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HEADER HYDROLASE 21-NOV-04 1WCS TITLE A MUTANT OF TRYPANOSOMA RANGELI SIALIDASE DISPLAYING TRANS- TITLE 2 SIALIDASE ACTIVITY COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 23-660; COMPND 5 EC: 3.2.1.18; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA RANGELI; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 4 EXPRESSION_SYSTEM_STRAIN: BL21 KEYWDS TRANS-SIALIDASE, SIALIDASE, TRYPANOSOMA CRUZI, TRYPANOSOMA KEYWDS 2 RANGELI, PROTEIN ENGINEERING, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR G.PARIS,L.RATIER,M.F.AMAYA,T.NGUYEN,P.M.ALZARI,C.FRASCH REVDAT 1 15-DEC-04 1WCS 0 JRNL AUTH G.PARIS,L.RATIER,M.F.AMAYA,T.NGUYEN,P.M.ALZARI, JRNL AUTH 2 A.C.FRASCH JRNL TITL A SIALIDASE MUTANT DISPLAYING TRANS-SIALIDASE JRNL TITL 2 ACTIVITY. JRNL REF J.MOL.BIOL. V. 345 923 2005 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0003 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 158.11 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 16895 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 + TEST SET) : 0.248 REMARK 3 R VALUE (WORKING SET) : 0.244 REMARK 3 FREE R VALUE : 0.336 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 905 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH : NULL REMARK 3 BIN RESOLUTION RANGE LOW : NULL REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE SET COUNT : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 4841 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.75000 REMARK 3 B22 (A**2) : 2.75000 REMARK 3 B33 (A**2) : -5.51000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.517 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : NULL REMARK 3 ION PROBE RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 1WCS 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 3.102 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-21743 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-DEC-2003 REMARK 200 TEMPERATURE (KELVIN) : 110.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9756 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17626 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : 0.10000 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) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.51000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1N1S REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,3/4+Z REMARK 290 4555 1/2+Y,1/2-X,1/4+Z REMARK 290 5555 1/2-X,1/2+Y,3/4-Z REMARK 290 6555 1/2+X,1/2-Y,1/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,1/2-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 78.16750 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.34550 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.34550 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 117.25125 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.34550 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.34550 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.08375 