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Database: PDB
Entry: 2XZJ
LinkDB: 2XZJ
Original site: 2XZJ 
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  <I/SIGMA(I)> 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  <I/SIGMA(I)> 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                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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