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PDBsum entry 2xzj

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2xzj
Jmol
Contents
Protein chains
386 a.a.
Ligands
GOL ×2
KFN ×2
Metals
_NA ×2
Waters ×1146
HEADER    HYDROLASE                               26-NOV-10   2XZJ
TITLE     THE ASPERGILLUS FUMIGATUS SIALIDASE IS A KDNASE: STRUCTURAL
TITLE    2 AND MECHANISTIC INSIGHTS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: EXTRACELLULAR SIALIDASE/NEURAMINIDASE, PUTATIVE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: RESIDUES 21-406;
COMPND   5 SYNONYM: KDNASE;
COMPND   6 EC: 3.2.1.18;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;
SOURCE   3 ORGANISM_TAXID: 330879;
SOURCE   4 STRAIN: AF293;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS    HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.C.TELFORD,J.H.F.YEUNG,M.J.KIEFEL,A.G.WATTS,S.HADER,J.CHAN,
AUTHOR   2 A.J.BENNET,M.M.MOORE,G.L.TAYLOR
REVDAT   3   17-AUG-11 2XZJ    1       JRNL   REMARK HETSYN VERSN
REVDAT   2   02-FEB-11 2XZJ    1       JRNL
REVDAT   1   19-JAN-11 2XZJ    0
JRNL        AUTH   J.C.TELFORD,J.H.YEUNG,G.XU,M.J.KIEFEL,A.G.WATTS,
JRNL        AUTH 2 S.HADER,J.CHAN,A.J.BENNET,M.M.MOORE,G.L.TAYLOR
JRNL        TITL   THE ASPERGILLUS FUMIGATUS SIALIDASE IS A KDNASE:
JRNL        TITL 2 STRUCTURAL AND MECHANISTIC INSIGHTS.
JRNL        REF    J.BIOL.CHEM.                  V. 286 10783 2011
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   21247893
JRNL        DOI    10.1074/JBC.M110.207043
REMARK   2
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.38
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.83
REMARK   3   NUMBER OF REFLECTIONS             : 65781
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) : 0.20361
REMARK   3   R VALUE            (WORKING SET) : 0.20053
REMARK   3   FREE R VALUE                     : 0.26214
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 3469
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) : 1.841
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.888
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4346
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.33
REMARK   3   BIN R VALUE           (WORKING SET) : 0.238
REMARK   3   BIN FREE R VALUE SET COUNT          : 231
REMARK   3   BIN FREE R VALUE                    : 0.316
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5935
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 48
REMARK   3   SOLVENT ATOMS            : 1146
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.133
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.38
REMARK   3    B22 (A**2) : 0.24
REMARK   3    B33 (A**2) : -0.59
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.08
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.165
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.162
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.103
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.244
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.902
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.847
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6127 ; 0.011 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8318 ; 1.325 ; 1.948
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   772 ; 6.505 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   286 ;29.860 ;22.867
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   942 ;12.967 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;16.033 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   873 ; 0.086 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4802 ; 0.007 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  3808 ; 0.553 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6095 ; 0.919 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2319 ; 1.607 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2221 ; 2.331 ; 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   : 1.40
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 2XZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-10.
REMARK 100 THE PDBE ID CODE IS EBI-46412.
