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HEADER HYDROLASE 21-JUN-96 1EUR TITLE SIALIDASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NEURAMINIDASE; COMPND 5 EC: 3.2.1.18; COMPND 6 OTHER_DETAILS: 41KD FORM SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA VIRIDIFACIENS; SOURCE 3 ATCC: 31146 KEYWDS NEURAMINIDASE, SIALIDASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR A.GASKELL,S.J.CRENNELL,G.L.TAYLOR REVDAT 1 11-JAN-97 1EUR 0 JRNL AUTH A.GASKELL,S.CRENNELL,G.TAYLOR JRNL TITL THE THREE DOMAINS OF A BACTERIAL SIALIDASE: A JRNL TITL 2 BETA-PROPELLER, AN IMMUNOGLOBULIN MODULE AND A JRNL TITL 3 GALACTOSE-BINDING JELLY-ROLL. JRNL REF STRUCTURE V. 3 1197 1995 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.TAYLOR,L.DINELEY,M.GLOWKA,G.LAVER REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC REMARK 1 TITL 2 STUDY OF NEURAMINIDASE FROM MICROMONOSPORA REMARK 1 TITL 3 VIRIDIFACIENS REMARK 1 REF J.MOL.BIOL. V. 225 1135 1992 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.82 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 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) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 28814 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) : 0.173 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 : 2701 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 270 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.20 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) : 0.15 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) : 2.57 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 : PARAM19X.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1EUR 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 : 1993 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : MULTIWIRE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : SIEMENS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29469 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 (%) : 93.4 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : 0.05500 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 3.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 24.07000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.37500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.36500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.37500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.07000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.36500 REMARK 290 SMTRY3 4 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 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 43 REMARK 465 PRO A 44 REMARK 465 PRO A 45 REMARK 465 GLY A 46 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 349 SD MET A 349 CE -0.075 REMARK 500 MET A 368 SD MET A 368 CE -0.077 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 GLY A 86 N - CA - C ANGL. DEV. =-17.8 DEGREES REMARK 500 ARG A 276 N - CA - C ANGL. DEV. =-10.9 DEGREES REMARK 500 GLY A 292 N - CA - C ANGL. DEV. =-15.0 DEGREES REMARK 500 GLY A 293 N - CA - C ANGL. DEV. =-17.7 DEGREES REMARK 500 HIS A 294 N - CA - C ANGL. DEV. = 14.0 DEGREES REMARK 500 SER A 295 N - CA - C ANGL. DEV. =-11.1 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 641 DISTANCE = 9.12 ANGSTROMS REMARK 525 HOH 661 DISTANCE = 6.69 ANGSTROMS REMARK 525 HOH 670 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH 688 DISTANCE = 7.72 ANGSTROMS REMARK 525 HOH 691 DISTANCE = 6.16 ANGSTROMS REMARK 525 HOH 700 DISTANCE = 6.95 ANGSTROMS REMARK 525 HOH 708 DISTANCE = 5.07 ANGSTROMS REMARK 525 HOH 712 DISTANCE = 6.20 ANGSTROMS REMARK 525 HOH 713 DISTANCE = 7.68 ANGSTROMS REMARK 525 HOH 715 DISTANCE = 8.20 ANGSTROMS REMARK 525 HOH 718 DISTANCE = 5.96 ANGSTROMS REMARK 525 HOH 726 DISTANCE = 5.09 ANGSTROMS REMARK 525 HOH 759 DISTANCE = 7.36 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: ACT REMARK 800 SITE_DESCRIPTION: ACTIVE SITE. DBREF 1EUR A 43 