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HEADER HYDROLASE 01-DEC-03 1USX TITLE CRYSTAL STRUCTURE OF THE NEWCASTLE DISEASE VIRUS TITLE 2 HEMAGGLUTININ-NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN; COMPND 3 CHAIN: A, B, C; COMPND 4 FRAGMENT: HEAD DOMAIN, RESIDUES 124-577; COMPND 5 EC: 3.2.1.18 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NEWCASTLE DISEASE VIRUS; SOURCE 3 STRAIN: KANSAS KEYWDS HYDROLASE, NEURAMINIDASE, HEMAGGLUTININ-NEURAMINIDASE, KEYWDS 2 HEMAGGLUTININ, SIALIDASE EXPDTA X-RAY DIFFRACTION AUTHOR V.ZAITSEV,M.VON ITZSTEIN,D.GROVES,M.KIEFEL,T.TAKIMOTO, AUTHOR 2 A.PORTNER,G.TAYLOR REVDAT 2 26-MAR-04 1USX 1 AUTHOR REVDAT 1 19-MAR-04 1USX 0 JRNL AUTH V.ZAITSEV,M.VON ITZSTEIN,D.GROVES,M.KIEFEL, JRNL AUTH 2 T.TAKIMOTO,A.PORTNER,G.TAYLOR JRNL TITL SECOND SIALIC ACID BINDING SITE IN NEWCASTLE JRNL TITL 2 DISEASE VIRUS HEMAGGLUTININ-NEURAMINIDASE: JRNL TITL 3 IMPLICATIONS FOR FUSION. JRNL REF J.VIROL. V. 78 3733 2004 JRNL REFN ASTM JOVIAM US ISSN 0022-538X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.CRENNELL,T.TAKIMOTO,A.PORTNER,G.TAYLOR REMARK 1 TITL CRYSTAL STRUCTURE OF THE MULTIFUNCTIONAL REMARK 1 TITL 2 PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE REMARK 1 REF NAT.STRUCT.BIOL. V. 7 1068 2000 REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REFERENCE 2 REMARK 1 AUTH T.TAKIMOTO,G.L.TAYLOR,S.J.CRENNELL,R.A.SCROGGS, REMARK 1 AUTH 2 A.PORTNER REMARK 1 TITL CRYSTALLIZATION OF NEWCASTLE DISEASE VIRUS REMARK 1 TITL 2 HEMAGGLUTININ-NEURAMINIDASE GLYCOPROTEIN REMARK 1 REF VIROLOGY V. 270 208 2000 REMARK 1 REFN ASTM VIRLAX US ISSN 0042-6822 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 79.6 REMARK 3 NUMBER OF REFLECTIONS : 41877 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) : 0.225 REMARK 3 FREE R VALUE : 0.289 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2095 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 : 10338 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 159 REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 49.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.07000 REMARK 3 B22 (A**2) : 2.07000 REMARK 3 B33 (A**2) : -4.14000 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) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.46 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED 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 : FLAT MODEL REMARK 3 KSOL : 0.38 REMARK 3 BSOL : 25.80 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1USX COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-14087 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-APR-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 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 MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43065 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 81.5 REMARK 200 DATA REDUNDANCY : 10.200 REMARK 200 R MERGE (I) : 0.07800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 71.