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HEADER HYDROLASE 19-NOV-04 1WCQ TITLE MUTAGENESIS OF THE NUCLEOPHILIC TYROSINE IN A BACTERIAL TITLE 2 SIALIDASE TO PHENYLALANINE. COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A, B, C; COMPND 4 FRAGMENT: SIALIDASE, RESIDUES 47-647; COMPND 5 SYNONYM: NEURAMINIDASE; COMPND 6 EC: 3.2.1.18; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA VIRIDIFACIENS; SOURCE 3 ATCC: 31146; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET28A KEYWDS SIALIDASE, MICROMONOSPORA VIRIDIFACIENS, HYDROLASE KEYWDS 2 NEURAMINIDASE, GLYCOSIDASE EXPDTA X-RAY DIFFRACTION AUTHOR S.NEWSTEAD,J.N.WATSON,A.J.BENNET,G.TAYLOR REVDAT 2 20-DEC-06 1WCQ 1 JRNL REVDAT 1 12-OCT-05 1WCQ 0 JRNL AUTH J.N.WATSON,S.NEWSTEAD,A.A.NARINE,G.TAYLOR, JRNL AUTH 2 A.J.BENNET JRNL TITL TWO NUCLEOPHILIC MUTANTS OF THE MICROMONOSPORA JRNL TITL 2 VIRIDIFACIENS SIALIDASE OPERATE WITH RETENTION OF JRNL TITL 3 CONFIGURATION BY TWO DIFFERENT MECHANISMS. JRNL REF CHEMBIOCHEM V. 6 1999 2005 JRNL REFN GE ISSN 1439-4227 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 124.03 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 105259 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) : 0.178 REMARK 3 R VALUE (WORKING SET) : 0.175 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5544 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH : NULL REMARK 3 BIN RESOLUTION RANGE LOW : NULL REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE SET COUNT : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 14833 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.34 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.81000 REMARK 3 B22 (A**2) : -0.81000 REMARK 3 B33 (A**2) : 1.21000 REMARK 3 B12 (A**2) : -0.40000 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): 0.212 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.191 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.672 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : NULL REMARK 3 ION PROBE RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 1WCQ 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 3.103 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-21729 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-SEP-2004 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.933 REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220) REMARK 200 OPTICS : TOROIDAL MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110911 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 57.830 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.4000 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) : 2.21 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.00 REMARK 200 R MERGE FOR SHELL (I) : 0.47000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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 1EUU REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % PEG 3350, 0.2 M AMMONIUM REMARK 280 CITRATE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,2/3+Z REMARK 290 3555 -X+Y,-X,1/3+Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,1/3-Z REMARK 290 6555 -X,-X+Y,2/3-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.83333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.41667 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 53.41667 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 106.83333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 3 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, X, 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 350 BIOMOLECULE: 3 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH X 18 LIES ON A SPECIAL POSITION. 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 C 47 REMARK 465 GLU C 48 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O HOH X 61 O HOH X 124 1.89 REMARK 500 O HOH Y 83 O HOH Y 178 2.10 REMARK 500 O HOH X 62 O HOH X 63 2.15 REMARK 500 O HOH Y 4 O HOH Y 12 2.15 REMARK 500 O HOH X 143 O HOH X 144 2.18 REMARK 500 O HOH Y 25 O HOH Y 48 2.18 REMARK 500 O ASN B 59 O HOH Y 7 2.19 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 PRO A 76 CB PRO A 76 CG 0.146 REMARK 500 ILE A 189 CG1 ILE A 189 CD1 0.169 REMARK 500 GLN A 451 CG GLN A 451 CD 0.140 REMARK 500 GLN A 451 CD GLN A 451 OE1 -0.131 REMARK 500 GLN A 451 CD GLN A 451 NE2 0.422 REMARK 500 ILE B 189 CG1 ILE B 189 CD1 0.136 REMARK 500 PRO B 411 CB PRO B 411 CG 0.156 REMARK 500 ASP B 595 CB ASP B 595 CG 0.177 REMARK 500 ASP B 595 CG ASP B 595 OD1 0.484 REMARK 500 GLN C 419 CG GLN C 419 CD 0.151 REMARK 500 GLN C 419 CD GLN C 419 OE1 0.172 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 ILE A 410 N - CA - C ANGL. DEV. =-10.9 DEGREES REMARK 500 GLN A 451 OE1 - CD - NE2 ANGL. DEV. = 12.8 DEGREES REMARK 500 GLN A 451 CG - CD - NE2 ANGL. DEV. =-20.9 DEGREES REMARK 500 ASP B 595 CB - CG - OD1 ANGL. DEV. =-25.4 DEGREES REMARK 500 ASP B 595 CB - CG - OD2 ANGL. DEV. = 14.6 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH Y 36 DISTANCE = 5.10 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: DAN BINDING SITE FOR CHAIN C DBREF 1WCQ A 47 647 UNP Q02834 NANH_MICVI 47 647 DBREF 1WCQ B 47 647 UNP Q02834 NANH_MICVI 47 647 DBREF 1WCQ C 47 647 UNP Q02834 NANH_MICVI 47 647 SEQADV 1WCQ PHE A 370 UNP Q02834 TYR 370 ENGINEERED MUTATION SEQADV 1WCQ PHE B 370 UNP Q02834 TYR 370 ENGINEERED MUTATION SEQADV 1WCQ PHE C 370 UNP Q02834 TYR 370 ENGINEERED MUTATION SEQRES 1 A 601 GLY GLU PRO LEU TYR THR GLU GLN ASP LEU ALA VAL ASN SEQRES 2 A 601 GLY ARG GLU GLY PHE PRO ASN TYR ARG ILE PRO ALA LEU SEQRES 3 A 601 THR VAL THR PRO ASP GLY ASP LEU LEU ALA SER TYR ASP SEQRES 4 A 601 GLY ARG PRO THR GLY ILE ASP ALA PRO GLY PRO ASN SER SEQRES 5 A 601 ILE LEU GLN ARG ARG SER THR ASP GLY GLY ARG THR TRP SEQRES 6 A 601 GLY GLU GLN GLN VAL VAL SER ALA GLY GLN THR THR ALA SEQRES 7 A 601 PRO ILE LYS GLY PHE SER ASP PRO SER TYR LEU VAL ASP SEQRES 8 A 601 ARG GLU THR GLY THR ILE PHE ASN PHE HIS VAL TYR SER SEQRES 9 A 601 GLN ARG GLN GLY PHE ALA GLY SER ARG PRO GLY THR ASP SEQRES 10 A 601 PRO ALA ASP PRO ASN VAL LEU HIS ALA ASN VAL ALA THR SEQRES 11 A 601 SER THR ASP GLY GLY LEU THR TRP SER HIS ARG THR ILE SEQRES 12 A 601 THR ALA ASP ILE THR PRO ASP PRO GLY TRP ARG SER ARG SEQRES 13 A 601 PHE ALA ALA SER GLY GLU GLY ILE GLN LEU ARG TYR GLY SEQRES 14 A 601 