HEADER GLYCOSIDASE 07-JUL-98 3SIL TITLE SIALIDASE FROM SALMONELLA TYPHIMURIUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: 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 KEYWDS GLYCOSIDASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR E.F.GARMAN,G.M.SHELDRICK REVDAT 2 13-JAN-99 3SIL 2 COMPND REMARK HEADER LINK REVDAT 2 2 2 SOURCE CONECT REVDAT 1 11-NOV-98 3SIL 0 JRNL AUTH E.F.GARMAN,J.WOUTERS,T.R.SCHNEIDER,E.R.VIMR, JRNL AUTH 2 W.G.LAVER,G.M.SHELDRICK JRNL TITL AN ENZYME AT ATOMIC RESOLUTION: THE 1.05 A JRNL TITL 2 STRUCTURE OF SALMONELLA TYPHIMURIUM NEURAMINIDASE JRNL TITL 3 (SIALIDASE) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.J.CRENNELL,E.F.GARMAN,C.PHILIPPON,A.VASELLA, REMARK 1 AUTH 2 W.G.LAVER,E.R.VIMR,G.L.TAYLOR REMARK 1 TITL THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 REMARK 1 TITL 2 NEURAMINIDASE AND ITS COMPLEXES WITH THREE REMARK 1 TITL 3 INHIBITORS AT HIGH RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 259 264 1996 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 2 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 2 REMARK 2 RESOLUTION. 1.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.1 REMARK 3 CROSS-VALIDATION METHOD : FREE R REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.116 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.116 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.147 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.100 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4529 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 148474 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.094 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.094 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.121 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 3.000 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3544 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 117026 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3082 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 60 REMARK 3 SOLVENT ATOMS : 561 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3526.40 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2797.80 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 47 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 33361 REMARK 3 NUMBER OF RESTRAINTS : 41703 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.014 REMARK 3 ANGLE DISTANCES (A) : 0.030 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.020 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.035 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.127 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.142 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.034 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.031 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.114 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL. (1973) 91: 201- REMARK 3 228 REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE REMARK 3 R (NO CUTOFF). REMARK 4 REMARK 4 3SIL 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 : 01-MAY-1995 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.86 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : BW7B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.862 REMARK 200 MONOCHROMATOR : NULL 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 : 148478 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050 REMARK 200 RESOLUTION RANGE LOW (A) : 11.