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HEADER HYDROLASE 09-MAR-04 1VCJ TITLE INFLUENZA B VIRUS NEURAMINIDASE COMPLEXED WITH 1-(4-CARBOXY- TITLE 2 2-(3-PENTYLAMINO)PHENYL)-5-AMINOMETHYL-5-HYDROXYMETHYL- TITLE 3 PYRROLIDIN-2-ONE COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CATALYTIC DOMAIN RESIDUES 78-466; COMPND 5 EC: 3.2.1.18 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA B VIRUS; SOURCE 3 ORGANISM_COMMON: VIRUS; SOURCE 4 STRAIN: B-LEE-40 KEYWDS NEURAMINIDASE, BENZOIC ACID INHIBITORS, SMALL MOLECULE KEYWDS 2 INHIBITOR, PROTEIN-INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR B.S.LOMMER,S.M.ALI,S.N.BAJPAI,W.J.BROUILLETTE,G.M.AIR,M.LUO REVDAT 2 21-JUN-05 1VCJ 1 JRNL REVDAT 1 23-MAR-04 1VCJ 0 SPRSDE 23-MAR-04 1VCJ 1UJA JRNL AUTH B.S.LOMMER,S.M.ALI,S.N.BAJPAI,W.J.BROUILLETTE, JRNL AUTH 2 G.M.AIR,M.LUO JRNL TITL A BENZOIC ACID INHIBITOR INDUCES A NOVEL JRNL TITL 2 CONFORMATIONAL CHANGE IN THE ACTIVE SITE OF JRNL TITL 3 INFLUENZA B VIRUS NEURAMINIDASE. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 1017 2004 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 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) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 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 : 18434 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHUOT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1843 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) : 2.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2940 REMARK 3 BIN FREE R VALUE : 0.3230 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 : 3031 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 25 REMARK 3 SOLVENT ATOMS : 106 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) : 0.29 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) : 0.35 REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.69 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 1VCJ 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 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB006463. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-OCT-1999 REMARK 200 TEMPERATURE (KELVIN) : 295.0 REMARK 200 PH : 6.80 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE MONOCHROMATOR, 0.3 REMARK 200 MM PINHOLE COLLIMATOR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SADIE REMARK 200 DATA SCALING SOFTWARE : SAINT REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18434 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 81.9 REMARK 200 DATA REDUNDANCY : 2.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08400 REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : 63.2 REMARK 200 DATA REDUNDANCY IN SHELL : 1.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.20700 REMARK 200 FOR SHELL : 2.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT 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 (%): 60.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM CHLORIDE, SODIUM REMARK 280 NITRATE, CALCIUM CHLORIDE, SODIUM AZIDE, PH 6.80, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K 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 62.18000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.18000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.18000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.18000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.18000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.18000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.18000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.18000 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 124.36000 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 62.18000 REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -62.18000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 62.18000 REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 62.18000 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 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 936 O HOH 812 1.80 REMARK 500 O HOH 649 O HOH 969 2.07 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 CG MET A 239 SD 0.114 REMARK 500 ARG A 260 CG ARG A 260 CD 0.115 REMARK 500 ARG A 260 CZ ARG A 260 NH1 -0.062 REMARK 500 MET A 464 SD MET A 464 CE 0.072 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 149 N - CA - C ANGL. DEV. = 10.5 DEGREES REMARK 500 TYR A 210 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 GLN A 225 N - CA - C ANGL. DEV. = 12.9 DEGREES REMARK 500 ALA A 290 N - CA - C ANGL. DEV. =-13.7 DEGREES REMARK 500 TYR A 296 N - CA - C ANGL. DEV. = 12.5 DEGREES REMARK 500 LYS A 435 N - CA - CB ANGL. DEV. =-14.8 DEGREES REMARK 500 LEU A 455 N - CA - C ANGL. DEV. = 13.0 DEGREES