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PDBsum entry 2vw0

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Hydrolase PDB id
2vw0
Jmol
Contents
Protein chain
657 a.a.
Ligands
GOL ×2
Waters ×426
HEADER    HYDROLASE                               13-JUN-08   2VW0
TITLE     CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM STREPTOCOCCUS
TITLE    2 PNEUMONIAE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE B;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: NANB SIALIDASE, NEURAMINIDASE B;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE   3 ORGANISM_TAXID: 1313;
SOURCE   4 STRAIN: TIGR;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS    HYDROLASE, SIALIDASE, GLYCOSIDASE, DRUG DESIGN,
KEYWDS   2 NEURAMINIDASE, VIRULENCE FACTOR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.XU,J.A.POTTER,R.J.M.RUSSELL,M.R.OGGIONI,P.W.ANDREW,
AUTHOR   2 G.L.TAYLOR
REVDAT   3   24-FEB-09 2VW0    1       VERSN
REVDAT   2   18-NOV-08 2VW0    1       SOURCE JRNL   REMARK
REVDAT   1   24-JUN-08 2VW0    0
JRNL        AUTH   G.XU,J.A.POTTER,R.J.M.RUSSELL,M.R.OGGIONI,
JRNL        AUTH 2 P.W.ANDREW,G.L.TAYLOR
JRNL        TITL   CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
JRNL        TITL 2 STREPTOCOCCUS PNEUMONIAE
JRNL        REF    J.MOL.BIOL.                   V. 384   436 2008
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   18835278
JRNL        DOI    10.1016/J.JMB.2008.09.032
REMARK   2
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 32865
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) : 0.175
REMARK   3   R VALUE            (WORKING SET) : 0.172
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1733
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2340
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000
REMARK   3   BIN FREE R VALUE SET COUNT          : 112
REMARK   3   BIN FREE R VALUE                    : 0.2940
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5181
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 12
REMARK   3   SOLVENT ATOMS            : 426
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.67
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.91000
REMARK   3    B22 (A**2) : -1.51000
REMARK   3    B33 (A**2) : 3.42000
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): 0.298
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.226
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.964
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5300 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7164 ; 1.298 ; 1.950
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   656 ; 6.671 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   249 ;38.406 ;25.020
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   920 ;13.877 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;13.501 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   779 ; 0.085 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4016 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1861 ; 0.179 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3475 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   315 ; 0.172 ; 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):    10 ; 0.272 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.248 ; 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):  3384 ; 0.642 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5251 ; 1.088 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2248 ; 1.566 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1913 ; 2.431 ; 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  : NULL
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 2VW0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-08.
REMARK 100 THE PDBE ID CODE IS EBI-36563.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8
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
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34651
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.30
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 6.1
REMARK 200  R MERGE                    (I) : 0.11
