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HEADER HYDROLASE 15-FEB-99 1B9V TITLE NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE TITLE 2 MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND TITLE 3 WATER MOLECULES IN TEH ACTIVE SITE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (NEURAMINIDASE); COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SIALIDASE; COMPND 5 EC: 3.2.1.18 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA B VIRUS; SOURCE 3 STRAIN: B/LEE/40 KEYWDS INFLUENZA, NEURAMINIDASE, SIALIDASE, B/LEE/40 EXPDTA X-RAY DIFFRACTION AUTHOR J.B.FINLEY,V.R.ATIGADDA,F.DUARTE,J.J.ZAHAO,W.J.BROUILLETTE, AUTHOR 2 G.M.AIR,M.LUO REVDAT 3 01-MAY-00 1B9V 1 DBREF REVDAT 2 23-DEC-99 1B9V 1 JRNL HEADER COMPND REVDAT 1 27-FEB-99 1B9V 0 JRNL AUTH J.B.FINLEY,V.R.ATIGADDA,F.DUARTE,J.J.ZHAO, JRNL AUTH 2 W.J.BROUILLETTE,G.M.AIR,M.LUO JRNL TITL NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS JRNL TITL 2 NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH JRNL TITL 3 CONSERVED RESIDUES AND WATER MOLECULES IN THE JRNL TITL 4 ACTIVE SITE. JRNL REF J.MOL.BIOL. V. 293 1107 1999 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.85 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 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) (%) : 70.2 REMARK 3 NUMBER OF REFLECTIONS : 19008 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) : 0.183 REMARK 3 FREE R VALUE : 0.271 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 : 3040 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 41 REMARK 3 SOLVENT ATOMS : 107 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) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.39 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 1B9V 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 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB000492. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : AUG-1997 REMARK 200 TEMPERATURE (KELVIN) : 293.0 REMARK 200 PH : 6.80 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : MULTIWIRE REMARK 200 DETECTOR MANUFACTURER : SIEMENS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT REMARK 200 DATA SCALING SOFTWARE : SAINT REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13395 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.364 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 80.2 REMARK 200 DATA REDUNDANCY : 2.320 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08200 REMARK 200 FOR THE DATA SET : 9.9800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.2 REMARK 200 DATA REDUNDANCY IN SHELL : 2.32 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.22800 REMARK 200 FOR SHELL : 3.170 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: 1IVB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8 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 62.35100 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.35100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.35100 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.35100 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.35100 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.35100 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.35100 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.35100 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 124.70200 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 62.35100 REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -62.35100 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 62.35100 REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 62.35100 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 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 -0.099 REMARK 500 PRO A 328 CB PRO A 328 CG 0.038 REMARK 500 MET A 369 SD MET A 369 CE -0.063 REMARK 500 MET A 429 SD MET A 429 CE 0.047 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 TYR A 210 N - CA - C ANGL. DEV. =-11.5 DEGREES REMARK 500 THR A 211 N - CA - C ANGL. DEV. = 9.1 DEGREES REMARK 500 LEU A 222 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 GLN A 225 N - CA - C ANGL. DEV. = 12.3 DEGREES REMARK 500 CYS A 229 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 THR A 278 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 ALA A 290 N - CA - C ANGL. DEV. =-13.3 DEGREES REMARK 500 ASP A 293 N - CA - C ANGL. DEV. =-11.3 DEGREES REMARK 500 LYS A 304 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 GLU A 338 N - CA - C ANGL. DEV. = 8.5 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 903 DISTANCE = 7.34 ANGSTROMS REMARK 525 HOH 972 DISTANCE = 10.46 ANGSTROMS REMARK 525 HOH 975 DISTANCE = 9.43 ANGSTROMS DBREF 1B9V A 77 466 UNP P03474 NRAM_INBLE 77 466 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 HET NAG 467 14 HET CA A 500 1 HET CA 501 1 HET RA2 468 25 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM CA CALCIUM ION HETNAM RA2 1-[4-CARBOXY-2-(3-PENTYLAMINO)PHENYL]-5,5'- HETNAM 2 RA2 DI(HYDROXYMETHYL)PYRROLIDIN-2-ONE HETSYN NAG NAG FORMUL 2 NAG C8 H15 N O6 FORMUL 3 CA 2(CA 2+) FORMUL 5 RA2 C18 H26 N2 O5 FORMUL 6 HOH *107(H2 O) HELIX 1 1 PRO A 100 ARG A 102 5 3 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 GLY A 179 HIS A 183 0 SHEET 2 B 4 TRP A 188 ASP A 194 -1 N ILE A 191 O SER A 180 SHEET 3 B 4 LEU A 201 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 THR A 241 -1 N TYR A 237 O ASN A 230 SHEET 3 C 4 CYS A 251 ARG A 257 -1 N ILE A 256 O CYS A 236 SHEET 4 C 4 ARG A 260 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 4 PHE A 352 ARG A 356 0 SHEET 2 E 4 ILE A 361 THR A 368 -1 N TRP A 364 O VAL A 353 SHEET 3 E 4 MET A 377 TYR A 383 -1 N ARG A 382 O ARG A 363 SHEET 4 E 4 GLY A 398 VAL A 401 -1 N VAL A 401 O MET A 377 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 CISPEP 1 GLN A 138 PRO A 139 0 -0.22 CISPEP 2 THR A 325 PRO A 326 0 -0.05 CRYST1 124.702 124.702 71.573 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 0.008019 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008019 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013972 0.00000