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HEADER HYDROLASE 13-JUL-94 2SIL TITLE THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE TITLE 2 AND ITS COMPLEX WITH A TRANSITION STATE ANALOGUE AT 1.6 TITLE 3 ANGSTROMS RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM; SOURCE 3 GENE: PSX62; SOURCE 4 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL; SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PSX62 KEYWDS HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR G.L.TAYLOR,S.J.CRENNELL,E.F.GARMAN,E.R.VIMR,W.G.LAVER REVDAT 1 31-AUG-94 2SIL 0 SPRSDE 31-AUG-94 2SIL 1SIL JRNL AUTH S.J.CRENNELL,E.F.GARMAN,C.PHILIPPON,A.VASELLA, JRNL AUTH 2 W.G.LAVER,E.R.VIMR,G.L.TAYLOR JRNL TITL THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 JRNL TITL 2 NEURAMINIDASE AND ITS COMPLEXES WITH THREE JRNL TITL 3 INHIBITORS AT HIGH RESOLUTION. JRNL REF J.MOL.BIOL. V. 259 264 1996 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.J.CRENNELL,E.F.GARMAN,W.G.LAVER,E.R.VIMR, REMARK 1 AUTH 2 G.L.TAYLOR REMARK 1 TITL CRYSTAL STRUCTURE OF A BACTERIAL SIALIDASE (FROM REMARK 1 TITL 2 SALMONELLA TYPHIMURIUM LT2) SHOWS THE SAME FOLD AS REMARK 1 TITL 3 AN INFLUENZA VIRUS NEURAMINIDASE REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 9852 1993 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REFERENCE 2 REMARK 1 AUTH G.L.TAYLOR,E.R.VIMR,E.F.GARMAN,W.G.LAVER REMARK 1 TITL PURIFICATION, CRYSTALLISATION AND PRELIMINARY REMARK 1 TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM REMARK 1 TITL 3 VIBRIO CHOLERAE AND SALMONELLA TYPHIMURIUM REMARK 1 REF J.MOL.BIOL. V. 226 1287 1992 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : TNT, X-PLOR REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 35140 REMARK 3 REMARK 3 USING DATA ABOVE SIGMA CUTOFF. REMARK 3 CROSS-VALIDATION METHOD :NULL REMARK 3 FREE R VALUE TEST SET SELECTION :NULL REMARK 3 R VALUE (WORKING + TEST SET) :0.166 REMARK 3 R VALUE (WORKING SET) :0.166 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 REMARK 3 USING ALL DATA, NO SIGMA CUTOFF. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2954 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 195 REMARK 3 REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT REMARK 3 BOND LENGTHS (A) : NULL ; NULL ; NULL REMARK 3 BOND ANGLES (DEGREES) : NULL ; NULL ; NULL REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL REMARK 3 REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 RESTRAINT LIBRARIES. REMARK 3 STEREOCHEMISTRY : NULL REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2SIL 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 (2007-03-18) 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 : 59728 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 55.9 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 (%): 42.62 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14 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 23.75000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.95000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.25000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.95000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.75000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.25000 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 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 601 O HOH 674 2.16 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 LYS A 199 CE LYS A 199 NZ 0.149 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 ARG A 90 CG - CD - NE ANGL. DEV. =-21.1 DEGREES REMARK 500 ARG A 90 CD - NE - CZ ANGL. DEV. = 22.5 DEGREES REMARK 500 THR A 159 N - CA - CB ANGL. DEV. =-21.5 DEGREES REMARK 500 ARG A 251 CD - NE - CZ ANGL. DEV. = 30.2 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 VAL A 178 126.69 84.22 REMARK 500 SER A 230 -36.03 55.57 REMARK 500 HIS A 278 -31.28 72.71 REMARK 500 VAL A 351 -107.15 64.20 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 