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.32000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CCP4 REMARK 200 STARTING MODEL: PDB ENTRY 1E8V REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 141.98000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 57.53500 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 57.53500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 70.99000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 57.53500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 57.53500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 212.97000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 57.53500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.53500 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 70.99000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 57.53500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.53500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 212.97000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 141.98000 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 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, 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 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 141.98000 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 VAL A 571 REMARK 465 ARG A 572 REMARK 465 GLU A 573 REMARK 465 ALA A 574 REMARK 465 ARG A 575 REMARK 465 SER A 576 REMARK 465 GLY A 577 REMARK 465 VAL B 571 REMARK 465 ARG B 572 REMARK 465 GLU B 573 REMARK 465 ALA B 574 REMARK 465 ARG B 575 REMARK 465 SER B 576 REMARK 465 GLY B 577 REMARK 465 VAL C 571 REMARK 465 ARG C 572 REMARK 465 GLU C 573 REMARK 465 ALA C 574 REMARK 465 ARG C 575 REMARK 465 SER C 576 REMARK 465 GLY C 577 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 GLY A 570 CA C O REMARK 470 GLY B 570 CA C O REMARK 470 GLY C 570 CA C O 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 ASP A 569 C GLY A 570 N -0.076 REMARK 500 GLY B 124 N GLY B 124 CA 0.059 REMARK 500 MET B 249 SD MET B 249 CE 0.055 REMARK 500 MET B 270 SD MET B 270 CE 0.054 REMARK 500 MET B 429 SD MET B 429 CE -0.064 REMARK 500 ASP B 569 C GLY B 570 N -0.078 REMARK 500 ASP C 569 C GLY C 570 N -0.075 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 208 N - CA - C ANGL. DEV. = -9.6 DEGREES REMARK 500 TYR A 442 N - CA - C ANGL. DEV. =-14.4 DEGREES REMARK 500 VAL A 466 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 LEU A 492 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 THR A 509 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 VAL A 534 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 LEU B 193 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 TYR B 442 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 ARG B 513 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 VAL B 534 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 SER C 228 N - CA - C ANGL. DEV. =-10.1 DEGREES REMARK 500 THR C 430 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 TYR C 442 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 LEU C 492 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 ASN C 500 N - CA - C ANGL. DEV. = 11.2 DEGREES REMARK 500 THR C 509 N - CA - C ANGL. DEV. = 9.1 DEGREES REMARK 500 ARG C 513 N - CA - C ANGL. DEV. =-10.0 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 433 -108.38 72.03 REMARK 500 LEU