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HEADER HYDROLASE 30-JAN-98 1A4Q TITLE INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH TITLE 2 DIHYDROPYRAN-PHENETHYL-PROPYL-CARBOXAMIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RESIDUES 76-465; COMPND 5 SYNONYM: SIALIDASE; COMPND 6 EC: 3.2.1.18 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA B VIRUS; SOURCE 3 STRAIN: B/BEIJING/1/87 KEYWDS HYDROLASE, GLYCOSIDASE, GLYCOSYLATED PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.CLEASBY,O.SINGH,T.SKARZYNSKI,A.J.WONACOTT REVDAT 2 20-APR-99 1A4Q 3 ATOM HET SOURCE COMPND REVDAT 2 2 3 REMARK HETATM KEYWDS HEADER REVDAT 2 3 3 MODRES TER CONECT REVDAT 1 02-MAR-99 1A4Q 0 JRNL AUTH N.R.TAYLOR,A.CLEASBY,O.SINGH,T.SKARZYNSKI, JRNL AUTH 2 A.J.WONACOTT,P.W.SMITH,S.L.SOLLIS,P.D.HOWES, JRNL AUTH 3 P.C.CHERRY,R.BETHELL,P.COLMAN,J.VARGHESE JRNL TITL DIHYDROPYRANCARBOXAMIDES RELATED TO ZANAMIVIR: A JRNL TITL 2 NEW SERIES OF INHIBITORS OF INFLUENZA VIRUS JRNL TITL 3 SIALIDASES. 2. CRYSTALLOGRAPHIC AND MOLECULAR JRNL TITL 4 MODELING STUDY OF COMPLEXES OF JRNL TITL 5 4-AMINO-4H-PYRAN-6-CARBOXAMIDES AND SIALIDASE FROM JRNL TITL 6 INFLUENZA VIRUS TYPES A AND B. JRNL REF J.MED.CHEM. V. 41 798 1998 JRNL REFN ASTM JMCMAR US ISSN 0022-2623 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH W.P.BURMEISTER,R.W.RUIGROK,S.CUSACK REMARK 1 TITL THE 2.2 A RESOLUTION CRYSTAL STRUCTURE OF REMARK 1 TITL 2 INFLUENZA B NEURAMINIDASE AND ITS COMPLEX WITH REMARK 1 TITL 3 SIALIC ACID REMARK 1 REF EMBO J. V. 11 49 1992 REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REFERENCE 2 REMARK 1 AUTH W.P.BURMEISTER,R.S.DANIELS,S.DAYAN,J.GAGNON, REMARK 1 AUTH 2 S.CUSACK,R.W.RUIGROK REMARK 1 TITL SEQUENCE AND CRYSTALLIZATION OF INFLUENZA VIRUS REMARK 1 TITL 2 B/BEIJING/1/87 NEURAMINIDASE REMARK 1 REF VIROLOGY V. 180 266 1991 REMARK 1 REFN ASTM VIRLAX US ISSN 0042-6822 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 77031 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL 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 : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.70 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8601 REMARK 3 BIN R VALUE (WORKING SET) : 0.2860 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 : 6072 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 87 REMARK 3 SOLVENT ATOMS : 497 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 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) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 2.70 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.16 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) : 2.000 ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.000 ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : 2.700 ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.000 ; 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 : ENGH.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPENGH.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE TWO MONOMERS IN THE REMARK 3 CRYSTALLOGRAPHIC ASYMMETRIC UNIT HAVE BEEN REFINED REMARK 3 INDEPENDENTLY. REMARK 4 REMARK 4 1A4Q 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 (2007-03-16) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : FEB-1995 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.80 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX9.6 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.89 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 208669 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 34.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : 0.09200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER REMARK 200 SOFTWARE USED: X-PLOR 3.8 REMARK 200 STARTING MODEL: 1NSC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.8 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,1/3+Z REMARK 290 3555 -X+Y,-X,2/3+Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,2/3-Z REMARK 290 6555 -X,-X+Y,1/3-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 73.70000 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 147.40000 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 147.40000 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 73.70000 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 2 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 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 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 MET A 238 CG - SD - CE ANGL. DEV. = 23.4 DEGREES REMARK 500 THR B 165 N - CA - CB ANGL. DEV. =-18.3 DEGREES REMARK 500 MET B 238 CG - SD - CE ANGL. DEV. = 18.9 DEGREES REMARK 500 VAL B 270 N - CA - CB ANGL. DEV. =-17.8 DEGREES REMARK 500 LYS B 434 CA - CB - CG ANGL. DEV. = 16.6 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 291 DISTANCE = 5.50 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CHA REMARK 800 SITE_DESCRIPTION: HIGH AFFINITY CALCIUM BINDING SITE IN CHAIN A. REMARK 800 SITE_IDENTIFIER: CLA REMARK 800 SITE_DESCRIPTION: LOW AFFINITY CALCIUM BINDING SITE IN CHAIN A. REMARK 800 SITE_IDENTIFIER: LIA REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR INHIBITOR IN CHAIN A. REMARK 800 SITE_IDENTIFIER: CHB REMARK 800 SITE_DESCRIPTION: HIGH AFFINITY CALCIUM BINDING SITE IN CHAIN B. REMARK 800 SITE_IDENTIFIER: CLB REMARK 800 SITE_DESCRIPTION: LOW AFFINITY CALCIUM BINDING SITE IN CHAIN B. REMARK 800 SITE_IDENTIFIER: LIB REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR INHIBITOR IN CHAIN B. DBREF 1A4Q A 76 465 UNP P27907 NRAM_INBBE 76 465 DBREF 1A4Q B 76 465 UNP P27907 NRAM_INBBE 76 465 SEQRES 1 A 390 GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY SEQRES 2 A 390 SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG SEQRES 3 A 390 PHE GLY GLU ALA ARG GLY ASN SER ALA PRO LEU ILE ILE SEQRES 4 A 390 ARG GLU PRO PHE ILE ALA CYS GLY PRO LYS GLU CYS LYS SEQRES 5 A 390 HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY SEQRES 6 A 390 TYR TYR ASN GLY THR ARG GLU ASP ARG ASN LYS LEU ARG SEQRES 7 A 390 HIS LEU ILE SER VAL LYS LEU GLY LYS ILE PRO THR VAL SEQRES 8 A 390 GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER SEQRES 9 A 390 ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL SEQRES 10 A 390 ASP GLY PRO ASP SER ASN ALA LEU ILE LYS ILE LYS TYR SEQRES 11 A 390 GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA ASN SEQRES 12 A 390 ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE SEQRES 13 A 390 GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA SEQRES 14 A 390 SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU SEQRES 15 A 390 GLY ARG ILE ILE LYS GLU ILE PHE PRO THR GLY ARG VAL SEQRES 16 A 390 GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN SEQRES 17 A 390 LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR SEQRES 18 A 390 ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP SEQRES 19 A 390 THR ALA GLU ILE ARG LEU MET CYS THR GLU THR TYR LEU SEQRES 20 A 390 ASP THR PRO ARG PRO ASP ASP GLY SER ILE THR GLY PRO SEQRES 21 A 390 CYS GLU SER ASN GLY ASP LYS GLY ARG GLY GLY ILE LYS SEQRES 22 A 390 GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY SEQRES 23 A 390 ARG TRP TYR SER ARG THR MET SER LYS THR GLU ARG MET SEQRES 24 A 390 GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP SEQRES 25 A 390 THR ASP SER ASP ALA LEU ALA HIS SER GLY VAL MET VAL SEQRES 26 A 390 SER MET LYS GLU PRO GLY TRP TYR SER PHE GLY PHE GLU SEQRES 27 A 390 ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE SEQRES 28 A 390 GLU MET VAL HIS ASP GLY GLY LYS LYS THR TRP HIS SER SEQRES 29 A 390 ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN SEQRES 30 A 390 LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU SEQRES 1 B 390 GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY SEQRES 2 B 390 SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG SEQRES 3 B 390 PHE GLY GLU ALA ARG GLY ASN SER ALA PRO LEU ILE ILE SEQRES 4 B 390 ARG GLU PRO PHE ILE ALA CYS GLY PRO LYS GLU CYS LYS SEQRES 5 B 390 HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY SEQRES 6 B 390 TYR TYR ASN GLY THR ARG GLU ASP ARG ASN LYS LEU ARG SEQRES 7 B 390 HIS LEU ILE SER VAL LYS LEU GLY LYS ILE PRO THR VAL SEQRES 8 B 390 GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER SEQRES 9 B 390 ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL SEQRES 10 B 390 ASP GLY PRO ASP SER ASN ALA LEU ILE LYS ILE LYS TYR SEQRES 11 B 390 GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA ASN SEQRES 12 B 390 ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE SEQRES 13 B 390 GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA SEQRES 14 B 390 SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU SEQRES 15 B 390 GLY ARG ILE ILE LYS GLU ILE PHE PRO THR GLY ARG VAL SEQRES 16 B 390 GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN SEQRES 17 B 390 LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR SEQRES 18 B 390 ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP SEQRES 19 B 390 THR ALA GLU ILE ARG LEU MET CYS THR GLU THR TYR LEU SEQRES 20 B 390 ASP THR PRO ARG PRO ASP ASP GLY SER ILE THR GLY PRO SEQRES 21 B 390 CYS GLU SER ASN GLY ASP LYS GLY ARG GLY GLY ILE LYS SEQRES 22 B 390 GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY SEQRES 23 B 390 ARG TRP TYR SER ARG THR MET SER LYS THR GLU ARG MET SEQRES 24 B 390 GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP SEQRES 25 B 390 THR ASP SER ASP ALA LEU ALA HIS SER GLY VAL MET VAL SEQRES 26 B 390 SER MET LYS GLU PRO GLY TRP TYR SER PHE GLY PHE GLU SEQRES 27 B 390 ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE SEQRES 28 B 390 GLU MET VAL HIS ASP GLY