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                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70073
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.84
REMARK 200  RESOLUTION RANGE LOW       (A) : 12.40
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 3.1
REMARK 200  R MERGE                    (I) : 0.09
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.8
REMARK 200  R MERGE FOR SHELL          (I) : 0.15
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 2XCY
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.03500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 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 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: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ILE B    21
REMARK 465     ASN B    22
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    ASN A   406     O    HOH A  2625              2.08
REMARK 500   O    HOH A  2623     O    HOH A  2624              1.66
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    LEU A  90   CA  -  CB  -  CG  ANGL. DEV. = -16.4 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
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    ILE A  60       67.97     61.02
REMARK 500    ALA A 201      -87.09   -114.99
REMARK 500    ASN A 235       45.30   -145.64
REMARK 500    ALA A 295       67.60     65.48
REMARK 500    ILE B  60       66.12     66.39
REMARK 500    ALA B 201      -87.15   -118.02
REMARK 500    THR B 320      -36.94   -134.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA A 500  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 116   O
REMARK 620 2 GLY A 118   O    87.2
REMARK 620 3 HOH A2282   O    94.8  88.5
REMARK 620 4 ASN A  89   OD1  84.8 159.0  72.8
REMARK 620 5 ASP A  87   OD1 174.0  95.8  80.1  90.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B 500  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 116   O
REMARK 620 2 GLY B 118   O    83.8
REMARK 620 3 HOH B2196   O    90.1  82.8
REMARK 620 4 ASP B  87   OD1 167.3  90.6  77.8
REMARK 620 5 ASN B  89   OD1  89.3 151.6  69.7  90.3
REMARK 620 6 HOH B2144   O   107.7 122.1 150.0  84.9  86.2
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KFN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KFN B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XCY   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS
REMARK 900  SIALIDASE
REMARK 900 RELATED ID: 2XZI   RELATED DB: PDB
REMARK 900  THE ASPERGILLUS FUMIGATUS SIALIDASE IS A
REMARK 900  KDNASE: STRUCTURAL AND MECHANISTIC INSIGHTS
REMARK 900 RELATED ID: 2XZK   RELATED DB: PDB
REMARK 900  THE ASPERGILLUS FUMIGATUS SIALIDASE IS A
REMARK 900  KDNASE: STRUCTURAL AND MECHANISTIC INSIGHTS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CRYSTALLIZED PROTEIN LACKS FIRST 20 AMINO ACIDS (SIGNAL
REMARK 999 SEQUENCE)
DBREF  2XZJ A   21   406  UNP    Q4WQS0   Q4WQS0_ASPFU    21    406