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.34550 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.34550 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 117.25125 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.34550 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.34550 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.08375 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 78.16750 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 THR A 407 REMARK 465 PRO A 408 REMARK 465 PRO A 409 REMARK 465 SER A 410 REMARK 465 LYS A 411 REMARK 465 GLY A 412 REMARK 465 GLY A 635 REMARK 465 GLY A 636 REMARK 465 ALA A 637 REMARK 465 GLY A 638 REMARK 465 THR A 639 REMARK 465 ALA A 640 REMARK 465 ALA A 641 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 26 OG REMARK 470 GLN A 126 CG CD OE1 NE2 REMARK 470 ARG A 128 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 159 CG CD CE NZ REMARK 470 LYS A 548 CG CD CE NZ REMARK 470 ASP A 634 CG OD1 OD2 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 PHE A 62 OG SER A 65 2.14 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 GLU A 299 CG GLU A 299 CD 0.262 REMARK 500 GLU A 299 CD GLU A 299 OE2 0.183 REMARK 500 GLY A 300 C GLY A 300 O 0.181 REMARK 500 LYS A 301 CE LYS A 301 NZ 0.331 REMARK 500 GLY A 300 C LYS A 301 N 0.236 REMARK 500 GLN A 329 CG GLN A 329 CD 0.221 REMARK 500 ARG A 526 CZ ARG A 526 NH1 0.097 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 LYS A 301 CD - CE - NZ ANGL. DEV. =-11.8 DEGREES REMARK 500 LEU A 531 CA - CB - CG ANGL. DEV. = 10.1 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 183 135.53 82.28 DBREF 1WCS A 1 1 UNP O44049 O44049_TRYRA 1 1 DBREF 1WCS A 2 2 UNP O44049 O44049_TRYRA 2 2 DBREF 1WCS A 3 3 UNP O44049 O44049_TRYRA 3 3 DBREF 1WCS A 4 641 UNP O44049 O44049 23 660 SEQADV 1WCS ILE A 53 UNP O44049 THR 72 CONFLICT SEE REMARK 9 SEQADV 1WCS VAL A 99 UNP O44049 MET 118 ENGINEERED MUTATION SEQADV 1WCS PRO A 101 UNP O44049 ALA 120 ENGINEERED MUTATION SEQADV 1WCS TYR A 123 UNP O44049 SER 142 ENGINEERED MUTATION SEQADV 1WCS VAL A 180 UNP O44049 ILE 199 CONFLICT SEE REMARK 9 SEQADV 1WCS ALA A 189 UNP O44049 ILE 208 CONFLICT SEE REMARK 9 SEQADV 1WCS TYR A 252 UNP O44049 GLY 271 ENGINEERED MUTATION SEQADV 1WCS PRO A 287 UNP O44049 GLN 306 ENGINEERED MUTATION SEQADV 1WCS LEU A 375 UNP O44049 PHE 394 CONFLICT SEE REMARK 9 SEQADV 1WCS ALA A 413 UNP O44049 GLY 432 CONFLICT SEE REMARK 9 SEQADV 1WCS VAL A 609 UNP O44049 ILE 628 CONFLICT SEE REMARK 9 SEQRES 1 A 641 ALA ALA SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU SEQRES 2 A 641 PHE LYS ARG LYS ASN SER THR VAL PRO PHE GLU GLU SER SEQRES 3 A 641 ASN GLY THR ILE ARG GLU ARG VAL VAL HIS SER PHE ARG SEQRES 4 A 641 ILE PRO THR ILE VAL ASN VAL ASP GLY VAL MET VAL ALA SEQRES 5 A 641 ILE ALA ASP ALA ARG TYR GLU THR SER PHE ASP ASN SER SEQRES 6 A 641 PHE ILE GLU THR ALA VAL LYS TYR SER VAL ASP ASP GLY SEQRES 7 A 641 ALA THR TRP ASN THR GLN ILE