GLY LYS LYS THR TRP HIS SER SEQRES 29 B 390 ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN SEQRES 30 B 390 LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU MODRES 1A4Q ASN A 283 ASN N-GLYCOSYLATED MODRES 1A4Q ASN B 283 ASN N-GLYCOSYLATED MODRES ASN A 283 ASN GLYCOSYLATION SITE MODRES ASN B 283 ASN GLYCOSYLATION SITE HET NAG A 1 14 HET NAG B 1 14 HET CA A 2 1 HET CA B 2 1 HET CA 3 1 HET DPC A 2 28 HET DPC B 2 28 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM CA CALCIUM ION HETNAM DPC 5-ACETYLAMINO-4-AMINO-6-(PHENETHYL-PROPYL-CARBAMOYL)- HETNAM 2 DPC 5,6-DIHYDRO-4H-PYRAN-2-CARBOXYLIC ACID HETSYN NAG NAG FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 5 CA 3(CA 2+) FORMUL 8 DPC 2(C20 H27 N3 O5) FORMUL 10 HOH *497(H2 O) HELIX 1 1 PRO A 99 PHE A 102 5 4 HELIX 2 2 ASP A 196 ASN A 198 5 3 HELIX 3 3 PRO B 99 PHE B 102 5 4 HELIX 4 4 ASP B 196 ASN B 198 5 3 SHEET 1 1A 4 ILE A 113 CYS A 121 0 SHEET 2 1A 4 CYS A 126 THR A 132 -1 N LEU A 131 O ARG A 115 SHEET 3 1A 4 HIS A 154 LYS A 159 -1 O VAL A 158 N HIS A 128 SHEET 4 1A 4 ILE A 170 ALA A 174 -1 O ILE A 170 N SER A 157 SHEET 1 2A 4 SER A 177 HIS A 182 0 SHEET 2 2A 4 TRP A 187 ASP A 193 -1 N VAL A 192 O SER A 177 SHEET 3 2A 4 LEU A 200 TYR A 205 -1 N LYS A 202 O GLY A 191 SHEET 4 2A 4 ALA A 208 HIS A 214 -1 N TYR A 213 O ILE A 201 SHEET 1 3AA 4 ARG A 222 THR A 223 0 SHEET 2 3AA 4 ASP A 234 GLY A 242 -1 O THR A 240 N ARG A 222 SHEET 3 3AA 4 SER A 248 ARG A 256 -1 N LEU A 253 O LEU A 237 SHEET 4 3AA 4 ARG A 259 ILE A 264 -1 N ARG A 259 O ARG A 256 SHEET 1 3BA 4 ASN A 229 ILE A 231 0 SHEET 2 3BA 4 ASP A 234 GLY A 242 -1 O TYR A 236 N ASN A 229 SHEET 3 3BA 4 SER A 248 ARG A 256 -1 N LEU A 253 O LEU A 237 SHEET 4 3BA 4 ARG A 259 ILE A 264 -1 N ARG A 259 O ARG A 256 SHEET 1 4A 4 GLU A 274 PHE A 280 0 SHEET 2 4A 4 THR A 285 ARG A 291 -1 O ARG A 291 N GLU A 274 SHEET 3 4A 4 PRO A 300 ASN A 305 -1 O PRO A 300 N CYS A 290 SHEET 4 4A 4 THR A 310 LEU A 315 -1 O THR A 310 N ASN A 305 SHEET 1 5A 4 PHE A 351 ARG A 355 0 SHEET 2 5A 4 ILE A 360 ARG A 366 -1 O TRP A 363 N VAL A 352 SHEET 3 5A 4 MET A 376 TYR A 382 -1 N GLU A 377 O ARG A 366 SHEET 4 5A 4 ALA A 394 VAL A 400 -1 N ALA A 394 O VAL A 380 SHEET 1 6A 4 SER A 409 LYS A 415 0 SHEET 2 6A 4 ASP A 420 HIS A 430 -1 O GLY A 425 N PHE A 410 SHEET 3 6A 4 SER A 439 LEU A 447 -1 O ALA A 443 N ILE A 426 SHEET 4 6A 4 PHE A 91 ILE A 97 -1 O ILE A 97 N THR A 442 SHEET 1 1B 4 ILE B 113 CYS B 121 0 SHEET 2 1B 4 CYS B 126 THR B 132 -1 N LEU B 131 O ARG B 115 SHEET 3 1B 4 HIS B 154 LYS B 159 -1 O VAL B 158 N HIS B 128 SHEET 4 1B 4 ILE B 170 ALA B 174 -1 O ILE B 170 N SER B 157 SHEET 1 2B 4 SER B 177 HIS B 182 0 SHEET 2 2B 4 TRP B 187 ASP B 193 -1 N VAL B 192 O SER B 177 SHEET 3 2B 4 LEU B 200 TYR B 205 -1 N LYS B 202 O GLY B 191 SHEET 4 2B 4 ALA B 208 HIS B 214 -1 N TYR B 213 O ILE B 201 SHEET 1 3AB 4 ARG B 222 THR B 223 0 SHEET 2 3AB 4 ASP B 234 GLY B 242 -1 O THR B 240 N ARG B 222 SHEET 3 3AB 4 SER B 248 ARG B 256 -1 N LEU B 253 O LEU B 237 SHEET 4 3AB 4 ARG B 259 ILE B 264 -1 N ARG B 259 O ARG B 256 SHEET 1 3BB 4 ASN B 229 ILE B 231 0 SHEET 2 3BB 4 ASP B 234 GLY B 242 -1 O TYR B 236 N ASN B 229 SHEET 3 3BB 4 SER B 248 ARG B 256 -1 N LEU B 253 O LEU