PRO HIS ALA GLY ARG LEU ILE GLN GLN TYR THR ILE ILE SEQRES 15 A 601 ASN ALA ALA GLY ALA PHE GLN ALA VAL SER VAL TYR SER SEQRES 16 A 601 ASP ASP HIS GLY ARG THR TRP ARG ALA GLY GLU ALA VAL SEQRES 17 A 601 GLY VAL GLY MET ASP GLU ASN LYS THR VAL GLU LEU SER SEQRES 18 A 601 ASP GLY ARG VAL LEU LEU ASN SER ARG ASP SER ALA ARG SEQRES 19 A 601 SER GLY TYR ARG LYS VAL ALA VAL SER THR ASP GLY GLY SEQRES 20 A 601 HIS SER TYR GLY PRO VAL THR ILE ASP ARG ASP LEU PRO SEQRES 21 A 601 ASP PRO THR ASN ASN ALA SER ILE ILE ARG ALA PHE PRO SEQRES 22 A 601 ASP ALA PRO ALA GLY SER ALA ARG ALA LYS VAL LEU LEU SEQRES 23 A 601 PHE SER ASN ALA ALA SER GLN THR SER ARG SER GLN GLY SEQRES 24 A 601 THR ILE ARG MET SER CYS ASP ASP GLY GLN THR TRP PRO SEQRES 25 A 601 VAL SER LYS VAL PHE GLN PRO GLY SER MET SER PHE SER SEQRES 26 A 601 THR LEU THR ALA LEU PRO ASP GLY THR TYR GLY LEU LEU SEQRES 27 A 601 TYR GLU PRO GLY THR GLY ILE ARG TYR ALA ASN PHE ASN SEQRES 28 A 601 LEU ALA TRP LEU GLY GLY ILE CYS ALA PRO PHE THR ILE SEQRES 29 A 601 PRO ASP VAL ALA LEU GLU PRO GLY GLN GLN VAL THR VAL SEQRES 30 A 601 PRO VAL ALA VAL THR ASN GLN SER GLY ILE ALA VAL PRO SEQRES 31 A 601 LYS PRO SER LEU GLN LEU ASP ALA SER PRO ASP TRP GLN SEQRES 32 A 601 VAL GLN GLY SER VAL GLU PRO LEU MET PRO GLY ARG GLN SEQRES 33 A 601 ALA LYS GLY GLN VAL THR ILE THR VAL PRO ALA GLY THR SEQRES 34 A 601 THR PRO GLY ARG TYR ARG VAL GLY ALA THR LEU ARG THR SEQRES 35 A 601 SER ALA GLY ASN ALA SER THR THR PHE THR VAL THR VAL SEQRES 36 A 601 GLY LEU LEU ASP GLN ALA ARG MET SER ILE ALA ASP VAL SEQRES 37 A 601 ASP SER GLU GLU THR ALA ARG GLU ASP GLY ARG ALA SER SEQRES 38 A 601 ASN VAL ILE ASP GLY ASN PRO SER THR PHE TRP HIS THR SEQRES 39 A 601 GLU TRP SER ARG ALA ASP ALA PRO GLY TYR PRO HIS ARG SEQRES 40 A 601 ILE SER LEU ASP LEU GLY GLY THR HIS THR ILE SER GLY SEQRES 41 A 601 LEU GLN TYR THR ARG ARG GLN ASN SER ALA ASN GLU GLN SEQRES 42 A 601 VAL ALA ASP TYR GLU ILE TYR THR SER LEU ASN GLY THR SEQRES 43 A 601 THR TRP ASP GLY PRO VAL ALA SER GLY ARG PHE THR THR SEQRES 44 A 601 SER LEU ALA PRO GLN ARG ALA VAL PHE PRO ALA ARG ASP SEQRES 45 A 601 ALA ARG TYR ILE ARG LEU VAL ALA LEU SER GLU GLN THR SEQRES 46 A 601 GLY HIS LYS TYR ALA ALA VAL ALA GLU LEU GLU VAL GLU SEQRES 47 A 601 GLY GLN ARG SEQRES 1 B 601 GLY GLU PRO LEU TYR THR GLU GLN ASP LEU ALA VAL ASN SEQRES 2 B 601 GLY ARG GLU GLY PHE PRO ASN TYR ARG ILE PRO ALA LEU SEQRES 3 B 601 THR VAL THR PRO ASP GLY ASP LEU LEU ALA SER TYR ASP SEQRES 4 B 601 GLY ARG PRO THR GLY ILE ASP ALA PRO GLY PRO ASN SER SEQRES 5 B 601 ILE LEU GLN ARG ARG SER THR ASP GLY GLY ARG THR TRP SEQRES 6 B 601 GLY GLU GLN GLN VAL VAL SER ALA GLY GLN THR THR ALA SEQRES 7 B 601 PRO ILE LYS GLY PHE SER ASP PRO SER TYR LEU VAL ASP SEQRES 8 B 601 ARG GLU THR GLY THR ILE PHE ASN PHE HIS VAL TYR SER SEQRES 9 B 601 GLN ARG GLN GLY PHE ALA GLY SER ARG PRO GLY THR ASP SEQRES 10 B 601 PRO ALA ASP PRO ASN VAL LEU HIS ALA ASN VAL ALA THR SEQRES 11 B 601 SER THR ASP GLY GLY LEU THR TRP SER HIS ARG THR ILE SEQRES 12 B 601 THR ALA ASP ILE THR PRO ASP PRO GLY TRP ARG SER ARG SEQRES 13 B 601 PHE ALA ALA SER GLY GLU GLY ILE GLN LEU ARG TYR GLY SEQRES 14 B 601 