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Database: PDB
Entry: 2YA6
LinkDB: 2YA6
Original site: 2YA6 
HEADER    HYDROLASE                               18-FEB-11   2YA6              
TITLE     CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4)            
TITLE    2 IN COMPLEX WITH DANA                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEURAMINIDASE A;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 280-754;                        
COMPND   5 SYNONYM: NANA;                                                       
COMPND   6 EC: 3.2.1.18;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: THE SEQUENCE NUMBERING ABOVE CORRESPONDS TO THE       
COMPND   9  CLOSEST UNIPROT SEQUENCE MATCH UNP B2DJD9. THE SEQUENCE NUMBERING   
COMPND  10  FOR THE ENTRY SHOULD BE 303-777                                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 170187;                                              
SOURCE   4 STRAIN: TIGR4;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    HYDROLASE, SIALIDASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.GUT,G.XU,G.L.TAYLOR,M.A.WALSH                                       
REVDAT   2   08-JUN-11 2YA6    1       JRNL                                     
REVDAT   1   27-APR-11 2YA6    0                                                
JRNL        AUTH   H.GUT,G.XU,G.L.TAYLOR,M.A.WALSH                              
JRNL        TITL   STRUCTURAL BASIS FOR STREPTOCOCCUS PNEUMONIAE NANA           
JRNL        TITL 2 INHIBITION BY INFLUENZA ANTIVIRALS ZANAMIVIR AND             
JRNL        TITL 3 OSELTAMIVIR CARBOXYLATE.                                     
JRNL        REF    J.MOL.BIOL.                   V. 409   496 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21514303                                                     
JRNL        DOI    10.1016/J.JMB.2011.04.016                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.86                          
REMARK   3   NUMBER OF REFLECTIONS             : 61963                          
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) : 0.19660                         
REMARK   3   R VALUE            (WORKING SET) : 0.19552                         
REMARK   3   FREE R VALUE                     : 0.23774                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.5                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1578                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.004                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.056                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3685                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.288                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.374                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7456                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 57                                      
REMARK   3   SOLVENT ATOMS            : 583                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.2                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.647                         
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): 0.209         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.134         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.804         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7670 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10359 ; 1.263 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   942 ; 7.040 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   370 ;34.613 ;24.486       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1340 ;14.186 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;14.205 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1094 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5872 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3638 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5141 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   744 ; 0.144 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    32 ; 0.190 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.089 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4806 ; 0.732 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7504 ; 1.242 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3312 ; 1.570 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2855 ; 2.437 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2YA6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-47419.                                       
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) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL CUT                 
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONICS                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63554                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.8                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.46                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.86                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 200 MM KFORMATE,           
REMARK 280  20 MM TRIS PH 7.5 .                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       82.42850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.41750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       82.42850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.41750            
REMARK 290   SMTRY3   4  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     ALA A   285                                                      
REMARK 465     HIS A   286                                                      
REMARK 465     HIS A   287                                                      
REMARK 465     HIS A   288                                                      
REMARK 465     HIS A   289                                                      
REMARK 465     HIS A   290                                                      
REMARK 465     HIS A   291                                                      
REMARK 465     SER A   292                                                      
REMARK 465     SER A   293                                                      
REMARK 465     GLY A   294                                                      
REMARK 465     LEU A   295                                                      
REMARK 465     GLU A   296                                                      