520 DISTANCE = 6.13 ANGSTROMS REMARK 525 HOH 523 DISTANCE = 7.12 ANGSTROMS DBREF 2SIL A 2 382 UNP P29768 NANH_SALTY 1 381 SEQADV 2SIL ASP A 329 UNP P29768 ALA 328 CONFLICT SEQRES 1 A 381 THR VAL GLU LYS SER VAL VAL PHE LYS ALA GLU GLY GLU SEQRES 2 A 381 HIS PHE THR ASP GLN LYS GLY ASN THR ILE VAL GLY SER SEQRES 3 A 381 GLY SER GLY GLY THR THR LYS TYR PHE ARG ILE PRO ALA SEQRES 4 A 381 MET CYS THR THR SER LYS GLY THR ILE VAL VAL PHE ALA SEQRES 5 A 381 ASP ALA ARG HIS ASN THR ALA SER ASP GLN SER PHE ILE SEQRES 6 A 381 ASP THR ALA ALA ALA ARG SER THR ASP GLY GLY LYS THR SEQRES 7 A 381 TRP ASN LYS LYS ILE ALA ILE TYR ASN ASP ARG VAL ASN SEQRES 8 A 381 SER LYS LEU SER ARG VAL MET ASP PRO THR CYS ILE VAL SEQRES 9 A 381 ALA ASN ILE GLN GLY ARG GLU THR ILE LEU VAL MET VAL SEQRES 10 A 381 GLY LYS TRP ASN ASN ASN ASP LYS THR TRP GLY ALA TYR SEQRES 11 A 381 ARG ASP LYS ALA PRO ASP THR ASP TRP ASP LEU VAL LEU SEQRES 12 A 381 TYR LYS SER THR ASP ASP GLY VAL THR PHE SER LYS VAL SEQRES 13 A 381 GLU THR ASN ILE HIS ASP ILE VAL THR LYS ASN GLY THR SEQRES 14 A 381 ILE SER ALA MET LEU GLY GLY VAL GLY SER GLY LEU GLN SEQRES 15 A 381 LEU ASN ASP GLY LYS LEU VAL PHE PRO VAL GLN MET VAL SEQRES 16 A 381 ARG THR LYS ASN ILE THR THR VAL LEU ASN THR SER PHE SEQRES 17 A 381 ILE TYR SER THR ASP GLY ILE THR TRP SER LEU PRO SER SEQRES 18 A 381 GLY TYR CYS GLU GLY PHE GLY SER GLU ASN ASN ILE ILE SEQRES 19 A 381 GLU PHE ASN ALA SER LEU VAL ASN ASN ILE ARG ASN SER SEQRES 20 A 381 GLY LEU ARG ARG SER PHE GLU THR LYS ASP PHE GLY LYS SEQRES 21 A 381 THR TRP THR GLU PHE PRO PRO MET ASP LYS LYS VAL ASP SEQRES 22 A 381 ASN ARG ASN HIS GLY VAL GLN GLY SER THR ILE THR ILE SEQRES 23 A 381 PRO SER GLY ASN LYS LEU VAL ALA ALA HIS SER SER ALA SEQRES 24 A 381 GLN ASN LYS ASN ASN ASP TYR THR ARG SER ASP ILE SER SEQRES 25 A 381 LEU TYR ALA HIS ASN LEU TYR SER GLY GLU VAL LYS LEU SEQRES 26 A 381 ILE ASP ASP PHE TYR PRO LYS VAL GLY ASN ALA SER GLY SEQRES 27 A 381 ALA GLY TYR SER CYS LEU SER TYR ARG LYS ASN VAL ASP SEQRES 28 A 381 LYS GLU THR LEU TYR VAL VAL TYR GLU ALA ASN GLY SER SEQRES 29 A 381 ILE GLU PHE GLN ASP LEU SER ARG HIS LEU PRO VAL ILE SEQRES 30 A 381 LYS SER TYR ASN FTNOTE 1 CIS PROLINE - PRO 136 FORMUL 2 HOH *195(H2 O) HELIX 1 1 SER A 29 GLY A 31 5 3 HELIX 2 2 THR A 127 TYR A 131 5 5 HELIX 3 3 ASN A 160 GLY A 169 1 10 HELIX 4 4 HIS A 374 SER A 380 1 7 SHEET 1 A 4 LYS A 5 PHE A 9 0 SHEET 2 A 4 SER A 365 ASP A 370 -1 O ILE A 366 N VAL A 8 SHEET 3 A 4 LYS A 353 ALA A 362 -1 O VAL A 358 N GLN A 369 SHEET 4 A 4 SER A 343 ASN A 350 -1 O CYS A 344 N VAL A 359 SHEET 1 B 4 TYR A 35 THR A 43 0 SHEET 2 B 4 ILE A 49 ARG A 56 -1 O VAL A 50 N CYS A 42 SHEET 3 B 4 ILE A 66 SER A 73 -1 O ASP A 67 N ALA A 55 SHEET 4 B 4 ASN A 81 ILE A 86 -1 N ASN A 81 O ARG A 72 SHEET 1 C 5 SER A 155 LYS A 156 0 SHEET 2 C 5 ASP A 141 SER A 147 -1 N LYS A 146 O SER A 155 SHEET 3 C 5 ARG A 111 TRP A 121 -1 N ILE A 114 O SER A 147 SHEET 4 C 5 ARG A 97 ILE A 108 -1 N ARG A 97 O TRP A 121 SHEET 5 C 5 GLY A 179 SER A 180 1 O GLY A 179 N CYS A 103 SHEET 1 D 4 ASN A 232 GLU A 236 0 SHEET 2 D 4 LEU A 241 ILE A 245 -1 O VAL A 242 N ILE A 235 SHEET 3 D 4 PHE A 254 THR A 256 -1 O PHE A 254 N ASN A 243 SHEET 4 D 4 THR A 264 GLU A 265 -1 O THR A 264 N GLU A 255 SHEET 1 E 4 SER A 283 SER A 289 0 SHEET 2 E 4 LYS A 292 ALA A 300 -1 N LYS A 292 O SER A 289 SHEET 3 E 4 ILE A 312 HIS A 317 -1 N SER A 313 O SER A 299 SHEET 4 E 4 VAL A 324 TYR A 331 -1 O LYS A 325 N ALA A 316 SSBOND 1 CYS A 42 CYS A 103 CISPEP 1 ALA A 135 PRO A 136 0 1.56 SITE 1 ACT 13 ARG A 37 ARG A 56 ASP A 62 MET A 99 SITE 2 ACT 13 ASP A 100 TRP A 121 TRP A 128 LEU A 175 SITE 3 ACT 13 GLU A 231 ARG A 246 ARG A 309 TYR A 342 SITE 4 ACT 13 GLU A 361 CRYST1 47.500 82.500 91.900 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 0.021053 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012121 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010881 0.00000