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HEADER HYDROLASE 26-DEC-05 2FHR TITLE TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH 2,3- TITLE 2 DIFLUOROSIALIC ACID (COVALENT INTERMEDIATE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA RANGELI; SOURCE 3 ORGANISM_COMMON: MYCOPLASMA; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TOP10; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTRCHISA KEYWDS BETA-PROPELLER, COVALENT ENZYME-INTERMEDIATE COMPLEX, BETA- KEYWDS 2 SANDWICH EXPDTA X-RAY DIFFRACTION AUTHOR M.F.AMAYA,P.M.ALZARI,A.BUSCHIAZZO REVDAT 2 28-FEB-06 2FHR 1 JRNL REVDAT 1 17-JAN-06 2FHR 0 JRNL AUTH A.G.WATTS,P.OPPEZZO,S.G.WITHERS,P.M.ALZARI, JRNL AUTH 2 A.BUSCHIAZZO JRNL TITL STRUCTURAL AND KINETIC ANALYSIS OF TWO COVALENT JRNL TITL 2 SIALOSYL-ENZYME INTERMEDIATES ON TRYPANOSOMA JRNL TITL 3 RANGELI SIALIDASE. JRNL REF J.BIOL.CHEM. V. 281 4149 2006 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.8 REMARK 3 NUMBER OF REFLECTIONS : 36190 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.164 REMARK 3 R VALUE (WORKING SET) : 0.160 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.021 REMARK 3 FREE R VALUE TEST SET COUNT : 1817 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW : 2.26 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2523 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.45 REMARK 3 BIN R VALUE (WORKING SET) : 0.2030 REMARK 3 BIN FREE R VALUE SET COUNT : 140 REMARK 3 BIN FREE R VALUE : 0.2870 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 5295 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.16 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.64800 REMARK 3 B22 (A**2) : -1.06500 REMARK 3 B33 (A**2) : -1.58400 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): 0.236 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.212 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.365 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5018 ; 0.021 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4499 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6828 ; 1.841 ; 1.948 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10436 ; 0.895 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 633 ; 7.847 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 221 ;32.770 ;23.484 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 811 ;14.228 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;16.935 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 758 ; 0.110 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5647 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1048 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 947 ; 0.208 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4615 ; 0.195 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2413 ; 0.180 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3020 ; 0.089 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 386 ; 0.180 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.052 ; 0.200 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): 10 ; 0.164 