DBREF  2XZJ B   21   406  UNP    Q4WQS0   Q4WQS0_ASPFU    21    406
SEQRES   1 A  386  ILE ASN ASP PRO ALA LYS SER ALA ALA PRO TYR HIS ASP
SEQRES   2 A  386  GLU PHE PRO LEU PHE ARG SER ALA ASN MET ALA SER PRO
SEQRES   3 A  386  ASP LYS LEU SER THR GLY ILE GLY PHE HIS SER PHE ARG
SEQRES   4 A  386  ILE PRO ALA VAL VAL ARG THR THR THR GLY ARG ILE LEU
SEQRES   5 A  386  ALA PHE ALA GLU GLY ARG ARG HIS THR ASN GLN ASP PHE
SEQRES   6 A  386  GLY ASP ILE ASN LEU VAL TYR LYS ARG THR LYS THR THR
SEQRES   7 A  386  ALA ASN ASN GLY ALA SER PRO SER ASP TRP GLU PRO LEU
SEQRES   8 A  386  ARG GLU VAL VAL GLY SER GLY ALA GLY THR TRP GLY ASN
SEQRES   9 A  386  PRO THR PRO VAL VAL ASP ASP ASP ASN THR ILE TYR LEU
SEQRES  10 A  386  PHE LEU SER TRP ASN GLY ALA THR TYR SER GLN ASN GLY
SEQRES  11 A  386  LYS ASP VAL LEU PRO ASP GLY THR VAL THR LYS LYS ILE
SEQRES  12 A  386  ASP SER THR TRP GLU GLY ARG ARG HIS LEU TYR LEU THR
SEQRES  13 A  386  GLU SER ARG ASP ASP GLY ASN THR TRP SER LYS PRO VAL
SEQRES  14 A  386  ASP LEU THR LYS GLU LEU THR PRO ASP GLY TRP ALA TRP
SEQRES  15 A  386  ASP ALA VAL GLY PRO GLY ASN GLY ILE ARG LEU THR THR
SEQRES  16 A  386  GLY GLU LEU VAL ILE PRO ALA MET GLY ARG ASN ILE ILE
SEQRES  17 A  386  GLY ARG GLY ALA PRO GLY ASN ARG THR TRP SER VAL GLN
SEQRES  18 A  386  ARG LEU SER GLY ALA GLY ALA GLU GLY THR ILE VAL GLN
SEQRES  19 A  386  THR PRO ASP GLY LYS LEU TYR ARG ASN ASP ARG PRO SER
SEQRES  20 A  386  GLN LYS GLY TYR ARG MET VAL ALA ARG GLY THR LEU GLU
SEQRES  21 A  386  GLY PHE GLY ALA PHE ALA PRO ASP ALA GLY LEU PRO ASP
SEQRES  22 A  386  PRO ALA CYS GLN GLY SER VAL LEU ARG TYR ASN SER ASP
SEQRES  23 A  386  ALA PRO ALA ARG THR ILE PHE LEU ASN SER ALA SER GLY
SEQRES  24 A  386  THR SER ARG ARG ALA MET ARG VAL ARG ILE SER TYR ASP
SEQRES  25 A  386  ALA ASP ALA LYS LYS PHE ASN TYR GLY ARG LYS LEU GLU
SEQRES  26 A  386  ASP ALA LYS VAL SER GLY ALA GLY HIS GLU GLY GLY TYR
SEQRES  27 A  386  SER SER MET THR LYS THR GLY ASP TYR LYS ILE GLY ALA
SEQRES  28 A  386  LEU VAL GLU SER ASP PHE PHE ASN ASP GLY THR GLY LYS
SEQRES  29 A  386  ASN SER TYR ARG ALA ILE ILE TRP ARG ARG PHE ASN LEU
SEQRES  30 A  386  SER TRP ILE LEU ASN GLY PRO ASN ASN
SEQRES   1 B  386  ILE ASN ASP PRO ALA LYS SER ALA ALA PRO TYR HIS ASP
SEQRES   2 B  386  GLU PHE PRO LEU PHE ARG SER ALA ASN MET ALA SER PRO
SEQRES   3 B  386  ASP LYS LEU SER THR GLY ILE GLY PHE HIS SER PHE ARG
SEQRES   4 B  386  ILE PRO ALA VAL VAL ARG THR THR THR GLY ARG ILE LEU
SEQRES   5 B  386  ALA PHE ALA GLU GLY ARG ARG HIS THR ASN GLN ASP PHE
SEQRES   6 B  386  GLY ASP ILE ASN LEU VAL TYR LYS ARG THR LYS THR THR
SEQRES   7 B  386  ALA ASN ASN GLY ALA SER PRO SER ASP TRP GLU PRO LEU
SEQRES   8 B  386  ARG GLU VAL VAL GLY SER GLY ALA GLY THR TRP GLY ASN
SEQRES   9 B  386  PRO THR PRO VAL VAL ASP ASP ASP ASN THR ILE TYR LEU
SEQRES  10 B  386  PHE LEU SER TRP ASN GLY ALA THR TYR SER GLN ASN GLY
SEQRES  11 B  386  LYS ASP VAL LEU PRO ASP GLY THR VAL THR LYS LYS ILE
SEQRES  12 B  386  ASP SER THR TRP GLU GLY ARG ARG HIS LEU TYR LEU THR