REMARK 465     VAL A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     PHE A   299                                                      
REMARK 465     GLN A   300                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     PRO A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     GLY A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     ASN A   777                                                      
REMARK 465     ALA B   285                                                      
REMARK 465     HIS B   286                                                      
REMARK 465     HIS B   287                                                      
REMARK 465     HIS B   288                                                      
REMARK 465     HIS B   289                                                      
REMARK 465     HIS B   290                                                      
REMARK 465     HIS B   291                                                      
REMARK 465     SER B   292                                                      
REMARK 465     SER B   293                                                      
REMARK 465     GLY B   294                                                      
REMARK 465     LEU B   295                                                      
REMARK 465     GLU B   296                                                      
REMARK 465     VAL B   297                                                      
REMARK 465     LEU B   298                                                      
REMARK 465     PHE B   299                                                      
REMARK 465     GLN B   300                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     PRO B   302                                                      
REMARK 465     PRO B   303                                                      
REMARK 465     GLU B   304                                                      
REMARK 465     GLY B   305                                                      
REMARK 465     ALA B   306                                                      
REMARK 465     ASN B   777                                                      
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   OD1  ASN B   383     O    HOH B  2029              2.14            
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 333       66.40     71.02                                   
REMARK 500    ASP A 357       47.05    -85.70                                   
REMARK 500    TRP A 358     -176.16   -172.32                                   
REMARK 500    ASP A 402      116.66     66.24                                   
REMARK 500    ARG A 461     -166.05   -112.39                                   
REMARK 500    LYS A 549      -88.27    -93.16                                   
REMARK 500    SER A 581       -1.11   -140.10                                   
REMARK 500    HIS A 582     -124.73     41.87                                   
REMARK 500    THR A 631     -115.09   -118.93                                   
REMARK 500    TYR A 680       71.20     70.82                                   
REMARK 500    GLU A 691       78.42     35.28                                   
REMARK 500    LYS A 705     -153.75   -109.01                                   
REMARK 500    ASN A 708       75.16     56.67                                   
REMARK 500    ALA A 736     -118.45   -134.95                                   
REMARK 500    ASN B 324     -170.42    -67.39                                   
REMARK 500    ILE B 333       71.09     61.97                                   
REMARK 500    ASP B 357       49.31    -84.22                                   
REMARK 500    TRP B 358     -171.69   -175.44                                   
REMARK 500    ASP B 370       29.74   -147.25                                   
REMARK 500    ASP B 402      117.14     70.80                                   
REMARK 500    LYS B 412       -3.30     72.53                                   
REMARK 500    ARG B 461     -160.88   -107.29                                   
REMARK 500    LYS B 549      -86.99    -95.28                                   
REMARK 500    LYS B 567      136.56    -39.77                                   
REMARK 500    HIS B 582     -126.54     43.00                                   
REMARK 500    THR B 631     -116.89   -123.17                                   
REMARK 500    TYR B 680       73.56     73.74                                   
REMARK 500    LYS B 705     -159.88   -120.13                                   
REMARK 500    ASN B 708       72.32     65.30                                   
REMARK 500    LEU B 725      -63.93   -105.40                                   
REMARK 500    GLN B 731      116.53   -164.12                                   
REMARK 500    ALA B 736     -111.83   -129.29                                   
REMARK 500    ASN B 745      -41.95   -139.45                                   
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 DAN A1777                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B1777                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A1778                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1779                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1778                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A1780                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B1779                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B1780                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A1781                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2YA7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4           
REMARK 900  ) IN COMPLEX WITH ZANAMIVIR                                         
REMARK 900 RELATED ID: 2YA4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4           
REMARK 900  )                                                                   
REMARK 900 RELATED ID: 2YA8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4           
REMARK 900  ) IN COMPLEX WITH OSELTAMIVIR CARBOXYLATE                           
REMARK 900 RELATED ID: 2YA5   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4           
REMARK 900  ) IN COMPLEX WITH SIALIC ACID                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 HYPOTHETICAL PROTEIN SPNET_02001817 STREPTOCOCCUS                    
REMARK 999 PNEUMONIAE TIGR4. APPARENT CONFLICTS ARE DUE TO CURRENT              
REMARK 999 UNIPROT MAPPING. SEQUENCE REFERENCE: UNIREF100_UPI00005582E2.        
