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Database: PDB
Entry: 2VVZ
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Original site: 2VVZ 
HEADER    HYDROLASE                               13-JUN-08   2VVZ              
TITLE     STRUCTURE OF THE CATALYTIC DOMAIN OF STREPTOCOCCUS                    
TITLE    2 PNEUMONIAE SIALIDASE NANA                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE A;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 319-822;                        
COMPND   5 SYNONYM: NANA SIALIDASE, NEURAMINIDASE A;                            
COMPND   6 EC: 3.2.1.18;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 1313;                                                
SOURCE   4 STRAIN: R36A;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    SECRETED, CELL WALL, SIALIDASE, HYDROLASE,                            
KEYWDS   2 PEPTIDOGLYCAN-ANCHOR, GLYCOSIDASE, NEURAMINIDASE,                    
KEYWDS   3 VIRULENCE FACTOR                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.XU,X.LI,P.W.ANDREW,G.L.TAYLOR                                       
REVDAT   3   24-FEB-09 2VVZ    1       VERSN                                    
REVDAT   2   16-SEP-08 2VVZ    1       JRNL                                     
REVDAT   1   24-JUN-08 2VVZ    0                                                
JRNL        AUTH   G.XU,X.LI,P.W.ANDREW,G.L.TAYLOR                              
JRNL        TITL   STRUCTURE OF THE CATALYTIC DOMAIN OF STREPTOCOCCUS           
JRNL        TITL 2 PNEUMONIAE SIALIDASE NANA.                                   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  64   772 2008              
JRNL        REFN                   ISSN 1744-3091                               
JRNL        PMID   18765901                                                     
JRNL        DOI    10.1107/S1744309108024044                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.5  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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 34868                          
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) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1830                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2076                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.4590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7442                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.29000                                             
REMARK   3    B22 (A**2) : 0.72000                                              
REMARK   3    B33 (A**2) : -0.43000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.818         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.358         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.257         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.482        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.903                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.852                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7644 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10326 ; 1.145 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   938 ; 7.367 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   366 ;34.184 ;24.426       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1344 ;14.443 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;14.829 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1092 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5842 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3453 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5031 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   385 ; 0.145 ; 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):    34 ; 0.187 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.123 ; 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):  4788 ; 0.358 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7482 ; 0.633 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3292 ; 0.642 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2844 ; 1.063 ; 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   : 1.20                                          
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 2VVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-36556.                                       
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                             : 6.4                                
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 MRICOMAX-007 HF             
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 (SATURN 944)                   
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36773                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 2.9                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.25                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.60                               
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: PDB ENTRY 2BF6                                       
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): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1M MES PH 6.4            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       24.60300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.29800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.81300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.29800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.60300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.81300            