SEQRES  13 B  386  GLU SER ARG ASP ASP GLY ASN THR TRP SER LYS PRO VAL
SEQRES  14 B  386  ASP LEU THR LYS GLU LEU THR PRO ASP GLY TRP ALA TRP
SEQRES  15 B  386  ASP ALA VAL GLY PRO GLY ASN GLY ILE ARG LEU THR THR
SEQRES  16 B  386  GLY GLU LEU VAL ILE PRO ALA MET GLY ARG ASN ILE ILE
SEQRES  17 B  386  GLY ARG GLY ALA PRO GLY ASN ARG THR TRP SER VAL GLN
SEQRES  18 B  386  ARG LEU SER GLY ALA GLY ALA GLU GLY THR ILE VAL GLN
SEQRES  19 B  386  THR PRO ASP GLY LYS LEU TYR ARG ASN ASP ARG PRO SER
SEQRES  20 B  386  GLN LYS GLY TYR ARG MET VAL ALA ARG GLY THR LEU GLU
SEQRES  21 B  386  GLY PHE GLY ALA PHE ALA PRO ASP ALA GLY LEU PRO ASP
SEQRES  22 B  386  PRO ALA CYS GLN GLY SER VAL LEU ARG TYR ASN SER ASP
SEQRES  23 B  386  ALA PRO ALA ARG THR ILE PHE LEU ASN SER ALA SER GLY
SEQRES  24 B  386  THR SER ARG ARG ALA MET ARG VAL ARG ILE SER TYR ASP
SEQRES  25 B  386  ALA ASP ALA LYS LYS PHE ASN TYR GLY ARG LYS LEU GLU
SEQRES  26 B  386  ASP ALA LYS VAL SER GLY ALA GLY HIS GLU GLY GLY TYR
SEQRES  27 B  386  SER SER MET THR LYS THR GLY ASP TYR LYS ILE GLY ALA
SEQRES  28 B  386  LEU VAL GLU SER ASP PHE PHE ASN ASP GLY THR GLY LYS
SEQRES  29 B  386  ASN SER TYR ARG ALA ILE ILE TRP ARG ARG PHE ASN LEU
SEQRES  30 B  386  SER TRP ILE LEU ASN GLY PRO ASN ASN
HET     NA  A 500       1
HET    GOL  A 501       6
HET    KFN  A 503      17
HET     NA  B 500       1
HET    GOL  B 501       6
HET    KFN  B 503      17
HETNAM      NA SODIUM ION
HETNAM     GOL GLYCEROL
HETNAM     KFN (4S,5R,6R)-4,5-DIHYDROXY-6-[(1R,2R)-1,2,3-
HETNAM   2 KFN  TRIHYDROXYPROPYL]-5,6-DIHYDRO-4H-PYRAN-2-
HETNAM   3 KFN  CARBOXYLIC ACID
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3   NA    2(NA 1+)
FORMUL   4  GOL    2(C3 H8 O3)
FORMUL   5  KFN    2(C9 H14 O8)
FORMUL   6  HOH   *1146(H2 O)
HELIX    1   1 ASP A   23  ALA A   28  5                                   6
HELIX    2   2 SER A  104  ASP A  107  5                                   4
HELIX    3   3 LEU A  191  THR A  196  1                                   6
HELIX    4   4 GLU A  345  LYS A  348  5                                   4
HELIX    5   5 ASN A  396  ASN A  402  1                                   7
HELIX    6   6 ASP B   23  ALA B   28  5                                   6
HELIX    7   7 SER B  104  ASP B  107  5                                   4
HELIX    8   8 LEU B  191  THR B  196  1                                   6
HELIX    9   9 GLU B  345  LYS B  348  5                                   4
HELIX   10  10 ASN B  396  ASN B  402  1                                   7
SHEET    1  AA 4 HIS A  32  PHE A  38  0
SHEET    2  AA 4 ARG A 388  PHE A 395 -1  O  ILE A 390   N  LEU A  37
SHEET    3  AA 4 ILE A 369  ASP A 376 -1  O  ILE A 369   N  PHE A 395
SHEET    4  AA 4 HIS A 354  LYS A 363 -1  O  HIS A 354   N  ASP A 376
SHEET    1  AB 4 SER A  57  ARG A  65  0
SHEET    2  AB 4 ILE A  71  ARG A  78 -1  O  LEU A  72   N  VAL A  64