PRO HIS ALA GLY ARG LEU ILE GLN GLN TYR THR ILE ILE SEQRES 15 B 601 ASN ALA ALA GLY ALA PHE GLN ALA VAL SER VAL TYR SER SEQRES 16 B 601 ASP ASP HIS GLY ARG THR TRP ARG ALA GLY GLU ALA VAL SEQRES 17 B 601 GLY VAL GLY MET ASP GLU ASN LYS THR VAL GLU LEU SER SEQRES 18 B 601 ASP GLY ARG VAL LEU LEU ASN SER ARG ASP SER ALA ARG SEQRES 19 B 601 SER GLY TYR ARG LYS VAL ALA VAL SER THR ASP GLY GLY SEQRES 20 B 601 HIS SER TYR GLY PRO VAL THR ILE ASP ARG ASP LEU PRO SEQRES 21 B 601 ASP PRO THR ASN ASN ALA SER ILE ILE ARG ALA PHE PRO SEQRES 22 B 601 ASP ALA PRO ALA GLY SER ALA ARG ALA LYS VAL LEU LEU SEQRES 23 B 601 PHE SER ASN ALA ALA SER GLN THR SER ARG SER GLN GLY SEQRES 24 B 601 THR ILE ARG MET SER CYS ASP ASP GLY GLN THR TRP PRO SEQRES 25 B 601 VAL SER LYS VAL PHE GLN PRO GLY SER MET SER PHE SER SEQRES 26 B 601 THR LEU THR ALA LEU PRO ASP GLY THR TYR GLY LEU LEU SEQRES 27 B 601 TYR GLU PRO GLY THR GLY ILE ARG TYR ALA ASN PHE ASN SEQRES 28 B 601 LEU ALA TRP LEU GLY GLY ILE CYS ALA PRO PHE THR ILE SEQRES 29 B 601 PRO ASP VAL ALA LEU GLU PRO GLY GLN GLN VAL THR VAL SEQRES 30 B 601 PRO VAL ALA VAL THR ASN GLN SER GLY ILE ALA VAL PRO SEQRES 31 B 601 LYS PRO SER LEU GLN LEU ASP ALA SER PRO ASP TRP GLN SEQRES 32 B 601 VAL GLN GLY SER VAL GLU PRO LEU MET PRO GLY ARG GLN SEQRES 33 B 601 ALA LYS GLY GLN VAL THR ILE THR VAL PRO ALA GLY THR SEQRES 34 B 601 THR PRO GLY ARG TYR ARG VAL GLY ALA THR LEU ARG THR SEQRES 35 B 601 SER ALA GLY ASN ALA SER THR THR PHE THR VAL THR VAL SEQRES 36 B 601 GLY LEU LEU ASP GLN ALA ARG MET SER ILE ALA ASP VAL SEQRES 37 B 601 ASP SER GLU GLU THR ALA ARG GLU ASP GLY ARG ALA SER SEQRES 38 B 601 ASN VAL ILE ASP GLY ASN PRO SER THR PHE TRP HIS THR SEQRES 39 B 601 GLU TRP SER ARG ALA ASP ALA PRO GLY TYR PRO HIS ARG SEQRES 40 B 601 ILE SER LEU ASP LEU GLY GLY THR HIS THR ILE SER GLY SEQRES 41 B 601 LEU GLN TYR THR ARG ARG GLN ASN SER ALA ASN GLU GLN SEQRES 42 B 601 VAL ALA ASP TYR GLU ILE TYR THR SER LEU ASN GLY THR SEQRES 43 B 601 THR TRP ASP GLY PRO VAL ALA SER GLY ARG PHE THR THR SEQRES 44 B 601 SER LEU ALA PRO GLN ARG ALA VAL PHE PRO ALA ARG ASP SEQRES 45 B 601 ALA ARG TYR ILE ARG LEU VAL ALA LEU SER GLU GLN THR SEQRES 46 B 601 GLY HIS LYS TYR ALA ALA VAL ALA GLU LEU GLU VAL GLU SEQRES 47 B 601 GLY GLN ARG SEQRES 1 C 601 GLY GLU PRO LEU TYR THR GLU GLN ASP LEU ALA VAL ASN SEQRES 2 C 601 GLY ARG GLU GLY PHE PRO ASN TYR ARG ILE PRO ALA LEU SEQRES 3 C 601 THR VAL THR PRO ASP GLY ASP LEU LEU ALA SER TYR ASP SEQRES 4 C 601 GLY ARG PRO THR GLY ILE ASP ALA PRO GLY PRO ASN SER SEQRES 5 C 601 ILE LEU GLN ARG ARG SER THR ASP GLY GLY ARG THR TRP SEQRES 6 C 601 GLY GLU GLN GLN VAL VAL SER ALA GLY GLN THR THR ALA SEQRES 7 C 601 PRO ILE LYS GLY PHE SER ASP PRO SER TYR LEU VAL ASP SEQRES 8 C 601 ARG GLU THR GLY THR ILE PHE ASN PHE HIS VAL TYR SER SEQRES 9 C 601 GLN ARG GLN GLY PHE ALA GLY SER ARG PRO GLY THR ASP SEQRES 10 C 601 PRO ALA ASP PRO ASN VAL LEU HIS ALA ASN VAL ALA THR SEQRES 11 C 601 SER THR ASP GLY GLY LEU THR TRP SER HIS ARG THR ILE SEQRES 12 C 601 THR ALA ASP ILE THR PRO ASP PRO GLY TRP ARG SER ARG SEQRES 13 C 601 PHE ALA ALA SER GLY GLU GLY ILE GLN LEU ARG TYR GLY SEQRES 14 C 