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HEADER HYDROLASE 19-SEP-02 1MS1 TITLE MONOCLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, IN TITLE 2 COMPLEX WITH 3-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID TITLE 3 (DANA) COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANS-SIALIDASE; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: ENZYMATIC GLOBULAR CORE; COMPND 5 EC: 3.2.1.18; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI; SOURCE 3 ORGANISM_COMMON: PARASITIC FLAGELLATE PROTOZOAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DH5A-FT; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTRCHISA KEYWDS TRANSGLYCOSYLATION, BETA-PROPELLER, PROTEIN-CARBOHYDRATE KEYWDS 2 INTERACTIONS, SIALIDASE EXPDTA X-RAY DIFFRACTION AUTHOR A.BUSCHIAZZO,M.F.AMAYA,M.L.CREMONA,A.C.FRASCH,P.M.ALZARI REVDAT 1 25-MAR-03 1MS1 0 JRNL AUTH A.BUSCHIAZZO,M.F.AMAYA,M.L.CREMONA,A.C.FRASCH, JRNL AUTH 2 P.M.ALZARI JRNL TITL THE CRYSTAL STRUCTURE AND MODE OF ACTION OF JRNL TITL 2 TRANS-SIALIDASE, A KEY ENZYME IN TRYPANOSOMA CRUZI JRNL TITL 3 PATHOGENESIS JRNL REF MOL. CELL V. 10 757 2002 JRNL REFN ASTM MOCEFL US ISSN 1097-2765 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 124387 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) : 0.177 REMARK 3 R VALUE (WORKING SET) : 0.175 REMARK 3 FREE R VALUE : 0.199 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6594 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 8869 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2200 REMARK 3 BIN FREE R VALUE SET COUNT : 499 REMARK 3 BIN FREE R VALUE : 0.2570 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 10915 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.85 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.87000 REMARK 3 B22 (A**2) : -0.34000 REMARK 3 B33 (A**2) : -0.52000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.46000 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): NULL 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 : 0.959 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10071 ; 0.008 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13730 ; 1.325 ; 1.943 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1278 ; 4.403 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1727 ;15.825 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1513 ; 0.095 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7664 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4714 ; 0.217 ; 0.300 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): 1498 ; 0.147 ; 0.500 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): 55 ; 0.188 ; 0.300 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 37 ; 0.194 ; 0.500 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): 6221 ; 0.592 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10083 ; 1.103 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3850 ; 1.694 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3647 ; 2.810 ; 4.500 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 : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1MS1 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 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB017141. