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HEADER HYDROLASE 21-OCT-02 1N1V TITLE TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH DANA COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUE 23-660; COMPND 5 EC: 3.2.1.18; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA RANGELI; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 4 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PTRCHIS A KEYWDS BETA PROPELLER, LECTIN-LIKE FOLD EXPDTA X-RAY DIFFRACTION AUTHOR M.F.AMAYA,A.BUSCHIAZZO,T.NGUYEN,P.M.ALZARI REVDAT 1 07-JAN-03 1N1V 0 JRNL AUTH M.F.AMAYA,A.BUSCHIAZZO,T.NGUYEN,P.M.ALZARI JRNL TITL THE HIGH RESOLUTION STRUCTURES OF FREE AND JRNL TITL 2 INHIBITOR-BOUND TRYPANOSOMA RANGELI SIALIDASE AND JRNL TITL 3 ITS COMPARISON WITH T. CRUZI TRANS-SIALIDASE JRNL REF J.MOL.BIOL. V. 325 773 2003 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.BUSCHIAZZO,G.A.TAVARES,O.CAMPETELLA,S.SPINELLI, REMARK 1 AUTH 2 M.L.CREMONA,G.PARIS,M.F.AMAYA,A.C.FRASCH,P.M.ALZARI REMARK 1 TITL STRUCTURAL BASIS OF SIALYLTRANSFERASE ACTIVITY IN REMARK 1 TITL 2 TRYPANOSOMAL SIALIDASES REMARK 1 REF EMBO J. V. 19 16 2000 REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.94 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.5 REMARK 3 NUMBER OF REFLECTIONS : 37736 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 + TEST SET) : 0.180 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.219 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2010 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW : 2.15 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1646 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.1960 REMARK 3 BIN FREE R VALUE SET COUNT : 92 REMARK 3 BIN FREE R VALUE : 0.2320 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 5148 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.15 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.01000 REMARK 3 B22 (A**2) : -0.01000 REMARK 3 B33 (A**2) : 0.01000 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4960 ; 0.011 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6747 ; 1.469 ; 1.941 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 626 ; 4.764 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 843 ;16.735 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 758 ; 0.102 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3766 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2311 ; 0.224 ; 0.300 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 613 ; 0.135 ; 0.500 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 34 ; 0.219 ; 0.300 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.087 ; 0.500 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3107 ; 0.704 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5006 ; 1.290 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1853 ; 1.977 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1741 ; 3.158 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1N1V 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 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB017414. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JUN-2000 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39923 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 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 (%) : 89.4 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05200 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14 REMARK 200 COMPLETENESS FOR SHELL (%) : 52.3 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.20800 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: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1N1S REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.11 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-8000, SODIUM CACODYLATE, REMARK 280 AMMONIUM SULFATE, PH 7, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291K 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 37.93100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.91050 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.70200 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.91050 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.93100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.70200 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 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 THR A 407 REMARK 465 PRO A 408 REMARK 465 PRO A 409 REMARK 465 SER A 410 REMARK 465 LYS A 411 REMARK 465 GLY A 412 REMARK 465 GLY A 635 REMARK 465 GLY A 636 REMARK 465 ALA A 637 REMARK 465 GLY A 638 REMARK 465 THR A 639 REMARK 465 ALA A 640 REMARK 465 ALA A 641 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 26 OG REMARK 470 GLN A 126 CG CD OE1 NE2 REMARK 470 ARG A 128 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 159 CG CD CE NZ REMARK 470 GLU A 544 CG CD OE1 OE2 REMARK 470 LYS A 548 CG CD CE NZ REMARK 470 ASP A 634 CG OD1 OD2 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 99 SD MET A 99 CE 0.116 REMARK 500 MET A 317 SD MET A 317 CE -0.091 REMARK 500 PRO A 568 CB PRO A 568 CG 0.072 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 VAL A 367 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 ASP A 634 N - CA - C ANGL. DEV. = 10.6 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 VAL A 183 120.65 84.16 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MZ6 RELATED DB: PDB REMARK 900 NATURAL (GLYCOSYLATED) SIALIDASE FROM TRYPANOSOMA RANGELI REMARK 900 RELATED ID: 1MZ5 RELATED DB: PDB REMARK 900 NATURAL (GLYCOSYLATED) SIALIDASE FROM TRYPANOSOMA RANGELI REMARK 900 IN COMPLEX WITH THE INHIBITOR DANA REMARK 900 RELATED ID: 1N1S RELATED DB: PDB REMARK 900 TRYPANOSOMA RANGELI SIALIDASE REMARK 900 RELATED ID: 1N1T RELATED DB: PDB REMARK 900 TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH DANA AT 1.6 A REMARK 900 RELATED ID: 1N1Y RELATED DB: PDB REMARK 900 TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH SIALIC ACID REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE AUTHOR MAINTAINS THAT THE SEQUENCE IN REMARK 999 THE SEQUENCE DATABASE IS INCORRECT. DBREF 1N1V A 4 641 UNP O44049 O44049_TRYRA 23 660 SEQADV 1N1V ALA A 1 UNP O44049 CLONING ARTIFACT SEQADV 1N1V ALA A 2 UNP O44049 CLONING ARTIFACT SEQADV 1N1V SER A 3 UNP O44049 CLONING ARTIFACT SEQADV 1N1V ILE A 53 UNP O44049 THR 72 SEE REMARK 999 SEQADV 1N1V VAL A 180 UNP O44049 ILE 199 SEE REMARK 999 SEQADV 1N1V ALA A 189 UNP O44049 GLY 208 SEE REMARK 999 SEQADV 1N1V LEU A 375 UNP O44049 PHE 394 SEE REMARK 999 SEQADV 1N1V VAL A 609 UNP O44049 ILE 628 SEE REMARK 999 SEQRES 1 A 641 ALA ALA SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU SEQRES 2 A 641 PHE LYS ARG LYS ASN SER THR VAL PRO PHE