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HEADER HYDROLASE, HYDROLASE INHIBITOR 05-OCT-02 1MZ6 TITLE TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH THE INHIBITOR TITLE 2 DANA COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: MATURE SIALIDASE; COMPND 5 EC: 3.2.1.18 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA RANGELI KEYWDS INIBITOR COMPLEX, TRYPANOSOMAL SIALIDASE, SIALYLTRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR A.BUSCHIAZZO,G.A.TAVARES,O.CAMPETELLA,S.SPINELLI, AUTHOR 2 M.L.CREMONA,G.PARIS,M.F.AMAYA,A.C.C.FRASCH,P.M.ALZARI REVDAT 1 16-OCT-02 1MZ6 0 JRNL AUTH A.BUSCHIAZZO,G.A.TAVARES,O.CAMPETELLA,S.SPINELLI, JRNL AUTH 2 M.L.CREMONA,G.PARIS,M.F.AMAYA,A.C.C.FRASCH, JRNL AUTH 3 P.M.ALZARI JRNL TITL STRUCTURAL BASIS OF SIALYLTRANSFERASE ACTIVITY IN JRNL TITL 2 TRYPANOSOMAL SIALIDASES JRNL REF EMBO J. V. 19 16 2000 JRNL REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.90 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) : 2.90 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 : 16159 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) : 0.209 REMARK 3 R VALUE (WORKING SET) : 0.205 REMARK 3 FREE R VALUE : 0.287 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 869 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW : 2.97 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1031 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2320 REMARK 3 BIN FREE R VALUE SET COUNT : 59 REMARK 3 BIN FREE R VALUE : 0.3670 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 4889 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.26 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.46000 REMARK 3 B22 (A**2) : -0.32000 REMARK 3 B33 (A**2) : -0.15000 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): 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 : 0.900 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.776 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4961 ; 0.017 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6751 ; 2.395 ; 1.954 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 617 ; 4.585 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 828 ;23.086 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 767 ; 0.143 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3739 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2544 ; 0.283 ; 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): 528 ; 0.173 ; 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): 31 ; 0.288 ; 0.300 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.075 ; 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): 3065 ; 0.594 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4936 ; 1.121 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1896 ; 1.818 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1815 ; 3.041 ; 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 1MZ6 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 RCSB017320. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-NOV-1997 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : LURE REMARK 200 BEAMLINE : D41A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.375 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE 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 : 17063 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.13800 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.30600 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: UNLIGANDED T. RANGELI SIALIDASE 1MZ5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-8000, AMMONIUM SULFATE, REMARK 280 MORPHOLINOETHANESULFONATE, PH 6.5, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 293K 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 38.10000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.65000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.90000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.65000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.10000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.90000 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 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 404 REMARK 465 PRO A 405 REMARK 465 PRO A 406 REMARK 465 SER A 407 REMARK 465 LYS A 408 REMARK 465 GLY A 409 REMARK 465 GLY A 410 REMARK 465 ARG A 591 REMARK 465 SER A 592 REMARK 465 LYS A 593 REMARK 465 ASP A 631 REMARK 465 GLY A 632 REMARK 465 GLY A 633 REMARK 465 ALA A 634 REMARK 465 GLY A 635 REMARK 465 THR A 636 REMARK 465 ALA A 637 REMARK 465 ALA A 638 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 23 OG REMARK 470 ARG A 28 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 31 CG1 CG2 REMARK 470 GLN A 123 CG CD OE1 NE2 REMARK 470 ARG A 125 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 156 CG CD CE NZ REMARK 470 GLU A 167 CG CD OE1 OE2 REMARK 470 ASN A 391 CG OD1 ND2 REMARK 470 GLU A 541 CG CD OE1 OE2 REMARK 470 LYS A 545 CG CD CE NZ 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 322 SD MET A 322 CE -0.105 REMARK 500 PRO A 509 CB PRO A 509 CG 0.128 REMARK 500 MET A 627 SD MET A 627 CE -0.157 REMARK 500 ILE A 628 CG1 ILE A 628 CD1 -0.115 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 LEU A 494 CA - CB - CG ANGL. DEV. = 19.5 DEGREES REMARK 500 LEU A 542 CA - CB - CG ANGL. DEV. = 15.7 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 180 124.39 91.35 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MZ5 RELATED DB: PDB REMARK 900 TRYPANOSOMA RANGELI SIALIDASE 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: 1MS1 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) 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 DBREF 1MZ6 A 1 638 UNP O44049 O44049_TRYRA 23 660 SEQADV 1MZ6 VAL A 177 UNP O44049 ILE 199 CONFLICT SEQRES 1 A 638 LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS ARG SEQRES 2 A 638 LYS ASN SER THR VAL PRO PHE GLU GLU SER ASN GLY THR SEQRES 3 A 638 ILE ARG GLU ARG VAL VAL HIS SER PHE ARG ILE PRO THR SEQRES 4 A 638 ILE VAL ASN VAL ASP GLY VAL MET VAL ALA THR ALA ASP SEQRES 5 A 638 ALA ARG TYR GLU THR SER PHE ASP ASN SER PHE ILE GLU SEQRES 6 A 638 THR ALA VAL LYS TYR SER VAL ASP ASP GLY ALA THR TRP SEQRES 7 A 638 ASN THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SER SEQRES 8 A 638 VAL SER ARG VAL MET ASP ALA THR VAL ILE VAL LYS GLY SEQRES 9 A 638 ASN LYS LEU TYR ILE LEU VAL GLY SER PHE ASN LYS THR SEQRES 10 A 638 ARG ASN SER TRP THR GLN HIS ARG ASP GLY SER ASP TRP SEQRES 