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Database: PDB
Entry: 2XCY
LinkDB: 2XCY
Original site: 2XCY 
HEADER    HYDROLASE                               27-APR-10   2XCY              
TITLE     CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS SIALIDASE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXTRACELLULAR SIALIDASE/NEURAMINIDASE, PUTATIVE;           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 21-406;                                           
COMPND   5 EC: 3.2.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;                          
SOURCE   3 ORGANISM_TAXID: 5085;                                                
SOURCE   4 ATCC: ATCC 13073;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    HYDROLASE, GLYCOSIDASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.TELFORD,J.YEUNG,G.XU,A.BENNET,M.M.MOORE,G.L.TAYLOR                
REVDAT   3   21-SEP-11 2XCY    1       JRNL   REMARK VERSN                      
REVDAT   2   02-FEB-11 2XCY    1       JRNL   REMARK                            
REVDAT   1   12-MAY-10 2XCY    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) : 12.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.48                          
REMARK   3   NUMBER OF REFLECTIONS             : 56944                          
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) : 0.15528                         
REMARK   3   R VALUE            (WORKING SET) : 0.15322                         
REMARK   3   FREE R VALUE                     : 0.19406                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3022                            
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) : 1.837                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.884                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3071                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.217                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 150                          
REMARK   3   BIN FREE R VALUE                    : 0.276                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5940                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 1049                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.2                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.755                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00                                                 
REMARK   3    B22 (A**2) : 0.00                                                 
REMARK   3    B33 (A**2) : 0.00                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.149         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.069         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.230         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6094 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8275 ; 1.134 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   774 ; 6.284 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   287 ;28.941 ;22.892       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   943 ;12.814 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;15.166 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   864 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4796 ; 0.005 ; 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):  3811 ; 0.433 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6101 ; 0.808 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2283 ; 1.368 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2171 ; 2.206 ; 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 2XCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-43745.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-10                          
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          : RIGAKU MIRCOMAX 007HF              
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59980                              
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     (%) : 84.2                               
REMARK 200  DATA REDUNDANCY                : 3.1                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.60                              
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     (%) : 64.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.20                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
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       29.09500            
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     1                                                      
REMARK 465     ASN B     2                                                      
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   359     O    HOH A  2533              2.17            
REMARK 500   O    HOH A  2002     O    HOH B  2386              2.15            
REMARK 500   O    HOH A  2266     O    HOH A  2551              2.10            
REMARK 500   O    HOH B  2197     O    HOH B  2254              1.77            
REMARK 500   O    HOH B  2304     O    HOH B  2317              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2254     O    HOH B  2320     1657     2.19            
REMARK 500   O    HOH B  2461     O    HOH A  2492     1747     2.08            
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  40       64.89     65.66                                   
REMARK 500    ALA A 181      -86.07   -110.07                                   
REMARK 500    ASN A 215       46.48   -145.81                                   
REMARK 500    ALA A 275       69.78     63.58                                   
REMARK 500    ILE B  40       66.71     66.52                                   
REMARK 500    ASN B  81       19.01     58.86                                   