DBREF  2YA6 A  303   777  UNP    B2DJD9   B2DJD9_STRPN   280    754             
DBREF  2YA6 B  303   777  UNP    B2DJD9   B2DJD9_STRPN   280    754             
SEQADV 2YA6 ALA A  285  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS A  286  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS A  287  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS A  288  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS A  289  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS A  290  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS A  291  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 SER A  292  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 SER A  293  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 GLY A  294  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 LEU A  295  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 GLU A  296  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 VAL A  297  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 LEU A  298  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 PHE A  299  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 GLN A  300  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 GLY A  301  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 PRO A  302  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 LYS A  440  UNP  B2DJD9    GLU   417 SEE REMARK 999                 
SEQADV 2YA6 ASP A  584  UNP  B2DJD9    ASN   561 SEE REMARK 999                 
SEQADV 2YA6 ALA B  285  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS B  286  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS B  287  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS B  288  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS B  289  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS B  290  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 HIS B  291  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 SER B  292  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 SER B  293  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 GLY B  294  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 LEU B  295  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 GLU B  296  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 VAL B  297  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 LEU B  298  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 PHE B  299  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 GLN B  300  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 GLY B  301  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 PRO B  302  UNP  B2DJD9              EXPRESSION TAG                 
SEQADV 2YA6 LYS B  440  UNP  B2DJD9    GLU   417 SEE REMARK 999                 
SEQADV 2YA6 ASP B  584  UNP  B2DJD9    ASN   561 SEE REMARK 999                 
SEQRES   1 A  493  ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL          
SEQRES   2 A  493  LEU PHE GLN GLY PRO PRO GLU GLY ALA ALA LEU THR GLU          
SEQRES   3 A  493  LYS THR ASP ILE PHE GLU SER GLY ARG ASN GLY ASN PRO          
SEQRES   4 A  493  ASN LYS ASP GLY ILE LYS SER TYR ARG ILE PRO ALA LEU          
SEQRES   5 A  493  LEU LYS THR ASP LYS GLY THR LEU ILE ALA GLY ALA ASP          
SEQRES   6 A  493  GLU ARG ARG LEU HIS SER SER ASP TRP GLY ASP ILE GLY          
SEQRES   7 A  493  MET VAL ILE ARG ARG SER GLU ASP ASN GLY LYS THR TRP          
SEQRES   8 A  493  GLY ASP ARG VAL THR ILE THR ASN LEU ARG ASP ASN PRO          
SEQRES   9 A  493  LYS ALA SER ASP PRO SER ILE GLY SER PRO VAL ASN ILE          
SEQRES  10 A  493  ASP MET VAL LEU VAL GLN ASP PRO GLU THR LYS ARG ILE          
SEQRES  11 A  493  PHE SER ILE TYR ASP MET PHE PRO GLU GLY LYS GLY ILE          