601 PRO HIS ALA GLY ARG LEU ILE GLN GLN TYR THR ILE ILE SEQRES 15 C 601 ASN ALA ALA GLY ALA PHE GLN ALA VAL SER VAL TYR SER SEQRES 16 C 601 ASP ASP HIS GLY ARG THR TRP ARG ALA GLY GLU ALA VAL SEQRES 17 C 601 GLY VAL GLY MET ASP GLU ASN LYS THR VAL GLU LEU SER SEQRES 18 C 601 ASP GLY ARG VAL LEU LEU ASN SER ARG ASP SER ALA ARG SEQRES 19 C 601 SER GLY TYR ARG LYS VAL ALA VAL SER THR ASP GLY GLY SEQRES 20 C 601 HIS SER TYR GLY PRO VAL THR ILE ASP ARG ASP LEU PRO SEQRES 21 C 601 ASP PRO THR ASN ASN ALA SER ILE ILE ARG ALA PHE PRO SEQRES 22 C 601 ASP ALA PRO ALA GLY SER ALA ARG ALA LYS VAL LEU LEU SEQRES 23 C 601 PHE SER ASN ALA ALA SER GLN THR SER ARG SER GLN GLY SEQRES 24 C 601 THR ILE ARG MET SER CYS ASP ASP GLY GLN THR TRP PRO SEQRES 25 C 601 VAL SER LYS VAL PHE GLN PRO GLY SER MET SER PHE SER SEQRES 26 C 601 THR LEU THR ALA LEU PRO ASP GLY THR TYR GLY LEU LEU SEQRES 27 C 601 TYR GLU PRO GLY THR GLY ILE ARG TYR ALA ASN PHE ASN SEQRES 28 C 601 LEU ALA TRP LEU GLY GLY ILE CYS ALA PRO PHE THR ILE SEQRES 29 C 601 PRO ASP VAL ALA LEU GLU PRO GLY GLN GLN VAL THR VAL SEQRES 30 C 601 PRO VAL ALA VAL THR ASN GLN SER GLY ILE ALA VAL PRO SEQRES 31 C 601 LYS PRO SER LEU GLN LEU ASP ALA SER PRO ASP TRP GLN SEQRES 32 C 601 VAL GLN GLY SER VAL GLU PRO LEU MET PRO GLY ARG GLN SEQRES 33 C 601 ALA LYS GLY GLN VAL THR ILE THR VAL PRO ALA GLY THR SEQRES 34 C 601 THR PRO GLY ARG TYR ARG VAL GLY ALA THR LEU ARG THR SEQRES 35 C 601 SER ALA GLY ASN ALA SER THR THR PHE THR VAL THR VAL SEQRES 36 C 601 GLY LEU LEU ASP GLN ALA ARG MET SER ILE ALA ASP VAL SEQRES 37 C 601 ASP SER GLU GLU THR ALA ARG GLU ASP GLY ARG ALA SER SEQRES 38 C 601 ASN VAL ILE ASP GLY ASN PRO SER THR PHE TRP HIS THR SEQRES 39 C 601 GLU TRP SER ARG ALA ASP ALA PRO GLY TYR PRO HIS ARG SEQRES 40 C 601 ILE SER LEU ASP LEU GLY GLY THR HIS THR ILE SER GLY SEQRES 41 C 601 LEU GLN TYR THR ARG ARG GLN ASN SER ALA ASN GLU GLN SEQRES 42 C 601 VAL ALA ASP TYR GLU ILE TYR THR SER LEU ASN GLY THR SEQRES 43 C 601 THR TRP ASP GLY PRO VAL ALA SER GLY ARG PHE THR THR SEQRES 44 C 601 SER LEU ALA PRO GLN ARG ALA VAL PHE PRO ALA ARG ASP SEQRES 45 C 601 ALA ARG TYR ILE ARG LEU VAL ALA LEU SER GLU GLN THR SEQRES 46 C 601 GLY HIS LYS TYR ALA ALA VAL ALA GLU LEU GLU VAL GLU SEQRES 47 C 601 GLY GLN ARG HET NA A1648 1 HET NA B1648 1 HET NA C1648 1 HET DAN A1651 20 HET DAN B1652 20 HET DAN C1651 20 HET GOL A1649 6 HET GOL A1650 6 HET GOL B1649 6 HET GOL B1650 6 HET GOL B1651 6 HET GOL C1649 6 HET GOL C1650 6 HETNAM NA SODIUM ION HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID HETNAM GOL GLYCEROL FORMUL 4 NA 3(NA 1+) FORMUL 7 DAN 3(C11 H17 N O8) FORMUL 10 GOL 7(C3 H8 O3) FORMUL 17 HOH *1078(H2 O) HELIX 1 1 ALA A 326 LYS A 329 5 4 HELIX 2 2 ASN A 397 GLY A 402 1 6 HELIX 3 3 ASP A 505 MET A 509 5 5 HELIX 4 4 ARG A 525 ASP A 531 5 7 HELIX 5 5 THR B 190 THR B 194 5 5 HELIX 6 6 ALA B 326 LYS B 329 5 4 HELIX 7 7 ASN B 397 GLY B 402 1 6 HELIX 8 8 ASP B 505 MET B 509 5 5 HELIX 9 9 ARG B 525 ASP B 531 5 7 HELIX 10 10 THR C 190 THR C 194 5 5 HELIX 11 11 TYR C 214 ALA C 218 5 5 HELIX 12 12 ALA C 326 LYS C 329 5 4 HELIX 13 13 ASN C 397 GLY C 402 1 6 HELIX 14 14 ASP C 505 MET C 