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: PQS                                                   
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: PQS                                                   
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     GLU A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     ASP A   792                                                      
REMARK 465     LEU A   793                                                      
REMARK 465     ILE A   794                                                      
REMARK 465     SER A   795                                                      
REMARK 465     PRO A   796                                                      
REMARK 465     THR A   797                                                      
REMARK 465     GLU A   798                                                      
REMARK 465     ALA A   799                                                      
REMARK 465     LYS A   800                                                      
REMARK 465     VAL A   801                                                      
REMARK 465     LYS A   802                                                      
REMARK 465     ARG A   803                                                      
REMARK 465     THR A   804                                                      
REMARK 465     ARG A   805                                                      
REMARK 465     GLU A   806                                                      
REMARK 465     MET A   807                                                      
REMARK 465     GLY A   808                                                      
REMARK 465     LYS A   809                                                      
REMARK 465     GLY A   810                                                      
REMARK 465     VAL A   811                                                      
REMARK 465     ILE A   812                                                      
REMARK 465     GLY A   813                                                      
REMARK 465     LEU A   814                                                      
REMARK 465     GLU A   815                                                      
REMARK 465     PHE A   816                                                      
REMARK 465     ASP A   817                                                      
REMARK 465     SER A   818                                                      
REMARK 465     GLU A   819                                                      
REMARK 465     VAL A   820                                                      
REMARK 465     LEU A   821                                                      
REMARK 465     VAL A   822                                                      
REMARK 465     GLU B   319                                                      
REMARK 465     GLY B   320                                                      
REMARK 465     ALA B   321                                                      
REMARK 465     ASP B   792                                                      
REMARK 465     LEU B   793                                                      
REMARK 465     ILE B   794                                                      
REMARK 465     SER B   795                                                      
REMARK 465     PRO B   796                                                      
REMARK 465     THR B   797                                                      
REMARK 465     GLU B   798                                                      
REMARK 465     ALA B   799                                                      
REMARK 465     LYS B   800                                                      
REMARK 465     VAL B   801                                                      
REMARK 465     LYS B   802                                                      
REMARK 465     ARG B   803                                                      
REMARK 465     THR B   804                                                      
REMARK 465     ARG B   805                                                      
REMARK 465     GLU B   806                                                      
REMARK 465     MET B   807                                                      
REMARK 465     GLY B   808                                                      
REMARK 465     LYS B   809                                                      
REMARK 465     GLY B   810                                                      
REMARK 465     VAL B   811                                                      
REMARK 465     ILE B   812                                                      
REMARK 465     GLY B   813                                                      
REMARK 465     LEU B   814                                                      
REMARK 465     GLU B   815                                                      
REMARK 465     PHE B   816                                                      
REMARK 465     ASP B   817                                                      
REMARK 465     SER B   818                                                      
REMARK 465     GLU B   819                                                      