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-MAR-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 155765 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 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 (%) : 99.2 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08600 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.42100 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 ID 1MZ5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.74 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRISHCL, ISOPROPANOL, PH REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 64.89650 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 MET A -13 REMARK 465 GLY A -12 REMARK 465 GLY A -11 REMARK 465 SER A -10 REMARK 465 HIS A -9 REMARK 465 HIS A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 GLY A -3 REMARK 465 MET A -2 REMARK 465 ALA A -1 REMARK 465 SER A 0 REMARK 465 ASP A 400 REMARK 465 PRO A 401 REMARK 465 ALA A 402 REMARK 465 ALA A 403 REMARK 465 SER A 404 REMARK 465 SER A 405 REMARK 465 SER A 406 REMARK 465 GLU A 407 REMARK 465 ARG A 408 REMARK 465 GLY A 409 REMARK 465 MET A 633 REMARK 465 ASP A 634 REMARK 465 MET B -13 REMARK 465 GLY B -12 REMARK 465 GLY B -11 REMARK 465 SER B -10 REMARK 465 HIS B -9 REMARK 465 HIS B -8 REMARK 465 HIS B -7 REMARK 465 HIS B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 REMARK 465 GLY B -3 REMARK 465 MET B -2 REMARK 465 ALA B -1 REMARK 465 SER B 0 REMARK 465 ASP B 400 REMARK 465 PRO B 401 REMARK 465 ALA B 402 REMARK 465 ALA B 403 REMARK 465 SER B 404 REMARK 465 SER B 405 REMARK 465 SER B 406 REMARK 465 GLU B 407 REMARK 465 ARG B 408 REMARK 465 GLY B 409 REMARK 465 MET B 633 REMARK 465 ASP B 634 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 GLU A 576 CG CD OE1 OE2 REMARK 470 ARG A 577 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 576 CG CD OE1 OE2 REMARK 470 ARG B 577 CG CD NE CZ NH1 NH2 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 282 O HOH 970 1.67 REMARK 500 O HOH 672 O HOH 711 1.97 REMARK 500 OH TYR A 342 C1 DAN 2700 2.02 REMARK 500 OH TYR B 342 C1 DAN 2701 2.06 REMARK 500 O HOH 832 O HOH 947 2.08 REMARK 500 ND1 HIS B 391 O HOH 904 2.11 REMARK 500 OE2 GLU B 230 O8 DAN 2701 2.13 REMARK 500 ND2 ASN B 318 OD1 ASN B 329 2.14 REMARK 500 O HOH 437 O HOH 879 2.14 REMARK 500 OD1 ASP A 96 O9 DAN 2700 2.15 REMARK 500 O HOH 501 O HOH 829 2.16 REMARK 500 O HOH 580 O HOH 859 2.16 REMARK 500 OH TYR B 342 O1B DAN 2701 2.17 REMARK 500 O HOH 888 O HOH 1012 2.18 REMARK 500 O HOH 787 O HOH 916 2.19 REMARK 500 O HOH 837 O HOH 1043 2.19 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 561 O HOH 965 1655 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 MET A 170 SD MET A 170 CE 0.056 REMARK 500 ILE A 327 CG1 ILE A 327 CD1 0.065 REMARK 500 PRO A 450 CB PRO