SEQRES  12 A  493  PHE GLY MET SER SER GLN LYS GLU GLU ALA TYR LYS LYS          
SEQRES  13 A  493  ILE ASP GLY LYS THR TYR GLN ILE LEU TYR ARG GLU GLY          
SEQRES  14 A  493  GLU LYS GLY ALA TYR THR ILE ARG GLU ASN GLY THR VAL          
SEQRES  15 A  493  TYR THR PRO ASP GLY LYS ALA THR ASP TYR ARG VAL VAL          
SEQRES  16 A  493  VAL ASP PRO VAL LYS PRO ALA TYR SER ASP LYS GLY ASP          
SEQRES  17 A  493  LEU TYR LYS GLY ASP GLN LEU LEU GLY ASN ILE TYR PHE          
SEQRES  18 A  493  THR THR ASN LYS THR SER PRO PHE ARG ILE ALA LYS ASP          
SEQRES  19 A  493  SER TYR LEU TRP MET SER TYR SER ASP ASP ASP GLY LYS          
SEQRES  20 A  493  THR TRP SER ALA PRO GLN ASP ILE THR PRO MET VAL LYS          
SEQRES  21 A  493  ALA ASP TRP MET LYS PHE LEU GLY VAL GLY PRO GLY THR          
SEQRES  22 A  493  GLY ILE VAL LEU ARG ASN GLY PRO HIS LYS GLY ARG ILE          
SEQRES  23 A  493  LEU ILE PRO VAL TYR THR THR ASN ASN VAL SER HIS LEU          
SEQRES  24 A  493  ASP GLY SER GLN SER SER ARG VAL ILE TYR SER ASP ASP          
SEQRES  25 A  493  HIS GLY LYS THR TRP HIS ALA GLY GLU ALA VAL ASN ASP          
SEQRES  26 A  493  ASN ARG GLN VAL ASP GLY GLN LYS ILE HIS SER SER THR          
SEQRES  27 A  493  MET ASN ASN ARG ARG ALA GLN ASN THR GLU SER THR VAL          
SEQRES  28 A  493  VAL GLN LEU ASN ASN GLY ASP VAL LYS LEU PHE MET ARG          
SEQRES  29 A  493  GLY LEU THR GLY ASP LEU GLN VAL ALA THR SER LYS ASP          
SEQRES  30 A  493  GLY GLY VAL THR TRP GLU LYS ASP ILE LYS ARG TYR PRO          
SEQRES  31 A  493  GLN VAL LYS ASP VAL TYR VAL GLN MET SER ALA ILE HIS          
SEQRES  32 A  493  THR MET HIS GLU GLY LYS GLU TYR ILE ILE LEU SER ASN          
SEQRES  33 A  493  ALA GLY GLY PRO LYS ARG GLU ASN GLY MET VAL HIS LEU          
SEQRES  34 A  493  ALA ARG VAL GLU GLU ASN GLY GLU LEU THR TRP LEU LYS          
SEQRES  35 A  493  HIS ASN PRO ILE GLN LYS GLY GLU PHE ALA TYR ASN SER          
SEQRES  36 A  493  LEU GLN GLU LEU GLY ASN GLY GLU TYR GLY ILE LEU TYR          
SEQRES  37 A  493  GLU HIS THR GLU LYS GLY GLN ASN ALA TYR THR LEU SER          
SEQRES  38 A  493  PHE ARG LYS PHE ASN TRP GLU PHE LEU SER LYS ASN              
SEQRES   1 B  493  ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL          
SEQRES   2 B  493  LEU PHE GLN GLY PRO PRO GLU GLY ALA ALA LEU THR GLU          
SEQRES   3 B  493  LYS THR ASP ILE PHE GLU SER GLY ARG ASN GLY ASN PRO          
SEQRES   4 B  493  ASN LYS ASP GLY ILE LYS SER TYR ARG ILE PRO ALA LEU          
SEQRES   5 B  493  LEU LYS THR ASP LYS GLY THR LEU ILE ALA GLY ALA ASP          
SEQRES   6 B  493  GLU ARG ARG LEU HIS SER SER ASP TRP GLY ASP ILE GLY          
SEQRES   7 B  493  MET VAL ILE ARG ARG SER GLU ASP ASN GLY LYS THR TRP          
SEQRES   8 B  493  GLY ASP ARG VAL THR ILE THR ASN LEU ARG ASP ASN PRO          
SEQRES   9 B  493  LYS ALA SER ASP PRO SER ILE GLY SER PRO VAL ASN ILE          
SEQRES  10 B  493  ASP MET VAL LEU VAL GLN ASP PRO GLU THR LYS ARG ILE          
SEQRES  11 B  493  PHE SER ILE TYR ASP MET PHE PRO GLU GLY LYS GLY ILE          
SEQRES  12 B  493  PHE GLY MET SER SER GLN LYS GLU GLU ALA TYR LYS LYS          
SEQRES  13 B  493  ILE ASP GLY LYS THR TYR GLN ILE LEU TYR ARG GLU GLY          
SEQRES  14 B  493  GLU LYS GLY ALA TYR THR ILE ARG GLU ASN GLY THR VAL          
SEQRES  15 B  493  TYR THR PRO ASP GLY LYS ALA THR ASP TYR ARG VAL VAL          
SEQRES  16 B  493  VAL ASP PRO VAL LYS PRO ALA TYR SER ASP LYS GLY ASP          
SEQRES  17 B  493  LEU TYR LYS GLY ASP GLN LEU LEU GLY ASN ILE TYR PHE          
SEQRES  18 B  493  THR THR ASN LYS THR SER PRO PHE ARG ILE ALA LYS ASP          
SEQRES  19 B  493  SER TYR LEU TRP MET SER TYR SER ASP ASP ASP GLY LYS          