B 237 SHEET 4 3BB 4 ARG B 259 ILE B 264 -1 N ARG B 259 O ARG B 256 SHEET 1 4B 4 GLU B 274 PHE B 280 0 SHEET 2 4B 4 THR B 285 ARG B 291 -1 O ARG B 291 N GLU B 274 SHEET 3 4B 4 PRO B 300 ASN B 305 -1 O PRO B 300 N CYS B 290 SHEET 4 4B 4 THR B 310 LEU B 315 -1 O THR B 310 N ASN B 305 SHEET 1 5B 4 PHE B 351 ARG B 355 0 SHEET 2 5B 4 ILE B 360 ARG B 366 -1 O TRP B 363 N VAL B 352 SHEET 3 5B 4 MET B 376 TYR B 382 -1 N GLU B 377 O ARG B 366 SHEET 4 5B 4 ALA B 394 VAL B 400 -1 N ALA B 394 O VAL B 380 SHEET 1 6B 4 SER B 409 LYS B 415 0 SHEET 2 6B 4 ASP B 420 HIS B 430 -1 O GLY B 425 N PHE B 410 SHEET 3 6B 4 SER B 439 LEU B 447 -1 O ALA B 443 N ILE B 426 SHEET 4 6B 4 PHE B 91 ILE B 97 -1 O ILE B 97 N THR B 442 TURN 1 A1 GLU A 104 GLY A 107 TURN 2 A2 TYR A 142 THR A 145 TURN 3 A3 LYS A 159 LYS A 162 TURN 4 A4 PRO A 195 ASN A 198 TURN 5 A5 TYR A 205 ALA A 208 TURN 6 A6 ILE A 231 ASP A 234 TURN 7 A7 SER A 243 GLY A 246 TURN 8 A8 ARG A 256 ARG A 259 TURN 9 A9 ASP A 328 SER A 331 TURN 10 A10 PRO A 335 SER A 338 TURN 11 A11 ASP A 385 THR A 388 TURN 12 A12 SER A 401 GLU A 404 TURN 13 A13 GLY A 433 THR A 436 TURN 14 A14 ASP A 462 LEU A 465 TURN 15 B1 GLU B 104 GLY B 107 TURN 16 B2 TYR B 142 THR B 145 TURN 17 B3 LYS B 159 LYS B 162 TURN 18 B4 PRO B 195 ASN B 198 TURN 19 B5 TYR B 205 ALA B 208 TURN 20 B6 ILE B 231 ASP B 234 TURN 21 B7 SER B 243 GLY B 246 TURN 22 B8 ARG B 256 ARG B 259 TURN 23 B9 ASP B 328 SER B 331 TURN 24 B10 PRO B 335 SER B 338 TURN 25 B11 ASP B 385 THR B 388 TURN 26 B12 SER B 401 GLU B 404 TURN 27 B13 GLY B 433 THR B 436 TURN 28 B14 ASP B 462 LEU B 465 SSBOND 1 CYS A 86 CYS A 419 SSBOND 2 CYS A 121 CYS A 126 SSBOND 3 CYS A 181 CYS A 228 SSBOND 4 CYS A 230 CYS A 235 SSBOND 5 CYS A 276 CYS A 290 SSBOND 6 CYS A 278 CYS A 288 SSBOND 7 CYS A 317 CYS A 336 SSBOND 8 CYS A 423 CYS A 446 SSBOND 9 CYS B 86 CYS B 419 SSBOND 10 CYS B 121 CYS B 126 SSBOND 11 CYS B 181 CYS B 228 SSBOND 12 CYS B 230 CYS B 235 SSBOND 13 CYS B 276 CYS B 290 SSBOND 14 CYS B 278 CYS B 288 SSBOND 15 CYS B 317 CYS B 336 SSBOND 16 CYS B 423 CYS B 446 LINK CA CA A 2 O ASP A 292 LINK CA CA A 2 O GLY A 345 LINK CA CA B 2 O ASP B 292 LINK C1 NAG A 1 ND2 ASN A 283 LINK C1 NAG B 1 ND2 ASN B 283 CISPEP 1 GLN A 137 PRO A 138 0 -0.60 CISPEP 2 THR A 324 PRO A 325 0 -0.88 CISPEP 3 GLN B 137 PRO B 138 0 -2.94 CISPEP 4 THR B 324 PRO B 325 0 -2.82 SITE 1 CHA 5 ASP A 323 GLY A 343 GLY A 345 THR A 296 SITE 2 CHA 5 ASP A 292 SITE 1 CLA 1 GLU A 167 SITE 1 LIA 10 ASP A 323 ARG A 115 ARG A 291 ARG A 149 SITE 2 LIA 10 ILE A 220 ARG A 222 TRP A 176 GLU A 274 SITE 3 LIA 10 ASP A 148 TYR A 408 SITE 1 CHB 5 ASP B 323 GLY B 343 GLY B 345 THR B 296 SITE 2 CHB 5 ASP B 292 SITE 1 CLB 1 GLU B 167 SITE 1 LIB 10 ASP B 323 ARG B 115 ARG B 291 ARG B 149 SITE 2 LIB 10 ILE B 220 ARG B 222 TRP B 176 GLU B 274 SITE 3 LIB 10 ASP B 148 TYR B 408 CRYST1 88.300 88.300 221.100 90.00 90.00 120.00 P 31 2 1 12 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 0.011325 0.006539 0.000000 0.00000 SCALE2 0.000000 0.013077 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004523 0.00000 MTRIX1 1 0.250000 0.433000 -0.866000 0.00000 1 MTRIX2 1 0.433000 0.750000 0.500000 0.00000 1 MTRIX3 1 0.866000 -0.500000 0.000000 0.00000 1