A 450 CG 0.066 REMARK 500 MET A 594 SD MET A 594 CE 0.061 REMARK 500 GLN A 624 CB GLN A 624 CG -0.051 REMARK 500 ILE B 81 CG1 ILE B 81 CD1 0.049 REMARK 500 MET B 170 SD MET B 170 CE -0.066 REMARK 500 MET B 259 SD MET B 259 CE -0.066 REMARK 500 MET B 297 SD MET B 297 CE 0.126 REMARK 500 ILE B 327 CG1 ILE B 327 CD1 0.058 REMARK 500 MET B 551 SD MET B 551 CE 0.064 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 PRO A 193 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 SER B 393 N - CA - C ANGL. DEV. =-10.7 DEGREES REMARK 500 ARG B 544 CA - CB - CG ANGL. DEV. =-15.9 DEGREES REMARK 500 ARG B 544 CG - CD - NE ANGL. DEV. =-14.7 DEGREES REMARK 500 ARG B 544 CD - NE - CZ ANGL. DEV. = 9.6 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 1085 DISTANCE = 5.07 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MR5 RELATED DB: PDB REMARK 900 ORTHORHOMBIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE REMARK 900 RELATED ID: 1MS0 RELATED DB: PDB REMARK 900 MONOCLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, IN REMARK 900 COMPLEX WITH 3-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID REMARK 900 (DANA)AND LACTOSE REMARK 900 RELATED ID: 1MS3 RELATED DB: PDB REMARK 900 MONOCLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE REMARK 900 RELATED ID: 1MS4 RELATED DB: PDB REMARK 900 TRICLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE REMARK 900 RELATED ID: 1MS5 RELATED DB: PDB REMARK 900 TRICLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, SOAKED REMARK 900 WITH N-ACETYLNEURAMINYL-A-2,3-THIO-GALACTOSIDE (NA-S-GAL) REMARK 900 RELATED ID: 1MS8 RELATED DB: PDB REMARK 900 TRICLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, IN REMARK 900 COMPLEX WITH 3-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID REMARK 900 (DANA) REMARK 900 RELATED ID: 1MS9 RELATED DB: PDB REMARK 900 TRICLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, IN REMARK 900 COMPLEX WITH LACTOSE REMARK 900 RELATED ID: 1MZ5 RELATED DB: PDB REMARK 900 TRYPANOSOMA RANGELI SIALIDASE REMARK 900 RELATED ID: 1MZ6 RELATED DB: PDB REMARK 900 TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH INHIBITOR DANA REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHOR INDICATES THAT THE SEQUENCE IN THE DATABASE REMARK 999 IS INCORRECT DBREF 1MS1 A 1 634 UNP Q26964 Q26964_TRYCR 2 635 DBREF 1MS1 B 1 634 UNP Q26964 Q26964_TRYCR 2 635 SEQADV 1MS1 MET A -13 UNP Q26964 HIS TAG SEQADV 1MS1 GLY A -12 UNP Q26964 HIS TAG SEQADV 1MS1 GLY A -11 UNP Q26964 HIS TAG SEQADV 1MS1 SER A -10 UNP Q26964 HIS TAG SEQADV 1MS1 HIS A -9 UNP Q26964 HIS TAG SEQADV 1MS1 HIS A -8 UNP Q26964 HIS TAG SEQADV 1MS1 HIS A -7 UNP Q26964 HIS TAG SEQADV 1MS1 HIS A -6 UNP Q26964 HIS TAG SEQADV 1MS1 HIS A -5 UNP Q26964 HIS TAG SEQADV 1MS1 HIS A -4 UNP Q26964 HIS TAG SEQADV 1MS1 GLY A -3 UNP Q26964 HIS TAG SEQADV 1MS1 MET A -2 UNP Q26964 HIS TAG SEQADV 1MS1 ALA A -1 UNP Q26964 HIS TAG SEQADV 1MS1 SER A 0 UNP Q26964 HIS TAG SEQADV 1MS1 PHE A 58 UNP Q26964 ASN 59 ENGINEERED SEQADV 1MS1 THR