A 552 -54.33 63.64 REMARK 500 VAL B 302 -33.57 67.40 REMARK 500 ASN B 433 -111.05 63.96 REMARK 500 LEU B 552 -42.26 47.71 REMARK 500 VAL C 302 -38.91 69.29 REMARK 500 LEU C 552 -44.70 61.39 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: DAN BINDING SITE FOR CHAIN C DBREF 1USX A 124 577 UNP P32884 HEMA_NDVB 124 577 DBREF 1USX B 124 577 UNP P32884 HEMA_NDVB 124 577 DBREF 1USX C 124 577 UNP P32884 HEMA_NDVB 124 577 SEQRES 1 A 454 GLY ALA PRO ILE HIS ASP PRO ASP PHE ILE GLY GLY ILE SEQRES 2 A 454 GLY LYS GLU LEU ILE VAL ASP ASN ALA SER ASP VAL THR SEQRES 3 A 454 SER PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE SEQRES 4 A 454 ILE PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE SEQRES 5 A 454 PRO SER PHE ASP MET SER ALA THR HIS TYR CYS TYR THR SEQRES 6 A 454 HIS ASN VAL ILE LEU SER GLY CYS ARG ASP HIS SER HIS SEQRES 7 A 454 SER HIS GLN TYR LEU ALA LEU GLY VAL LEU ARG THR THR SEQRES 8 A 454 ALA THR GLY ARG ILE PHE PHE SER THR LEU ARG SER ILE SEQRES 9 A 454 SER LEU ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SEQRES 10 A 454 SER ALA THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS SEQRES 11 A 454 VAL THR GLU THR GLU GLU GLU ASP TYR ASN SER ALA VAL SEQRES 12 A 454 PRO THR LEU MET ALA HIS GLY ARG LEU GLY PHE ASP GLY SEQRES 13 A 454 GLN TYR HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE SEQRES 14 A 454 GLU ASP TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SEQRES 15 A 454 SER PHE ILE ASP GLY ARG VAL TRP PHE SER VAL TYR GLY SEQRES 16 A 454 GLY LEU LYS PRO ASN SER PRO SER ASP THR VAL GLN GLU SEQRES 17 A 454 GLY LYS TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS SEQRES 18 A 454 PRO ASP GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SEQRES 19 A 454 SER TYR LYS PRO GLY ARG PHE GLY GLY LYS ARG ILE GLN SEQRES 20 A 454 GLN ALA ILE LEU SER ILE LYS VAL SER THR SER LEU GLY SEQRES 21 A 454 GLU ASP PRO VAL LEU THR VAL PRO PRO ASN THR VAL THR SEQRES 22 A 454 LEU MET GLY ALA GLU GLY ARG ILE LEU THR VAL GLY THR SEQRES 23 A 454 SER HIS PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER SEQRES 24 A 454 PRO ALA LEU LEU TYR PRO MET THR VAL SER ASN LYS THR SEQRES 25 A 454 ALA THR LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR SEQRES 26 A 454 ARG PRO GLY SER ILE PRO CYS GLN ALA SER ALA ARG CYS SEQRES 27 A 454 PRO ASN SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR SEQRES 28 A 454 PRO LEU ILE PHE TYR ARG ASN HIS THR LEU ARG GLY VAL SEQRES 29 A 454 PHE GLY THR MET LEU ASP SER GLU GLN ALA ARG LEU ASN SEQRES 30 A 454 PRO ALA SER ALA VAL PHE ASP SER THR SER ARG SER ARG SEQRES 31 A 454 ILE THR ARG VAL SER SER SER SER THR LYS ALA ALA TYR SEQRES 32 A 454 THR THR SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS SEQRES 33 A 454 THR TYR CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU SEQRES 34 A 454 PHE GLY GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE SEQRES 35 A 454 LEU LYS ASN ASP GLY VAL ARG GLU ALA ARG SER GLY SEQRES 1 B 454 GLY ALA PRO ILE HIS ASP PRO ASP PHE ILE GLY GLY ILE SEQRES 2 B 454 GLY LYS GLU LEU ILE VAL ASP ASN ALA SER ASP VAL THR SEQRES 3 B 454 SER PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE SEQRES 4 B 454 ILE PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE SEQRES 5 B 454 PRO SER PHE ASP MET SER ALA THR HIS TYR CYS TYR THR SEQRES 6 B 454 HIS ASN VAL ILE LEU SER GLY CYS ARG ASP HIS SER HIS SEQRES 7 B 454 SER HIS GLN TYR LEU ALA LEU GLY VAL LEU ARG THR THR SEQRES 8 B 454 ALA THR GLY ARG ILE PHE PHE SER THR LEU ARG SER ILE SEQRES 9 B 454 SER LEU ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SEQRES 10 B 454 SER ALA THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS SEQRES 11 B 454 VAL THR GLU THR GLU GLU GLU ASP TYR ASN SER ALA VAL SEQRES 12 B 454 PRO THR LEU MET ALA HIS GLY ARG LEU GLY PHE ASP GLY SEQRES 13 B 454 GLN TYR HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE SEQRES 14 B 454 GLU ASP TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SEQRES 15 B 454 SER PHE ILE ASP GLY ARG VAL TRP PHE SER VAL TYR GLY SEQRES 16 B 454 GLY LEU LYS PRO ASN SER PRO SER ASP THR VAL GLN GLU SEQRES 17 B 454 GLY LYS TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS SEQRES 18 B 454 PRO ASP GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SEQRES 19 B 454 SER TYR LYS PRO GLY ARG PHE GLY GLY LYS ARG ILE GLN SEQRES 20 B 454 GLN ALA ILE LEU SER ILE LYS VAL SER THR SER LEU GLY SEQRES 21 B 454 GLU ASP PRO VAL LEU THR VAL PRO PRO ASN THR VAL THR SEQRES 22 B 454 LEU MET GLY ALA GLU GLY ARG ILE LEU THR VAL GLY THR SEQRES 23 B 454 SER HIS PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER SEQRES 24 B 454 PRO ALA LEU LEU TYR PRO MET THR VAL SER ASN LYS THR SEQRES 25 B 454 ALA THR LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR SEQRES 26 B 454 ARG PRO GLY SER ILE PRO CYS GLN ALA SER ALA ARG CYS SEQRES 27 B 454 PRO ASN SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR SEQRES 28 B 454 PRO LEU ILE PHE TYR ARG ASN HIS THR LEU ARG GLY VAL SEQRES 29 B 454 PHE GLY THR MET LEU ASP SER GLU GLN ALA ARG LEU ASN SEQRES 30 B 454 PRO ALA SER ALA VAL PHE ASP SER THR SER ARG SER ARG SEQRES 31 B 454 ILE THR ARG VAL SER SER SER SER THR LYS ALA ALA TYR SEQRES 32 B 454 THR THR SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS SEQRES 33 B 454 THR TYR CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU SEQRES 34 B 454 PHE GLY GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE SEQRES 35 B 454 LEU LYS ASN ASP GLY VAL ARG GLU ALA ARG SER GLY SEQRES 1 C 454 GLY ALA PRO ILE HIS ASP PRO ASP PHE ILE GLY GLY ILE SEQRES 2 C 454 GLY LYS GLU LEU ILE VAL ASP ASN ALA SER ASP VAL THR SEQRES 3 C 454 SER PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE SEQRES 4 C 454 ILE PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE SEQRES 5 C 454 PRO SER PHE ASP MET SER ALA THR HIS TYR CYS TYR THR SEQRES 6 C 454 HIS ASN VAL ILE LEU SER GLY CYS ARG ASP HIS SER HIS SEQRES 7 C 454 SER HIS GLN TYR LEU ALA LEU GLY VAL LEU ARG THR THR SEQRES 8 C 454 ALA THR GLY ARG ILE PHE PHE SER THR LEU ARG SER ILE SEQRES 9 C 454 SER LEU ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SEQRES 10 C 454 SER ALA THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS SEQRES 11 C 454 VAL THR GLU THR GLU GLU GLU ASP TYR ASN SER ALA VAL SEQRES 12 C 454 PRO THR LEU MET ALA HIS GLY ARG LEU GLY PHE ASP GLY SEQRES 13 C 454 GLN TYR HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE SEQRES 14 C 454 GLU ASP TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SEQRES 15 C 454 SER PHE ILE ASP GLY ARG VAL TRP PHE SER VAL TYR GLY SEQRES 16 C 454 GLY LEU LYS PRO ASN SER PRO SER ASP THR VAL GLN GLU SEQRES 17 C 454 GLY LYS TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS SEQRES 18 C 454 PRO ASP GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SEQRES 19 C 454 SER TYR LYS PRO GLY ARG PHE GLY GLY LYS ARG ILE GLN SEQRES 20 C 454 GLN ALA ILE LEU SER ILE LYS VAL SER THR SER LEU GLY SEQRES 21 C 454 GLU ASP PRO VAL LEU THR VAL PRO PRO ASN THR VAL THR SEQRES 22 C 454 LEU MET GLY ALA GLU GLY ARG ILE LEU THR VAL GLY THR SEQRES 23 C 454 SER HIS PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER SEQRES 24 C 454 PRO ALA LEU LEU TYR PRO MET THR VAL SER ASN LYS THR SEQRES 25 C 454 ALA THR LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR SEQRES 26 C 454 ARG PRO GLY SER ILE PRO CYS GLN ALA SER ALA ARG CYS SEQRES 27 C 454 PRO ASN SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR SEQRES 28 C 454 PRO LEU ILE PHE TYR ARG ASN HIS THR LEU ARG GLY VAL SEQRES 29 C 454 PHE GLY THR MET LEU ASP SER GLU GLN ALA ARG LEU ASN SEQRES 30 C 454 PRO ALA SER ALA VAL PHE ASP SER THR SER ARG SER ARG SEQRES 31 C 454 ILE THR ARG VAL SER SER SER SER THR LYS ALA ALA TYR SEQRES 32 C 454 THR THR SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS SEQRES 33 C 454 THR TYR CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU SEQRES 34 C 454 PHE GLY GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE SEQRES 35 C 454 LEU LYS ASN ASP GLY VAL ARG GLU ALA ARG SER GLY HET SIA A1571 20 HET SIA B1570 20 HET SIA C1570 20 HET DAN A1570 20 HET WIA A1572 13 HET WIA B1571 13 HET DAN B1572 20 HET WIA C1571 13 HET DAN C1572 20 HETNAM SIA O-SIALIC ACID HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID HETNAM WIA METHYL(6S)-1-THIO-L-MANNO-HEXODIALDO-6,2-PYRANOSIDE FORMUL 4 SIA 3(C11 H19 N O9) FORMUL 7 DAN 3(C11 H17 N O8) FORMUL 8 WIA 3(C7 H12 O5 S) HELIX 1 1 ASP A 147 THR A 149 5 3 HELIX 2 2 THR A 257 TYR A 262 1 6 HELIX 3 3 ASP A 287 PHE A 292 1 6 HELIX 4 4 SER A 324 VAL A 329 1 6 HELIX 5 5 GLU A 347 SER A 357 1 11 HELIX 6 6 SER A 358 LYS A 360 5 3 HELIX 7 7 PRO A 361 GLY A 365 5 5 HELIX 8 8 ASP B 147 THR B 149 5 3 HELIX 9 9 THR B 257 ASN B 263 1 7 HELIX 10 10 ASP B 287 PHE B 292 1 6 HELIX 11 11 SER B 324 GLU B 331 1 8 HELIX 12 12 GLU B 347 SER B 358 1 12 HELIX 13 13 PRO B 361 GLY B 365 5 5 HELIX 14 14 ASP C 129 ILE C 133 5 5 HELIX 15 15 ASP C 147 THR C 149 5 3 HELIX 16 16 THR C 257 TYR C 262 1 6 HELIX 17 17 ASP C 287 PHE C 292 1 6 HELIX 18 18 SER C 324 GLN C 330 1 7 HELIX 19 19 GLU C 347 SER C 358 1 12 HELIX 20 20 PRO C 361 GLY C 365 5 5 SHEET 1 AA 4 ILE A 141 VAL A 142 0 SHEET 2 AA 4 PRO A 473 PHE A 478 1 O LEU A 476 N ILE A 141 SHEET 3 AA 4 LEU A 484 THR A 490 -1 N ARG A 485 O ILE A 477 SHEET 4 AA 4 SER A 503 PHE A 506 -1 O ALA A 504 N GLY A 489 SHEET 1 AB 4 PHE A 151 PRO A 153 0 SHEET 2 AB 4 PHE A 556 LYS A 567 -1 O LEU A 566 N TYR A 152 SHEET 3 AB 4 LYS A 539 SER A 549 -1 O THR A 540 N ILE A 565 SHEET 4 AB 4 ALA A 524 VAL A 534 -1 N ALA A 525 O GLU A 547 SHEET 1 AC 4 CYS