REMARK 465     VAL B   820                                                      
REMARK 465     LEU B   821                                                      
REMARK 465     VAL B   822                                                      
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   OG   SER A   332  -  O    HOH A  2002              2.15            
REMARK 500   O    THR A   703  -  O    GLU A   709              1.96            
REMARK 500   N    ALA A   776  -  O    HOH A  2002              2.19            
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 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    ARG A 347      -88.10   -141.38                                   
REMARK 500    HIS A 369     -136.34   -165.05                                   
REMARK 500    ASP A 372       40.46    -78.18                                   
REMARK 500    ASP A 385       32.17    -91.86                                   
REMARK 500    ASP A 417      112.13     66.48                                   
REMARK 500    ILE A 442      -39.52     98.94                                   
REMARK 500    ALA A 472      -99.28    -40.31                                   
REMARK 500    TYR A 473      119.11     66.47                                   
REMARK 500    GLU A 477     -103.19     44.84                                   
REMARK 500    VAL A 481      -82.40    -62.59                                   
REMARK 500    TYR A 482      131.16     97.39                                   
REMARK 500    ALA A 488       76.76    -67.80                                   
REMARK 500    ASP A 490     -152.92    -60.93                                   
REMARK 500    TYR A 491      -56.91     66.11                                   
REMARK 500    LYS A 499      -83.65    169.72                                   
REMARK 500    PRO A 500     -147.49    -75.73                                   
REMARK 500    ALA A 501       34.64    -78.80                                   
REMARK 500    LEU A 514     -120.53    -69.13                                   
REMARK 500    LYS A 564      -82.60    -89.30                                   
REMARK 500    HIS A 597     -112.06     47.51                                   
REMARK 500    THR A 646     -118.95   -118.56                                   
REMARK 500    TYR A 695       61.68     69.51                                   
REMARK 500    GLU A 709      -55.89   -141.67                                   
REMARK 500    TYR A 710      144.34     69.09                                   
REMARK 500    LYS A 720      177.33     78.46                                   
REMARK 500    GLU A 732      -91.75    -79.26                                   
REMARK 500    GLU A 733      -61.89   -140.97                                   
REMARK 500    ALA A 751     -118.66   -124.40                                   
REMARK 500    ALA A 776      103.24    112.21                                   
REMARK 500    ASN B 339     -166.64    -72.09                                   
REMARK 500    ILE B 348       83.08     62.52                                   
REMARK 500    ASP B 372       43.65    -77.60                                   
REMARK 500    ASP B 385       40.23   -102.78                                   
REMARK 500    ASP B 417      123.20     67.42                                   
REMARK 500    PRO B 437     -176.23    -65.90                                   
REMARK 500    ILE B 442      -43.30     99.82                                   
REMARK 500    LYS B 459       95.56     56.96                                   
REMARK 500    ALA B 472      -92.48    -51.75                                   
REMARK 500    TYR B 473      121.85     73.55                                   
REMARK 500    ARG B 476     -150.84   -103.36                                   
REMARK 500    ASP B 490      -51.48     57.52                                   
REMARK 500    LYS B 499      -77.76   -110.58                                   
REMARK 500    PRO B 500     -109.71    -38.64                                   
REMARK 500    ASP B 543       41.70    -96.24                                   
REMARK 500    LYS B 564      -73.26    -88.65                                   
REMARK 500    HIS B 597     -123.34     45.87                                   
REMARK 500    THR B 646     -116.85   -109.49                                   
REMARK 500    TYR B 695       71.11     62.32                                   
REMARK 500    GLU B 709      -30.11   -136.77                                   
REMARK 500    TYR B 710      125.04     70.33                                   
REMARK 500    ASN B 715     -167.06   -163.33                                   
REMARK 500    LYS B 720      178.24     85.26                                   
REMARK 500    LEU B 740      -66.39   -103.59                                   
REMARK 500    ALA B 751     -100.20   -132.64                                   
REMARK 500    ALA B 776      112.08     79.03                                   
REMARK 500    LEU B 779       95.08     48.74                                   
REMARK 500    PHE B 784      149.93    163.07                                   
REMARK 500    TRP B 786      -38.43    154.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  368     HIS A  369                   74.19                    
REMARK 500 VAL A  498     LYS A  499                  -45.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS A 499        21.8      L          L   OUTSIDE RANGE           