SEQRES  20 B  493  THR TRP SER ALA PRO GLN ASP ILE THR PRO MET VAL LYS          
SEQRES  21 B  493  ALA ASP TRP MET LYS PHE LEU GLY VAL GLY PRO GLY THR          
SEQRES  22 B  493  GLY ILE VAL LEU ARG ASN GLY PRO HIS LYS GLY ARG ILE          
SEQRES  23 B  493  LEU ILE PRO VAL TYR THR THR ASN ASN VAL SER HIS LEU          
SEQRES  24 B  493  ASP GLY SER GLN SER SER ARG VAL ILE TYR SER ASP ASP          
SEQRES  25 B  493  HIS GLY LYS THR TRP HIS ALA GLY GLU ALA VAL ASN ASP          
SEQRES  26 B  493  ASN ARG GLN VAL ASP GLY GLN LYS ILE HIS SER SER THR          
SEQRES  27 B  493  MET ASN ASN ARG ARG ALA GLN ASN THR GLU SER THR VAL          
SEQRES  28 B  493  VAL GLN LEU ASN ASN GLY ASP VAL LYS LEU PHE MET ARG          
SEQRES  29 B  493  GLY LEU THR GLY ASP LEU GLN VAL ALA THR SER LYS ASP          
SEQRES  30 B  493  GLY GLY VAL THR TRP GLU LYS ASP ILE LYS ARG TYR PRO          
SEQRES  31 B  493  GLN VAL LYS ASP VAL TYR VAL GLN MET SER ALA ILE HIS          
SEQRES  32 B  493  THR MET HIS GLU GLY LYS GLU TYR ILE ILE LEU SER ASN          
SEQRES  33 B  493  ALA GLY GLY PRO LYS ARG GLU ASN GLY MET VAL HIS LEU          
SEQRES  34 B  493  ALA ARG VAL GLU GLU ASN GLY GLU LEU THR TRP LEU LYS          
SEQRES  35 B  493  HIS ASN PRO ILE GLN LYS GLY GLU PHE ALA TYR ASN SER          
SEQRES  36 B  493  LEU GLN GLU LEU GLY ASN GLY GLU TYR GLY ILE LEU TYR          
SEQRES  37 B  493  GLU HIS THR GLU LYS GLY GLN ASN ALA TYR THR LEU SER          
SEQRES  38 B  493  PHE ARG LYS PHE ASN TRP GLU PHE LEU SER LYS ASN              
HET    DAN  A1777      20                                                       
HET    DAN  B1777      20                                                       
HET    FMT  A1778       3                                                       
HET     CL  A1779       1                                                       
HET     CL  B1778       1                                                       
HET    FMT  A1780       3                                                       
HET    FMT  B1779       3                                                       
HET    FMT  B1780       3                                                       
HET    FMT  A1781       3                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     FMT FORMIC ACID                                                      
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID                     
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4  FMT    5(C H2 O2)                                                   
FORMUL   5  DAN    2(C11 H17 N O8)                                              
FORMUL   6  HOH   *583(H2 O)                                                    
HELIX    1   1 ASP A  392  GLY A  396  5                                   5    
HELIX    2   2 LYS A  425  MET A  430  5                                   6    
HELIX    3   3 LYS A  484  SER A  488  5                                   5    
HELIX    4   4 ILE A  539  LYS A  544  1                                   6    
HELIX    5   5 SER A  581  SER A  586  1                                   6    
HELIX    6   6 ASN A  625  GLN A  629  5                                   5    
HELIX    7   7 TRP A  771  LYS A  776  1                                   6    
HELIX    8   8 ASP B  392  GLY B  396  5                                   5    
HELIX    9   9 LYS B  425  GLY B  429  5                                   5    
HELIX   10  10 LYS B  484  SER B  488  5                                   5    
HELIX   11  11 ILE B  539  LYS B  544  1                                   6    
HELIX   12  12 SER B  581  SER B  586  1                                   6    
HELIX   13  13 ASN B  625  GLN B  629  5                                   5    