A 262 UNP Q26964 SER 263 SEE REMARK 999 SEQADV 1MS1 HIS A 476 UNP Q26964 ARG 477 SEE REMARK 999 SEQADV 1MS1 LEU A 484 UNP Q26964 VAL 485 SEE REMARK 999 SEQADV 1MS1 LYS A 495 UNP Q26964 SER 496 ENGINEERED SEQADV 1MS1 GLY A 496 UNP Q26964 VAL 497 ENGINEERED SEQADV 1MS1 LYS A 520 UNP Q26964 GLU 521 ENGINEERED SEQADV 1MS1 VAL A 558 UNP Q26964 GLU 559 SEE REMARK 999 SEQADV 1MS1 GLY A 593 UNP Q26964 ASP 594 ENGINEERED SEQADV 1MS1 ASP A 597 UNP Q26964 ILE 598 ENGINEERED SEQADV 1MS1 ARG A 599 UNP Q26964 HIS 600 ENGINEERED SEQADV 1MS1 MET B -13 UNP Q26964 HIS TAG SEQADV 1MS1 GLY B -12 UNP Q26964 HIS TAG SEQADV 1MS1 GLY B -11 UNP Q26964 HIS TAG SEQADV 1MS1 SER B -10 UNP Q26964 HIS TAG SEQADV 1MS1 HIS B -9 UNP Q26964 HIS TAG SEQADV 1MS1 HIS B -8 UNP Q26964 HIS TAG SEQADV 1MS1 HIS B -7 UNP Q26964 HIS TAG SEQADV 1MS1 HIS B -6 UNP Q26964 HIS TAG SEQADV 1MS1 HIS B -5 UNP Q26964 HIS TAG SEQADV 1MS1 HIS B -4 UNP Q26964 HIS TAG SEQADV 1MS1 GLY B -3 UNP Q26964 HIS TAG SEQADV 1MS1 MET B -2 UNP Q26964 HIS TAG SEQADV 1MS1 ALA B -1 UNP Q26964 HIS TAG SEQADV 1MS1 SER B 0 UNP Q26964 HIS TAG SEQADV 1MS1 PHE B 58 UNP Q26964 ASN 59 ENGINEERED SEQADV 1MS1 THR B 262 UNP Q26964 SER 263 SEE REMARK 999 SEQADV 1MS1 HIS B 476 UNP Q26964 ARG 477 SEE REMARK 999 SEQADV 1MS1 LEU B 484 UNP Q26964 VAL 485 SEE REMARK 999 SEQADV 1MS1 LYS B 495 UNP Q26964 SER 496 ENGINEERED SEQADV 1MS1 GLY B 496 UNP Q26964 VAL 497 ENGINEERED SEQADV 1MS1 LYS B 520 UNP Q26964 GLU 521 ENGINEERED SEQADV 1MS1 VAL B 558 UNP Q26964 GLU 559 SEE REMARK 999 SEQADV 1MS1 GLY B 593 UNP Q26964 ASP 594 ENGINEERED SEQADV 1MS1 ASP B 597 UNP Q26964 ILE 598 ENGINEERED SEQADV 1MS1 ARG B 599 UNP Q26964 HIS 600 ENGINEERED SEQRES 1 A 648 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA SEQRES 2 A 648 SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS SEQRES 3 A 648 ARG GLN SER SER LYS VAL PRO PHE GLU LYS ASP GLY LYS SEQRES 4 A 648 VAL THR GLU ARG VAL VAL HIS SER PHE ARG LEU PRO ALA SEQRES 5 A 648 LEU VAL ASN VAL ASP GLY VAL MET VAL ALA ILE ALA ASP SEQRES 6 A 648 ALA ARG TYR GLU THR SER PHE ASP ASN SER LEU ILE ASP SEQRES 7 A 648 THR VAL ALA LYS TYR SER VAL ASP ASP GLY GLU THR TRP SEQRES 8 A 648 GLU THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SER SEQRES 9 A 648 VAL SER ARG VAL VAL ASP PRO THR VAL ILE VAL LYS GLY SEQRES 10 A 648 ASN LYS LEU TYR VAL LEU VAL GLY SER TYR ASN SER SER SEQRES 11 A 648 ARG SER TYR TRP THR SER HIS GLY ASP ALA ARG ASP TRP SEQRES 12 A 648 ASP ILE LEU LEU ALA VAL GLY GLU VAL THR LYS SER THR SEQRES 13 A 648 ALA GLY GLY LYS ILE THR ALA SER ILE LYS TRP GLY SER SEQRES 14 A 648 PRO VAL SER LEU LYS GLU PHE PHE PRO ALA GLU MET GLU SEQRES 15 A 648 GLY MET HIS THR ASN GLN PHE LEU GLY GLY ALA GLY VAL SEQRES 16 A 648 ALA ILE VAL ALA SER ASN GLY ASN LEU VAL TYR PRO VAL SEQRES 17 A 648 GLN VAL THR ASN LYS LYS LYS GLN VAL PHE SER LYS ILE SEQRES 18 A 648 PHE TYR SER GLU ASP GLU GLY LYS THR TRP LYS PHE GLY SEQRES 19 A 648 LYS GLY ARG SER ALA PHE GLY CYS SER GLU PRO VAL ALA SEQRES 20 A 648 LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN THR ARG VAL SEQRES 21 A 648 ASP TYR ARG ARG ARG LEU VAL TYR GLU SER SER ASP MET SEQRES 22 A 648 GLY ASN THR TRP LEU GLU ALA VAL GLY THR LEU SER ARG SEQRES 23 A 648 VAL TRP GLY PRO SER PRO LYS SER ASN GLN PRO GLY SER SEQRES 24 A 648 GLN SER SER PHE THR ALA VAL THR ILE GLU GLY MET ARG SEQRES 25 A 648 VAL MET LEU PHE THR HIS PRO LEU ASN PHE LYS GLY ARG SEQRES 26 A 648 TRP LEU ARG ASP ARG LEU ASN LEU TRP LEU THR ASP ASN SEQRES 27 A 648 GLN ARG ILE TYR ASN VAL GLY GLN VAL SER ILE GLY ASP SEQRES 28 A 648 GLU ASN SER ALA TYR SER SER VAL LEU TYR LYS ASP ASP SEQRES 29 A 648 LYS LEU TYR CYS LEU HIS GLU ILE ASN SER ASN GLU VAL SEQRES 30 A 648 TYR SER LEU VAL PHE ALA ARG LEU VAL GLY GLU LEU ARG SEQRES 31 A 648 ILE ILE LYS SER VAL LEU GLN SER TRP LYS ASN TRP ASP SEQRES 32 A 648 SER HIS LEU SER SER ILE CYS THR PRO ALA ASP PRO ALA SEQRES 33 A 648 ALA SER SER SER GLU ARG GLY CYS GLY PRO ALA VAL THR SEQRES 34 A 648 THR VAL GLY LEU VAL GLY PHE LEU SER HIS SER ALA THR SEQRES 35 A 648 LYS THR GLU TRP GLU ASP ALA TYR ARG CYS VAL ASN ALA SEQRES 36 A 648 SER THR ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU LYS SEQRES 37 A 648 PHE ALA GLY VAL GLY GLY GLY ALA LEU TRP PRO VAL SER SEQRES 38 A 648 GLN GLN GLY GLN ASN GLN ARG TYR HIS PHE ALA ASN HIS SEQRES 39 A 648 ALA PHE THR LEU VAL ALA SER VAL THR ILE HIS GLU VAL SEQRES 40 A 648 PRO LYS GLY ALA SER PRO LEU LEU GLY ALA SER LEU ASP SEQRES 41 A 648 SER SER GLY GLY LYS LYS LEU LEU GLY LEU SER TYR ASP SEQRES 42 A 648 LYS ARG HIS GLN TRP GLN PRO ILE TYR GLY SER THR PRO SEQRES 43 A 648 VAL THR PRO THR GLY SER TRP GLU MET GLY LYS ARG TYR SEQRES 44 A 648 HIS VAL VAL LEU THR MET ALA ASN LYS ILE GLY SER VAL SEQRES 45 A 648 TYR ILE ASP GLY GLU PRO LEU GLU GLY SER GLY GLN THR SEQRES 46 A 648 VAL VAL PRO ASP GLU ARG THR PRO ASP ILE SER HIS PHE SEQRES 47 A 648 TYR VAL GLY GLY TYR LYS ARG SER GLY MET PRO THR ASP SEQRES 48 A 648 SER ARG VAL THR VAL ASN ASN VAL LEU LEU TYR ASN ARG SEQRES 49 A 648 GLN LEU ASN ALA GLU GLU ILE ARG THR LEU PHE LEU SER SEQRES 50 A 648 GLN ASP LEU ILE GLY THR GLU ALA HIS MET ASP SEQRES 1 B 648 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA SEQRES 2 B 648 SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS SEQRES 3 B 648 ARG GLN SER SER LYS VAL PRO PHE GLU LYS ASP GLY LYS SEQRES 4 B 648 VAL THR GLU ARG VAL VAL HIS SER PHE ARG LEU PRO ALA SEQRES 5 B 648 LEU VAL ASN VAL ASP GLY VAL MET VAL ALA ILE ALA ASP SEQRES 6 B 648 ALA ARG TYR GLU THR SER PHE ASP ASN SER LEU ILE ASP SEQRES 7 B 648 THR VAL ALA LYS TYR SER VAL ASP ASP GLY GLU THR TRP SEQRES 8 B 648 GLU THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SER SEQRES 9 B 648 VAL SER ARG VAL VAL ASP PRO THR VAL ILE VAL LYS GLY SEQRES 10 B 648 ASN LYS LEU TYR VAL LEU VAL GLY SER TYR ASN SER SER SEQRES 11 B 648 ARG SER TYR TRP THR SER HIS GLY ASP ALA ARG ASP TRP SEQRES 12 B 648 ASP ILE LEU LEU ALA VAL GLY GLU VAL THR LYS SER THR SEQRES 13 B 648 ALA GLY GLY LYS ILE THR ALA SER ILE LYS TRP GLY SER SEQRES 14 B 648 PRO VAL SER LEU