REMARK 500    LYS B 459        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A1792                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B1792                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1793                 
DBREF  2VVZ A  319   822  UNP    P62575   NANA_STRPN     319    822             
DBREF  2VVZ B  319   822  UNP    P62575   NANA_STRPN     319    822             
SEQRES   1 A  504  GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU          
SEQRES   2 A  504  SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS          
SEQRES   3 A  504  SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY          
SEQRES   4 A  504  THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER          
SEQRES   5 A  504  SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER          
SEQRES   6 A  504  GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE          
SEQRES   7 A  504  THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER          
SEQRES   8 A  504  ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN          
SEQRES   9 A  504  ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET          
SEQRES  10 A  504  PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN          
SEQRES  11 A  504  LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR          
SEQRES  12 A  504  GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR          
SEQRES  13 A  504  ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS          
SEQRES  14 A  504  ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO          
SEQRES  15 A  504  ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN          
SEQRES  16 A  504  LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS THR SER          
SEQRES  17 A  504  PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER          
SEQRES  18 A  504  TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN          
SEQRES  19 A  504  ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE          
SEQRES  20 A  504  LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN          
SEQRES  21 A  504  GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR          
SEQRES  22 A  504  THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN SER SER          
SEQRES  23 A  504  ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS          
SEQRES  24 A  504  ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY          
SEQRES  25 A  504  GLN LYS ILE HIS SER SER THR MET ASN ASN ARG ARG ALA          
SEQRES  26 A  504  GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY          
SEQRES  27 A  504  ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU          
SEQRES  28 A  504  GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU          
SEQRES  29 A  504  LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR          
SEQRES  30 A  504  VAL GLN MET SER ALA ILE HIS THR MET HIS GLU GLY LYS          
SEQRES  31 A  504  GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG          
SEQRES  32 A  504  GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN          
SEQRES  33 A  504  GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS          
SEQRES  34 A  504  GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN          
SEQRES  35 A  504  GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY          
SEQRES  36 A  504  GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP          
SEQRES  37 A  504  ASP PHE LEU SER LYS ASP LEU ILE SER PRO THR GLU ALA          
SEQRES  38 A  504  LYS VAL LYS ARG THR ARG GLU MET GLY LYS GLY VAL ILE          
SEQRES  39 A  504  GLY LEU GLU PHE ASP SER GLU VAL LEU VAL                      
SEQRES   1 B  504  GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU          
SEQRES   2 B  504  SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS          
SEQRES   3 B  504  SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY          
SEQRES   4 B  504  THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER          
SEQRES   5 B  504  SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER          
SEQRES   6 B  504  GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE          
SEQRES   7 B  504  THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER          
SEQRES   8 B  504  ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN          
SEQRES   9 B  504  ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET          
SEQRES  10 B  504  PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN          
SEQRES  11 B  504  LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR          
SEQRES  12 B  504  GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR          
SEQRES  13 B  504  ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS          
SEQRES  14 B  504  ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO          
SEQRES  15 B  504  ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN          
SEQRES  16 B  504  LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS THR SER          
SEQRES  17 B  504  PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER          
SEQRES  18 B  504  TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN          
SEQRES  19 B  504  ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE          
SEQRES  20 B  504  LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN          