SHEET    3  AB 4 ILE A  88  ARG A  94 -1  O  ASN A  89   N  GLY A  77
SHEET    4  AB 4 ARG A 112  VAL A 115 -1  O  ARG A 112   N  TYR A  92
SHEET    1  AC 4 THR A 121  VAL A 129  0
SHEET    2  AC 4 ILE A 135  ASN A 142 -1  O  TYR A 136   N  VAL A 128
SHEET    3  AC 4 HIS A 172  SER A 178 -1  O  HIS A 172   N  TRP A 141
SHEET    4  AC 4 VAL A 189  ASP A 190 -1  O  VAL A 189   N  LEU A 175
SHEET    1  AD 2 TYR A 146  SER A 147  0
SHEET    2  AD 2 LYS A 161  LYS A 162  1  O  LYS A 161   N  SER A 147
SHEET    1  AE 4 ILE A 211  ARG A 212  0
SHEET    2  AE 4 LEU A 218  ALA A 222 -1  O  VAL A 219   N  ILE A 211
SHEET    3  AE 4 ARG A 225  ARG A 230 -1  O  ARG A 225   N  ALA A 222
SHEET    4  AE 4 THR A 237  ARG A 242 -1  O  THR A 237   N  ARG A 230
SHEET    1  AF 4 ILE A 252  GLN A 254  0
SHEET    2  AF 4 LEU A 260  ASP A 264 -1  O  TYR A 261   N  VAL A 253
SHEET    3  AF 4 GLY A 270  THR A 278 -1  O  MET A 273   N  ASP A 264
SHEET    4  AF 4 GLY A 281  PHE A 282  1  O  GLY A 281   N  THR A 278
SHEET    1  AG 4 ILE A 252  GLN A 254  0
SHEET    2  AG 4 LEU A 260  ASP A 264 -1  O  TYR A 261   N  VAL A 253
SHEET    3  AG 4 GLY A 270  THR A 278 -1  O  MET A 273   N  ASP A 264
SHEET    4  AG 4 ALA A 286  ASP A 293 -1  O  ALA A 286   N  VAL A 274
SHEET    1  AH 2 GLY A 281  PHE A 282  0
SHEET    2  AH 2 GLY A 270  THR A 278  1  O  THR A 278   N  GLY A 281
SHEET    1  AI 4 SER A 299  ASN A 304  0
SHEET    2  AI 4 ARG A 310  SER A 316 -1  O  ARG A 310   N  TYR A 303
SHEET    3  AI 4 MET A 325  SER A 330 -1  O  ARG A 326   N  ASN A 315
SHEET    4  AI 4 ARG A 342  LYS A 343 -1  O  ARG A 342   N  VAL A 327
SHEET    1  BA 4 HIS B  32  PHE B  38  0
SHEET    2  BA 4 ARG B 388  PHE B 395 -1  O  ILE B 390   N  LEU B  37
SHEET    3  BA 4 ILE B 369  ASP B 376 -1  O  ILE B 369   N  PHE B 395
SHEET    4  BA 4 HIS B 354  LYS B 363 -1  O  HIS B 354   N  ASP B 376
SHEET    1  BB 4 SER B  57  ARG B  65  0
SHEET    2  BB 4 ILE B  71  ARG B  78 -1  O  LEU B  72   N  VAL B  64
SHEET    3  BB 4 ILE B  88  ARG B  94 -1  O  ASN B  89   N  GLY B  77
SHEET    4  BB 4 ARG B 112  VAL B 115 -1  O  ARG B 112   N  TYR B  92
SHEET    1  BC 4 THR B 121  VAL B 129  0
SHEET    2  BC 4 ILE B 135  ASN B 142 -1  O  TYR B 136   N  VAL B 128
SHEET    3  BC 4 HIS B 172  SER B 178 -1  O  HIS B 172   N  TRP B 141
SHEET    4  BC 4 VAL B 189  ASP B 190 -1  O  VAL B 189   N  LEU B 175
SHEET    1  BD 2 TYR B 146  SER B 147  0
SHEET    2  BD 2 LYS B 161  LYS B 162  1  O  LYS B 161   N  SER B 147
SHEET    1  BE 4 ILE B 211  ARG B 212  0
SHEET    2  BE 4 LEU B 218  ALA B 222 -1  O  VAL B 219   N  ILE B 211
SHEET    3  BE 4 ARG B 225  ARG B 230 -1  O  ARG B 225   N  ALA B 222
SHEET    4  BE 4 THR B 237  ARG B 242 -1  O  THR B 237   N  ARG B 230
SHEET    1  BF 4 GLY B 250  GLN B 254  0
SHEET    2  BF 4 LEU B 260  ASP B 264 -1  O  TYR B 261   N  VAL B 253
SHEET    3  BF 4 GLY B 270  THR B 278 -1  O  MET B 273   N  ASP B 264
SHEET    4  BF 4 GLY B 281  PHE B 282  1  O  GLY B 281   N  THR B 278