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 35 ; 0.263 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.160 ; 0.200 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): 3947 ; 1.246 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1296 ; 0.264 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5036 ; 1.566 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2249 ; 2.409 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1791 ; 3.428 ; 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 : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 0 A 372 REMARK 3 ORIGIN FOR THE GROUP (A): 47.2950 -4.5410 55.0480 REMARK 3 T TENSOR REMARK 3 T11: -0.0157 T22: -0.0290 REMARK 3 T33: -0.0345 T12: 0.0174 REMARK 3 T13: 0.0022 T23: -0.0073 REMARK 3 L TENSOR REMARK 3 L11: 0.3379 L22: 0.4237 REMARK 3 L33: 0.2876 L12: -0.0703 REMARK 3 L13: 0.0034 L23: 0.0736 REMARK 3 S TENSOR REMARK 3 S11: -0.0063 S12: 0.0037 S13: 0.0000 REMARK 3 S21: 0.0416 S22: 0.0396 S23: -0.0143 REMARK 3 S31: 0.0847 S32: 0.0312 S33: -0.0332 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 422 A 631 REMARK 3 ORIGIN FOR THE GROUP (A): 20.8240 22.4640 36.1120 REMARK 3 T TENSOR REMARK 3 T11: -0.0403 T22: -0.0119 REMARK 3 T33: -0.0338 T12: -0.0185 REMARK 3 T13: 0.0067 T23: 0.0066 REMARK 3 L TENSOR REMARK 3 L11: 0.5539 L22: 0.7952 REMARK 3 L33: 0.3209 L12: -0.3607 REMARK 3 L13: 0.1697 L23: -0.2232 REMARK 3 S TENSOR REMARK 3 S11: 0.0364 S12: 0.0179 S13: 0.0319 REMARK 3 S21: -0.0861 S22: -0.0507 S23: -0.0132 REMARK 3 S31: 0.0347 S32: -0.0094 S33: 0.0144 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL PLUS MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS TLS PARAMETERS HAVE BEEN REFINED REMARK 4 REMARK 4 2FHR 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 RCSB035891. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-NOV-2003 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 : 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) : 0.979158 REMARK 200 MONOCHROMATOR : SI 311 CHANNEL-CUT REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC Q210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36222 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 72.170 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.8 REMARK 200 DATA REDUNDANCY : 2.500 REMARK 200 R MERGE (I) : 0.06700 REMARK 200 R SYM (I) : 0.06700 REMARK 200 FOR THE DATA SET : 9.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.34000 REMARK 200 R SYM FOR SHELL (I) : 0.34000 REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.51 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULFATE, SODIUM REMARK 280 CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 291K, PH 6.50 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 37.43650 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.37550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.50350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.37550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.43650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.50350 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 