SEQRES  21 B  504  GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR          
SEQRES  22 B  504  THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN SER SER          
SEQRES  23 B  504  ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS          
SEQRES  24 B  504  ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY          
SEQRES  25 B  504  GLN LYS ILE HIS SER SER THR MET ASN ASN ARG ARG ALA          
SEQRES  26 B  504  GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY          
SEQRES  27 B  504  ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU          
SEQRES  28 B  504  GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU          
SEQRES  29 B  504  LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR          
SEQRES  30 B  504  VAL GLN MET SER ALA ILE HIS THR MET HIS GLU GLY LYS          
SEQRES  31 B  504  GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG          
SEQRES  32 B  504  GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN          
SEQRES  33 B  504  GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS          
SEQRES  34 B  504  GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN          
SEQRES  35 B  504  GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY          
SEQRES  36 B  504  GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP          
SEQRES  37 B  504  ASP PHE LEU SER LYS ASP LEU ILE SER PRO THR GLU ALA          
SEQRES  38 B  504  LYS VAL LYS ARG THR ARG GLU MET GLY LYS GLY VAL ILE          
SEQRES  39 B  504  GLY LEU GLU PHE ASP SER GLU VAL LEU VAL                      
HET    DAN  A1792      20                                                       
HET    DAN  B1792      20                                                       
HET     CL  A1793       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID                     
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  DAN    2(C11 H17 N O8)                                              
FORMUL   5  HOH   *124(H2 O1)                                                   
HELIX    1   1 ILE A  554  LYS A  559  1                                   6    
HELIX    2   2 TRP A  786  LYS A  791  1                                   6    
HELIX    3   3 ASP B  407  GLY B  411  5                                   5    
HELIX    4   4 ILE B  554  LYS B  559  1                                   6    
HELIX    5   5 ASN B  578  LYS B  582  5                                   5    
HELIX    6   6 SER B  596  SER B  601  1                                   6    
HELIX    7   7 TRP B  786  LYS B  791  1                                   6    
SHEET    1  AA 4 THR A 327  PHE A 330  0                                        
SHEET    2  AA 4 THR A 778  ASN A 785 -1  O  LEU A 779   N  ILE A 329           
SHEET    3  AA 4 GLU A 762  HIS A 769 -1  O  TYR A 763   N  PHE A 784           
SHEET    4  AA 4 ASN A 753  GLY A 759 -1  O  SER A 754   N  LEU A 766           
SHEET    1  AB 3 SER A 345  TYR A 346  0                                        
SHEET    2  AB 3 LEU A 359  ARG A 366 -1  O  ARG A 366   N  SER A 345           
SHEET    3  AB 3 ALA A 350  LYS A 353 -1  O  ALA A 350   N  GLY A 362           
SHEET    1  AC 4 SER A 345  TYR A 346  0                                        
SHEET    2  AC 4 LEU A 359  ARG A 366 -1  O  ARG A 366   N  SER A 345           
SHEET    3  AC 4 ILE A 376  SER A 383 -1  O  GLY A 377   N  GLU A 365           
SHEET    4  AC 4 VAL A 394  THR A 397 -1  O  VAL A 394   N  ILE A 380           
SHEET    1  AD 5 GLN A 552  ASP A 553  0                                        
SHEET    2  AD 5 TYR A 535  SER A 541 -1  O  MET A 538   N  GLN A 552           
SHEET    3  AD 5 ILE A 429  PHE A 436 -1  O  ILE A 429   N  SER A 541           
SHEET    4  AD 5 VAL A 414  GLN A 422 -1  O  VAL A 414   N  PHE A 436           
SHEET    5  AD 5 GLY A 571  THR A 572  1  O  GLY A 571   N  LEU A 420           
SHEET    1  AE 2 TYR A 453  ILE A 456  0                                        
SHEET    2  AE 2 LYS A 459  GLN A 462 -1  O  LYS A 459   N  ILE A 456           
SHEET    1  AF 2 TYR A 465  ARG A 466  0                                        
SHEET    2  AF 2 PHE A 528  ARG A 529 -1  O  ARG A 529   N  TYR A 465           
SHEET    1  AG 3 VAL A 493  VAL A 494  0                                        
SHEET    2  AG 3 ASP A 507  TYR A 509 -1  O  TYR A 509   N  VAL A 493           
SHEET    3  AG 3 LEU A 515  ASN A 517 -1  O  GLY A 516   N  LEU A 508           
SHEET    1  AH 3 LEU A 566  VAL A 568  0                                        
SHEET    2  AH 3 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567           
SHEET    3  AH 3 ILE A 574  VAL A 575 -1  O  ILE A 574   N  LEU A 586           
SHEET    1  AI 4 LEU A 566  VAL A 568  0                                        
SHEET    2  AI 4 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567           
SHEET    3  AI 4 SER A 603  SER A 609 -1  O  SER A 603   N  THR A 591           
SHEET    4  AI 4 HIS A 617  ALA A 618 -1  O  HIS A 617   N  TYR A 608           
SHEET    1  AJ 2 ARG A 626  VAL A 628  0                                        
SHEET    2  AJ 2 GLN A 631  ILE A 633 -1  O  GLN A 631   N  VAL A 628           
SHEET    1  AK 4 SER A 648  GLN A 652  0                                        
SHEET    2  AK 4 VAL A 658  MET A 662 -1  O  LYS A 659   N  VAL A 651           
SHEET    3  AK 4 ASP A 668  SER A 674 -1  O  GLN A 670   N  MET A 662           
SHEET    4  AK 4 LYS A 686  LYS A 692 -1  O  LYS A 686   N  VAL A 671           