A 172 MET A 180 0 SHEET 2 AC 4 TYR A 185 ILE A 192 -1 O CYS A 186 N ASP A 179 SHEET 3 AC 4 HIS A 203 THR A 213 -1 O HIS A 203 N VAL A 191 SHEET 4 AC 4 ILE A 219 LEU A 229 -1 O PHE A 220 N ARG A 212 SHEET 1 AD 4 ARG A 235 THR A 243 0 SHEET 2 AD 4 GLY A 246 LYS A 253 -1 O GLY A 246 N THR A 243 SHEET 3 AD 4 MET A 270 GLY A 276 -1 O ALA A 271 N CYS A 251 SHEET 4 AD 4 TYR A 281 ASP A 285 -1 O HIS A 282 N ARG A 274 SHEET 1 AE 3 TRP A 295 PRO A 300 0 SHEET 2 AE 3 ARG A 311 LEU A 320 -1 O TYR A 317 N TYR A 299 SHEET 3 AE 3 SER A 306 ILE A 308 -1 O SER A 306 N TRP A 313 SHEET 1 AF 4 TRP A 295 PRO A 300 0 SHEET 2 AF 4 ARG A 311 LEU A 320 -1 O TYR A 317 N TYR A 299 SHEET 3 AF 4 ARG A 368 LYS A 377 -1 O ARG A 368 N LEU A 320 SHEET 4 AF 4 VAL A 387 THR A 389 -1 O VAL A 387 N SER A 375 SHEET 1 AG 4 GLY A 402 VAL A 407 0 SHEET 2 AG 4 SER A 410 GLN A 415 -1 O SER A 410 N VAL A 407 SHEET 3 AG 4 ALA A 424 SER A 432 -1 O LEU A 425 N GLN A 415 SHEET 4 AG 4 TYR A 442 PHE A 444 -1 O TYR A 442 N LEU A 426 SHEET 1 AH 4 GLY A 402 VAL A 407 0 SHEET 2 AH 4 SER A 410 GLN A 415 -1 O SER A 410 N VAL A 407 SHEET 3 AH 4 ALA A 424 SER A 432 -1 O LEU A 425 N GLN A 415 SHEET 4 AH 4 THR A 435 LEU A 438 -1 O THR A 435 N SER A 432 SHEET 1 BA 5 ILE B 141 VAL B 142 0 SHEET 2 BA 5 TYR B 474 PHE B 478 1 O LEU B 476 N ILE B 141 SHEET 3 BA 5 LEU B 484 LEU B 492 -1 N ARG B 485 O ILE B 477 SHEET 4 BA 5 PRO B 501 PHE B 506 -1 O ALA B 502 N MET B 491 SHEET 5 BA 5 THR B 515 ARG B 516 -1 O THR B 515 N SER B 503 SHEET 1 BB 4 PHE B 151 PRO B 153 0 SHEET 2 BB 4 PHE B 556 LYS B 567 -1 O LEU B 566 N TYR B 152 SHEET 3 BB 4 LYS B 539 SER B 549 -1 O THR B 540 N ILE B 565 SHEET 4 BB 4 ALA B 524 VAL B 534 -1 N ALA B 525 O GLU B 547 SHEET 1 BC 4 CYS B 172 MET B 180 0 SHEET 2 BC 4 TYR B 185 ILE B 192 -1 O CYS B 186 N ASP B 179 SHEET 3 BC 4 HIS B 203 THR B 213 -1 O HIS B 203 N VAL B 191 SHEET 4 BC 4 ILE B 219 LEU B 229 -1 O PHE B 220 N ARG B 212 SHEET 1 BD 4 ARG B 235 ALA B 242 0 SHEET 2 BD 4 GLY B 246 LYS B 253 -1 O ASP B 248 N SER B 241 SHEET 3 BD 4 LEU B 269 GLY B 276 -1 O LEU B 269 N LYS B 253 SHEET 4 BD 4 TYR B 281 LEU B 286 -1 O HIS B 282 N ARG B 274 SHEET 1 BE 3 TRP B 295 PRO B 300 0 SHEET 2 BE 3 ARG B 311 LEU B 320 -1 O TYR B 317 N TYR B 299 SHEET 3 BE 3 SER B 306 ILE B 308 -1 O SER B 306 N TRP B 313 SHEET 1 BF 4 TRP B 295 PRO B 300 0 SHEET 2 BF 4 ARG B 311 LEU B 320 -1 O TYR B 317 N TYR B 299 SHEET 3 BF 4 ARG B 368 LYS B 377 -1 O ARG B 368 N LEU B 320 SHEET 4 BF 4 GLU B 384 THR B 389 -1 O GLU B 384 N LYS B 377 SHEET 1 BG 7 GLY B 402 VAL B 407 0 SHEET 2 BG 7 SER B 410 GLN B 415 -1 O SER B 410 N VAL B 407 SHEET 3 BG 7 ALA B 424 SER B 432 -1 N LEU B 425 O GLN B 415 SHEET 4 BG 7 THR B 435 LEU B 438 -1 O THR B 435 N SER B 432 SHEET 5 BG 7 ALA B 424 SER B 432 -1 O THR B 430 N THR B 437 SHEET 6 BG 7 TYR B 442 PHE B 444 -1 O TYR B 442 N LEU B 426 SHEET 7 BG 7 ALA B 424 SER B 432 -1 O ALA B 424 N PHE B 444 SHEET 1 CA 5 ILE C 141 VAL C 142 0 SHEET 2 CA 5 TYR C 474 PHE C 478 1 O LEU C 476 N ILE C 141 SHEET 3 CA 5 LEU C 484 LEU C 492 -1 N ARG C 485 O ILE C 477 SHEET 4 CA 5 PRO C 501 ASP C 507 -1 O ALA C 502 N MET C 491 SHEET 5 CA 5 ARG C 511 ARG C 516 -1 N SER C 512 O VAL C 505 SHEET 