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HEADER HYDROLASE (O-GLYCOSYL) 12-DEC-94 1IVB TITLE STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS TITLE 2 NEURAMINIDASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: INFLUENZA VIRUS B/LEE/40 NEURAMINIDASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA B VIRUS KEYWDS HYDROLASE (O-GLYCOSYL) EXPDTA X-RAY DIFFRACTION AUTHOR M.J.JEDRZEJAS,M.LUO REVDAT 1 31-MAR-95 1IVB 0 JRNL AUTH M.J.JEDRZEJAS,S.SINGH,W.J.BROUILLETTE,W.G.LAVER, JRNL AUTH 2 G.M.AIR,M.LUO JRNL TITL STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA JRNL TITL 2 VIRUS NEURAMINIDASE. JRNL REF BIOCHEMISTRY V. 34 3144 1995 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.SINGH,M.J.JEDRZEJAS,G.M.AIR,M.LUO,W.G.LAVER, REMARK 1 AUTH 2 W.J.BROUILLETTE REMARK 1 TITL STRUCTURE-BASED INHIBITORS OF INFLUENZA VIRAL REMARK 1 TITL 2 NEURAMINIDASE. A BENZOIC ACID LEAD WITH NOVEL REMARK 1 TITL 3 INTERACTION REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH M.N.JANAKIRAMAN,C.L.WHITE,W.G.LAVER,G.M.AIR,M.LUO REMARK 1 TITL STRUCTURE OF INFLUENZA VIRUS NEURAMINIDASE REMARK 1 TITL 2 B(SLASH)LEE(SLASH)40 COMPLEXED WITH SIALIC ACID REMARK 1 TITL 3 AND A DEHYDRO ANALOG AT 1.8 ANGSTROMS RESOLUTION: REMARK 1 TITL 4 IMPLICATIONS FOR THE CATALYTIC MECHANISM REMARK 1 REF BIOCHEMISTRY V. 33 8172 1994 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.N.VARGHESE,P.M.COLMAN REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE NEURAMINIDASE REMARK 1 TITL 2 OF INFLUENZA VIRUS A(SLASH)TOKYO(SLASH)3(SLASH)67 REMARK 1 TITL 3 AT 2.2 ANGSTROMS RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 221 473 1991 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 4 REMARK 1 AUTH W.R.TULIP,J.N.VARGHESE,A.T.BAKER,A.VAN DONKELAAR, REMARK 1 AUTH 2 W.G.LAVER,R.G.WEBSTER,P.M.COLMAN REMARK 1 TITL REFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA REMARK 1 TITL 2 VIRUS NEURAMINIDASE AND ESCAPE MUTANTS REMARK 1 REF J.MOL.BIOL. V. 221 487 1991 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000 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 : 14129 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) : 0.189 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 : 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 : 3736 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 49 REMARK 3 SOLVENT ATOMS : 0 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) : 0.016 REMARK 3 BOND ANGLES (DEGREES) : 2.14 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IVB 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 (2007-03-17) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15271 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL 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: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.59 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 1/2-Y,1/2+X,Z REMARK 290 4555 1/2+Y,1/2-X,Z REMARK 290 5555 1/2-X,1/2+Y,-Z REMARK 290 6555 1/2+X,1/2-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 62.27000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.27000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.27000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.27000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.27000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.27000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.27000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.27000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 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 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 124.54000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 62.27000 REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -62.27000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 62.27000 REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 62.27000 REMARK 350 BIOMT3 4 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 CA CA 501 LIES ON A SPECIAL POSITION. 