HELIX   14  14 TRP B  771  LYS B  776  1                                   6    
SHEET    1  AA 4 THR A 312  PHE A 315  0                                        
SHEET    2  AA 4 THR A 763  ASN A 770 -1  O  LEU A 764   N  ILE A 314           
SHEET    3  AA 4 GLU A 747  HIS A 754 -1  O  TYR A 748   N  PHE A 769           
SHEET    4  AA 4 ASN A 738  GLY A 744 -1  O  SER A 739   N  LEU A 751           
SHEET    1  AB 4 SER A 330  LYS A 338  0                                        
SHEET    2  AB 4 LEU A 344  ARG A 351 -1  O  ILE A 345   N  LEU A 337           
SHEET    3  AB 4 ILE A 361  SER A 368 -1  O  GLY A 362   N  GLU A 350           
SHEET    4  AB 4 VAL A 379  THR A 382 -1  O  VAL A 379   N  ILE A 365           
SHEET    1  AC 5 GLN A 537  ASP A 538  0                                        
SHEET    2  AC 5 TYR A 520  SER A 526 -1  O  MET A 523   N  GLN A 537           
SHEET    3  AC 5 ILE A 414  PHE A 421 -1  O  ILE A 414   N  SER A 526           
SHEET    4  AC 5 VAL A 399  GLN A 407 -1  O  VAL A 399   N  PHE A 421           
SHEET    5  AC 5 GLY A 556  THR A 557  1  O  GLY A 556   N  LEU A 405           
SHEET    1  AD 2 TYR A 438  ILE A 441  0                                        
SHEET    2  AD 2 LYS A 444  ARG A 451 -1  O  LYS A 444   N  ILE A 441           
SHEET    1  AE 7 GLN A 498  ASN A 502  0                                        
SHEET    2  AE 7 ASP A 492  LYS A 495 -1  O  LEU A 493   N  LEU A 500           
SHEET    3  AE 7 ALA A 473  VAL A 478 -1  O  ARG A 477   N  TYR A 494           
SHEET    4  AE 7 THR A 465  TYR A 467 -1  O  VAL A 466   N  THR A 474           
SHEET    5  AE 7 TYR A 458  ILE A 460 -1  O  THR A 459   N  TYR A 467           
SHEET    6  AE 7 LYS A 444  ARG A 451 -1  O  GLN A 447   N  ILE A 460           
SHEET    7  AE 7 PHE A 513  ILE A 515  1  O  ARG A 514   N  TYR A 450           
SHEET    1  AF 7 GLN A 498  ASN A 502  0                                        
SHEET    2  AF 7 ASP A 492  LYS A 495 -1  O  LEU A 493   N  LEU A 500           
SHEET    3  AF 7 ALA A 473  VAL A 478 -1  O  ARG A 477   N  TYR A 494           
SHEET    4  AF 7 THR A 465  TYR A 467 -1  O  VAL A 466   N  THR A 474           
SHEET    5  AF 7 TYR A 458  ILE A 460 -1  O  THR A 459   N  TYR A 467           
SHEET    6  AF 7 LYS A 444  ARG A 451 -1  O  GLN A 447   N  ILE A 460           
SHEET    7  AF 7 TYR A 438  ILE A 441 -1  O  LYS A 439   N  TYR A 446           
SHEET    1  AG 2 PHE A 513  ILE A 515  0                                        
SHEET    2  AG 2 LYS A 444  ARG A 451  1  O  TYR A 450   N  ARG A 514           
SHEET    1  AH 2 MET A 548  VAL A 553  0                                        
SHEET    2  AH 2 ILE A 570  ASN A 578 -1  O  TYR A 575   N  GLY A 552           
SHEET    1  AI 2 ILE A 559  VAL A 560  0                                        
SHEET    2  AI 2 ILE A 570  ASN A 578  1  O  LEU A 571   N  ILE A 559           
SHEET    1  AJ 4 HIS A 602  ALA A 603  0                                        
SHEET    2  AJ 4 SER A 588  SER A 594 -1  O  TYR A 593   N  HIS A 602           
SHEET    3  AJ 4 ILE A 570  ASN A 578 -1  O  ILE A 570   N  SER A 594           
SHEET    4  AJ 4 ILE A 559  VAL A 560  1  O  ILE A 559   N  LEU A 571           
SHEET    1  AK 4 HIS A 602  ALA A 603  0                                        
SHEET    2  AK 4 SER A 588  SER A 594 -1  O  TYR A 593   N  HIS A 602           
SHEET    3  AK 4 ILE A 570  ASN A 578 -1  O  ILE A 570   N  SER A 594           
SHEET    4  AK 4 MET A 548  VAL A 553 -1  N  LYS A 549   O  THR A 577           
SHEET    1  AL 2 ARG A 611  VAL A 613  0                                        
SHEET    2  AL 2 GLN A 616  ILE A 618 -1  O  GLN A 616   N  VAL A 613           
SHEET    1  AM 4 SER A 633  GLN A 637  0                                        