DBREF 1VCJ A 78 466 UNP P03474 NRAM_INBLE 78 466 SEQADV 1VCJ ARG A 382 UNP P03474 LYS 382 CONFLICT SEQRES 1 A 389 PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY SER SEQRES 2 A 389 THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG PHE SEQRES 3 A 389 GLY GLU ILE LYS GLY ASN SER ALA PRO LEU ILE ILE ARG SEQRES 4 A 389 GLU PRO PHE VAL ALA CYS GLY PRO LYS GLU CYS ARG HIS SEQRES 5 A 389 PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY TYR SEQRES 6 A 389 TYR ASN GLY THR ARG LYS ASP ARG ASN LYS LEU ARG HIS SEQRES 7 A 389 LEU VAL SER VAL LYS LEU GLY LYS ILE PRO THR VAL GLU SEQRES 8 A 389 ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER ALA SEQRES 9 A 389 CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL ASP SEQRES 10 A 389 GLY PRO ASP ASN ASP ALA LEU VAL LYS ILE LYS TYR GLY SEQRES 11 A 389 GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA HIS ASN SEQRES 12 A 389 ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE GLY SEQRES 13 A 389 GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA SER SEQRES 14 A 389 GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU GLY SEQRES 15 A 389 ARG ILE ILE LYS GLU ILE LEU PRO THR GLY ARG VAL GLU SEQRES 16 A 389 HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN LYS SEQRES 17 A 389 THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR ALA SEQRES 18 A 389 LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP THR SEQRES 19 A 389 ALA GLU ILE ARG LEU MET CYS THR LYS THR TYR LEU ASP SEQRES 20 A 389 THR PRO ARG PRO ASP ASP GLY SER ILE ALA GLY PRO CYS SEQRES 21 A 389 GLU SER ASN GLY ASP LYS TRP LEU GLY GLY ILE LYS GLY SEQRES 22 A 389 GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY ARG SEQRES 23 A 389 TRP TYR SER ARG THR MET SER LYS THR ASN ARG MET GLY SEQRES 24 A 389 MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP THR SEQRES 25 A 389 ASP SER ASP ALA LEU THR LEU SER GLY VAL MET VAL SER SEQRES 26 A 389 ILE GLU GLU PRO GLY TRP TYR SER PHE GLY PHE GLU ILE SEQRES 27 A 389 LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE GLU SEQRES 28 A 389 MET VAL HIS ASP GLY GLY LYS ASP THR TRP HIS SER ALA SEQRES 29 A 389 ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN LEU SEQRES 30 A 389 LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU HET IBA 1 25 HETNAM IBA 4-[(2R)-2-(AMINOMETHYL)-2-(HYDROXYMETHYL)-5- HETNAM 2 IBA OXOPYRROLIDIN-1-YL]-3-[(1-ETHYLPROPYL)AMINO]BENZOIC HETNAM 3 IBA ACID HETSYN IBA 1-(4-CARBOXY-2-(3-PENTYLAMINO)PHENYL)-5-AMINOMETHYL-5- HETSYN 2 IBA HYDROXYMETHYL-PYRROLIDIN-2-ONE FORMUL 2 IBA C18 H27 N3 O4 FORMUL 3 HOH *106(H2 O) HELIX 1 1 SER A 99 GLY A 104 5 6 HELIX 2 2 PRO A 196 ASP A 199 5 4 SHEET 1 A 4 PHE A 92 ILE A 98 0 SHEET 2 A 4 SER A 440 LEU A 448 -1 O ILE A 445 N ALA A 95 SHEET 3 A 4 ASP A 421 HIS A 431 -1 N HIS A 431 O SER A 440 SHEET 4 A 4 SER A 410 LYS A 416 -1 N ILE A 415 O VAL A 422 SHEET 1 B 4 LEU A 113 CYS A 122 0 SHEET 2 B 4 CYS A 127 ALA A 137 -1 O ALA A 136 N ILE A 114 SHEET 3 B 4 HIS A 155 LYS A 160 -1 O VAL A 157 N ALA A 131 SHEET 4 B 4 ILE A 171 ALA A 175 -1 O HIS A 173 N LEU A 156 SHEET 1 C 4 SER A 178 HIS A 183 0 SHEET 2 C 4 TRP A 188 ASP A 194 -1 O ILE A 191 N SER A 180 SHEET 3 C 4 LEU A 201 TYR A 206 -1 O LYS A 205 N TYR A 190 SHEET 4 C 4 ALA A 209 HIS A 215 -1 O ASP A 212 N ILE A 204 SHEET 1 D 3 ARG A 223 THR A 224 0 SHEET 2 D 3 ASP A 235 GLY A 243 -1 O THR A 241 N ARG A 223 SHEET 3 D 3 ASN A 230 ILE A 232 -1 N ILE A 232 O ASP A 235 SHEET 1 E 4 ARG A 223 THR A 224 0 SHEET 2 E 4 ASP A 235 GLY A 243 -1 O THR A 241 N ARG A 223 SHEET 3 E 4 SER A 249 ARG A 257 -1 O ILE A 256 N CYS A 236 SHEET 4 E 4 ARG A 260 ILE A 265 -1 O ILE A 265 N PHE A 253 SHEET 1 F 5 THR A 268 GLY A 269 0 SHEET 2 F 5 THR A 311 LEU A 316 1 O ILE A 314 N THR A 268 SHEET 3 F 5 PRO A 301 ASN A 306 -1 N ASN A 306 O THR A 311 SHEET 4 F 5 THR A 286 ARG A 292 -1 N ILE A 287 O LEU A 305 SHEET 5 F 5 GLU A 275 PHE A 281 -1 N GLU A 275 O ARG A 292 SHEET 1 G 4 PHE A 352 ARG A 356 0 SHEET 2 G 4 ILE A 361 ARG A 367 -1 O TRP A 364 N VAL A 353 SHEET 3 G 4 MET A 375 TYR A 383 -1 O TYR A 380 N TYR A 365 SHEET 4 G 4 THR A 395 PRO A 406 -1 O SER A 397 N LEU A 379 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 SG CYS A 87 SG CYS A 420 LINK SG CYS A 122 SG CYS A 127 LINK SG CYS A 182 SG CYS A 229 LINK SG CYS A 231 SG CYS A 236 LINK SG CYS A 277 SG CYS A 291 LINK SG CYS A 279 SG CYS A 289 LINK SG CYS A 318 SG CYS A 337 LINK SG CYS A 424 SG CYS A 447 CISPEP 1 GLN A 138 PRO A 139 0 -0.70 CISPEP 2 THR A 325 PRO A 326 0 0.10 CRYST1 124.360 124.360 71.470 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 0.008041 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008041 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013992 0.00000