509 5 5 HELIX 15 15 ARG C 525 ASP C 531 5 7 SHEET 1 AA 4 TYR A 51 VAL A 58 0 SHEET 2 AA 4 GLY A 390 PHE A 396 -1 O ILE A 391 N LEU A 56 SHEET 3 AA 4 TYR A 381 TYR A 385 -1 O TYR A 381 N PHE A 396 SHEET 4 AA 4 SER A 371 ALA A 375 -1 O THR A 372 N LEU A 384 SHEET 1 AB 4 TYR A 67 VAL A 74 0 SHEET 2 AB 4 LEU A 80 GLY A 86 -1 O LEU A 81 N THR A 73 SHEET 3 AB 4 SER A 98 SER A 104 -1 O SER A 98 N GLY A 86 SHEET 4 AB 4 GLN A 115 SER A 118 -1 O GLN A 115 N GLN A 101 SHEET 1 AC 5 SER A 185 THR A 188 0 SHEET 2 AC 5 HIS A 171 SER A 177 -1 O VAL A 174 N ARG A 187 SHEET 3 AC 5 ILE A 143 SER A 150 -1 O ILE A 143 N SER A 177 SHEET 4 AC 5 GLY A 128 VAL A 136 -1 O GLY A 128 N SER A 150 SHEET 5 AC 5 GLY A 207 GLU A 208 1 O GLY A 207 N TYR A 134 SHEET 1 AD 3 SER A 201 ALA A 204 0 SHEET 2 AD 3 LEU A 221 ILE A 228 -1 O THR A 226 N PHE A 203 SHEET 3 AD 3 ILE A 210 GLN A 211 -1 O ILE A 210 N ILE A 222 SHEET 1 AE 4 SER A 201 ALA A 204 0 SHEET 2 AE 4 LEU A 221 ILE A 228 -1 O THR A 226 N PHE A 203 SHEET 3 AE 4 PHE A 234 SER A 241 -1 O GLN A 235 N ILE A 227 SHEET 4 AE 4 ARG A 249 ALA A 250 -1 O ARG A 249 N TYR A 240 SHEET 1 AF 4 ASN A 261 GLU A 265 0 SHEET 2 AF 4 VAL A 271 SER A 275 -1 O LEU A 272 N VAL A 264 SHEET 3 AF 4 TYR A 283 SER A 289 -1 O LYS A 285 N SER A 275 SHEET 4 AF 4 THR A 300 PRO A 306 -1 O THR A 300 N VAL A 286 SHEET 1 AG 4 SER A 313 ARG A 316 0 SHEET 2 AG 4 LEU A 331 ALA A 336 -1 O LEU A 332 N ILE A 315 SHEET 3 AG 4 SER A 343 SER A 350 -1 O THR A 346 N ASN A 335 SHEET 4 AG 4 VAL A 359 SER A 367 -1 O VAL A 359 N MET A 349 SHEET 1 AH 4 PHE A 408 THR A 409 0 SHEET 2 AH 4 GLN A 420 THR A 428 -1 O ALA A 426 N THR A 409 SHEET 3 AH 4 GLN A 462 THR A 470 -1 O ALA A 463 N VAL A 427 SHEET 4 AH 4 GLN A 449 VAL A 454 -1 O GLN A 449 N THR A 470 SHEET 1 AI 4 VAL A 413 LEU A 415 0 SHEET 2 AI 4 ALA A 493 VAL A 501 1 O THR A 498 N VAL A 413 SHEET 3 AI 4 GLY A 478 ARG A 487 -1 O GLY A 478 N VAL A 501 SHEET 4 AI 4 SER A 439 ASP A 443 -1 O SER A 439 N ARG A 487 SHEET 1 AJ 5 SER A 510 VAL A 514 0 SHEET 2 AJ 5 HIS A 552 ARG A 571 -1 O SER A 555 N ALA A 512 SHEET 3 AJ 5 GLN A 610 ALA A 626 -1 O GLN A 610 N TYR A 569 SHEET 4 AJ 5 ASP A 582 SER A 588 -1 O GLU A 584 N VAL A 625 SHEET 5 AJ 5 TRP A 594 ARG A 602 -1 O ASP A 595 N THR A 587 SHEET 1 AK 4 SER A 510 VAL A 514 0 SHEET 2 AK 4 HIS A 552 ARG A 571 -1 O SER A 555 N ALA A 512 SHEET 3 AK 4 ALA A 637 GLY A 645 -1 N ALA A 639 O THR A 570 SHEET 4 AK 4 TRP A 538 HIS A 539 -1 O TRP A 538 N VAL A 638 SHEET 1 BA 4 TYR B 51 VAL B 58 0 SHEET 2 BA 4 GLY B 390 PHE B 396 -1 O ILE B 391 N LEU B 56 SHEET 3 BA 4 TYR B 381 TYR B 385 -1 O TYR B 381 N PHE B 396 SHEET 4 BA 4 SER B 371 ALA B 375 -1 O THR B 372 N LEU B 384 SHEET 1 BB 4 TYR B 67 VAL B 74 0 SHEET 2 BB 4 LEU B 80 GLY B 86 -1 O LEU B 81 N THR B 73 SHEET 3 BB 4 SER B 98 SER B 104 -1 O SER B 98 N GLY B 86 SHEET 4 BB 4 GLN B 115 SER B 118 -1 O GLN B 115 N GLN B 101 SHEET 1 BC 5 SER B 185 THR B 188 0 SHEET 2 BC 5 HIS B 171 SER B 177 -1 O VAL B 174 N ARG B 187 SHEET 3 BC 5 ILE B 143 SER B 150 -1 O ILE B 143 N SER B 177 SHEET 4 BC 5 GLY B 128 VAL B 136 -1 O GLY B 128 N SER B 150 SHEET 5 BC 5 GLY B 207 GLU B 208 1 O GLY B 207 N TYR B 134 