ALA ILE LYS ASN SER ARG SEQRES 8 A 641 ALA SER SER VAL SER ARG VAL VAL ASP PRO THR VAL ILE SEQRES 9 A 641 VAL LYS GLY ASN LYS LEU TYR ILE LEU VAL GLY SER PHE SEQRES 10 A 641 ASN LYS THR ARG ASN TYR TRP THR GLN HIS ARG ASP GLY SEQRES 11 A 641 SER ASP TRP GLU PRO LEU LEU VAL VAL GLY GLU VAL THR SEQRES 12 A 641 LYS SER ALA ALA ASN GLY LYS THR THR ALA THR ILE SER SEQRES 13 A 641 TRP GLY LYS PRO VAL SER LEU LYS PRO LEU PHE PRO ALA SEQRES 14 A 641 GLU PHE ASP GLY ILE LEU THR LYS GLU PHE VAL GLY GLY SEQRES 15 A 641 VAL GLY ALA ALA ILE VAL ALA SER ASN GLY ASN LEU VAL SEQRES 16 A 641 TYR PRO VAL GLN ILE ALA ASP MET GLY GLY ARG VAL PHE SEQRES 17 A 641 THR LYS ILE MET TYR SER GLU ASP ASP GLY ASN THR TRP SEQRES 18 A 641 LYS PHE ALA GLU GLY ARG SER LYS PHE GLY CYS SER GLU SEQRES 19 A 641 PRO ALA VAL LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN SEQRES 20 A 641 ASN ARG VAL ASP TYR ASN ARG ARG LEU VAL TYR GLU SER SEQRES 21 A 641 SER ASP MET GLY LYS THR TRP VAL GLU ALA LEU GLY THR SEQRES 22 A 641 LEU SER HIS VAL TRP THR ASN SER PRO THR SER ASN GLN SEQRES 23 A 641 PRO ASP CYS GLN SER SER PHE VAL ALA VAL THR ILE GLU SEQRES 24 A 641 GLY LYS ARG VAL MET LEU PHE THR HIS PRO LEU ASN LEU SEQRES 25 A 641 LYS GLY ARG TRP MET ARG ASP ARG LEU HIS LEU TRP MET SEQRES 26 A 641 THR ASP ASN GLN ARG ILE PHE ASP VAL GLY GLN ILE SER SEQRES 27 A 641 ILE GLY ASP GLU ASN SER GLY TYR SER SER VAL LEU TYR SEQRES 28 A 641 LYS ASP ASP LYS LEU TYR SER LEU HIS GLU ILE ASN THR SEQRES 29 A 641 ASN ASP VAL TYR SER LEU VAL PHE VAL ARG LEU ILE GLY SEQRES 30 A 641 GLU LEU GLN LEU MET LYS SER VAL VAL ARG THR TRP LYS SEQRES 31 A 641 GLU GLU ASP ASN HIS LEU ALA SER ILE CYS THR PRO VAL SEQRES 32 A 641 VAL PRO ALA THR PRO PRO SER LYS GLY ALA CYS GLY ALA SEQRES 33 A 641 ALA VAL PRO THR ALA GLY LEU VAL GLY PHE LEU SER HIS SEQRES 34 A 641 SER ALA ASN GLY SER VAL TRP GLU ASP VAL TYR ARG CYS SEQRES 35 A 641 VAL ASP ALA ASN VAL ALA ASN ALA GLU ARG VAL PRO ASN SEQRES 36 A 641 GLY LEU LYS PHE ASN GLY VAL GLY GLY GLY ALA VAL TRP SEQRES 37 A 641 PRO VAL ALA ARG GLN GLY GLN THR ARG ARG TYR GLN PHE SEQRES 38 A 641 ALA ASN TYR ARG PHE THR LEU VAL ALA THR VAL THR ILE SEQRES 39 A 641 ASP GLU LEU PRO LYS GLY THR SER PRO LEU LEU GLY ALA SEQRES 40 A 641 GLY LEU GLU GLY PRO GLY ASP ALA LYS LEU LEU GLY LEU SEQRES 41 A 641 SER TYR ASP LYS ASN ARG GLN TRP ARG PRO LEU TYR GLY SEQRES 42 A 641 ALA ALA PRO ALA SER PRO THR GLY SER TRP GLU LEU HIS SEQRES 43 A 641 LYS LYS TYR HIS VAL VAL LEU THR MET ALA ASP ARG GLN SEQRES 44 A 641 GLY SER VAL TYR VAL ASP GLY GLN PRO LEU ALA GLY SER SEQRES 45 A 641 GLY ASN THR VAL VAL ARG GLY ALA THR LEU PRO ASP ILE SEQRES 46 A 641 SER HIS PHE TYR ILE GLY GLY PRO ARG SER LYS GLY ALA SEQRES 47 A 641 PRO THR ASP SER ARG VAL THR VAL THR ASN VAL VAL LEU SEQRES 48 A 641 TYR ASN ARG ARG LEU ASN SER SER GLU ILE ARG THR LEU SEQRES 49 A 641 PHE LEU SER GLN ASP MET ILE GLY THR ASP GLY GLY ALA SEQRES 50 A 641 GLY THR ALA ALA HELIX 1 1 TYR A 123 HIS A 127 5 5 HELIX 2 2 LYS A 164 