQRES 53 A 679 GLY GLN ALA HET SKD 467 20 HETNAM SKD 2-ACETYLAMINO-7-(1,2-DIHYDROXY-ETHYL)-3-HYDROXY-6,8- HETNAM 2 SKD DIOXA-BICYCLO[3.2.1]OCTANE-5-CARBOXYLIC ACID HETSYN SKD 2,7-ANHYDRO-NEU5AC FORMUL 2 SKD C11 H17 N O8 FORMUL 3 HOH *593(H2 O) HELIX 1 1 ALA A 108 ALA A 113 1 6 HELIX 2 2 ILE A 224 ASP A 226 5 3 HELIX 3 3 ASP A 264 VAL A 273 1 10 HELIX 4 4 GLY A 362 ASN A 364 5 3 HELIX 5 5 SER A 400 ASN A 402 5 3 HELIX 6 6 GLU A 436 GLY A 438 5 3 HELIX 7 7 SER A 527 PHE A 529 5 3 HELIX 8 8 GLY A 690 ASP A 692 5 3 HELIX 9 9 ILE A 752 LEU A 755 1 4 SHEET 1 A 6 VAL A 92 ILE A 94 0 SHEET 2 A 6 GLY A 250 TYR A 258 -1 N ILE A 252 O VAL A 92 SHEET 3 A 6 GLY A 117 SER A 125 -1 N LYS A 124 O THR A 251 SHEET 4 A 6 ASN A 191 ASP A 198 -1 N ALA A 197 O GLY A 117 SHEET 5 A 6 GLN A 203 ALA A 208 -1 N PHE A 207 O ALA A 194 SHEET 6 A 6 GLU A 211 ASP A 217 -1 N LEU A 216 O CYS A 204 SHEET 1 B 5 ASN A 232 LEU A 235 0 SHEET 2 B 5 ILE A 131 GLY A 138 -1 N GLY A 138 O ASN A 232 SHEET 3 B 5 ARG A 147 THR A 154 -1 N ILE A 153 O GLN A 132 SHEET 4 B 5 ILE A 159 ASN A 165 -1 N ARG A 164 O HIS A 148 SHEET 5 B 5 ASN A 171 ARG A 176 -1 N ARG A 176 O ILE A 159 SHEET 1 C 2 THR A 238 ARG A 240 0 SHEET 2 C 2 LYS A 243 ALA A 245 -1 N ALA A 245 O THR A 238 SHEET 1 D 3 TYR A 291 ARG A 293 0 SHEET 2 D 3 VAL A 305 ARG A 312 -1 N ARG A 312 O TYR A 291 SHEET 3 D 3 ILE A 323 SER A 330 -1 N SER A 330 O VAL A 305 SHEET 1 E 2 SER A 296 THR A 299 0 SHEET 2 E 2 VAL A 305 ALA A 308 -1 N ALA A 308 O SER A 296 SHEET 1 F 3 SER A 372 ILE A 374 0 SHEET 2 F 3 ILE A 387 MET A 394 -1 N MET A 394 O SER A 372 SHEET 3 F 3 ASN A 506 SER A 513 -1 N SER A 513 O ILE A 387 SHEET 1 G 2 VAL A 377 ASP A 381 0 SHEET 2 G 2 ARG A 386 PHE A 390 -1 N PHE A 390 O VAL A 377 SHEET 1 H 4 PHE A 409 VAL A 412 0 SHEET 2 H 4 LYS A 415 LEU A 420 -1 N TYR A 417 O LYS A 410 SHEET 3 H 4 TYR A 432 ILE A 434 -1 N ILE A 434 O LEU A 418 SHEET 4 H 4 ILE A 440 ASN A 442 -1 N TYR A 441 O THR A 433 SHEET 1 I 2 LEU A 420 TRP A 422 0 SHEET 2 I 2 PHE A 500 ALA A 502 -1 N LYS A 501 O ARG A 421 SHEET 1 J 2 PHE A 451 VAL A 453 0 SHEET 2 J 2 LEU A 459 GLN A 461 -1 N TYR A 460 O ARG A 452 SHEET 1 K 2 THR A 467 LYS A 469 0 SHEET 2 K 2 ASP A 488 ASN A 490 -1 N VAL A 489 O CYS A 468 SHEET 1 L 2 TYR A 471 SER A 476 0 SHEET 2 L 2 ASN A 479 LYS A 484 -1 N SER A 483 O ASP A 472 SHEET 1 M 4 PHE A 536 VAL A 539 0 SHEET 2 M 4 LEU A 556 LYS A 563 -1 N LYS A 563 O PHE A 536 SHEET 3 M 4 LEU A 568 SER A 573 -1 N SER A 573 O LEU A 556 SHEET 4 M 4 THR A 581 GLU A 584 -1 N VAL A 583 O PHE A 570 SHEET 1 N 3 ALA A 596 GLU A 600 0 SHEET 2 N 3 LEU A 606 LEU A 610 -1 N TYR A 609 O GLN A 597 SHEET 3 N 3 ALA A 618 SER A 622 -1 N SER A 622 O LEU A 606 SHEET 1 O 4 SER A 648 TYR A 652 0 SHEET 2 O 4 ALA A 661 PRO A 667 -1 N SER A 665 O SER A 648 SHEET 3 O 4 GLY A 676 ASP A 685 -1 N GLY A 681 O ILE A 662 SHEET 4 O 4 TYR A 694 ALA A 703 -1 N TYR A 702 O ILE A 678 SHEET 1 P 3 SER A 714 GLU A 718 0 SHEET 2 P 3 VAL A 724 GLU A 729 -1 N LEU A 727 O CYS A 715 SHEET 3 P 3 LEU A 745 TYR A 750 -1 N TYR A 750 O VAL A 724 SHEET 1 Q 2 ILE A 85 ASN A 90 0 SHEET 2 Q 2 ASP A 254 TYR A 258 -1 N VAL A 257 O LEU A 86 CRYST1 46.364 69.275 72.469 113.48 95.41 107.31 P 1 1 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 0.021568 0.006722 0.005661 0.00000 SCALE2 0.000000 0.015120 0.007592 0.00000 SCALE3 0.000000 0.000000 0.015510 0.00000