SHEET 1 BD 3 SER B 201 ALA B 204 0 SHEET 2 BD 3 LEU B 221 ILE B 228 -1 O THR B 226 N PHE B 203 SHEET 3 BD 3 ILE B 210 GLN B 211 -1 O ILE B 210 N ILE B 222 SHEET 1 BE 4 SER B 201 ALA B 204 0 SHEET 2 BE 4 LEU B 221 ILE B 228 -1 O THR B 226 N PHE B 203 SHEET 3 BE 4 PHE B 234 SER B 241 -1 O GLN B 235 N ILE B 227 SHEET 4 BE 4 ARG B 249 ALA B 250 -1 O ARG B 249 N TYR B 240 SHEET 1 BF 4 ASN B 261 GLU B 265 0 SHEET 2 BF 4 VAL B 271 SER B 275 -1 O LEU B 272 N VAL B 264 SHEET 3 BF 4 TYR B 283 SER B 289 -1 O LYS B 285 N SER B 275 SHEET 4 BF 4 THR B 300 PRO B 306 -1 O THR B 300 N VAL B 286 SHEET 1 BG 4 SER B 313 ARG B 316 0 SHEET 2 BG 4 LEU B 331 ALA B 336 -1 O LEU B 332 N ILE B 315 SHEET 3 BG 4 SER B 343 SER B 350 -1 O THR B 346 N ASN B 335 SHEET 4 BG 4 VAL B 359 SER B 367 -1 O VAL B 359 N MET B 349 SHEET 1 BH 4 PHE B 408 THR B 409 0 SHEET 2 BH 4 GLN B 420 THR B 428 -1 O ALA B 426 N THR B 409 SHEET 3 BH 4 GLN B 462 THR B 470 -1 O ALA B 463 N VAL B 427 SHEET 4 BH 4 GLN B 449 VAL B 454 -1 O GLN B 449 N THR B 470 SHEET 1 BI 4 VAL B 413 LEU B 415 0 SHEET 2 BI 4 GLY B 491 VAL B 501 1 O THR B 498 N VAL B 413 SHEET 3 BI 4 GLY B 478 THR B 488 -1 O GLY B 478 N VAL B 501 SHEET 4 BI 4 SER B 439 ASP B 443 -1 O SER B 439 N ARG B 487 SHEET 1 BJ 9 SER B 510 VAL B 514 0 SHEET 2 BJ 9 HIS B 552 ARG B 571 -1 O SER B 555 N ALA B 512 SHEET 3 BJ 9 TRP B 538 HIS B 539 0 SHEET 4 BJ 9 ALA B 637 GLY B 645 -1 O VAL B 638 N TRP B 538 SHEET 5 BJ 9 HIS B 552 ARG B 571 -1 N SER B 565 O GLU B 644 SHEET 6 BJ 9 ASP B 595 ARG B 602 0 SHEET 7 BJ 9 ASP B 582 SER B 588 -1 O TYR B 583 N GLY B 601 SHEET 8 BJ 9 GLN B 610 ALA B 626 -1 N ARG B 620 O SER B 588 SHEET 9 BJ 9 HIS B 552 ARG B 571 -1 O HIS B 552 N ALA B 626 SHEET 1 CA 4 TYR C 51 VAL C 58 0 SHEET 2 CA 4 GLY C 390 PHE C 396 -1 O ILE C 391 N LEU C 56 SHEET 3 CA 4 TYR C 381 TYR C 385 -1 O TYR C 381 N PHE C 396 SHEET 4 CA 4 SER C 371 ALA C 375 -1 O THR C 372 N LEU C 384 SHEET 1 CB 4 TYR C 67 VAL C 74 0 SHEET 2 CB 4 LEU C 80 GLY C 86 -1 O LEU C 81 N THR C 73 SHEET 3 CB 4 SER C 98 SER C 104 -1 O SER C 98 N GLY C 86 SHEET 4 CB 4 GLN C 115 SER C 118 -1 O GLN C 115 N GLN C 101 SHEET 1 CC 5 SER C 185 THR C 188 0 SHEET 2 CC 5 HIS C 171 SER C 177 -1 O VAL C 174 N ARG C 187 SHEET 3 CC 5 ILE C 143 SER C 150 -1 O ILE C 143 N SER C 177 SHEET 4 CC 5 GLY C 128 VAL C 136 -1 O GLY C 128 N SER C 150 SHEET 5 CC 5 GLY C 207 GLU C 208 1 O GLY C 207 N TYR C 134 SHEET 1 CD 7 SER C 201 ALA C 204 0 SHEET 2 CD 7 LEU C 221 ILE C 228 -1 O THR C 226 N PHE C 203 SHEET 3 CD 7 ILE C 210 GLN C 211 -1 O ILE C 210 N ILE C 222 SHEET 4 CD 7 LEU C 221 ILE C 228 -1 O ILE C 222 N ILE C 210 SHEET 5 CD 7 ARG C 249 ALA C 250 0 SHEET 6 CD 7 PHE C 234 SER C 241 -1 O TYR C 240 N ARG C 249 SHEET 7 CD 7 LEU C 221 ILE C 228 -1 O LEU C 221 N SER C 241 SHEET 1 CE 4 ASN C 261 GLU C 265 0 SHEET 2 CE 4 VAL C 271 SER C 275 -1 O LEU C 272 N VAL C 264 SHEET 3 CE 4 TYR C 283 SER C 289 -1 O LYS C 285 N SER C 275 SHEET 4 CE 4 THR C 300 PRO C 306 -1 O THR C 300 N VAL C 286 SHEET 1 CF 4 SER C 313 ARG C 316 0 SHEET 2 CF 4 LEU C 331 ALA C 336 -1 O LEU C 332 N ILE C 315 SHEET 3 CF 4 SER C 343 SER C 350 -1 O THR C 346 N ASN C 335 SHEET 4 CF 4 VAL