1 CB 4 PHE C 151 PRO C 153 0 SHEET 2 CB 4 PHE C 556 LYS C 567 -1 O LEU C 566 N TYR C 152 SHEET 3 CB 4 LYS C 539 SER C 549 -1 O THR C 540 N ILE C 565 SHEET 4 CB 4 ALA C 524 VAL C 534 -1 N ALA C 525 O GLU C 547 SHEET 1 CC 4 CYS C 172 MET C 180 0 SHEET 2 CC 4 TYR C 185 ILE C 192 -1 O CYS C 186 N ASP C 179 SHEET 3 CC 4 HIS C 203 THR C 213 -1 O HIS C 203 N VAL C 191 SHEET 4 CC 4 ILE C 219 LEU C 229 -1 O PHE C 220 N ARG C 212 SHEET 1 CD 4 ARG C 235 THR C 243 0 SHEET 2 CD 4 GLY C 246 LYS C 253 -1 O GLY C 246 N THR C 243 SHEET 3 CD 4 LEU C 269 LEU C 275 -1 O LEU C 269 N LYS C 253 SHEET 4 CD 4 TYR C 281 ASP C 285 -1 O HIS C 282 N ARG C 274 SHEET 1 CE 7 TRP C 295 PRO C 300 0 SHEET 2 CE 7 ARG C 311 LEU C 320 -1 O TYR C 317 N TYR C 299 SHEET 3 CE 7 SER C 306 ILE C 308 -1 O SER C 306 N TRP C 313 SHEET 4 CE 7 ARG C 311 LEU C 320 -1 O ARG C 311 N ILE C 308 SHEET 5 CE 7 GLU C 384 THR C 389 0 SHEET 6 CE 7 ARG C 368 LYS C 377 -1 O ILE C 373 N THR C 389 SHEET 7 CE 7 ARG C 311 LEU C 320 -1 O VAL C 312 N ILE C 376 SHEET 1 CF 7 GLY C 402 VAL C 407 0 SHEET 2 CF 7 SER C 410 GLN C 415 -1 O SER C 410 N VAL C 407 SHEET 3 CF 7 ALA C 424 THR C 430 -1 O TYR C 427 N LEU C 413 SHEET 4 CF 7 THR C 437 LEU C 438 -1 O THR C 437 N THR C 430 SHEET 5 CF 7 ALA C 424 THR C 430 -1 O THR C 430 N THR C 437 SHEET 6 CF 7 TYR C 442 PHE C 444 -1 O TYR C 442 N LEU C 426 SHEET 7 CF 7 ALA C 424 THR C 430 -1 O ALA C 424 N PHE C 444 SSBOND 1 CYS A 172 CYS A 196 SSBOND 2 CYS A 186 CYS A 247 SSBOND 3 CYS A 238 CYS A 251 SSBOND 4 CYS A 344 CYS A 461 SSBOND 5 CYS A 455 CYS A 465 SSBOND 6 CYS A 531 CYS A 542 SSBOND 7 CYS B 172 CYS B 196 SSBOND 8 CYS B 186 CYS B 247 SSBOND 9 CYS B 238 CYS B 251 SSBOND 10 CYS B 344 CYS B 461 SSBOND 11 CYS B 455 CYS B 465 SSBOND 12 CYS B 531 CYS B 542 SSBOND 13 CYS C 172 CYS C 196 SSBOND 14 CYS C 186 CYS C 247 SSBOND 15 CYS C 238 CYS C 251 SSBOND 16 CYS C 344 CYS C 461 SSBOND 17 CYS C 455 CYS C 465 SSBOND 18 CYS C 531 CYS C 542 LINK C2 SIA A1571 S1 WIA A1572 LINK C2 SIA B1570 S1 WIA B1571 LINK C2 SIA C1570 S1 WIA C1571 CISPEP 1 ILE A 453 PRO A 454 0 0.55 CISPEP 2 ILE B 453 PRO B 454 0 -0.06 CISPEP 3 ILE C 453 PRO C 454 0 0.06 SITE 1 AC1 9 ARG A 174 GLU A 258 TYR A 299 TYR A 317 SITE 2 AC1 9 ARG A 363 GLU A 401 ARG A 416 ARG A 498 SITE 3 AC1 9 TYR A 526 SITE 1 AC2 7 THR A 168 GLY A 169 PHE B 156 THR B 515 SITE 2 AC2 7 ARG B 516 SER B 518 SER B 519 SITE 1 AC4 8 ARG B 174 ILE B 175 GLU B 258 TYR B 317 SITE 2 AC4 8 GLU B 401 ARG B 416 ARG B 498 TYR B 526 SITE 1 AC5 6 PHE A 156 THR A 515 ARG A 516 SER A 519 SITE 2 AC5 6 THR B 168 GLY B 169 SITE 1 AC6 1 SER A 519 SITE 1 AC7 6 PHE C 156 GLY C 169 THR C 515 ARG C 516 SITE 2 AC7 6 SER C 518 SER C 519 SITE 1 AC8 1 SER C 519 SITE 1 AC9 7 ARG C 174 GLU C 258 TYR C 317 GLU C 401 SITE 2 AC9 7 ARG C 416 ARG C 498 TYR C 526 CRYST1 115.070 115.070 283.960 90.00 90.00 90.00 P 41 21 2 24 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 0.008690 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008690 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003522 0.00000 MTRIX1 1 0.702240 0.704600 0.102020 -0.20411 1 MTRIX2 1 0.703150 -0.708860 0.055680 0.26087 1 MTRIX3 1 0.111550 0.032640 -0.993220 0.62620 1