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 6
REMARK 200  R MERGE FOR SHELL          (I) : 0.46
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.80
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 1SLI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 8000, 0.1M IMIDAZOLE PH
REMARK 280  8
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   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.68000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.07450
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.70850
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.07450
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.68000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.70850
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 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 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     1
REMARK 465     ASN A     2
REMARK 465     LYS A     3
REMARK 465     ARG A     4
REMARK 465     GLY A     5
REMARK 465     LEU A     6
REMARK 465     TYR A     7
REMARK 465     SER A     8
REMARK 465     LYS A     9
REMARK 465     LEU A    10
REMARK 465     GLY A    11
REMARK 465     ILE A    12
REMARK 465     SER A    13
REMARK 465     VAL A    14
REMARK 465     VAL A    15
REMARK 465     GLY A    16
REMARK 465     ILE A    17
REMARK 465     SER A    18
REMARK 465     LEU A    19
REMARK 465     LEU A    20
REMARK 465     MET A    21
REMARK 465     GLY A    22
REMARK 465     VAL A    23
REMARK 465     PRO A    24
REMARK 465     THR A    25
REMARK 465     LEU A    26
REMARK 465     ILE A    27
REMARK 465     HIS A    28
REMARK 465     ALA A    29
REMARK 465     ASN A    30
REMARK 465     GLU A    31
REMARK 465     LEU A    32
REMARK 465     ASN A    33
REMARK 465     TYR A    34
REMARK 465     GLY A    35
REMARK 465     GLN A    36
REMARK 465     LEU A    37
REMARK 465     SER A    38
REMARK 465     ILE A    39
REMARK 465     LYS A   697
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    HOH A  2030  -  O    HOH A  2087              2.17
REMARK 500   O    HOH A  2074  -  O    HOH A  2199              2.07
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  47       69.42     27.54
REMARK 500    LYS A  80       50.70   -141.64
REMARK 500    ASN A 212       51.91    -91.09
REMARK 500    SER A 226       59.44   -111.50
REMARK 500    ILE A 246       67.21     69.40
REMARK 500    SER A 273     -177.63    175.86
REMARK 500    ASP A 327       98.18     65.00
REMARK 500    LYS A 484       30.81    -99.79
REMARK 500    PRO A 534       39.61    -77.36
REMARK 500    THR A 558     -168.17   -128.52
REMARK 500    GLN A 592      136.62    -36.34
REMARK 500    ASP A 643       99.19    -68.79
REMARK 500    TYR A 651      116.84   -160.60
REMARK 500    ALA A 652     -122.60   -120.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1697
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1698
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VVZ   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE CATALYTIC DOMAIN OF
REMARK 900  STREPTOCOCCUS PNEUMONIAE SIALIDASE NANA
REMARK 900 RELATED ID: 2VW1   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
REMARK 900   STREPTOCOCCUS PNEUMONIAE
REMARK 900 RELATED ID: 2VW2   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
REMARK 900   STREPTOCOCCUS PNEUMONIAE
DBREF  2VW0 A    1   697  UNP    Q54727   NANB_STRPN       1    697
SEQRES   1 A  697  MET ASN LYS ARG GLY LEU TYR SER LYS LEU GLY ILE SER
SEQRES   2 A  697  VAL VAL GLY ILE SER LEU LEU MET GLY VAL PRO THR LEU
SEQRES   3 A  697  ILE HIS ALA ASN GLU LEU ASN TYR GLY GLN LEU SER ILE
SEQRES   4 A  697  SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU ASN ASN
SEQRES   5 A  697  LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP LYS LEU
SEQRES   6 A  697  SER GLY GLU SER GLN THR VAL VAL MET LYS PHE LYS ALA
SEQRES   7 A  697  ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY LEU SER
SEQRES   8 A  697  ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE SER ILE
SEQRES   9 A  697  PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU ILE ARG