SHEET    1  AL 4 SER A 699  HIS A 702  0                                        
SHEET    2  AL 4 ILE A 711  ALA A 716 -1  O  ILE A 712   N  ILE A 701           
SHEET    3  AL 4 GLU A 722  VAL A 731 -1  O  MET A 725   N  ASN A 715           
SHEET    4  AL 4 LEU A 737  GLU A 749 -1  O  THR A 738   N  ARG A 730           
SHEET    1  BA 7 THR B 327  ASP B 328  0                                        
SHEET    2  BA 7 SER B 780  PHE B 784 -1  O  PHE B 781   N  THR B 327           
SHEET    3  BA 7 GLU B 762  HIS B 769 -1  O  TYR B 763   N  PHE B 784           
SHEET    4  BA 7 LEU B 737  GLY B 759 -1  N  ALA B 751   O  GLU B 768           
SHEET    5  BA 7 GLU B 722  VAL B 731 -1  N  ASN B 723   O  GLY B 748           
SHEET    6  BA 7 ILE B 711  ASN B 715 -1  O  ILE B 711   N  ALA B 729           
SHEET    7  BA 7 SER B 699  HIS B 702 -1  O  SER B 699   N  SER B 714           
SHEET    1  BB 4 SER B 345  LYS B 353  0                                        
SHEET    2  BB 4 LEU B 359  ARG B 366 -1  O  ILE B 360   N  LEU B 352           
SHEET    3  BB 4 ILE B 376  SER B 383 -1  O  GLY B 377   N  GLU B 365           
SHEET    4  BB 4 VAL B 394  THR B 397 -1  O  VAL B 394   N  ILE B 380           
SHEET    1  BC 5 GLN B 552  ASP B 553  0                                        
SHEET    2  BC 5 TYR B 535  SER B 541 -1  O  MET B 538   N  GLN B 552           
SHEET    3  BC 5 ILE B 429  PHE B 436 -1  O  ILE B 429   N  SER B 541           
SHEET    4  BC 5 VAL B 414  GLN B 422 -1  O  VAL B 414   N  PHE B 436           
SHEET    5  BC 5 GLY B 571  THR B 572  1  O  GLY B 571   N  LEU B 420           
SHEET    1  BD 7 TYR B 453  LYS B 455  0                                        
SHEET    2  BD 7 THR B 460  ARG B 466 -1  O  TYR B 461   N  LYS B 454           
SHEET    3  BD 7 THR B 474  ILE B 475 -1  O  ILE B 475   N  GLN B 462           
SHEET    4  BD 7 THR B 480  TYR B 482 -1  O  TYR B 482   N  THR B 474           
SHEET    5  BD 7 ALA B 488  VAL B 494 -1  N  THR B 489   O  VAL B 481           
SHEET    6  BD 7 ASP B 507  LYS B 510 -1  O  TYR B 509   N  VAL B 493           
SHEET    7  BD 7 GLN B 513  ASN B 517 -1  O  GLN B 513   N  LYS B 510           
SHEET    1  BE 3 TYR B 453  LYS B 455  0                                        
SHEET    2  BE 3 THR B 460  ARG B 466 -1  O  TYR B 461   N  LYS B 454           
SHEET    3  BE 3 PHE B 528  ILE B 530 -1  O  ARG B 529   N  TYR B 465           
SHEET    1  BF 7 LEU B 566  VAL B 568  0                                        
SHEET    2  BF 7 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567           
SHEET    3  BF 7 ILE B 574  VAL B 575 -1  O  ILE B 574   N  LEU B 586           
SHEET    4  BF 7 ILE B 585  THR B 591 -1  O  LEU B 586   N  ILE B 574           
SHEET    5  BF 7 HIS B 617  ALA B 618                                           
SHEET    6  BF 7 SER B 603  SER B 609 -1  O  TYR B 608   N  HIS B 617           
SHEET    7  BF 7 ILE B 585  THR B 591 -1  O  ILE B 585   N  SER B 609           
SHEET    1  BG 2 ARG B 626  VAL B 628  0                                        
SHEET    2  BG 2 GLN B 631  ILE B 633 -1  O  GLN B 631   N  VAL B 628           
SHEET    1  BH 4 SER B 648  GLN B 652  0                                        
SHEET    2  BH 4 VAL B 658  MET B 662 -1  O  LYS B 659   N  VAL B 651           
SHEET    3  BH 4 ASP B 668  SER B 674 -1  O  GLN B 670   N  MET B 662           
SHEET    4  BH 4 LYS B 686  LYS B 692 -1  O  LYS B 686   N  VAL B 671           
CISPEP   1 LYS A  708    GLU A  709          0       -18.28                     
CISPEP   2 GLY A  718    PRO A  719          0        -6.62                     
CISPEP   3 ASN A  734    GLY A  735          0       -10.72                     
CISPEP   4 ALA A  776    TYR A  777          0        -8.46                     
CISPEP   5 GLY B  458    LYS B  459          0        -9.99                     
CISPEP   6 LYS B  708    GLU B  709          0         1.77                     
CISPEP   7 GLY B  718    PRO B  719          0        -2.66                     
CISPEP   8 ASN B  734    GLY B  735          0         0.23                     
CISPEP   9 ALA B  776    TYR B  777          0         0.42                     
CISPEP  10 ASN B  785    TRP B  786          0        -7.97                     
SITE     1 AC1 16 ARG A 347  ILE A 348  ARG A 366  ASP A 372                    
SITE     2 AC1 16 ILE A 416  ASP A 417  ASP A 434  ILE A 442                    
SITE     3 AC1 16 TYR A 590  LEU A 598  GLN A 602  ARG A 663                    
SITE     4 AC1 16 TYR A 695  ARG A 721  TYR A 752  HOH A2094                    
SITE     1 AC2 14 ARG B 347  ILE B 348  ARG B 366  ASP B 372                    
SITE     2 AC2 14 ILE B 416  ASP B 417  ASP B 434  ILE B 442                    
SITE     3 AC2 14 TYR B 590  GLN B 602  ARG B 663  TYR B 695                    
SITE     4 AC2 14 ARG B 721  TYR B 752                                          
SITE     1 AC3  6 GLY A 516  ASN A 517  PHE A 520  LYS A 524                    
SITE     2 AC3  6 THR A 525  SER A 526                                          
CRYST1   49.206   95.626  226.596  90.00  90.00  90.00 P 21 21 21    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      0.020323  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010457  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004413        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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