SHEET    1  BG 4 GLY B 250  GLN B 254  0
SHEET    2  BG 4 LEU B 260  ASP B 264 -1  O  TYR B 261   N  VAL B 253
SHEET    3  BG 4 GLY B 270  THR B 278 -1  O  MET B 273   N  ASP B 264
SHEET    4  BG 4 ALA B 286  ASP B 293 -1  O  ALA B 286   N  VAL B 274
SHEET    1  BH 2 GLY B 281  PHE B 282  0
SHEET    2  BH 2 GLY B 270  THR B 278  1  O  THR B 278   N  GLY B 281
SHEET    1  BI 4 SER B 299  ASN B 304  0
SHEET    2  BI 4 ARG B 310  SER B 316 -1  O  ARG B 310   N  TYR B 303
SHEET    3  BI 4 MET B 325  SER B 330 -1  O  ARG B 326   N  ASN B 315
SHEET    4  BI 4 ARG B 342  LYS B 343 -1  O  ARG B 342   N  VAL B 327
LINK        NA    NA A 500                 O   GLY A 116     1555   1555  2.35
LINK        NA    NA A 500                 O   GLY A 118     1555   1555  2.41
LINK        NA    NA A 500                 O   HOH A2282     1555   1555  2.36
LINK        NA    NA A 500                 OD1 ASN A  89     1555   1555  2.45
LINK        NA    NA A 500                 OD1 ASP A  87     1555   1555  2.26
LINK        NA    NA B 500                 O   GLY B 118     1555   1555  2.41
LINK        NA    NA B 500                 O   HOH B2196     1555   1555  2.37
LINK        NA    NA B 500                 OD1 ASP B  87     1555   1555  2.30
LINK        NA    NA B 500                 OD1 ASN B  89     1555   1555  2.37
LINK        NA    NA B 500                 O   HOH B2144     1555   1555  2.56
LINK        NA    NA B 500                 O   GLY B 116     1555   1555  2.29
CISPEP   1 GLY A  206    PRO A  207          0         7.10
CISPEP   2 ALA A  307    PRO A  308          0        -6.21
CISPEP   3 GLY B  206    PRO B  207          0         4.00
CISPEP   4 ALA B  307    PRO B  308          0        -6.58
SITE     1 AC1  5 ASP A  87  ASN A  89  GLY A 116  GLY A 118
SITE     2 AC1  5 HOH A2282
SITE     1 AC2  5 HOH A2628  ASP B 132  ASN B 133  ARG B 179
SITE     2 AC2  5 HOH B2215
SITE     1 AC3 16 ARG A  59  ARG A  78  ASP A  84  GLN A 148
SITE     2 AC3 16 TRP A 202  GLU A 249  ARG A 265  ARG A 322
SITE     3 AC3 16 TYR A 358  HOH A2154  HOH A2456  HOH A2629
SITE     4 AC3 16 HOH A2630  HOH A2631  HOH A2633  HOH A2634
SITE     1 AC4  6 ASP B  87  ASN B  89  GLY B 116  GLY B 118
SITE     2 AC4  6 HOH B2144  HOH B2196
SITE     1 AC5 10 LYS B 348  SER B 350  GLY B 351  ALA B 352
SITE     2 AC5 10 GLY B 353  HIS B 354  HOH B2481  HOH B2504
SITE     3 AC5 10 HOH B2505  HOH B2506
SITE     1 AC6 16 ARG B  59  ARG B  78  ASP B  84  GLN B 148
SITE     2 AC6 16 TRP B 202  GLU B 249  ARG B 265  ARG B 322
SITE     3 AC6 16 TYR B 358  HOH B2356  HOH B2507  HOH B2508
SITE     4 AC6 16 HOH B2509  HOH B2510  HOH B2511  HOH B2512
CRYST1   75.800   58.070   94.400  90.00  99.92  90.00 P 1 21 1      4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013193  0.000000  0.002307        0.00000
SCALE2      0.000000  0.017221  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010754        0.00000
      
PROCHECK
Go to PROCHECK summary
 References