LYS GLU PHE PHE PRO ALA GLU MET GLU SEQRES 15 B 648 GLY MET HIS THR ASN GLN PHE LEU GLY GLY ALA GLY VAL SEQRES 16 B 648 ALA ILE VAL ALA SER ASN GLY ASN LEU VAL TYR PRO VAL SEQRES 17 B 648 GLN VAL THR ASN LYS LYS LYS GLN VAL PHE SER LYS ILE SEQRES 18 B 648 PHE TYR SER GLU ASP GLU GLY LYS THR TRP LYS PHE GLY SEQRES 19 B 648 LYS GLY ARG SER ALA PHE GLY CYS SER GLU PRO VAL ALA SEQRES 20 B 648 LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN THR ARG VAL SEQRES 21 B 648 ASP TYR ARG ARG ARG LEU VAL TYR GLU SER SER ASP MET SEQRES 22 B 648 GLY ASN THR TRP LEU GLU ALA VAL GLY THR LEU SER ARG SEQRES 23 B 648 VAL TRP GLY PRO SER PRO LYS SER ASN GLN PRO GLY SER SEQRES 24 B 648 GLN SER SER PHE THR ALA VAL THR ILE GLU GLY MET ARG SEQRES 25 B 648 VAL MET LEU PHE THR HIS PRO LEU ASN PHE LYS GLY ARG SEQRES 26 B 648 TRP LEU ARG ASP ARG LEU ASN LEU TRP LEU THR ASP ASN SEQRES 27 B 648 GLN ARG ILE TYR ASN VAL GLY GLN VAL SER ILE GLY ASP SEQRES 28 B 648 GLU ASN SER ALA TYR SER SER VAL LEU TYR LYS ASP ASP SEQRES 29 B 648 LYS LEU TYR CYS LEU HIS GLU ILE ASN SER ASN GLU VAL SEQRES 30 B 648 TYR SER LEU VAL PHE ALA ARG LEU VAL GLY GLU LEU ARG SEQRES 31 B 648 ILE ILE LYS SER VAL LEU GLN SER TRP LYS ASN TRP ASP SEQRES 32 B 648 SER HIS LEU SER SER ILE CYS THR PRO ALA ASP PRO ALA SEQRES 33 B 648 ALA SER SER SER GLU ARG GLY CYS GLY PRO ALA VAL THR SEQRES 34 B 648 THR VAL GLY LEU VAL GLY PHE LEU SER HIS SER ALA THR SEQRES 35 B 648 LYS THR GLU TRP GLU ASP ALA TYR ARG CYS VAL ASN ALA SEQRES 36 B 648 SER THR ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU LYS SEQRES 37 B 648 PHE ALA GLY VAL GLY GLY GLY ALA LEU TRP PRO VAL SER SEQRES 38 B 648 GLN GLN GLY GLN ASN GLN ARG TYR HIS PHE ALA ASN HIS SEQRES 39 B 648 ALA PHE THR LEU VAL ALA SER VAL THR ILE HIS GLU VAL SEQRES 40 B 648 PRO LYS GLY ALA SER PRO LEU LEU GLY ALA SER LEU ASP SEQRES 41 B 648 SER SER GLY GLY LYS LYS LEU LEU GLY LEU SER TYR ASP SEQRES 42 B 648 LYS ARG HIS GLN TRP GLN PRO ILE TYR GLY SER THR PRO SEQRES 43 B 648 VAL THR PRO THR GLY SER TRP GLU MET GLY LYS ARG TYR SEQRES 44 B 648 HIS VAL VAL LEU THR MET ALA ASN LYS ILE GLY SER VAL SEQRES 45 B 648 TYR ILE ASP GLY GLU PRO LEU GLU GLY SER GLY GLN THR SEQRES 46 B 648 VAL VAL PRO ASP GLU ARG THR PRO ASP ILE SER HIS PHE SEQRES 47 B 648 TYR VAL GLY GLY TYR LYS ARG SER GLY MET PRO THR ASP SEQRES 48 B 648 SER ARG VAL THR VAL ASN ASN VAL LEU LEU TYR ASN ARG SEQRES 49 B 648 GLN LEU ASN ALA GLU GLU ILE ARG THR LEU PHE LEU SER SEQRES 50 B 648 GLN ASP LEU ILE GLY THR GLU ALA HIS MET ASP HET DAN 2700 26 HET DAN 2701 26 HET GOL 2800 6 HET GOL 2801 6 HET GOL 2802 6 HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID HETNAM GOL GLYCEROL FORMUL 3 DAN 2(C11 H17 N O8) FORMUL 5 GOL 3(C3 H8 O3) FORMUL 8 HOH *1096(H2 O) HELIX 1 1 TYR A 119 HIS A 123 5 5 HELIX 2 2 LYS A 160 PHE A 163 5 4 HELIX 3 3 LEU A 371 ILE A 395 1 25 HELIX 4 4 SER A 467 GLY A 470 5 4 HELIX 5 5 TYR A 475 ASN A 479 5 5 HELIX 6 6 ASN A 613 SER A 623 1 11 HELIX 7 7 TYR B 119 HIS B 123 5 5 HELIX 8 8 LYS B 160 PHE B 163 