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 VAL A 401 REMARK 465 PRO A 402 REMARK 465 ALA A 403 REMARK 465 THR A 404 REMARK 465 PRO A 405 REMARK 465 PRO A 406 REMARK 465 SER A 407 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 GLN A 123 CG CD OE1 NE2 REMARK 470 ASN A 145 CG OD1 ND2 REMARK 470 LYS A 147 CG CD CE NZ 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 OH TYR A 343 C2 FSI 700 1.42 REMARK 500 OG SER A 427 OE2 GLU A 434 2.11 REMARK 500 O HOH 91 O HOH 335 2.18 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 PRO A 466 CB PRO A 466 CG -0.144 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 ARG A 251 CG - CD - NE ANGL. DEV. =-11.0 DEGREES REMARK 500 ASP A 511 N - CA - C ANGL. DEV. =-11.4 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 180 133.12 85.58 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLY A 409 GLY A 410 -143.03 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2A75 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF TRYPANOSOMA RANGELI SIALIDASE IN REMARK 900 COMPLEX WITH 2,3-DIFLUOROSIALIC ACID REMARK 900 RELATED ID: 2AGS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN IN COMPLEX WITH 2- REMARK 900 KETO-3- DEOXY-D-GLYCERO-D-GALACTO-2,3-DIFLUORO-NONONIC ACID REMARK 900 (2,3- DIFLUORO-KDN), A COVALENT LIGAND REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHORS INDICATE THAT THE SEQUENCE IN THE DATABASE IS REMARK 999 INCORRECT DBREF 2FHR A 1 638 GB 2894810 AAC95493 23 660 SEQADV 2FHR MET A -13 GB 2894810 INITIATING METHIONINE SEQADV 2FHR GLY A -12 GB 2894810 CLONING ARTIFACT SEQADV 2FHR GLY A -11 GB 2894810 CLONING ARTIFACT SEQADV 2FHR SER A -10 GB 2894810 CLONING ARTIFACT SEQADV 2FHR HIS A -9 GB 2894810 HIS TAG SEQADV 2FHR HIS A -8 GB 2894810 HIS TAG SEQADV 2FHR HIS A -7 GB 2894810 HIS TAG SEQADV 2FHR HIS A -6 GB 2894810 HIS TAG SEQADV 2FHR HIS A -5 GB 2894810 HIS TAG SEQADV 2FHR HIS A -4 GB 2894810 HIS TAG SEQADV 2FHR GLY A -3 GB 2894810 CLONING ARTIFACT SEQADV 2FHR MET A -2 GB 2894810 CLONING ARTIFACT SEQADV 2FHR ALA A -1 GB 2894810 CLONING ARTIFACT SEQADV 2FHR SER A 0 GB 2894810 CLONING ARTIFACT SEQADV 2FHR ILE A 50 GB 2894810 THR 72 SEE REMARK 999 SEQADV 2FHR ALA A 186 GB 2894810 GLY 208 SEE REMARK 999 SEQADV 2FHR LEU A 372 GB 2894810 PHE 394 SEE REMARK 999 SEQADV 2FHR VAL A 606 GB 2894810 ILE 628 SEE REMARK 999 SEQRES 1 A 652 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA SEQRES 2 A 652 SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS SEQRES 3 A 652 ARG LYS ASN SER THR VAL PRO PHE GLU GLU SER ASN GLY SEQRES 4 A 652 THR ILE ARG GLU ARG VAL VAL HIS SER PHE ARG ILE PRO SEQRES 5 A 652 THR ILE VAL ASN VAL ASP GLY VAL MET VAL ALA ILE ALA SEQRES 6 A 652 ASP ALA ARG TYR GLU THR SER PHE ASP ASN SER PHE ILE SEQRES 7 A 652 GLU THR ALA VAL LYS TYR SER VAL ASP ASP GLY ALA THR SEQRES 8 A 652 TRP ASN THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SEQRES 9 A 652 SER VAL SER ARG VAL MET ASP ALA THR VAL ILE VAL LYS SEQRES 10 A 652 GLY ASN LYS LEU TYR ILE LEU VAL GLY SER PHE ASN LYS SEQRES 11 A 652 THR ARG ASN SER TRP