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 239 SD MET A 239 CE 0.108 REMARK 500 MET A 357 SD MET A 357 CE 0.107 REMARK 500 MET A 429 SD MET A 429 CE 0.109 REMARK 500 MET A 464 SD MET A 464 CE 0.132 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 THR A 189 N - CA - C ANGL. DEV. =-13.9 DEGREES REMARK 500 ALA A 290 N - CA - C ANGL. DEV. =-17.4 DEGREES REMARK 500 TYR A 296 N - CA - C ANGL. DEV. = 16.4 DEGREES REMARK 500 GLN A 355 N - CA - C ANGL. DEV. =-12.8 DEGREES REMARK 500 LEU A 379 CA - CB - CG ANGL. DEV. = 21.8 DEGREES REMARK 500 LYS A 435 N - CA - C ANGL. DEV. = 13.9 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 SER A 283 -169.54 148.83 DBREF 1IVB A 77 466 UNP P03474 NRAM_INBLE 77 466 SEQADV 1IVB ARG A 382 UNP P03474 LYS 382 CONFLICT 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 ILE LYS GLY ASN SER ALA PRO LEU ILE ILE SEQRES 4 A 390 ARG GLU PRO PHE VAL ALA CYS GLY PRO LYS GLU CYS ARG 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 LYS ASP ARG ASN LYS LEU ARG SEQRES 7 A 390 HIS LEU VAL 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 ASN ASP ALA LEU VAL LYS ILE LYS TYR SEQRES 11 A 390 GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA HIS 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 LEU 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 LYS THR TYR LEU SEQRES 20 A 390 ASP THR PRO ARG PRO ASP ASP GLY SER ILE ALA GLY PRO SEQRES 21 A 390 CYS GLU SER ASN GLY ASP LYS TRP LEU 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 ASN 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 THR LEU SER GLY VAL MET VAL SEQRES 26 A 390 SER ILE GLU 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 ASP 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 MODRES 1IVB ASN A 284 ASN GLYCOSYLATION SITE FTNOTE 1 CIS PROLINE - PRO 139 FTNOTE 2 CIS PROLINE - PRO 326 HET NAG 467 28 HET CA 500 1 HET CA 501 1 HET ST1 471 19 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM CA CALCIUM ION HETNAM ST1 4-(ACETYLAMINO)-3-HYDROXY-5-NITROBENZOIC ACID HETSYN NAG NAG FORMUL 2 NAG C8 H15 N O6 FORMUL 3 CA 2(CA 2+) FORMUL 5 ST1 C9 H8 N2 O6 HELIX 1 1 PRO A 100 PHE A 103 5 4 SHEET 1 A 4 PHE A 119 CYS A 122 0 SHEET 2 A 4 CYS A 127 THR A 133 -1 N PHE A 130 O PHE A 119 SHEET 3 A 4 HIS A 155 LYS A 160 -1 N VAL A 159 O HIS A 129 SHEET 4 A 4 ILE A 171 ALA A 175 -1 N MET A 174 O LEU A 156 SHEET 1 B 4 SER A 178 HIS A 183 0 SHEET 2 B 4 TRP A 188 PRO A 196 -1 N VAL A 193 O SER A 178 SHEET 3 B 4 ASP A 199 TYR A 206 -1 N LYS A 205 O TYR A 190 SHEET 4 B 4 ALA A 209 HIS A 215 -1 N TYR A 214 O VAL A 202 SHEET 1 C 4 ASN A 230 ILE A 232 0 SHEET 2 C 4 ASP A 235 ILE A 240 -1 N TYR A 237 O ASN A 230 SHEET 3 C 4 ARG A 252 ILE A 256 -1 N ILE A 256 O CYS A 236 SHEET 4 C 4 ILE A 261 LEU A 266 -1 N ILE A 265 O PHE A 253 SHEET 1 D 4 THR A 278 PHE A 281 0 SHEET 2 D 4 THR A 286 ALA A 290 -1 N ALA A 290 O THR A 278 SHEET 3 D 4 PRO A 301 ASN A 306 -1 N LEU A 305 O ILE A 287 SHEET 4 D 4 THR A 311 LEU A 316 -1 N ARG A 315 O PHE A 302 SHEET 1 E 3 PHE A 352 ARG A 356 0 SHEET 2 E 3 ILE A 361 ARG A 367 -1 N TRP A 364 O VAL A 353 SHEET 3 E 3 GLU A 378 TYR A 383 -1 N ARG A 382 O ARG A 363 SHEET 1 F 4 SER A 410 LYS A 416 0 SHEET 2 F 4 ASP A 421 ASP A 432 -1 N GLY A 426 O PHE A 411 SHEET 3 F 4 HIS A 439 LEU A 448 -1 N TYR A 446 O ILE A 425 SHEET 4 F 4 PHE A 92 ILE A 98 -1 N ILE A 98 O THR A 443 SSBOND 1 CYS A 87 CYS A 420 SSBOND 2 CYS A 122 CYS A 127 SSBOND 3 CYS A 182 CYS A 229 SSBOND 4 CYS A 231 CYS A 236 SSBOND 5 CYS A 277 CYS A 291 SSBOND 6 CYS A 279 CYS A 289 SSBOND 7 CYS A 318 CYS A 337 SSBOND 8 CYS A 424 CYS A 447 LINK ND2 ASN A 284 C1 NAG 467 CISPEP 1 GLN A 138 PRO A 139 0 0.00 CISPEP 2 THR A 325 PRO A 326 0 0.49 SITE 1 CAT 11 ARG A 116 GLU A 117 ASP A 149 ARG A 150 SITE 2 CAT 11 TRP A 177 ILE A 221 ARG A 223 GLU A 275 SITE 3 CAT 11 ARG A 292 ARG A 374 TYR A 409 CRYST1 124.540 124.540 71.820 90.00 90.00 90.00 P 4 21 2 8 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 0.008030 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008030 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013924 0.00000