PHE A 167 5 4 HELIX 3 3 LEU A 375 SER A 398 1 24 HELIX 4 4 TYR A 479 ASN A 483 5 5 HELIX 5 5 ASN A 617 LEU A 626 1 10 SHEET 1 AA 4 SER A 9 PHE A 14 0 SHEET 2 AA 4 TYR A 368 ARG A 374 -1 O LEU A 370 N PHE A 14 SHEET 3 AA 4 LYS A 355 ASN A 363 -1 O SER A 358 N VAL A 373 SHEET 4 AA 4 SER A 347 LYS A 352 -1 O SER A 348 N LEU A 359 SHEET 1 AB 2 VAL A 21 GLU A 24 0 SHEET 2 AB 2 ILE A 30 ARG A 33 -1 O ARG A 31 N PHE A 23 SHEET 1 AC 4 SER A 37 VAL A 46 0 SHEET 2 AC 4 VAL A 49 ARG A 57 -1 O VAL A 49 N VAL A 46 SHEET 3 AC 4 ILE A 67 SER A 74 -1 O GLU A 68 N ALA A 56 SHEET 4 AC 4 ASN A 82 ILE A 87 -1 O ASN A 82 N TYR A 73 SHEET 1 AD 5 THR A 151 TRP A 157 0 SHEET 2 AD 5 TRP A 133 ALA A 146 -1 O GLU A 141 N SER A 156 SHEET 3 AD 5 LYS A 109 PHE A 117 -1 O LEU A 110 N GLY A 140 SHEET 4 AD 5 ARG A 97 LYS A 106 -1 O ARG A 97 N PHE A 117 SHEET 5 AD 5 GLY A 184 ALA A 185 1 O GLY A 184 N VAL A 103 SHEET 1 AE 3 THR A 151 TRP A 157 0 SHEET 2 AE 3 TRP A 133 ALA A 146 -1 O GLU A 141 N SER A 156 SHEET 3 AE 3 VAL A 161 SER A 162 -1 O VAL A 161 N LEU A 137 SHEET 1 AF 3 THR A 176 GLY A 181 0 SHEET 2 AF 3 LEU A 194 ASP A 202 -1 O GLN A 199 N VAL A 180 SHEET 3 AF 3 ILE A 187 VAL A 188 -1 O ILE A 187 N VAL A 195 SHEET 1 AG 4 THR A 176 GLY A 181 0 SHEET 2 AG 4 LEU A 194 ASP A 202 -1 O GLN A 199 N VAL A 180 SHEET 3 AG 4 VAL A 207 SER A 214 -1 O PHE A 208 N ILE A 200 SHEET 4 AG 4 LYS A 222 PHE A 223 -1 O LYS A 222 N TYR A 213 SHEET 1 AH 4 CYS A 232 TRP A 240 0 SHEET 2 AH 4 LYS A 243 VAL A 250 -1 O LYS A 243 N TRP A 240 SHEET 3 AH 4 VAL A 257 SER A 260 -1 O TYR A 258 N ILE A 246 SHEET 4 AH 4 VAL A 268 GLU A 269 -1 O VAL A 268 N GLU A 259 SHEET 1 AI 4 PHE A 293 ILE A 298 0 SHEET 2 AI 4 LYS A 301 PRO A 309 -1 O LYS A 301 N ILE A 298 SHEET 3 AI 4 LEU A 321 THR A 326 -1 O HIS A 322 N HIS A 308 SHEET 4 AI 4 ILE A 331 GLN A 336 -1 O PHE A 332 N MET A 325 SHEET 1 AJ 4 LEU A 423 LEU A 427 0 SHEET 2 AJ 4 VAL A 604 TYR A 612 -1 O VAL A 609 N LEU A 427 SHEET 3 AJ 4 GLY A 456 LYS A 458 -1 O LEU A 457 N VAL A 606 SHEET 4 AJ 4 ARG A 452 VAL A 453 -1 O VAL A 453 N GLY A 456 SHEET 1 AK 5 LEU A 423 LEU A 427 0 SHEET 2 AK 5 VAL A 604 TYR A 612 -1 O VAL A 609 N LEU A 427 SHEET 3 AK 5 ARG A 485 ILE A 494 -1 O THR A 487 N TYR A 612 SHEET 4 AK 5 TYR A 549 ALA A 556 -1 O TYR A 549 N VAL A 492 SHEET 5 AK 5 GLN A 559 VAL A 564 -1 O GLN A 559 N ALA A 556 SHEET 1 AL 2 ALA A 431 ASN A 432 0 SHEET 2 AL 2 VAL A 435 TRP A 436 -1 O VAL A 435 N ASN A 432 SHEET 1 AM 5 GLY A 465 PRO A 469 0 SHEET 2 AM 5 HIS A 587 GLY A 591 -1 O PHE A 588 N TRP A 468 SHEET 3 AM 5 THR A 501 GLY A 508 -1 O LEU A 504 N GLY A 591 SHEET 4 AM 5 LYS A 516 ASP A 523 -1 N LEU A 517 O ALA A 507 SHEET 5 AM 5 GLN A 527 TYR A 532 -1 O GLN A 527 N ASP A 523 SSBOND 1 CYS A 400 CYS A 414 CRYST1 94.691 94.691 156.335 90.00 90.00 90.00 P 43 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 0.010561 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010561 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006397 0.00000