THR GLN HIS ARG ASP GLY SER ASP SEQRES 12 A 652 TRP GLU PRO LEU LEU VAL VAL GLY GLU VAL THR LYS SER SEQRES 13 A 652 ALA ALA ASN GLY LYS THR THR ALA THR ILE SER TRP GLY SEQRES 14 A 652 LYS PRO VAL SER LEU LYS PRO LEU PHE PRO ALA GLU PHE SEQRES 15 A 652 ASP GLY ILE LEU THR LYS GLU PHE ILE GLY GLY VAL GLY SEQRES 16 A 652 ALA ALA ILE VAL ALA SER ASN GLY ASN LEU VAL TYR PRO SEQRES 17 A 652 VAL GLN ILE ALA ASP MET GLY GLY ARG VAL PHE THR LYS SEQRES 18 A 652 ILE MET TYR SER GLU ASP ASP GLY ASN THR TRP LYS PHE SEQRES 19 A 652 ALA GLU GLY ARG SER LYS PHE GLY CYS SER GLU PRO ALA SEQRES 20 A 652 VAL LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN ASN ARG SEQRES 21 A 652 VAL ASP GLY ASN ARG ARG LEU VAL TYR GLU SER SER ASP SEQRES 22 A 652 MET GLY LYS THR TRP VAL GLU ALA LEU GLY THR LEU SER SEQRES 23 A 652 HIS VAL TRP THR ASN SER PRO THR SER ASN GLN GLN ASP SEQRES 24 A 652 CYS GLN SER SER PHE VAL ALA VAL THR ILE GLU GLY LYS SEQRES 25 A 652 ARG VAL MET LEU PHE THR HIS PRO LEU ASN LEU LYS GLY SEQRES 26 A 652 ARG TRP MET ARG ASP ARG LEU HIS LEU TRP MET THR ASP SEQRES 27 A 652 ASN GLN ARG ILE PHE ASP VAL GLY GLN ILE SER ILE GLY SEQRES 28 A 652 ASP GLU ASN SER GLY TYR SER SER VAL LEU TYR LYS ASP SEQRES 29 A 652 ASP LYS LEU TYR SER LEU HIS GLU ILE ASN THR ASN ASP SEQRES 30 A 652 VAL TYR SER LEU VAL PHE VAL ARG LEU ILE GLY GLU LEU SEQRES 31 A 652 GLN LEU MET LYS SER VAL VAL ARG THR TRP LYS GLU GLU SEQRES 32 A 652 ASP ASN HIS LEU ALA SER ILE CYS THR PRO VAL VAL PRO SEQRES 33 A 652 ALA THR PRO PRO SER LYS GLY GLY CYS GLY ALA ALA VAL SEQRES 34 A 652 PRO THR ALA GLY LEU VAL GLY PHE LEU SER HIS SER ALA SEQRES 35 A 652 ASN GLY SER VAL TRP GLU ASP VAL TYR ARG CYS VAL ASP SEQRES 36 A 652 ALA ASN VAL ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU SEQRES 37 A 652 LYS PHE ASN GLY VAL GLY GLY GLY ALA VAL TRP PRO VAL SEQRES 38 A 652 ALA ARG GLN GLY GLN THR ARG ARG TYR GLN PHE ALA ASN SEQRES 39 A 652 TYR ARG PHE THR LEU VAL ALA THR VAL THR ILE ASP GLU SEQRES 40 A 652 LEU PRO LYS GLY THR SER PRO LEU LEU GLY ALA GLY LEU SEQRES 41 A 652 GLU GLY PRO GLY ASP ALA LYS LEU LEU GLY LEU SER TYR SEQRES 42 A 652 ASP LYS ASN ARG GLN TRP ARG PRO LEU TYR GLY ALA ALA SEQRES 43 A 652 PRO ALA SER PRO THR GLY SER TRP GLU LEU HIS LYS LYS SEQRES 44 A 652 TYR HIS VAL VAL LEU THR MET ALA ASP ARG GLN GLY SER SEQRES 45 A 652 VAL TYR VAL ASP GLY GLN PRO LEU ALA GLY SER GLY ASN SEQRES 46 A 652 THR VAL VAL ARG GLY ALA THR LEU PRO ASP ILE SER HIS SEQRES 47 A 652 PHE TYR ILE GLY GLY PRO ARG SER LYS GLY ALA PRO THR SEQRES 48 A 652 ASP SER ARG VAL THR VAL THR ASN VAL VAL LEU TYR ASN SEQRES 49 A 652 ARG ARG LEU ASN SER SER GLU ILE ARG THR LEU PHE LEU SEQRES 50 A 652 SER GLN ASP MET ILE GLY THR ASP GLY GLY ALA GLY THR SEQRES 51 A 652 ALA ALA HET SO4 801 5 HET SO4 802 5 HET FSI 700 21 HET GOL 903 6 HETNAM SO4 SULFATE ION HETNAM FSI 5-(ACETYLAMINO)-2,6-ANHYDRO-3,5-DIDEOXY-3- HETNAM 2 FSI FLUORONONONIC ACID HETNAM GOL GLYCEROL HETSYN FSI 3-FLUOROSIALIC ACID FORMUL 2 SO4 2(O4 S 2-) FORMUL 4 FSI C11 H18 F N O8 FORMUL 5 GOL C3 H8 O3 FORMUL 6 HOH *388(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 