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Database: PDB
Entry: 2XZI
LinkDB: 2XZI
Original site: 2XZI 
HEADER    HYDROLASE                               26-NOV-10   2XZI              
TITLE     THE ASPERGILLUS FUMIGATUS SIALIDASE IS A KDNASE:                      
TITLE    2 STRUCTURAL 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 2XZI    1       JRNL   REMARK HETSYN VERSN               
REVDAT   2   02-FEB-11 2XZI    1       JRNL                                     
REVDAT   1   19-JAN-11 2XZI    0                                                
JRNL        AUTH   J.C.TELFORD,J.H.F.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.    1.45 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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.33                          
REMARK   3   NUMBER OF REFLECTIONS             : 135232                         
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) : 0.18045                         
REMARK   3   R VALUE            (WORKING SET) : 0.17917                         
REMARK   3   FREE R VALUE                     : 0.20459                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 7087                            
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) : 1.451                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.489                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9541                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.255                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 479                          
REMARK   3   BIN FREE R VALUE                    : 0.277                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6021                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 107                                     
REMARK   3   SOLVENT ATOMS            : 1155                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.220                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03                                                
REMARK   3    B22 (A**2) : 0.27                                                 
REMARK   3    B33 (A**2) : -0.28                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.09                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.069         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.070         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.044         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.093         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6287 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8567 ; 1.286 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   809 ; 6.551 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   298 ;30.431 ;23.087       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   969 ;12.088 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    61 ;15.328 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   906 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4925 ; 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):  3861 ; 0.615 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6199 ; 1.046 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2426 ; 1.624 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2347 ; 2.495 ; 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 2XZI 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-46409.                                       
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        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
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   : 143277                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.45                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.30                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.40                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.24                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
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       28.99500            
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 A    21                                                      
REMARK 465     ILE B    21                                                      
REMARK 465     ASN B    22                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A 406    CB   CG   OD1  ND2                                  
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 B  2158     O    HOH B  2364              2.08            
REMARK 500   O    ASN A   379     O    HOH A  2543              2.11            
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       64.56     65.95                                   
REMARK 500    ALA A 201      -85.18   -112.05                                   
REMARK 500    ASN A 235       47.32   -141.27                                   
REMARK 500    ALA A 295       69.96     65.36                                   
REMARK 500    THR A 320      -31.17   -130.27                                   
REMARK 500    ILE B  60       62.84     68.49                                   
REMARK 500    ASN B 101       18.78     59.17                                   
REMARK 500    ALA B 201      -84.95   -110.91                                   
REMARK 500    ALA B 295       70.08     64.55                                   
REMARK 500    THR B 320      -34.40   -130.91                                   
REMARK 500    ARG B 323       34.74    -99.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDM B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 505                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2XZJ   RELATED DB: PDB                                   