GLU GLU SER SEQRES 3 A 641 ASN GLY THR ILE ARG GLU ARG VAL VAL HIS SER PHE ARG SEQRES 4 A 641 ILE PRO THR ILE VAL ASN VAL ASP GLY VAL MET VAL ALA SEQRES 5 A 641 ILE ALA ASP ALA ARG TYR GLU THR SER PHE ASP ASN SER SEQRES 6 A 641 PHE ILE GLU THR ALA VAL LYS TYR SER VAL ASP ASP GLY SEQRES 7 A 641 ALA THR TRP ASN THR GLN ILE ALA ILE LYS ASN SER ARG SEQRES 8 A 641 ALA SER SER VAL SER ARG VAL MET ASP ALA THR VAL ILE SEQRES 9 A 641 VAL LYS GLY ASN LYS LEU TYR ILE LEU VAL GLY SER PHE SEQRES 10 A 641 ASN LYS THR ARG ASN SER TRP THR GLN HIS ARG ASP GLY SEQRES 11 A 641 SER ASP TRP GLU PRO LEU LEU VAL VAL GLY GLU VAL THR SEQRES 12 A 641 LYS SER ALA ALA ASN GLY LYS THR THR ALA THR ILE SER SEQRES 13 A 641 TRP GLY LYS PRO VAL SER LEU LYS PRO LEU PHE PRO ALA SEQRES 14 A 641 GLU PHE ASP GLY ILE LEU THR LYS GLU PHE VAL GLY GLY SEQRES 15 A 641 VAL GLY ALA ALA ILE VAL ALA SER ASN GLY ASN LEU VAL SEQRES 16 A 641 TYR PRO VAL GLN ILE ALA ASP MET GLY GLY ARG VAL PHE SEQRES 17 A 641 THR LYS ILE MET TYR SER GLU ASP ASP GLY ASN THR TRP SEQRES 18 A 641 LYS PHE ALA GLU GLY ARG SER LYS PHE GLY CYS SER GLU SEQRES 19 A 641 PRO ALA VAL LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN SEQRES 20 A 641 ASN ARG VAL ASP GLY ASN ARG ARG LEU VAL TYR GLU SER SEQRES 21 A 641 SER ASP MET GLY LYS THR TRP VAL GLU ALA LEU GLY THR SEQRES 22 A 641 LEU SER HIS VAL TRP THR ASN SER PRO THR SER ASN GLN SEQRES 23 A 641 GLN ASP CYS GLN SER SER PHE VAL ALA VAL THR ILE GLU SEQRES 24 A 641 GLY LYS ARG VAL MET LEU PHE THR HIS PRO LEU ASN LEU SEQRES 25 A 641 LYS GLY ARG TRP MET ARG ASP ARG LEU HIS LEU TRP MET SEQRES 26 A 641 THR ASP ASN GLN ARG ILE PHE ASP VAL GLY GLN ILE SER SEQRES 27 A 641 ILE GLY ASP GLU ASN SER GLY TYR SER SER VAL LEU TYR SEQRES 28 A 641 LYS ASP ASP LYS LEU TYR SER LEU HIS GLU ILE ASN THR SEQRES 29 A 641 ASN ASP VAL TYR SER LEU VAL PHE VAL ARG LEU ILE GLY SEQRES 30 A 641 GLU LEU GLN LEU MET LYS SER VAL VAL ARG THR TRP LYS SEQRES 31 A 641 GLU GLU ASP ASN HIS LEU ALA SER ILE CYS THR PRO VAL SEQRES 32 A 641 VAL PRO ALA THR PRO PRO SER LYS GLY GLY CYS GLY ALA SEQRES 33 A 641 ALA VAL PRO THR ALA GLY LEU VAL GLY PHE LEU SER HIS SEQRES 34 A 641 SER ALA ASN GLY SER VAL TRP GLU ASP VAL TYR ARG CYS SEQRES 35 A 641 VAL ASP ALA ASN VAL ALA ASN ALA GLU ARG VAL PRO ASN SEQRES 36 A 641 GLY LEU LYS PHE ASN GLY VAL GLY GLY GLY ALA VAL TRP SEQRES 37 A 641 PRO VAL ALA ARG GLN GLY GLN THR ARG ARG TYR GLN PHE SEQRES 38 A 641 ALA ASN TYR ARG PHE THR LEU VAL ALA THR VAL THR ILE SEQRES 39 A 641 ASP GLU LEU PRO LYS GLY THR SER PRO LEU LEU GLY ALA SEQRES 40 A 641 GLY LEU GLU GLY PRO GLY ASP ALA LYS LEU LEU GLY LEU SEQRES 41 A 641 SER TYR ASP LYS ASN ARG GLN TRP ARG PRO LEU TYR GLY SEQRES 42 A 641 ALA ALA PRO ALA SER PRO THR GLY SER TRP GLU LEU HIS SEQRES 43 A 641 LYS LYS TYR HIS VAL VAL LEU THR MET ALA ASP ARG GLN SEQRES 44 A 641 GLY SER VAL TYR VAL ASP GLY GLN PRO LEU ALA GLY SER SEQRES 45 A 641 GLY ASN THR VAL VAL ARG GLY ALA THR LEU PRO ASP ILE SEQRES 46 A 641 SER HIS PHE TYR ILE GLY GLY PRO ARG SER LYS GLY ALA SEQRES 47 A 641 PRO THR ASP SER ARG VAL THR VAL THR ASN VAL VAL LEU SEQRES 48 A 641 TYR ASN ARG ARG LEU ASN SER SER GLU ILE ARG THR LEU SEQRES 49 A 641 PHE LEU SER GLN ASP MET ILE GLY THR ASP GLY GLY ALA SEQRES 50 A 641 GLY THR ALA ALA HET SO4 801 5 HET SO4 802 5 HET DAN 670 20 HETNAM SO4 SULFATE ION HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID FORMUL 2 SO4 2(O4 S 2-) FORMUL 4 DAN C11 H17 N O8 FORMUL 5 HOH *295(H2 O) HELIX 1 1 SER A 123 HIS A 127 5 5 HELIX 2 2 LYS A 164 PHE A 167 5 4 HELIX 3 3 LEU A 375 ILE A 399 1 25 HELIX 4 4 ALA A 471 GLY A 474 5 4 HELIX 5 5 TYR A 479 TYR A 484 5 6 HELIX 6 6 ASN A 617 GLN A 628 1 12 SHEET 1 A 4 SER A 9 PHE A 14 0 SHEET 2 A 4 VAL A 367 ARG A 374 -1 N LEU A 370 O PHE A 14 SHEET 3 A 4 LYS A 355 THR A 364 -1 O SER A 358 N VAL A 373 SHEET 4 A 4 SER A 347 LYS A 352 -1 O SER A 348 N LEU A 359 SHEET 1 B 2 THR A 20 GLU A 24 0 SHEET 2 B 2 ILE A 30 VAL A 34 -1 N ARG A 31 O PHE A 23 SHEET 1 C 4 SER A 37 VAL A 46 0 SHEET 2 C 4 VAL A 49 ARG A 57 -1 O VAL A 49 N VAL A 46 SHEET 3 C 4 ILE A 67 SER A 74 -1 O GLU A 68 N ALA A 56 SHEET 4 C 4 ASN A 82 ILE A 87 -1 N ASN A 82 O TYR A 73 SHEET 1 D 7 THR A 151 TRP A 157 0 SHEET 2 D 7 TRP A 133 ALA A 146 -1 N GLU A 141 O SER A 156 SHEET 3 D 7 VAL A 161 SER A 162 -1 N VAL A 161 O LEU A 137 SHEET 4 D 7 TRP A 133 ALA A 146 -1 O LEU A 137 N VAL A 161 SHEET 5 D 7 LYS A 109 PHE A 117 -1 N LEU A 110 O GLY A 140 SHEET 6 D 7 ARG A 97 LYS A 106 -1 O ARG A 97 N PHE A 117 SHEET 7 D 7 GLY A 184 ALA A 185 1 O GLY A 184 N VAL A 103 SHEET 1 E 7 GLU A 170 PHE A 171 0 SHEET 2 E 7 ILE A 174 GLY A 181 -1 O ILE A 174 N PHE A 171 SHEET 3 E 7 LEU A 194 ASP A 202 -1 N GLN A 199 O VAL A 180 SHEET 4 E 7 ILE A 187 VAL A 188 -1 O ILE A 187 N VAL A 195 SHEET 5 E 7 LEU A 194 ASP A 202 -1 N VAL A 195 O ILE A 187 SHEET 6 E 7 VAL A 207 SER A 214 -1 O PHE A 208 N ILE A 200 SHEET 7 E 7 LYS A 222 PHE A 223 -1 N LYS A 222 O TYR A 213 SHEET 1 F 4 SER A 233 TRP A 240 0 SHEET 2 F 4 LYS A 243 ARG A 249 -1 O LYS A 243 N TRP A 240 SHEET 3 F 4 VAL A 257 SER A 260 -1 O TYR A 258 N ILE A 246 SHEET 4 F 4 VAL A 268 GLU A 269 -1 O VAL A 268 N GLU A 259 SHEET 1 G 4 PHE A 293 ILE A 298 0 SHEET 2 G 4 LYS A 301 PRO A 309 -1 O LYS A 301 N ILE A 298 SHEET 3 G 4 LEU A 321 THR A 326 -1 N HIS A 322 O HIS A 308 SHEET 4 G 4 ILE A 331 GLN A 336 -1 N PHE A 332 O MET A 325 SHEET 1 H19 TRP A 528 TYR A 532 0 SHEET 2 H19 LYS A 516 ASP A 523 -1 O GLY A 519 N LEU A 531 SHEET 3 H19 THR A 501 LEU A 509 -1 N SER A 502 O TYR A 522 SHEET 4 H19 ILE A 585 GLY A 591 -1 N SER A 586 O GLY A 508 SHEET 5 H19 GLY A 465 PRO A 469 -1 N ALA A 466 O ILE A 590 SHEET 6 H19 ALA A 445 ALA A 448 -1 N ASN A 446 O VAL A 467 SHEET 7 H19 VAL A 435 ASP A 438 -1 N TRP A 436 O ALA A 445 SHEET 8 H19 LEU A 423 ASN A 432 -1 N SER A 428 O GLU A 437 SHEET 9 H19 VAL A 604 TYR A 612 -1 O VAL A 609 N LEU A 427 SHEET 10 H19 GLY A 456 PHE A 459 -1 O LEU A 457 N VAL A 606 SHEET 11 H19 ALA A 450 VAL A 453 -1 O GLU A 451 N LYS A 458 SHEET 12 H19 GLY A 456 PHE A 459 -1 O GLY A 456 N VAL A 453 SHEET 13 H19 VAL A 604 TYR A 612 -1 O VAL A 604 N PHE A 459 SHEET 14 H19 PHE A 486 ILE A 494 -1 O THR A 487 N TYR A 612 SHEET 15 H19 TYR A 549 ALA A 556 -1 N TYR A 549 O VAL A 492 SHEET 16 H19 GLN A 559 VAL A 564 -1 N GLN A 559 O ALA A 556 SHEET 17 H19 GLN A 567 PRO A 568 -1 O GLN A 567 N VAL A 564 SHEET 18 H19 GLN A 559 VAL A 564 -1 N VAL A 564 O GLN A 567 SHEET 19 H19 ASN A 574 THR A 575 -1 O ASN A 574 N GLY A 560 SSBOND 1 CYS A 400 CYS A 414 CRYST1 75.862 93.404 105.821 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 0.013182 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010706 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009450 0.00000