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PDBsum entry 1wcs

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Hydrolase PDB id
1wcs
Jmol
Contents
Protein chain
628 a.a.
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 ORGANISM_TAXID: 5698;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   6 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   2   24-FEB-09 1WCS    1       VERSN
REVDAT   1   15-DEC-04 1WCS    0
JRNL        AUTH   G.PARIS,L.RATIER,M.F.AMAYA,T.NGUYEN,P.M.ALZARI,
JRNL        AUTH 2 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                   ISSN 0022-2836
JRNL        PMID   15588836
JRNL        DOI    10.1016/J.JMB.2004.09.031
REMARK   2
REMARK   2 RESOLUTION.    2.8  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 : MAXIMUM LIKELIHOOD
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           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1227
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920
REMARK   3   BIN FREE R VALUE SET COUNT          : 63
REMARK   3   BIN FREE R VALUE                    : 0.4960
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4841
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          :
REMARK   3   SOLVENT ATOMS            : 0
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): 0.440
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.887
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.901
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.819
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4952 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6739 ; 1.429 ; 1.927
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   626 ; 6.790 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   216 ;34.578 ;23.472
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   788 ;18.871 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;21.241 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   755 ; 0.091 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3778 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2411 ; 0.227 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3242 ; 0.314 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   194 ; 0.170 ; 0.200
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):    28 ; 0.186 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.094 ; 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):  3184 ; 0.425 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5018 ; 0.749 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2038 ; 1.012 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1721 ; 1.573 ; 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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 3
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     1        A   376
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8577  29.4334  25.6154
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1983 T22:  -0.2637
REMARK   3      T33:  -0.2240 T12:   0.0724
REMARK   3      T13:  -0.0016 T23:  -0.0133
REMARK   3    L TENSOR
REMARK   3      L11:   3.0330 L22:   1.4189
REMARK   3      L33:   5.5635 L12:   0.0027
REMARK   3      L13:  -2.1114 L23:  -0.4390
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2128 S12:  -0.3400 S13:  -0.0803
REMARK   3      S21:   0.0310 S22:   0.1125 S23:  -0.0207
REMARK   3      S31:   0.5678 S32:   0.4184 S33:   0.1003
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   423        A   634
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3542   6.0773  58.2581
REMARK   3    T TENSOR
REMARK   3      T11:   0.4285 T22:   0.7440
REMARK   3      T33:   0.3301 T12:   0.3487
REMARK   3      T13:  -0.0601 T23:   0.1673
REMARK   3    L TENSOR
REMARK   3      L11:   1.5933 L22:   2.2314
REMARK   3      L33:   3.8441 L12:  -0.5604
REMARK   3      L13:   0.2600 L23:  -2.8508
REMARK   3    S TENSOR
REMARK   3      S11:   0.1570 S12:  -0.4670 S13:  -0.3314
REMARK   3      S21:   0.4192 S22:  -0.0678 S23:  -0.0896
REMARK   3      S31:   0.1871 S32:   0.3987 S33:  -0.0893
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   377        A   422
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2509  -0.5467  37.4015
REMARK   3    T TENSOR
REMARK   3      T11:   0.6919 T22:   0.4945
REMARK   3      T33:   0.4593 T12:   0.3801
REMARK   3      T13:  -0.0346 T23:   0.1423
REMARK   3    L TENSOR
REMARK   3      L11:   1.0598 L22:   3.9087
REMARK   3      L33:   0.7519 L12:  -0.9078
REMARK   3      L13:   0.5529 L23:   0.7310
REMARK   3    S TENSOR
REMARK   3      S11:   0.7006 S12:  -0.4176 S13:  -0.7246
REMARK   3      S21:   0.3045 S22:  -0.7514 S23:   0.2848
REMARK   3      S31:   0.8498 S32:   0.0748 S33:   0.0507
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : 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.
REMARK   4
REMARK   4 1WCS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-NOV-04.