SEQRES  10 A  697  ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER ARG PRO
SEQRES  11 A  697  ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA VAL GLU
SEQRES  12 A  697  ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP LYS THR
SEQRES  13 A  697  TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE SER GLU
SEQRES  14 A  697  THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE ASN GLY
SEQRES  15 A  697  ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG GLU GLY
SEQRES  16 A  697  LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP GLU ILE
SEQRES  17 A  697  SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU VAL SER
SEQRES  18 A  697  THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE PHE GLN
SEQRES  19 A  697  SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG ILE PRO
SEQRES  20 A  697  THR LEU TYR THR LEU SER SER GLY ARG VAL LEU SER SER
SEQRES  21 A  697  ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER LYS SER
SEQRES  22 A  697  LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP ASN GLY
SEQRES  23 A  697  LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS PHE ASN
SEQRES  24 A  697  ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG ASP ASN
SEQRES  25 A  697  LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA SER PHE
SEQRES  26 A  697  ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER GLY LYS
SEQRES  27 A  697  THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY ILE GLY
SEQRES  28 A  697  ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE LYS GLU
SEQRES  29 A  697  ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS ASN GLY
SEQRES  30 A  697  ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN GLY VAL
SEQRES  31 A  697  VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN TYR THR
SEQRES  32 A  697  ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY LYS SER
SEQRES  33 A  697  LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP SER GLY
SEQRES  34 A  697  SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL PRO MET
SEQRES  35 A  697  ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL THR PRO
SEQRES  36 A  697  THR ASN TYR ILE ALA MET THR THR SER GLN ASN ARG GLY
SEQRES  37 A  697  GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO PHE LEU
SEQRES  38 A  697  GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO GLY GLN
SEQRES  39 A  697  GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE PHE ALA
SEQRES  40 A  697  THR TYR THR SER GLY GLU LEU THR TYR LEU ILE SER ASP
SEQRES  41 A  697  ASP SER GLY GLN THR TRP LYS LYS SER SER ALA SER ILE
SEQRES  42 A  697  PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET VAL GLU
SEQRES  43 A  697  LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG THR THR
SEQRES  44 A  697  THR GLY LYS ILE ALA TYR MET THR SER ARG ASP SER GLY
SEQRES  45 A  697  GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY ILE GLN
SEQRES  46 A  697  GLN THR SER TYR GLY THR GLN VAL SER ALA ILE LYS TYR
SEQRES  47 A  697  SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE LEU SER
SEQRES  48 A  697  THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY GLN LEU
SEQRES  49 A  697  VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER ILE ASP
SEQRES  50 A  697  TRP LYS TYR HIS TYR ASP ILE ASP LEU PRO SER TYR GLY
SEQRES  51 A  697  TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN HIS HIS
SEQRES  52 A  697  ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP SER ARG
SEQRES  53 A  697  ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR ILE ASP
SEQRES  54 A  697  LEU GLU ILE ASN ASP LEU THR LYS
HET    GOL  A1697       6
HET    GOL  A1698       6
HETNAM     GOL GLYCEROL
FORMUL   2  GOL    2(C3 H8 O3)
FORMUL   3  HOH   *426(H2 O1)
HELIX    1   1 ILE A   57  LEU A   62  1                                   6
HELIX    2   2 ASP A   63  LEU A   65  5                                   3
HELIX    3   3 SER A  216  SER A  221  1                                   6
HELIX    4   4 GLU A  691  THR A  696  1                                   6
SHEET    1  AA 6 PHE A  43  ASN A  51  0