SHEET    2  AM 4 VAL A 643  MET A 647 -1  O  LYS A 644   N  VAL A 636           
SHEET    3  AM 4 ASP A 653  SER A 659 -1  O  GLN A 655   N  MET A 647           
SHEET    4  AM 4 LYS A 671  LYS A 677 -1  O  LYS A 671   N  VAL A 656           
SHEET    1  AN 4 SER A 684  HIS A 690  0                                        
SHEET    2  AN 4 LYS A 693  ALA A 701 -1  O  LYS A 693   N  HIS A 690           
SHEET    3  AN 4 GLU A 707  VAL A 716 -1  O  MET A 710   N  ASN A 700           
SHEET    4  AN 4 LEU A 722  GLU A 734 -1  O  THR A 723   N  ARG A 715           
SHEET    1  BA 4 THR B 312  PHE B 315  0                                        
SHEET    2  BA 4 THR B 763  ASN B 770 -1  O  LEU B 764   N  ILE B 314           
SHEET    3  BA 4 GLU B 747  HIS B 754 -1  O  TYR B 748   N  PHE B 769           
SHEET    4  BA 4 ASN B 738  GLU B 742 -1  O  SER B 739   N  LEU B 751           
SHEET    1  BB 4 SER B 330  LYS B 338  0                                        
SHEET    2  BB 4 LEU B 344  ARG B 351 -1  O  ILE B 345   N  LEU B 337           
SHEET    3  BB 4 ILE B 361  SER B 368 -1  O  GLY B 362   N  GLU B 350           
SHEET    4  BB 4 VAL B 379  THR B 382 -1  O  VAL B 379   N  ILE B 365           
SHEET    1  BC 5 GLN B 537  ASP B 538  0                                        
SHEET    2  BC 5 TYR B 520  SER B 526 -1  O  MET B 523   N  GLN B 537           
SHEET    3  BC 5 ILE B 414  PHE B 421 -1  O  ILE B 414   N  SER B 526           
SHEET    4  BC 5 VAL B 399  GLN B 407 -1  O  VAL B 399   N  PHE B 421           
SHEET    5  BC 5 GLY B 556  THR B 557  1  O  GLY B 556   N  LEU B 405           
SHEET    1  BD 2 TYR B 438  ILE B 441  0                                        
SHEET    2  BD 2 LYS B 444  ARG B 451 -1  O  LYS B 444   N  ILE B 441           
SHEET    1  BE 7 GLN B 498  ASN B 502  0                                        
SHEET    2  BE 7 ASP B 492  LYS B 495 -1  O  LEU B 493   N  LEU B 500           
SHEET    3  BE 7 ALA B 473  VAL B 478 -1  O  ARG B 477   N  TYR B 494           
SHEET    4  BE 7 THR B 465  TYR B 467 -1  O  VAL B 466   N  THR B 474           
SHEET    5  BE 7 ALA B 457  ILE B 460 -1  O  THR B 459   N  TYR B 467           
SHEET    6  BE 7 LYS B 444  ARG B 451 -1  O  GLN B 447   N  ILE B 460           
SHEET    7  BE 7 PHE B 513  ARG B 514  1  O  ARG B 514   N  TYR B 450           
SHEET    1  BF 7 GLN B 498  ASN B 502  0                                        
SHEET    2  BF 7 ASP B 492  LYS B 495 -1  O  LEU B 493   N  LEU B 500           
SHEET    3  BF 7 ALA B 473  VAL B 478 -1  O  ARG B 477   N  TYR B 494           
SHEET    4  BF 7 THR B 465  TYR B 467 -1  O  VAL B 466   N  THR B 474           
SHEET    5  BF 7 ALA B 457  ILE B 460 -1  O  THR B 459   N  TYR B 467           
SHEET    6  BF 7 LYS B 444  ARG B 451 -1  O  GLN B 447   N  ILE B 460           
SHEET    7  BF 7 TYR B 438  ILE B 441 -1  O  LYS B 439   N  TYR B 446           
SHEET    1  BG 2 PHE B 513  ARG B 514  0                                        
SHEET    2  BG 2 LYS B 444  ARG B 451  1  O  TYR B 450   N  ARG B 514           
SHEET    1  BH 2 LEU B 551  VAL B 553  0                                        
SHEET    2  BH 2 ILE B 570  THR B 576 -1  O  TYR B 575   N  GLY B 552           
SHEET    1  BI 2 ILE B 559  VAL B 560  0                                        
SHEET    2  BI 2 ILE B 570  THR B 576  1  O  LEU B 571   N  ILE B 559           
SHEET    1  BJ 4 HIS B 602  ALA B 603  0                                        
SHEET    2  BJ 4 SER B 588  SER B 594 -1  O  TYR B 593   N  HIS B 602           
SHEET    3  BJ 4 ILE B 570  THR B 576 -1  O  ILE B 570   N  SER B 594           
SHEET    4  BJ 4 ILE B 559  VAL B 560  1  O  ILE B 559   N  LEU B 571           