LEU A 372 SER A 395 1 24 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 PHE A 369 N VAL A 8 SHEET 3 A 4 LYS A 352 THR A 361 -1 N SER A 355 O VAL A 370 SHEET 4 A 4 SER A 344 LYS A 349 -1 N LYS A 349 O LYS A 352 SHEET 1 B 2 THR A 17 GLU A 21 0 SHEET 2 B 2 ILE A 27 VAL A 31 -1 O ARG A 28 N 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 O VAL A 48 N VAL A 41 SHEET 3 C 4 ILE A 64 SER A 71 -1 O GLU A 65 N ALA A 53 SHEET 4 C 4 ASN A 79 ILE A 84 -1 O GLN A 81 N VAL A 68 SHEET 1 D 3 THR A 148 TRP A 154 0 SHEET 2 D 3 TRP A 130 ALA A 143 -1 N GLU A 138 O SER A 153 SHEET 3 D 3 VAL A 158 SER A 159 -1 O VAL A 158 N LEU A 134 SHEET 1 E 5 THR A 148 TRP A 154 0 SHEET 2 E 5 TRP A 130 ALA A 143 -1 N GLU A 138 O SER A 153 SHEET 3 E 5 LYS A 106 PHE A 114 -1 N SER A 113 O GLU A 131 SHEET 4 E 5 ARG A 94 LYS A 103 -1 N ILE A 101 O TYR A 108 SHEET 5 E 5 GLY A 181 ALA A 182 1 O GLY A 181 N VAL A 100 SHEET 1 F 4 GLU A 167 PHE A 168 0 SHEET 2 F 4 ILE A 171 GLY A 178 -1 O ILE A 171 N PHE A 168 SHEET 3 F 4 LEU A 191 ASP A 199 -1 O GLN A 196 N ILE A 177 SHEET 4 F 4 ILE A 184 VAL A 185 -1 N ILE A 184 O VAL A 192 SHEET 1 G 5 GLU A 167 PHE A 168 0 SHEET 2 G 5 ILE A 171 GLY A 178 -1 O ILE A 171 N PHE A 168 SHEET 3 G 5 LEU A 191 ASP A 199 -1 O GLN A 196 N ILE A 177 SHEET 4 G 5 VAL A 204 SER A 211 -1 O LYS A 207 N VAL A 195 SHEET 5 G 5 LYS A 219 PHE A 220 -1 O LYS A 219 N TYR A 210 SHEET 1 H 4 SER A 230 TRP A 237 0 SHEET 2 H 4 LYS A 240 ARG A 246 -1 O ASN A 244 N ALA A 233 SHEET 3 H 4 VAL A 254 SER A 257 -1 O SER A 257 N LEU A 241 SHEET 4 H 4 VAL A 265 GLU A 266 -1 O VAL A 265 N GLU A 256 SHEET 1 I 4 PHE A 290 ILE A 295 0 SHEET 2 I 4 LYS A 298 PRO A 306 -1 O VAL A 300 N VAL A 293 SHEET 3 I 4 LEU A 318 THR A 323 -1 O TRP A 321 N PHE A 303 SHEET 4 I 4 ILE A 328 GLN A 333 -1 O PHE A 329 N MET A 322 SHEET 1 J11 ALA A 447 VAL A 450 0 SHEET 2 J11 GLY A 453 PHE A 456 -1 O LYS A 455 N GLU A 448 SHEET 3 J11 VAL A 601 TYR A 609 -1 O VAL A 603 N LEU A 454 SHEET 4 J11 LEU A 420 ALA A 428 -1 N GLY A 422 O LEU A 608 SHEET 5 J11 VAL A 432 ASP A 435 -1 O GLU A 434 N SER A 427 SHEET 6 J11 ALA A 442 ALA A 445 -1 O ALA A 442 N TRP A 433 SHEET 7 J11 GLY A 462 PRO A 466 -1 O VAL A 464 N ASN A 443 SHEET 8 J11 ILE A 582 GLY A 588 -1 O PHE A 585 N TRP A 465 SHEET 9 J11 THR A 498 LEU A 506 -1 N LEU A 501 O GLY A 588 SHEET 10 J11 LYS A 513 ASP A 520 -1 O LEU A 515 N ALA A 504 SHEET 11 J11 TRP A 525 TYR A 529 -1 O ARG A 526 N SER A 518 SHEET 1 K 7 ALA A 447 VAL A 450 0 SHEET 2 K 7 GLY A 453 PHE A 456 -1 O LYS A 455 N GLU A 448 SHEET 3 K 7 VAL A 601 TYR A 609 -1 O VAL A 603 N LEU A 454 SHEET 4 K 7 PHE A 483 ILE A 491 -1 N THR A 488 O THR A 604 SHEET 5 K 7 TYR A 546 ALA A 553 -1 O LEU A 550 N LEU A 485 SHEET 6 K 7 GLN A 556 VAL A 561 -1 O GLN A 556 N ALA A 553 SHEET 7 K 7 GLN A 564 PRO A 565 -1 O GLN A 564 N VAL A 561 SSBOND 1 CYS A 397 CYS A 411 CRYST1 74.873 95.007 110.751 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 0.013360 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010530 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009030 0.00000