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.05600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.60 REMARK 200 R MERGE FOR SHELL (I) : 0.34600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: PDB ENTRY 2SIL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.86 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 23.55000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.75000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.86500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.75000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.55000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.86500 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 REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 777 O HOH 1041 4566 2.19 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 46 CG LYS A 46 CD -0.092 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 ASN A 107 CB - CG - OD1 ANGL. DEV. = 14.2 DEGREES REMARK 500 ARG A 111 CA - CB - CG ANGL. DEV. = 15.5 DEGREES REMARK 500 LYS A 261 CG - CD - CE ANGL. DEV. = 13.8 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 178 122.34 89.77 REMARK 500 SER A 230 -35.34 61.42 REMARK 500 VAL A 351 -118.85 64.32 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 981 DISTANCE = 5.48 ANGSTROMS REMARK 525 HOH 1004 DISTANCE = 5.15 ANGSTROMS DBREF 3SIL A 4 382 UNP P29768 NANH_SALTY 3 381 SEQADV 3SIL ASP A 329 UNP P29768 ALA 328 ENGINEERED SEQRES 1 A 379 GLU LYS SER VAL VAL PHE LYS ALA GLU GLY GLU HIS PHE SEQRES 2 A 379 THR ASP GLN LYS GLY ASN THR ILE VAL GLY SER GLY SER SEQRES 3 A 379 GLY GLY THR THR LYS TYR PHE ARG ILE PRO ALA MET CYS SEQRES 4 A 379 THR THR SER LYS GLY THR ILE VAL VAL PHE ALA ASP ALA SEQRES 5 A 379 ARG HIS ASN THR ALA SER ASP GLN SER PHE ILE ASP THR SEQRES 6 A 379 ALA ALA ALA ARG SER THR ASP GLY GLY LYS THR TRP ASN SEQRES 7 A 379 LYS LYS ILE ALA ILE TYR ASN ASP ARG VAL ASN SER LYS SEQRES 8 A 379 LEU SER ARG VAL MET ASP PRO THR CYS ILE VAL ALA ASN SEQRES 9 A 379 ILE GLN GLY ARG GLU THR ILE LEU VAL MET VAL GLY LYS SEQRES 10 A 379 TRP ASN ASN ASN ASP LYS THR TRP GLY ALA TYR ARG ASP SEQRES 11 A 379 LYS ALA PRO ASP THR ASP TRP ASP LEU VAL LEU TYR LYS SEQRES 12 A 379 SER THR ASP ASP GLY VAL THR PHE SER LYS VAL GLU THR SEQRES 13 A 379 ASN ILE HIS ASP ILE VAL THR LYS ASN GLY THR ILE SER SEQRES 14 A 379 ALA MET LEU GLY GLY VAL GLY SER GLY LEU GLN LEU ASN SEQRES 15 A 379 ASP GLY LYS LEU VAL PHE PRO VAL GLN MET VAL ARG THR SEQRES 16 A 379 LYS ASN ILE THR THR VAL LEU ASN THR SER PHE ILE TYR SEQRES 17 A 379 SER THR ASP GLY ILE THR TRP SER LEU PRO SER GLY TYR SEQRES 18 A 379 CYS GLU GLY PHE GLY SER GLU ASN ASN ILE ILE GLU PHE SEQRES 19 A 379 ASN ALA SER LEU VAL ASN ASN ILE ARG ASN SER GLY LEU SEQRES 20 A 379 ARG ARG SER PHE GLU THR LYS ASP PHE GLY LYS THR TRP SEQRES 21 A 379 THR GLU PHE PRO PRO MET ASP LYS LYS VAL ASP ASN ARG SEQRES 22 A 379 ASN HIS GLY VAL GLN GLY SER THR ILE THR ILE PRO SER SEQRES 23 A 379 GLY ASN LYS LEU VAL ALA ALA HIS SER SER ALA GLN ASN SEQRES 24 A 379 LYS ASN ASN ASP TYR THR ARG SER ASP ILE SER LEU TYR SEQRES 25 A 379 ALA HIS ASN LEU TYR SER GLY GLU VAL LYS LEU ILE ASP SEQRES 26 A 379 ASP PHE TYR PRO LYS VAL GLY ASN ALA SER GLY ALA GLY SEQRES 27 A 379 TYR SER CYS LEU SER TYR ARG LYS ASN VAL ASP LYS GLU SEQRES 28 A 379 THR LEU TYR VAL VAL TYR GLU ALA ASN GLY SER ILE GLU SEQRES 29 A 379 PHE GLN ASP LEU SER ARG HIS LEU PRO VAL ILE LYS SER SEQRES 30 A 379 TYR ASN HET K 450 2 HET PO4 499 10 HET GOL 401 6 HET GOL 402 6 HET GOL 403 12 HET GOL 404 12 HET GOL 405 6 HET GOL 406 6 HETNAM K POTASSIUM ION HETNAM PO4 PHOSPHATE ION HETNAM GOL GLYCEROL FORMUL 2 K K 1+ FORMUL 3 PO4 O4 P 3- FORMUL 4 GOL 6(C3 H8 O3) FORMUL 10 HOH *561(H2 O) HELIX 1 1 SER A 29 GLY A 31 5 3 HELIX 2 2 TRP A 128 ALA A 130 5 3 HELIX 3 3 ILE A 161 ASN A 168 1 8 HELIX 4 4 SER A 372 LYS A 379 5 8 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 4 TRP A 218 LEU A 220 0 SHEET 2 E 4 LEU A 205 SER A 212 -1 N TYR A 211 O SER A 219 SHEET 3 E 4 LEU A 189 ARG A 197 -1 N MET A 195 O ASN A 206 SHEET 4 E 4 ILE A 171 GLY A 176 -1 N LEU A 175 O GLN A 194 SHEET 1 F 2 ASN A 232 PHE A 237 0 SHEET 2 F 2 SER A 240 ILE A 245 -1 N ASN A 244 O ASN A 233 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 LEU A 326 -1 N LYS A 325 O ALA A 316 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 SHEET 1 I 2 ILE A 312 LEU A 314 0 SHEET 2 I 2 ASP A 328 TYR A 331 -1 N TYR A 331 O ILE A 312 SSBOND 1 CYS A 42 CYS A 103 CISPEP 1 ALA A 135 PRO A 136 0 -2.77 CRYST1 47.100 81.730 91.500 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 0.021231 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012235 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010929 0.00000