SHEET    1  BK 4 HIS B 602  ALA B 603  0                                        
SHEET    2  BK 4 SER B 588  SER B 594 -1  O  TYR B 593   N  HIS B 602           
SHEET    3  BK 4 ILE B 570  THR B 576 -1  O  ILE B 570   N  SER B 594           
SHEET    4  BK 4 LEU B 551  VAL B 553 -1  O  GLY B 552   N  TYR B 575           
SHEET    1  BL 2 ARG B 611  VAL B 613  0                                        
SHEET    2  BL 2 GLN B 616  ILE B 618 -1  O  GLN B 616   N  VAL B 613           
SHEET    1  BM 4 SER B 633  GLN B 637  0                                        
SHEET    2  BM 4 VAL B 643  MET B 647 -1  O  LYS B 644   N  VAL B 636           
SHEET    3  BM 4 ASP B 653  SER B 659 -1  O  GLN B 655   N  MET B 647           
SHEET    4  BM 4 LYS B 671  LYS B 677 -1  O  LYS B 671   N  VAL B 656           
SHEET    1  BN 4 SER B 684  HIS B 690  0                                        
SHEET    2  BN 4 LYS B 693  ALA B 701 -1  O  LYS B 693   N  HIS B 690           
SHEET    3  BN 4 GLU B 707  VAL B 716 -1  O  MET B 710   N  ASN B 700           
SHEET    4  BN 4 LEU B 722  GLU B 734 -1  O  THR B 723   N  ARG B 715           
CISPEP   1 GLU A  691    GLY A  692          0       -28.28                     
CISPEP   2 GLY A  703    PRO A  704          0         2.14                     
CISPEP   3 ALA A  761    TYR A  762          0        -6.26                     
CISPEP   4 GLY B  703    PRO B  704          0         3.21                     
CISPEP   5 ALA B  761    TYR B  762          0        -8.81                     
SITE     1 AC1 19 ARG A 332  ILE A 333  ARG A 351  ASP A 357                    
SITE     2 AC1 19 ILE A 401  ASP A 402  ASP A 419  ILE A 427                    
SITE     3 AC1 19 PHE A 428  TYR A 575  LEU A 583  GLN A 587                    
SITE     4 AC1 19 ARG A 648  ARG A 706  TYR A 737  HOH A2295                    
SITE     5 AC1 19 HOH A2296  HOH A2297  HOH A2298                               
SITE     1 AC2 16 ARG B 332  ILE B 333  ARG B 351  ASP B 357                    
SITE     2 AC2 16 ASP B 402  ASP B 419  ILE B 427  PHE B 428                    
SITE     3 AC2 16 TYR B 575  GLN B 587  ARG B 648  ARG B 706                    
SITE     4 AC2 16 TYR B 737  HOH B2282  HOH B2283  HOH B2284                    
SITE     1 AC3  4 SER A 526  ASP A 527  ASP A 528  THR A 532                    
SITE     1 AC4  4 ASN A 502  LYS A 509  THR A 510  SER A 511                    
SITE     1 AC5  5 GLY B 501  ASN B 502  LYS B 509  THR B 510                    
SITE     2 AC5  5 SER B 511                                                     
SITE     1 AC6  4 PRO A 541  LYS A 544  ALA A 545  HOH A2168                    
SITE     1 AC7  7 TYR B 525  SER B 526  ASP B 527  ASP B 528                    
SITE     2 AC7  7 THR B 532  SER B 534  HOH B2285                               
SITE     1 AC8  5 HIS B 566  ARG B 569  GLU B 717  ASN B 719                    
SITE     2 AC8  5 HOH B2190                                                     
SITE     1 AC9  3 GLN A 741  HOH A2286  HOH A2300                               
CRYST1  164.857   48.835  125.383  90.00 104.13  90.00 C 1 2 1       8          
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      0.006066  0.000000  0.001527        0.00000                         
SCALE2      0.000000  0.020477  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008224        0.00000                         
MTRIX1   1 -0.829500 -0.476500  0.291400       48.74000    1                    
MTRIX2   1 -0.475900  0.329900 -0.815300       34.22000    1                    
MTRIX3   1  0.292300 -0.814900 -0.500400       27.38000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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