REMARK 500    ALA B  99       32.03    -92.86                                   
REMARK 500    ALA B 181      -84.18   -105.50                                   
REMARK 500    ASN B 215       42.39   -142.78                                   
REMARK 500    ALA B 275       64.52     65.30                                   
REMARK 500    THR B 300      -32.73   -131.43                                   
REMARK 500    ARG B 303       32.90    -99.39                                   
REMARK 500    ASP B 346       30.43    -95.01                                   
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  CL A1387                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1387                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1388                 
DBREF  2XCY A    1   386  UNP    Q4WQS0   Q4WQS0_ASPFU    21    406             
DBREF  2XCY B    1   386  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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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                          
MODRES 2XCY MSE A   23  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE A  203  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE A  253  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE A  305  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE A  341  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE B   23  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE B  203  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE B  253  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE B  305  MET  SELENOMETHIONINE                                   
MODRES 2XCY MSE B  341  MET  SELENOMETHIONINE                                   
HET    MSE  A  23       8                                                       
HET    MSE  A 203       8                                                       
HET    MSE  A 253       8                                                       
HET    MSE  A 305       8                                                       
HET    MSE  A 341       8                                                       
HET     CL  A1387       1                                                       
HET    MSE  B  23       8                                                       
HET    MSE  B 203       8                                                       
HET    MSE  B 253       8                                                       
HET    MSE  B 305       8                                                       
HET    MSE  B 341       8                                                       
HET     CL  B1387       1                                                       
HET    GOL  A1388       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   5  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   6  HOH   *1049(H2 O)                                                   
HELIX    1   1 ASP A    3  ALA A    8  5                                   6    
HELIX    2   2 SER A   84  ASP A   87  5                                   4    
HELIX    3   3 LEU A  171  THR A  176  1                                   6    
HELIX    4   4 GLU A  325  LYS A  328  5                                   4    
HELIX    5   5 ASN A  376  ASN A  382  1                                   7    
HELIX    6   6 ASP B    3  ALA B    8  5                                   6    
HELIX    7   7 SER B   84  ASP B   87  5                                   4    
HELIX    8   8 LEU B  171  THR B  176  1                                   6    
HELIX    9   9 GLU B  325  LYS B  328  5                                   4    
HELIX   10  10 ASN B  376  ASN B  382  1                                   7    
SHEET    1  AA 4 HIS A  12  PHE A  18  0                                        
SHEET    2  AA 4 ARG A 368  PHE A 375 -1  O  ILE A 370   N  LEU A  17           
SHEET    3  AA 4 ILE A 349  ASP A 356 -1  O  ILE A 349   N  PHE A 375           
SHEET    4  AA 4 HIS A 334  LYS A 343 -1  O  HIS A 334   N  ASP A 356           
SHEET    1  AB 4 SER A  37  ARG A  45  0                                        
SHEET    2  AB 4 ILE A  51  ARG A  58 -1  O  LEU A  52   N  VAL A  44           
SHEET    3  AB 4 ILE A  68  ARG A  74 -1  O  ASN A  69   N  GLY A  57           
SHEET    4  AB 4 ARG A  92  VAL A  95 -1  O  ARG A  92   N  TYR A  72           
SHEET    1  AC 4 THR A 101  VAL A 109  0                                        
SHEET    2  AC 4 ILE A 115  ASN A 122 -1  O  TYR A 116   N  VAL A 108           
SHEET    3  AC 4 HIS A 152  SER A 158 -1  O  HIS A 152   N  TRP A 121           
SHEET    4  AC 4 VAL A 169  ASP A 170 -1  O  VAL A 169   N  LEU A 155           
SHEET    1  AD 2 TYR A 126  SER A 127  0                                        
SHEET    2  AD 2 LYS A 141  LYS A 142  1  O  LYS A 141   N  SER A 127           
SHEET    1  AE 4 ILE A 191  ARG A 192  0                                        
SHEET    2  AE 4 LEU A 198  ALA A 202 -1  O  VAL A 199   N  ILE A 191           
SHEET    3  AE 4 ARG A 205  ALA A 212 -1  O  ARG A 205   N  ALA A 202           
SHEET    4  AE 4 ASN A 215  ARG A 222 -1  O  ASN A 215   N  ALA A 212           
SHEET    1  AF 4 ILE A 232  GLN A 234  0                                        
SHEET    2  AF 4 LEU A 240  ASP A 244 -1  O  TYR A 241   N  VAL A 233           
SHEET    3  AF 4 GLY A 250  THR A 258 -1  O  MSE A 253   N  ASP A 244           
SHEET    4  AF 4 GLY A 261  PHE A 262  1  O  GLY A 261   N  THR A 258           
SHEET    1  AG 4 ILE A 232  GLN A 234  0                                        
SHEET    2  AG 4 LEU A 240  ASP A 244 -1  O  TYR A 241   N  VAL A 233           
SHEET    3  AG 4 GLY A 250  THR A 258 -1  O  MSE A 253   N  ASP A 244           
SHEET    4  AG 4 ALA A 266  ASP A 273 -1  O  ALA A 266   N  VAL A 254           
