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HEADER GLYCOSIDASE 23-APR-96 1DIL TITLE SIALIDASE FROM SALMONELLA TYPHIMURIUM COMPLEXED WITH APANA TITLE 2 AND EPANA INHIBITORS 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 STRAIN: LT2; SOURCE 4 VARIANT: TA263, PROTOTROPH; SOURCE 5 GENE: NANH; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PSX62; SOURCE 9 EXPRESSION_SYSTEM_GENE: NANH; SOURCE 10 OTHER_DETAILS: RESIDUE MET 1 WAS EXCISED BY ESCHERICHIA SOURCE 11 COLI KEYWDS GLYCOSIDASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR E.F.GARMAN,S.C.CRENNELL,E.R.VIMR,W.G.LAVER,G.L.TAYLOR REVDAT 1 07-DEC-96 1DIL 0 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.TAYLOR,E.VIMR,E.GARMAN,G.LAVER REMARK 1 TITL PURIFICATION, CRYSTALLIZATION AND PRELIMINARY REMARK 1 TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM REMARK 1 TITL 3 VIBRIO CHOLERAE AND SALMONELLA TYPHIMURIUM LT2 REMARK 1 REF J.MOL.BIOL. V. 226 1287 1992 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 3 REMARK 1 AUTH K.WALLIMANN,A.VASELLA REMARK 1 TITL PHOSPHONIC-ACID ANALOGUES OF THE REMARK 1 TITL 2 N-ACETYL-2-DEOXYNEURAMINIC ACIDS: SYNTHESIS AND REMARK 1 TITL 3 INHIBITION OF VIBRIO CHOLERAE SIALIDASE REMARK 1 REF HELV.CHIM.ACTA V. 73 1359 1990 REMARK 1 REFN ASTM HCACAV SZ ISSN 0018-019X REMARK 2 REMARK 2 RESOLUTION. 1.90 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) : 1.90 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) (%) : 96.4 REMARK 3 NUMBER OF REFLECTIONS : 27455 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) : 0.187 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 : 2905 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 21 REMARK 3 SOLVENT ATOMS : 225 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.03 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) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.77 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 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.500 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 : STNA_APANA.PAR REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : STNA_APANA.TOP REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DIL 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 (2007-03-16) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-JUL-1993 REMARK 200 TEMPERATURE (KELVIN) : 293.0 REMARK 200 PH : NULL 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/MSC RU-H2R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE(002) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27890 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.05700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 0.12500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 5.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE MAP REMARK 200 SOFTWARE USED: X-PLOR 3.1 REMARK 200 STARTING MODEL: PDB ENTRY 2SIM REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 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 23.70000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.85000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.15000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.85000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.70000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.15000 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 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 = 6.65 ANGSTROMS REMARK 525 HOH 592 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH 669 DISTANCE = 5.76 ANGSTROMS REMARK 525 HOH 800 DISTANCE = 7.68 ANGSTROMS REMARK 525 HOH 801 DISTANCE = 6.99 ANGSTROMS REMARK 525 HOH 809 DISTANCE = 8.57 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: ACT REMARK 800 SITE_DESCRIPTION: ACTIVE SITE DBREF 1DIL A 2 382 UNP P29768 NANH_SALTY 1 381 SEQADV 1DIL 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 HET EQP 1 21 HET AXP 2 21 HET K 690 1 HETNAM EQP (4-ACETAMIDO-2,4-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-1- HETNAM 2 EQP OCTOPYRANOSYL)PHOSPHONIC ACID HETNAM AXP 4-ACETAMIDO-2,4-DIDEXOY-D-GLYCERO-BETA-D-GALACTO- HETNAM 2 AXP OCTOPYRANOSYLPHOSPHONIC ACID (AN AXIAL PHOSPHONATE) HETNAM K POTASSIUM ION FORMUL 2 EQP C10 H20 N O9 P FORMUL 2 AXP C10 H20 N O9 P FORMUL 3 K K 1+ FORMUL 4 HOH *226(H2 O) HELIX 1 1 TRP A 128 ALA A 130 5 3 HELIX 2 2 ILE A 161 ASN A 168 1 8 HELIX 3 3 SER A 372 SER A 380 5 9 SHEET 1 A 4 TYR A 35 ARG A 37 0 SHEET 2 A 4 ILE A 49 ARG A 56 -1 N ARG A 56 O TYR A 35 SHEET 3 A 4 ILE A 66 SER A 73 -1 N SER A 73 O ILE A 49 SHEET 4 A 4 ASN A 81 ILE A 86 -1 N ILE A 86 O THR A 68 SHEET 1 B 2 ALA A 40 THR A 43 0 SHEET 2 B 2 ILE A 49 PHE A 52 -1 N PHE A 52 O ALA A 40 SHEET 1 C 3 ARG A 97 MET A 99 0 SHEET 2 C 3 ILE A 114 TRP A 121 -1 N TRP A 121 O ARG A 97 SHEET 3 C 3 ASP A 141 SER A 147 -1 N SER A 147 O ILE A 114 SHEET 1 D 2 THR A 102 ILE A 108 0 SHEET 2 D 2 ARG A 111 MET A 117 -1 N MET A 117 O THR A 102 SHEET 1 E 3 LEU A 205 SER A 212 0 SHEET 2 E 3 LEU A 189 ARG A 197 -1 N MET A 195 O ASN A 206 SHEET 3 E 3 ILE A 171 GLY A 176 -1 N LEU A 175 O GLN A 194 SHEET 1 F 3 ASN A 232 PHE A 237 0 SHEET 2 F 3 SER A 240 ILE A 245 -1 N ASN A 244 O ASN A 233 SHEET 3 F 3 ARG A 252 THR A 256 -1 N THR A 256 O LEU A 241 SHEET 1 G 4 SER A 283 SER A 289 0 SHEET 2 G 4 LYS A 292 ALA A 300 -1 N SER A 298 O SER A 283 SHEET 3 G 4 ILE A 312 HIS A 317 -1 N HIS A 317 O ALA A 295 SHEET 4 G 4 VAL A 324 ASP A 328 -1 N ASP A 328 O LEU A 314 SHEET 1 H 4 SER A 343 ASN A 350 0 SHEET 2 H 4 LYS A 353 ALA A 362 -1 N VAL A 359 O CYS A 344 SHEET 3 H 4 SER A 365 ASP A 370 -1 N GLN A 369 O VAL A 358 SHEET 4 H 4 LYS A 5 PHE A 9 -1 N PHE A 9 O ILE A 366 SSBOND 1 CYS A 42 CYS A 103 LINK C2 EQP 1 O6 AXP 2 LINK C4 EQP 1 O4 AXP 2 LINK C6 EQP 1 O6 AXP 2 LINK C8 EQP 1 O8 AXP 2 LINK C10 EQP 1 O10 AXP 2 LINK O4 EQP 1 C4 AXP 2 LINK O6 EQP 1 C6 AXP 2 LINK O6 EQP 1 C2 AXP 2 LINK O7 EQP 1 C7 AXP 2 LINK O8 EQP 1 C8 AXP 2 LINK O9 EQP 1 C9 AXP 2 LINK C7 EQP 1 O7 AXP 2 LINK C9 EQP 1 O9 AXP 2 CISPEP 1 ALA A 135 PRO A 136 0 -0.06 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 47.400 82.300 91.700 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 0.021097 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012151 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010905 0.00000