REMARK 900  THE ASPERGILLUS FUMIGATUS SIALIDASE IS A                            
REMARK 900  KDNASE: STRUCTURAL AND MECHANISTIC INSIGHTS                         
REMARK 900 RELATED ID: 2XCY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS                          
REMARK 900  SIALIDASE                                                           
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  2XZI A   21   406  UNP    Q4WQS0   Q4WQS0_ASPFU    21    406             
DBREF  2XZI 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    KDM  A 500      18                                                       
HET    KDM  A 501      18                                                       
HET     NA  A 502       1                                                       
HET    GOL  A 503       6                                                       
HET    GOL  A 504       6                                                       
HET    NO2  A 505       3                                                       
HET    KDM  B 500      18                                                       
HET    KDM  B 501      18                                                       
HET     NA  B 502       1                                                       
HET    GOL  B 503       6                                                       
HET    GOL  B 504       6                                                       
HET    GOL  B 505       6                                                       
HETNAM     KDM (2R,4S,5R,6R)-2,4,5-TRIHYDROXY-6-[(1R,2R)-1,                     
HETNAM   2 KDM  2,3-TRIHYDROXYPROPYL]OXANE-2-CARBOXYLIC-ACID                    
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     NO2 NITRITE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  KDM    4(C9 H16 O9)                                                 
FORMUL   4   NA    2(NA 1+)                                                     
FORMUL   5  GOL    5(C3 H8 O3)                                                  
FORMUL   6  NO2    N O2 1-                                                      
FORMUL   7  HOH   *1155(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 GLY A 250  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 GLY A 250  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           
CISPEP   1 GLY A  206    PRO A  207          0         4.76                     
CISPEP   2 ALA A  307    PRO A  308          0        -6.91                     
CISPEP   3 GLY B  206    PRO B  207          0         8.80                     
CISPEP   4 ALA B  307    PRO B  308          0        -9.37                     
SITE     1 AC1 17 ARG A  59  ARG A  78  ASP A  84  GLN A 148                    
SITE     2 AC1 17 TRP A 202  GLU A 249  ARG A 265  ARG A 322                    
SITE     3 AC1 17 TYR A 358  HOH A2130  HOH A2396  HOH A2572                    
SITE     4 AC1 17 HOH A2573  HOH A2574  HOH A2576  HOH A2577                    
SITE     5 AC1 17 HOH A2581                                                     
SITE     1 AC2 13 SER A 321  ARG A 322  ARG A 323  ASP A 376                    
SITE     2 AC2 13 ARG A 388  HOH A2526  HOH A2539  HOH A2579                    
SITE     3 AC2 13 HOH A2580  HOH A2581  HOH A2582  HOH A2583                    
SITE     4 AC2 13 HOH A2584                                                     
SITE     1 AC3  6 ASP A  87  ASN A  89  GLY A 116  GLY A 118                    
SITE     2 AC3  6 HOH A2168  HOH A2237                                          
SITE     1 AC4  8 LEU A 213  THR A 215  GLY A 258  LYS A 259                    
SITE     2 AC4  8 THR A 278  LEU A 279  HOH A2585  HOH A2586                    
SITE     1 AC5  8 ASP A 132  ASN A 133  THR A 134  ARG A 179                    
SITE     2 AC5  8 HOH A2253  HOH A2587  HOH A2588  HOH A2589                    
SITE     1 AC6  4 ARG A 230  SER A 239  LEU A 279  HOH A2591                    
SITE     1 AC7 15 ARG B  59  ARG B  78  ASP B  84  GLN B 148                    
SITE     2 AC7 15 TRP B 202  GLU B 249  ARG B 265  ARG B 322                    
SITE     3 AC7 15 TYR B 358  GOL B 505  HOH B2373  HOH B2550                    
SITE     4 AC7 15 HOH B2551  HOH B2552  HOH B2553                               
SITE     1 AC8 11 SER B 321  ARG B 322  ARG B 323  ASP B 376                    
SITE     2 AC8 11 ARG B 388  HOH B2523  HOH B2535  HOH B2555                    
SITE     3 AC8 11 HOH B2556  HOH B2557  HOH B2558                               
SITE     1 AC9  6 ASP B  87  ASN B  89  GLY B 116  GLY B 118                    
SITE     2 AC9  6 HOH B2148  HOH B2211                                          
SITE     1 BC1  8 THR B 215  GLY B 258  LYS B 259  THR B 278                    
SITE     2 BC1  8 LEU B 279  HOH B2559  HOH B2560  HOH B2561                    
SITE     1 BC2  7 ASP B 132  ASN B 133  THR B 134  ARG B 179                    
SITE     2 BC2  7 HOH B2562  HOH B2563  HOH B2564                               
SITE     1 BC3  7 ARG B  59  ARG B  78  ASN B  82  ASP B  84                    
SITE     2 BC3  7 ARG B 388  KDM B 500  HOH B2137                               
CRYST1   75.810   57.990   94.830  90.00 100.14  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      0.013191  0.000000  0.002359        0.00000                         
SCALE2      0.000000  0.017244  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010713        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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