SHEET    1  AH 2 GLY A 261  PHE A 262  0                                        
SHEET    2  AH 2 GLY A 250  THR A 258  1  O  THR A 258   N  GLY A 261           
SHEET    1  AI 4 SER A 279  ASN A 284  0                                        
SHEET    2  AI 4 ARG A 290  SER A 296 -1  O  ARG A 290   N  TYR A 283           
SHEET    3  AI 4 MSE A 305  SER A 310 -1  O  ARG A 306   N  ASN A 295           
SHEET    4  AI 4 ARG A 322  LYS A 323 -1  O  ARG A 322   N  VAL A 307           
SHEET    1  BA 4 HIS B  12  PHE B  18  0                                        
SHEET    2  BA 4 ARG B 368  PHE B 375 -1  O  ILE B 370   N  LEU B  17           
SHEET    3  BA 4 ILE B 349  ASP B 356 -1  O  ILE B 349   N  PHE B 375           
SHEET    4  BA 4 HIS B 334  LYS B 343 -1  O  HIS B 334   N  ASP B 356           
SHEET    1  BB 4 SER B  37  ARG B  45  0                                        
SHEET    2  BB 4 ILE B  51  ARG B  58 -1  O  LEU B  52   N  VAL B  44           
SHEET    3  BB 4 ILE B  68  ARG B  74 -1  O  ASN B  69   N  GLY B  57           
SHEET    4  BB 4 ARG B  92  VAL B  95 -1  O  ARG B  92   N  TYR B  72           
SHEET    1  BC 4 GLY B 100  VAL B 109  0                                        
SHEET    2  BC 4 ILE B 115  GLY B 123 -1  O  TYR B 116   N  VAL B 108           
SHEET    3  BC 4 HIS B 152  SER B 158 -1  O  HIS B 152   N  TRP B 121           
SHEET    4  BC 4 VAL B 169  ASP B 170 -1  O  VAL B 169   N  LEU B 155           
SHEET    1  BD 2 TYR B 126  SER B 127  0                                        
SHEET    2  BD 2 LYS B 141  LYS B 142  1  O  LYS B 141   N  SER B 127           
SHEET    1  BE 4 ILE B 191  ARG B 192  0                                        
SHEET    2  BE 4 LEU B 198  ALA B 202 -1  O  VAL B 199   N  ILE B 191           
SHEET    3  BE 4 ARG B 205  ARG B 210 -1  O  ARG B 205   N  ALA B 202           
SHEET    4  BE 4 THR B 217  ARG B 222 -1  O  THR B 217   N  ARG B 210           
SHEET    1  BF 4 GLY B 230  GLN B 234  0                                        
SHEET    2  BF 4 LEU B 240  ASP B 244 -1  O  TYR B 241   N  VAL B 233           
SHEET    3  BF 4 GLY B 250  THR B 258 -1  O  MSE B 253   N  ASP B 244           
SHEET    4  BF 4 GLY B 261  PHE B 262  1  O  GLY B 261   N  THR B 258           
SHEET    1  BG 4 GLY B 230  GLN B 234  0                                        
SHEET    2  BG 4 LEU B 240  ASP B 244 -1  O  TYR B 241   N  VAL B 233           
SHEET    3  BG 4 GLY B 250  THR B 258 -1  O  MSE B 253   N  ASP B 244           
SHEET    4  BG 4 ALA B 266  ASP B 273 -1  O  ALA B 266   N  VAL B 254           
SHEET    1  BH 2 GLY B 261  PHE B 262  0                                        
SHEET    2  BH 2 GLY B 250  THR B 258  1  O  THR B 258   N  GLY B 261           
SHEET    1  BI 4 SER B 279  ASN B 284  0                                        
SHEET    2  BI 4 ARG B 290  SER B 296 -1  O  ARG B 290   N  TYR B 283           
SHEET    3  BI 4 MSE B 305  SER B 310 -1  O  ARG B 306   N  ASN B 295           
SHEET    4  BI 4 ARG B 322  LYS B 323 -1  O  ARG B 322   N  VAL B 307           
LINK         C   ASN A  22                 N   MSE A  23     1555   1555  1.33  
LINK         C   MSE A  23                 N   ALA A  24     1555   1555  1.33  
LINK         C   ALA A 202                 N   MSE A 203     1555   1555  1.33  
LINK         C   MSE A 203                 N   GLY A 204     1555   1555  1.33  
LINK         C   ARG A 252                 N   MSE A 253     1555   1555  1.33  
LINK         C   MSE A 253                 N   VAL A 254     1555   1555  1.33  
LINK         C   ALA A 304                 N   MSE A 305     1555   1555  1.33  
LINK         C   MSE A 305                 N   ARG A 306     1555   1555  1.33  
LINK         C   SER A 340                 N   MSE A 341     1555   1555  1.33  
LINK         C   MSE A 341                 N   THR A 342     1555   1555  1.33  
LINK         C   ASN B  22                 N   MSE B  23     1555   1555  1.33  
LINK         C   MSE B  23                 N   ALA B  24     1555   1555  1.33  
LINK         C   ALA B 202                 N   MSE B 203     1555   1555  1.33  
LINK         C   MSE B 203                 N   GLY B 204     1555   1555  1.34  
LINK         C   ARG B 252                 N   MSE B 253     1555   1555  1.33  
LINK         C   MSE B 253                 N   VAL B 254     1555   1555  1.34  
LINK         C   ALA B 304                 N   MSE B 305     1555   1555  1.34  
LINK         C   MSE B 305                 N   ARG B 306     1555   1555  1.33  
LINK         C   SER B 340                 N   MSE B 341     1555   1555  1.33  
LINK         C   MSE B 341                 N   THR B 342     1555   1555  1.33  
CISPEP   1 GLY A  186    PRO A  187          0         4.38                     
CISPEP   2 ALA A  287    PRO A  288          0        -5.46                     
CISPEP   3 GLY B  186    PRO B  187          0         2.96                     
CISPEP   4 ALA B  287    PRO B  288          0        -6.79                     
SITE     1 AC1  5 ARG A 245  ARG A 302  TYR A 338  HOH A2150                    
SITE     2 AC1  5 HOH A2515                                                     
SITE     1 AC2  4 ARG B 245  ARG B 302  TYR B 338  HOH B2446                    
SITE     1 AC3  6 ASP A 112  ASN A 113  THR A 114  ARG A 159                    
SITE     2 AC3  6 HOH A2562  HOH A2563                                          
CRYST1   75.890   58.190   94.700  90.00 100.01  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      0.013177  0.000000  0.002326        0.00000                         
SCALE2      0.000000  0.017185  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010723        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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