11 A 638 GLU PRO LEU LEU VAL VAL GLY GLU VAL THR LYS SER ALA SEQRES 12 A 638 ALA ASN GLY LYS THR THR ALA THR ILE SER TRP GLY LYS SEQRES 13 A 638 PRO VAL SER LEU LYS PRO LEU PHE PRO ALA GLU PHE ASP SEQRES 14 A 638 GLY ILE LEU THR LYS GLU PHE VAL GLY GLY VAL GLY ALA SEQRES 15 A 638 ALA ILE VAL GLY SER ASN GLY ASN LEU VAL TYR PRO VAL SEQRES 16 A 638 GLN ILE ALA ASP MET GLY GLY ARG VAL PHE THR LYS ILE SEQRES 17 A 638 MET TYR SER GLU ASP ASP GLY ASN THR TRP LYS PHE ALA SEQRES 18 A 638 GLU GLY ARG SER LYS PHE GLY CYS SER GLU PRO ALA VAL SEQRES 19 A 638 LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN ASN ARG VAL SEQRES 20 A 638 ASP GLY ASN ARG ARG LEU VAL TYR GLU SER SER ASP MET SEQRES 21 A 638 GLY LYS THR TRP VAL GLU ALA LEU GLY THR LEU SER HIS SEQRES 22 A 638 VAL TRP THR ASN SER PRO THR SER ASN GLN GLN ASP CYS SEQRES 23 A 638 GLN SER SER PHE VAL ALA VAL THR ILE GLU GLY LYS ARG SEQRES 24 A 638 VAL MET LEU PHE THR HIS PRO LEU ASN LEU LYS GLY ARG SEQRES 25 A 638 TRP MET ARG ASP ARG LEU HIS LEU TRP MET THR ASP ASN SEQRES 26 A 638 GLN ARG ILE PHE ASP VAL GLY GLN ILE SER ILE GLY ASP SEQRES 27 A 638 GLU ASN SER GLY TYR SER SER VAL LEU TYR LYS ASP ASP SEQRES 28 A 638 LYS LEU TYR SER LEU HIS GLU ILE ASN THR ASN ASP VAL SEQRES 29 A 638 TYR SER LEU VAL PHE VAL ARG PHE ILE GLY GLU LEU GLN SEQRES 30 A 638 LEU MET LYS SER VAL VAL ARG THR TRP LYS GLU GLU ASP SEQRES 31 A 638 ASN HIS LEU ALA SER ILE CYS THR PRO VAL VAL PRO ALA SEQRES 32 A 638 THR PRO PRO SER LYS GLY GLY CYS GLY ALA ALA VAL PRO SEQRES 33 A 638 THR ALA GLY LEU VAL GLY PHE LEU SER HIS SER ALA ASN SEQRES 34 A 638 GLY SER VAL TRP GLU ASP VAL TYR ARG CYS VAL ASP ALA SEQRES 35 A 638 ASN VAL ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU LYS SEQRES 36 A 638 PHE ASN GLY VAL GLY GLY GLY ALA VAL TRP PRO VAL ALA SEQRES 37 A 638 ARG GLN GLY GLN THR ARG ARG TYR GLN PHE ALA ASN TYR SEQRES 38 A 638 ARG PHE THR LEU VAL ALA THR VAL THR ILE ASP GLU LEU SEQRES 39 A 638 PRO LYS GLY THR SER PRO LEU LEU GLY ALA GLY LEU GLU SEQRES 40 A 638 GLY PRO GLY ASP ALA LYS LEU LEU GLY LEU SER TYR ASP SEQRES 41 A 638 LYS ASN ARG GLN TRP ARG PRO LEU TYR GLY ALA ALA PRO SEQRES 42 A 638 ALA SER PRO THR GLY SER TRP GLU LEU HIS LYS LYS TYR SEQRES 43 A 638 HIS VAL VAL LEU THR MET ALA ASP ARG GLN GLY SER VAL SEQRES 44 A 638 TYR VAL ASP GLY GLN PRO LEU ALA GLY SER GLY ASN THR SEQRES 45 A 638 VAL VAL ARG GLY ALA THR LEU PRO ASP ILE SER HIS PHE SEQRES 46 A 638 TYR ILE GLY GLY PRO ARG SER LYS GLY ALA PRO THR ASP SEQRES 47 A 638 SER ARG VAL THR VAL THR ASN ILE VAL LEU TYR ASN ARG SEQRES 48 A 638 ARG LEU ASN SER SER GLU ILE ARG THR LEU PHE LEU SER SEQRES 49 A 638 GLN ASP MET ILE GLY THR ASP GLY GLY ALA GLY THR ALA SEQRES 50 A 638 ALA MODRES 1MZ6 ASN A 15 ASN GLYCOSYLATION SITE MODRES 1MZ6 ASN A 24 ASN GLYCOSYLATION SITE MODRES 1MZ6 ASN A 115 ASN GLYCOSYLATION SITE MODRES 1MZ6 ASN A 429 ASN GLYCOSYLATION SITE MODRES 1MZ6 ASN A 614 ASN GLYCOSYLATION SITE HET NAG A 651 14 HET NAG A 652 14 HET NAG A 653 14 HET NAG A 654 14 HET NAG A 655 14 HET DAN 700 20 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID HETSYN NAG NAG FORMUL 2 NAG 5(C8 H15 N O6) FORMUL 7 DAN C11 H17 N O8 FORMUL 8 HOH *40(H2 O) HELIX 1 1 SER A 120 HIS A 124 5 5 HELIX 2 2 LYS A 161 PHE