5 4 HELIX 9 9 LEU B 371 SER B 393 1 23 HELIX 10 10 SER B 467 GLY B 470 5 4 HELIX 11 11 TYR B 475 HIS B 480 5 6 HELIX 12 12 ASN B 613 SER B 623 1 11 SHEET 1 A 4 SER A 6 PHE A 11 0 SHEET 2 A 4 VAL A 363 ARG A 370 -1 N LEU A 366 O PHE A 11 SHEET 3 A 4 LYS A 351 SER A 360 -1 O CYS A 354 N ALA A 369 SHEET 4 A 4 SER A 343 LYS A 348 -1 O SER A 344 N LEU A 355 SHEET 1 B 2 LYS A 17 LYS A 22 0 SHEET 2 B 2 LYS A 25 VAL A 30 -1 O LYS A 25 N LYS A 22 SHEET 1 C 4 SER A 33 VAL A 42 0 SHEET 2 C 4 VAL A 45 ARG A 53 -1 O VAL A 45 N VAL A 42 SHEET 3 C 4 ILE A 63 SER A 70 -1 O ASP A 64 N ALA A 52 SHEET 4 C 4 GLU A 78 ILE A 83 -1 N GLU A 78 O TYR A 69 SHEET 1 D 7 THR A 148 TRP A 153 0 SHEET 2 D 7 TRP A 129 SER A 141 -1 N GLU A 137 O LYS A 152 SHEET 3 D 7 VAL A 157 SER A 158 -1 O VAL A 157 N LEU A 133 SHEET 4 D 7 TRP A 129 SER A 141 -1 N LEU A 133 O VAL A 157 SHEET 5 D 7 LYS A 105 TYR A 113 -1 O LEU A 106 N GLY A 136 SHEET 6 D 7 ARG A 93 LYS A 102 -1 O ARG A 93 N TYR A 113 SHEET 7 D 7 GLY A 180 VAL A 181 1 O GLY A 180 N VAL A 99 SHEET 1 E 7 GLU A 166 MET A 167 0 SHEET 2 E 7 MET A 170 GLY A 177 -1 N MET A 170 O MET A 167 SHEET 3 E 7 LEU A 190 ASN A 198 -1 N GLN A 195 O LEU A 176 SHEET 4 E 7 ILE A 183 VAL A 184 -1 O ILE A 183 N VAL A 191 SHEET 5 E 7 LEU A 190 ASN A 198 -1 N VAL A 191 O ILE A 183 SHEET 6 E 7 VAL A 203 SER A 210 -1 O PHE A 204 N VAL A 196 SHEET 7 E 7 LYS A 218 PHE A 219 -1 O LYS A 218 N TYR A 209 SHEET 1 F 4 CYS A 228 TRP A 236 0 SHEET 2 F 4 LYS A 239 VAL A 246 -1 O LYS A 239 N TRP A 236 SHEET 3 F 4 VAL A 253 SER A 256 -1 O TYR A 254 N ILE A 242 SHEET 4 F 4 LEU A 264 GLU A 265 -1 O LEU A 264 N GLU A 255 SHEET 1 G 4 PHE A 289 ILE A 294 0 SHEET 2 G 4 MET A 297 PRO A 305 -1 O MET A 297 N ILE A 294 SHEET 3 G 4 LEU A 317 THR A 322 -1 N ASN A 318 O HIS A 304 SHEET 4 G 4 ILE A 327 GLN A 332 -1 N TYR A 328 O LEU A 321 SHEET 1 H19 TRP A 524 TYR A 528 0 SHEET 2 H19 LYS A 512 ASP A 519 -1 O GLY A 515 N ILE A 527 SHEET 3 H19 ALA A 497 SER A 504 -1 N SER A 498 O TYR A 518 SHEET 4 H19 HIS A 583 VAL A 586 -1 O HIS A 583 N SER A 504 SHEET 5 H19 GLY A 461 PRO A 465 -1 N ALA A 462 O VAL A 586 SHEET 6 H19 ALA A 441 ALA A 444 -1 O SER A 442 N LEU A 463 SHEET 7 H19 GLU A 431 ASP A 434 -1 N TRP A 432 O ALA A 441 SHEET 8 H19 LEU A 419 ALA A 427 -1 N SER A 424 O GLU A 433 SHEET 9 H19 VAL A 600 TYR A 608 -1 O VAL A 605 N LEU A 423 SHEET 10 H19 GLY A 452 PHE A 455 -1 O LEU A 453 N VAL A 602 SHEET 11 H19 ALA A 446 VAL A 449 -1 O GLU A 447 N LYS A 454 SHEET 12 H19 GLY A 452 PHE A 455 -1 N GLY A 452 O VAL A 449 SHEET 13 H19 VAL A 600 TYR A 608 -1 O VAL A 600 N PHE A 455 SHEET 14 H19 ALA A 481 ILE A 490 -1 O THR A 483 N TYR A 608 SHEET 15 H19 ARG A 544 ALA A 552 -1 N TYR A 545 O VAL A 488 SHEET 16 H19 ILE A 555 ILE A 560 -1 N ILE A 555 O ALA A 552 SHEET 17 H19 GLU A 563 PRO A 564 -1 O GLU A 563 N ILE A 560 SHEET 18 H19 ILE A 555 ILE A 560 -1 N ILE A 560 O GLU A 563 SHEET 19 H19 GLN A 570 THR A 571 -1 O GLN A 570 N GLY A 556 SHEET 1 I 4 SER B 6 PHE B 11 0 SHEET 2 I 4 VAL B 363 ARG B 370 -1 O LEU B 