SHEET    2  AA 6 LYS A 202  PHE A 211 -1  O  GLY A 203   N  LEU A  50
SHEET    3  AA 6 GLN A  70  LYS A  77 -1  O  THR A  71   N  PHE A 211
SHEET    4  AA 6 ASN A 144  ASP A 151 -1  O  ASN A 144   N  PHE A  76
SHEET    5  AA 6 THR A 156  VAL A 161 -1  O  THR A 156   N  ASP A 151
SHEET    6  AA 6 ILE A 164  THR A 170 -1  O  ILE A 164   N  VAL A 161
SHEET    1  AB 6 ILE A  55  ASP A  56  0
SHEET    2  AB 6 LYS A 185  LEU A 188 -1  O  LEU A 188   N  ILE A  55
SHEET    3  AB 6 LEU A  84  SER A  91 -1  O  GLY A  89   N  THR A 187
SHEET    4  AB 6 TYR A 101  ARG A 107 -1  O  PHE A 102   N  LEU A  90
SHEET    5  AB 6 ILE A 112  ASP A 118 -1  O  GLY A 113   N  PHE A 105
SHEET    6  AB 6 ILE A 123  ARG A 129 -1  O  ILE A 123   N  ASP A 118
SHEET    1  AC 2 LYS A 136  HIS A 137  0
SHEET    2  AC 2 GLN A 140  ALA A 141 -1  O  GLN A 140   N  HIS A 137
SHEET    1  AD 2 VAL A 191  ARG A 193  0
SHEET    2  AD 2 LYS A 196  HIS A 198 -1  O  LYS A 196   N  ARG A 193
SHEET    1  AE 3 TYR A 243  ARG A 245  0
SHEET    2  AE 3 VAL A 257  ARG A 264 -1  O  ASP A 262   N  ARG A 245
SHEET    3  AE 3 TYR A 250  THR A 251 -1  O  TYR A 250   N  LEU A 258
SHEET    1  AF 4 TYR A 243  ARG A 245  0
SHEET    2  AF 4 VAL A 257  ARG A 264 -1  O  ASP A 262   N  ARG A 245
SHEET    3  AF 4 ILE A 275  SER A 282 -1  O  ASN A 276   N  ALA A 263
SHEET    4  AF 4 ILE A 293  MET A 296 -1  O  ILE A 293   N  THR A 279
SHEET    1  AG 5 LYS A 475  LEU A 476  0
SHEET    2  AG 5 TYR A 458  SER A 464 -1  O  MET A 461   N  LYS A 475
SHEET    3  AG 5 THR A 339  MET A 346 -1  O  THR A 339   N  SER A 464
SHEET    4  AG 5 SER A 324  GLU A 332 -1  O  SER A 324   N  MET A 346
SHEET    5  AG 5 GLY A 493  GLN A 494  1  O  GLY A 493   N  ILE A 330
SHEET    1  AH 7 PHE A 362  ILE A 365  0
SHEET    2  AH 7 HIS A 368  LYS A 375 -1  O  HIS A 368   N  ILE A 365
SHEET    3  AH 7 TYR A 383  VAL A 385 -1  O  TYR A 383   N  LEU A 373
SHEET    4  AH 7 VAL A 390  ASN A 393 -1  O  TYR A 392   N  THR A 384
SHEET    5  AH 7 LYS A 398  ILE A 404 -1  O  LYS A 398   N  ASN A 393
SHEET    6  AH 7 VAL A 410  GLU A 412 -1  O  LEU A 411   N  THR A 403
SHEET    7  AH 7 LYS A 415  SER A 416 -1  O  LYS A 415   N  GLU A 412
SHEET    1  AI 3 PHE A 362  ILE A 365  0
SHEET    2  AI 3 HIS A 368  LYS A 375 -1  O  HIS A 368   N  ILE A 365
SHEET    3  AI 3 PHE A 451  LYS A 452 -1  O  LYS A 452   N  LYS A 374
SHEET    1  AJ 2 THR A 418  ASP A 425  0
SHEET    2  AJ 2 ARG A 432  PRO A 441 -1  O  ARG A 432   N  ASP A 425
SHEET    1  AK 3 TYR A 489  LEU A 490  0
SHEET    2  AK 3 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489
SHEET    3  AK 3 LEU A 496  ALA A 497 -1  O  LEU A 496   N  ILE A 505
SHEET    1  AL 4 TYR A 489  LEU A 490  0
SHEET    2  AL 4 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489
SHEET    3  AL 4 GLU A 513  SER A 519 -1  O  GLU A 513   N  THR A 510
SHEET    4  AL 4 LYS A 527  SER A 532 -1  O  LYS A 527   N  ILE A 518
SHEET    1  AM 4 ALA A 542  ARG A 548  0
SHEET    2  AM 4 VAL A 551  PHE A 556 -1  O  VAL A 551   N  LEU A 547
SHEET    3  AM 4 ALA A 564  SER A 568 -1  O  ALA A 564   N  PHE A 556
SHEET    4  AM 4 SER A 579  TYR A 580 -1  O  SER A 579   N  TYR A 565
SHEET    1  AN 4 SER A 594  LYS A 597  0
SHEET    2  AN 4 ALA A 607  PRO A 613 -1  O  ILE A 609   N  ILE A 596
SHEET    3  AN 4 GLY A 622  VAL A 629 -1  O  GLN A 623   N  THR A 612
SHEET    4  AN 4 ILE A 636  ASP A 643 -1  O  ASP A 637   N  LEU A 628
SHEET    1  AO 3 SER A 654  GLU A 658  0
SHEET    2  AO 3 ILE A 664  GLU A 669 -1  O  GLY A 665   N  THR A 657
SHEET    3  AO 3 VAL A 685  LEU A 690 -1  O  GLN A 686   N  PHE A 668
CISPEP   1 SER A  271    LYS A  272          0         2.37
SITE     1 AC1  3 SER A 253  LYS A 315  HOH A2424
SITE     1 AC2  7 TYR A 250  THR A 251  GLN A 494  ILE A 596
SITE     2 AC2  7 THR A 657  HOH A2425  HOH A2426
CRYST1   77.360   83.417  120.149  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      0.012927  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011988  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008323        0.00000
      
PROCHECK
Go to PROCHECK summary
 References