A 164 5 4 HELIX 3 3 PHE A 372 ALA A 394 1 23 HELIX 4 4 ALA A 468 GLY A 471 5 4 HELIX 5 5 TYR A 476 TYR A 481 5 6 HELIX 6 6 ASN A 614 GLN A 625 1 12 SHEET 1 A 4 SER A 6 PHE A 11 0 SHEET 2 A 4 VAL A 364 ARG A 371 -1 O LEU A 367 N PHE A 11 SHEET 3 A 4 LEU A 353 THR A 361 -1 O SER A 355 N VAL A 370 SHEET 4 A 4 VAL A 346 TYR A 348 -1 N LEU A 347 O TYR A 354 SHEET 1 B 2 THR A 17 GLU A 21 0 SHEET 2 B 2 ILE A 27 VAL A 31 -1 N ARG A 28 O PHE A 20 SHEET 1 C 4 SER A 34 VAL A 43 0 SHEET 2 C 4 VAL A 46 ARG A 54 -1 N VAL A 46 O VAL A 43 SHEET 3 C 4 ILE A 64 SER A 71 -1 O GLU A 65 N ALA A 53 SHEET 4 C 4 GLN A 81 ILE A 84 -1 N GLN A 81 O VAL A 68 SHEET 1 D 7 THR A 151 TRP A 154 0 SHEET 2 D 7 TRP A 130 THR A 140 -1 N GLU A 138 O SER A 153 SHEET 3 D 7 VAL A 158 SER A 159 -1 O VAL A 158 N LEU A 134 SHEET 4 D 7 TRP A 130 THR A 140 -1 N LEU A 134 O VAL A 158 SHEET 5 D 7 LYS A 106 PHE A 114 -1 N LEU A 107 O GLY A 137 SHEET 6 D 7 ARG A 94 LYS A 103 -1 N ARG A 94 O PHE A 114 SHEET 7 D 7 GLY A 181 ALA A 182 1 N GLY A 181 O ALA A 98 SHEET 1 E 7 GLU A 167 PHE A 168 0 SHEET 2 E 7 ILE A 171 GLY A 178 -1 N ILE A 171 O PHE A 168 SHEET 3 E 7 LEU A 191 ASP A 199 -1 N GLN A 196 O VAL A 177 SHEET 4 E 7 ILE A 184 VAL A 185 -1 O ILE A 184 N VAL A 192 SHEET 5 E 7 LEU A 191 ASP A 199 -1 N VAL A 192 O ILE A 184 SHEET 6 E 7 VAL A 204 SER A 211 -1 O PHE A 205 N ILE A 197 SHEET 7 E 7 LYS A 219 PHE A 220 -1 O LYS A 219 N TYR A 210 SHEET 1 F 4 CYS A 229 TRP A 237 0 SHEET 2 F 4 LYS A 240 VAL A 247 -1 N LYS A 240 O TRP A 237 SHEET 3 F 4 VAL A 254 SER A 257 -1 O TYR A 255 N ILE A 243 SHEET 4 F 4 VAL A 265 GLU A 266 -1 N VAL A 265 O GLU A 256 SHEET 1 G 4 SER A 289 ILE A 295 0 SHEET 2 G 4 LYS A 298 PRO A 306 -1 O LYS A 298 N ILE A 295 SHEET 3 G 4 LEU A 318 THR A 323 -1 N HIS A 319 O HIS A 305 SHEET 4 G 4 ILE A 328 GLN A 333 -1 N PHE A 329 O MET A 322 SHEET 1 H17 TRP A 525 TYR A 529 0 SHEET 2 H17 LYS A 513 ASP A 520 -1 O GLY A 516 N LEU A 528 SHEET 3 H17 THR A 498 LEU A 506 -1 N SER A 499 O TYR A 519 SHEET 4 H17 ILE A 582 GLY A 588 -1 N SER A 583 O GLY A 505 SHEET 5 H17 GLY A 462 PRO A 466 -1 O ALA A 463 N ILE A 587 SHEET 6 H17 ALA A 442 ALA A 445 -1 N ASN A 443 O VAL A 464 SHEET 7 H17 VAL A 432 ASP A 435 -1 O TRP A 433 N ALA A 442 SHEET 8 H17 LEU A 420 ALA A 428 -1 N SER A 425 O GLU A 434 SHEET 9 H17 VAL A 601 TYR A 609 -1 O ILE A 606 N LEU A 424 SHEET 10 H17 GLY A 453 PHE A 456 -1 O LEU A 454 N VAL A 603 SHEET 11 H17 ALA A 447 VAL A 450 -1 O GLU A 448 N LYS A 455 SHEET 12 H17 GLY A 453 PHE A 456 -1 O GLY A 453 N VAL A 450 SHEET 13 H17 VAL A 601 TYR A 609 -1 O VAL A 601 N PHE A 456 SHEET 14 H17 PHE A 483 ILE A 491 -1 O THR A 484 N TYR A 609 SHEET 15 H17 TYR A 546 ALA A 553 -1 N TYR A 546 O VAL A 489 SHEET 16 H17 GLN A 556 VAL A 561 -1 N GLN A 556 O ALA A 553 SHEET 17 H17 GLN A 564 PRO A 565 -1 O GLN A 564 N VAL A 561 SSBOND 1 CYS A 397 CYS A 411 LINK ND2 ASN A 15 C1 NAG A 654 LINK ND2 ASN A 24 C1 NAG A 655 LINK ND2 ASN A 115 C1 NAG A 653 LINK ND2 ASN A 429 C1 NAG A 652 LINK ND2 ASN A 614 C1 NAG A 651 CRYST1 76.200 93.800 105.300 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 0.013123 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010661 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009497 0.00000