407 UNP Q02834 NANH_MICVI 43 407 SEQRES 1 A 365 VAL PRO PRO GLY GLY GLU PRO LEU TYR THR GLU GLN ASP SEQRES 2 A 365 LEU ALA VAL ASN GLY ARG GLU GLY PHE PRO ASN TYR ARG SEQRES 3 A 365 ILE PRO ALA LEU THR VAL THR PRO ASP GLY ASP LEU LEU SEQRES 4 A 365 ALA SER TYR ASP GLY ARG PRO THR GLY ILE ASP ALA PRO SEQRES 5 A 365 GLY PRO ASN SER ILE LEU GLN ARG ARG SER THR ASP GLY SEQRES 6 A 365 GLY ARG THR TRP GLY GLU GLN GLN VAL VAL SER ALA GLY SEQRES 7 A 365 GLN THR THR ALA PRO ILE LYS GLY PHE SER ASP PRO SER SEQRES 8 A 365 TYR LEU VAL ASP ARG GLU THR GLY THR ILE PHE ASN PHE SEQRES 9 A 365 HIS VAL TYR SER GLN ARG GLN GLY PHE ALA GLY SER ARG SEQRES 10 A 365 PRO GLY THR ASP PRO ALA ASP PRO ASN VAL LEU HIS ALA SEQRES 11 A 365 ASN VAL ALA THR SER THR ASP GLY GLY LEU THR TRP SER SEQRES 12 A 365 HIS ARG THR ILE THR ALA ASP ILE THR PRO ASP PRO GLY SEQRES 13 A 365 TRP ARG SER ARG PHE ALA ALA SER GLY GLU GLY ILE GLN SEQRES 14 A 365 LEU ARG TYR GLY PRO HIS ALA GLY ARG LEU ILE GLN GLN SEQRES 15 A 365 TYR THR ILE ILE ASN ALA ALA GLY ALA PHE GLN ALA VAL SEQRES 16 A 365 SER VAL TYR SER ASP ASP HIS GLY ARG THR TRP ARG ALA SEQRES 17 A 365 GLY GLU ALA VAL GLY VAL GLY MET ASP GLU ASN LYS THR SEQRES 18 A 365 VAL GLU LEU SER ASP GLY ARG VAL LEU LEU ASN SER ARG SEQRES 19 A 365 ASP SER ALA ARG SER GLY TYR ARG LYS VAL ALA VAL SER SEQRES 20 A 365 THR ASP GLY GLY HIS SER TYR GLY PRO VAL THR ILE ASP SEQRES 21 A 365 ARG ASP LEU PRO ASP PRO THR ASN ASN ALA SER ILE ILE SEQRES 22 A 365 ARG ALA PHE PRO ASP ALA PRO ALA GLY SER ALA ARG ALA SEQRES 23 A 365 LYS VAL LEU LEU PHE SER ASN ALA ALA SER GLN THR SER SEQRES 24 A 365 ARG SER GLN GLY THR ILE ARG MET SER CYS ASP ASP GLY SEQRES 25 A 365 GLN THR TRP PRO VAL SER LYS VAL PHE GLN PRO GLY SER SEQRES 26 A 365 MET SER TYR SER THR LEU THR ALA LEU PRO ASP GLY THR SEQRES 27 A 365 TYR GLY LEU LEU TYR GLU PRO GLY THR GLY ILE ARG TYR SEQRES 28 A 365 ALA ASN PHE ASN LEU ALA TRP LEU GLY GLY ILE CYS ALA SEQRES 29 A 365 PRO FORMUL 2 HOH *268(H2 O) HELIX 1 1 ALA A 191 ILE A 193 5 3 HELIX 2 2 ARG A 327 LYS A 329 5 3 HELIX 3 3 LEU A 398 LEU A 401 1 4 SHEET 1 A 4 ALA A 71 VAL A 74 0 SHEET 2 A 4 LEU A 80 GLY A 86 -1 N SER A 83 O ALA A 71 SHEET 3 A 4 SER A 98 SER A 104 -1 N SER A 104 O LEU A 80 SHEET 4 A 4 GLN A 115 SER A 118 -1 N SER A 118 O ILE A 99 SHEET 1 B 4 GLY A 128 SER A 130 0 SHEET 2 B 4 ILE A 143 SER A 150 -1 N SER A 150 O GLY A 128 SHEET 3 B 4 HIS A 171 SER A 177 -1 N SER A 177 O ILE A 143 SHEET 4 B 4 SER A 185 THR A 188 -1 N ARG A 187 O VAL A 174 SHEET 1 C 2 SER A 133 ASP A 137 0 SHEET 2 C 2 THR A 142 PHE A 146 -1 N PHE A 146 O SER A 133 SHEET 1 D 3 SER A 201 ALA A 204 0 SHEET 2 D 3 LEU A 221 ILE A 228 -1 N ILE A 228 O SER A 201 SHEET 3 D 3 PHE A 234 SER A 241 -1 N SER A 241 O LEU A 221 SHEET 1 E 4 ASN A 261 GLU A 265 0 SHEET 2 E 4 VAL A 271 SER A 275 -1 N ASN A 274 O LYS A 262 SHEET 3 E 4 TYR A 283 SER A 289 -1 N SER A 289 O VAL A 271 SHEET 4 E 4 THR A 300 PRO A 306 -1 N LEU A 305 O ARG A 284 SHEET 1 F 4 SER A 313 ARG A 316 0 SHEET 2 F 4 LEU A 331 ALA A 336 -1 N SER A 334 O SER A 313 SHEET 3 F 4 GLY A 345 SER A 350 -1 N SER A 350 O LEU A 331 SHEET 4 F 4 VAL A 359 GLN A 364 -1 N GLN A 364 O GLY A 345 SHEET 1 G 4 SER A 371 ALA A 375 0 SHEET 2 G 4 TYR A 381 TYR A 385 -1 N LEU A 384 O THR A 372 SHEET 3 G 4 GLY A 390 PHE A 396 -1 N PHE A 396 O TYR A 381 SHEET 4 G 4 TYR A 51 VAL A 58 -1 N ALA A 57 O ILE A 391 CISPEP 1 ALA A 93 PRO A 94 0 -1.58 CISPEP 2 ALA A 124 PRO A 125 0 -0.18 CISPEP 3 ALA A 406 PRO A 407 0 0.22 SITE 1 ACT 14 ARG A 68 ARG A 87 ASP A 92 ASP A 131 SITE 2 ACT 14 VAL A 148 PHE A 155 LEU A 170 PHE A 203 SITE 3 ACT 14 ASP A 259 GLU A 260 ARG A 276 ARG A 342 SITE 4 ACT 14 TYR A 370 GLU A 386 CRYST1 48.140 82.730 84.750 90.00 90.00 90.00 P 21 21 21 4 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 0.020773 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012088 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011799 0.00000