C 359 SER C 367 -1 O VAL C 359 N MET C 349 SHEET 1 CG 4 PHE C 408 THR C 409 0 SHEET 2 CG 4 GLN C 420 THR C 428 -1 O ALA C 426 N THR C 409 SHEET 3 CG 4 GLN C 462 THR C 470 -1 O ALA C 463 N VAL C 427 SHEET 4 CG 4 GLN C 449 VAL C 454 -1 O GLN C 449 N THR C 470 SHEET 1 CH 4 VAL C 413 LEU C 415 0 SHEET 2 CH 4 ASN C 492 VAL C 501 1 O THR C 498 N VAL C 413 SHEET 3 CH 4 GLY C 478 ARG C 487 -1 O GLY C 478 N VAL C 501 SHEET 4 CH 4 SER C 439 ASP C 443 -1 O SER C 439 N ARG C 487 SHEET 1 CI 9 SER C 510 VAL C 514 0 SHEET 2 CI 9 HIS C 552 ARG C 571 -1 O SER C 555 N ALA C 512 SHEET 3 CI 9 TRP C 538 HIS C 539 0 SHEET 4 CI 9 ALA C 637 GLY C 645 -1 O VAL C 638 N TRP C 538 SHEET 5 CI 9 HIS C 552 ARG C 571 -1 N SER C 565 O GLU C 644 SHEET 6 CI 9 TRP C 594 ARG C 602 0 SHEET 7 CI 9 ASP C 582 SER C 588 -1 O TYR C 583 N GLY C 601 SHEET 8 CI 9 GLN C 610 ALA C 626 -1 N ARG C 620 O SER C 588 SHEET 9 CI 9 HIS C 552 ARG C 571 -1 O HIS C 552 N ALA C 626 SSBOND 1 CYS A 351 CYS A 405 SSBOND 2 CYS B 351 CYS B 405 SSBOND 3 CYS C 351 CYS C 405 LINK NA NA A1648 O ALA A 639 LINK NA NA A1648 O ASN A 533 LINK NA NA A1648 O THR A 536 LINK NA NA A1648 O ASN A 528 LINK NA NA A1648 OE2 GLU A 640 LINK NA NA A1648 OD1 ASP A 531 LINK NA NA B1648 O ASN B 528 LINK NA NA B1648 O ALA B 639 LINK NA NA B1648 O THR B 536 LINK NA NA B1648 OD1 ASP B 531 LINK NA NA B1648 O ASN B 533 LINK NA NA B1648 OG1 THR B 536 LINK NA NA B1648 OE2 GLU B 640 LINK NA NA C1648 O ASN C 533 LINK NA NA C1648 O THR C 536 LINK NA NA C1648 OG1 THR C 536 LINK NA NA C1648 O ALA C 639 LINK NA NA C1648 OD1 ASP C 531 LINK NA NA C1648 OE2 GLU C 640 LINK NA NA C1648 O ASN C 528 CISPEP 1 ALA A 93 PRO A 94 0 7.61 CISPEP 2 ALA A 124 PRO A 125 0 2.11 CISPEP 3 TYR A 550 PRO A 551 0 -1.00 CISPEP 4 GLY A 596 PRO A 597 0 9.40 CISPEP 5 ALA B 93 PRO B 94 0 -2.18 CISPEP 6 ALA B 124 PRO B 125 0 0.44 CISPEP 7 TYR B 550 PRO B 551 0 0.49 CISPEP 8 GLY B 596 PRO B 597 0 7.58 CISPEP 9 ALA C 93 PRO C 94 0 11.98 CISPEP 10 ALA C 124 PRO C 125 0 -5.44 CISPEP 11 TYR C 550 PRO C 551 0 3.19 CISPEP 12 GLY C 596 PRO C 597 0 6.51 SITE 1 AC1 6 ASN A 528 ASP A 531 ASN A 533 THR A 536 SITE 2 AC1 6 ALA A 639 GLU A 640 SITE 1 AC2 6 ASN B 528 ASP B 531 ASN B 533 THR B 536 SITE 2 AC2 6 ALA B 639 GLU B 640 SITE 1 AC3 6 ASN C 528 ASP C 531 ASN C 533 THR C 536 SITE 2 AC3 6 ALA C 639 GLU C 640 SITE 1 BC2 15 ARG B 68 ILE B 69 ARG B 87 ASP B 92 SITE 2 BC2 15 ASP B 131 PHE B 203 ASP B 259 GLU B 260 SITE 3 BC2 15 ARG B 276 ARG B 342 PHE B 370 HOH Y 81 SITE 4 BC2 15 HOH Y 397 HOH Y 398 HOH Y 399 SITE 1 BC3 14 ARG A 68 ILE A 69 ARG A 87 ASP A 92 SITE 2 BC3 14 ASP A 131 PHE A 203 ASP A 259 ARG A 276 SITE 3 BC3 14 ARG A 342 PHE A 370 HOH Z 23 HOH Z 24 SITE 4 BC3 14 HOH Z 319 HOH Z 320 SITE 1 BC4 15 ARG C 68 ILE C 69 ARG C 87 ASP C 92 SITE 2 BC4 15 ASP C 131 PHE C 203 PHE C 234 ASP C 259 SITE 3 BC4 15 GLU C 260 ARG C 276 ARG C 342 PHE C 370 SITE 4 BC4 15 HOH X 42 HOH X 358 HOH X 359 CRYST1 143.258 143.258 160.250 90.00 90.00 120.00 P 32 2 1 18 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 0.006980 0.004030 0.000000 0.00000 SCALE2 0.000000 0.008060 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006240 0.00000