366 N PHE B 11 SHEET 3 I 4 LYS B 351 SER B 360 -1 O CYS B 354 N ALA B 369 SHEET 4 I 4 SER B 343 LYS B 348 -1 O SER B 344 N LEU B 355 SHEET 1 J 2 LYS B 17 LYS B 22 0 SHEET 2 J 2 LYS B 25 VAL B 30 -1 O LYS B 25 N LYS B 22 SHEET 1 K 4 SER B 33 VAL B 42 0 SHEET 2 K 4 VAL B 45 ARG B 53 -1 O VAL B 45 N VAL B 42 SHEET 3 K 4 ILE B 63 SER B 70 -1 O ASP B 64 N ALA B 52 SHEET 4 K 4 GLU B 78 ILE B 83 -1 N GLU B 78 O TYR B 69 SHEET 1 L 7 THR B 148 TRP B 153 0 SHEET 2 L 7 TRP B 129 SER B 141 -1 N GLU B 137 O LYS B 152 SHEET 3 L 7 VAL B 157 SER B 158 -1 O VAL B 157 N LEU B 133 SHEET 4 L 7 TRP B 129 SER B 141 -1 N LEU B 133 O VAL B 157 SHEET 5 L 7 LYS B 105 TYR B 113 -1 N LEU B 106 O GLY B 136 SHEET 6 L 7 ARG B 93 LYS B 102 -1 O ARG B 93 N TYR B 113 SHEET 7 L 7 GLY B 180 VAL B 181 1 O GLY B 180 N VAL B 99 SHEET 1 M 7 GLU B 166 MET B 167 0 SHEET 2 M 7 MET B 170 GLY B 177 -1 O MET B 170 N MET B 167 SHEET 3 M 7 LEU B 190 ASN B 198 -1 N GLN B 195 O LEU B 176 SHEET 4 M 7 ILE B 183 VAL B 184 -1 O ILE B 183 N VAL B 191 SHEET 5 M 7 LEU B 190 ASN B 198 -1 N VAL B 191 O ILE B 183 SHEET 6 M 7 VAL B 203 SER B 210 -1 O PHE B 204 N VAL B 196 SHEET 7 M 7 LYS B 218 PHE B 219 -1 N LYS B 218 O TYR B 209 SHEET 1 N 4 CYS B 228 TRP B 236 0 SHEET 2 N 4 LYS B 239 VAL B 246 -1 O LYS B 239 N TRP B 236 SHEET 3 N 4 VAL B 253 SER B 256 -1 O TYR B 254 N ILE B 242 SHEET 4 N 4 LEU B 264 GLU B 265 -1 O LEU B 264 N GLU B 255 SHEET 1 O 4 PHE B 289 ILE B 294 0 SHEET 2 O 4 MET B 297 PRO B 305 -1 O MET B 297 N ILE B 294 SHEET 3 O 4 LEU B 317 THR B 322 -1 N ASN B 318 O HIS B 304 SHEET 4 O 4 ILE B 327 GLN B 332 -1 N TYR B 328 O LEU B 321 SHEET 1 P19 TRP B 524 TYR B 528 0 SHEET 2 P19 LYS B 512 TYR B 518 -1 O GLY B 515 N ILE B 527 SHEET 3 P19 SER B 498 SER B 504 -1 N SER B 498 O TYR B 518 SHEET 4 P19 HIS B 583 VAL B 586 -1 O HIS B 583 N SER B 504 SHEET 5 P19 GLY B 461 PRO B 465 -1 N ALA B 462 O VAL B 586 SHEET 6 P19 ALA B 441 ALA B 444 -1 O SER B 442 N LEU B 463 SHEET 7 P19 GLU B 431 ASP B 434 -1 N TRP B 432 O ALA B 441 SHEET 8 P19 LEU B 419 ALA B 427 -1 N SER B 424 O GLU B 433 SHEET 9 P19 VAL B 600 TYR B 608 -1 O VAL B 605 N LEU B 423 SHEET 10 P19 GLY B 452 PHE B 455 -1 O LEU B 453 N VAL B 602 SHEET 11 P19 ALA B 446 VAL B 449 -1 N GLU B 447 O LYS B 454 SHEET 12 P19 GLY B 452 PHE B 455 -1 O GLY B 452 N VAL B 449 SHEET 13 P19 VAL B 600 TYR B 608 -1 O VAL B 600 N PHE B 455 SHEET 14 P19 PHE B 482 ILE B 490 -1 O THR B 483 N TYR B 608 SHEET 15 P19 ARG B 544 ALA B 552 -1 O TYR B 545 N VAL B 488 SHEET 16 P19 ILE B 555 ILE B 560 -1 N ILE B 555 O ALA B 552 SHEET 17 P19 GLU B 563 PRO B 564 -1 O GLU B 563 N ILE B 560 SHEET 18 P19 ILE B 555 ILE B 560 -1 N ILE B 560 O GLU B 563 SHEET 19 P19 GLN B 570 THR B 571 -1 O GLN B 570 N GLY B 556 SSBOND 1 CYS A 396 CYS A 410 SSBOND 2 CYS B 396 CYS B 410 CRYST1 63.719 129.793 88.039 90.00 90.67 90.00 P 1 21 1 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 0.015694 0.000000 0.000184 0.00000 SCALE2 0.000000 0.007705 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011359 0.00000