REMARK 100 THE PDBE 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-03
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   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG-8000, 50MM SODIUM
REMARK 280  CACODYLATE, 100 MM AMMONIUM SULFATE, PH 6.5
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,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400  ENGINEERED RESIDUES CHAIN A, MET 118 VAL,
REMARK 400                               ALA 120 PRO,
REMARK 400                               SER 142 TYR,
REMARK 400                               GLY 271 TYR,
REMARK 400                               GLN 306 PRO
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           DISTANCE
REMARK 500   O    PHE A    62  -  OG   SER A    65              2.14
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 299   CD    GLU A 299   OE1     0.070
REMARK 500    GLU A 299   CD    GLU A 299   OE2     0.180
REMARK 500    GLU A 299   CG    GLU A 299   CD      0.263
REMARK 500    GLY A 300   C     GLY A 300   O       0.180
REMARK 500    LYS A 301   CE    LYS A 301   NZ      0.335
REMARK 500    GLY A 300   C     LYS A 301   N       0.239
REMARK 500    GLN A 329   CG    GLN A 329   CD      0.231
REMARK 500    ARG A 526   CZ    ARG A 526   NH1     0.097
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A 100   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES
REMARK 500    ASP A 132   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP A 216   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES
REMARK 500    ASP A 262   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP A 353   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ASP A 366   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A 526   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A   3     -159.62   -137.15
REMARK 500    ASN A  18      -51.88   -139.76
REMARK 500    SER A  26      -64.07    -10.52
REMARK 500    HIS A  36      -75.08    -58.81
REMARK 500    ASP A  63      -29.73    -37.19
REMARK 500    ASN A  64       73.31   -115.61
REMARK 500    LYS A 119      -30.83   -135.56
REMARK 500    ALA A 147     -134.08    -83.27
REMARK 500    ALA A 186     -151.49   -111.88
REMARK 500    ASN A 219      -76.40    -36.30
REMARK 500    GLU A 234       60.51     31.35
REMARK 500    THR A 273      -87.95   -143.56
REMARK 500    HIS A 276       -2.92     70.00
REMARK 500    SER A 284       11.86     58.41
REMARK 500    ASP A 288     -158.44    -88.14
REMARK 500    HIS A 308      131.18   -170.43
REMARK 500    ASN A 311       70.37     44.11
REMARK 500    ARG A 315     -129.77     57.14
REMARK 500    ARG A 320       80.14     54.91
REMARK 500    GLN A 329      -68.75   -142.12
REMARK 500    VAL A 403      102.24    -45.25
REMARK 500    PRO A 405       79.04    -68.62
REMARK 500    PHE A 426      112.95   -161.18
REMARK 500    SER A 428     -118.25   -110.07
REMARK 500    HIS A 429      -89.66    -73.01
REMARK 500    SER A 430       98.36    -18.18
REMARK 500    CYS A 442      -78.01    -90.30
REMARK 500    PRO A 454      101.54    -36.87
REMARK 500    VAL A 470      -62.38   -123.49
REMARK 500    ARG A 472       29.16    -71.63
REMARK 500    GLN A 475      -43.77    -19.14
REMARK 500    LEU A 504      -77.33   -139.35
REMARK 500    ASP A 514       56.60   -148.64
REMARK 500    HIS A 546        3.58     87.50
REMARK 500    ARG A 558      -12.34     67.76
REMARK 500    ASP A 584       62.69   -115.39
REMARK 500    HIS A 587     -159.85   -162.00
REMARK 500    SER A 595      -36.11   -145.12
REMARK 500    ARG A 603       78.66   -105.19
REMARK 500    ASN A 608       70.56     37.16
REMARK 500    ASN A 613       35.35    -90.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
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
REMARK 900   THE INHIBITORDANA
REMARK 900 RELATED ID: 1N1S   RELATED DB: PDB
REMARK 900  TRYPANOSOMA RANGELI SIALIDASE
REMARK 900 RELATED ID: 1N1T   RELATED DB: PDB
REMARK 900  TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH
REMARK 900   DANA AT 1.6 A
REMARK 900 RELATED ID: 1N1V   RELATED DB: PDB
REMARK 900  TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH
REMARK 900   DANA
REMARK 900 RELATED ID: 1N1Y   RELATED DB: PDB
REMARK 900  TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH
REMARK 900   SIALIC ACID
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS INDICATE THAT THE SEQUENCE IN THE SEQUENCE
REMARK 999 DATABASE (UNIPROT O44049) IS INCORRECT.
DBREF  1WCS A    1     1  PDB    1WCS     1WCS             1      1
DBREF  1WCS A    2     2  PDB    1WCS     1WCS             2      2
DBREF  1WCS A    3     3  PDB    1WCS     1WCS             3      3
DBREF  1WCS A    4   641  UNP    O44049   O44049          23    660
SEQADV 1WCS ILE A   53  UNP  O44049    THR    72 CONFLICT SEE REMARK 999
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 999
SEQADV 1WCS ALA A  189  UNP  O44049    ILE   208 CONFLICT SEE REMARK 999
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 999
SEQADV 1WCS ALA A  413  UNP  O44049    GLY   432 CONFLICT SEE REMARK 999
SEQADV 1WCS VAL A  609  UNP  O44049    ILE   628 CONFLICT SEE REMARK 999
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                          1555   1555  2.04
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
      
PROCHECK
Go to PROCHECK summary
 References