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Database: PDB
Entry: 2W20
LinkDB: 2W20
Original site: 2W20 
HEADER    HYDROLASE                               21-OCT-08   2W20              
TITLE     STRUCTURE OF THE CATALYTIC DOMAIN OF THE NATIVE NANA                  
TITLE    2 SIALIDASE FROM STREPTOCOCCUS PNEUMONIAE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE A;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 321-791;                        
COMPND   5 SYNONYM: NEURAMINIDASE A, NANA SIALIDASE;                            
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: 171101;                                              
SOURCE   4 STRAIN: R6;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    SECRETED, CELL WALL, HYDROLASE, SIALIDASE, GLYCOSIDASE,               
KEYWDS   2 NEURAMINIDASE, PEPTIDOGLYCAN-ANCHOR                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.XU,P.W.ANDREW,G.L.TAYLOR                                            
REVDAT   2   10-NOV-09 2W20    1       REMARK                                   
REVDAT   1   23-DEC-08 2W20    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.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 159301                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8003                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 40.2411 -  4.6338    0.88     4899   235  0.1801 0.1815        
REMARK   3     2  4.6338 -  3.6788    0.94     4991   261  0.1602 0.1778        
REMARK   3     3  3.6788 -  3.2140    0.96     5049   270  0.1735 0.1950        
REMARK   3     4  3.2140 -  2.9202    0.96     5019   279  0.1878 0.2126        
REMARK   3     5  2.9202 -  2.7109    0.97     5067   294  0.1971 0.2355        
REMARK   3     6  2.7109 -  2.5511    0.98     5060   256  0.2015 0.2253        
REMARK   3     7  2.5511 -  2.4234    0.98     5093   270  0.1966 0.2055        
REMARK   3     8  2.4234 -  2.3179    0.98     5059   276  0.1986 0.2409        
REMARK   3     9  2.3179 -  2.2287    0.98     5055   277  0.1976 0.2144        
REMARK   3    10  2.2287 -  2.1518    0.99     5035   273  0.1915 0.2150        
REMARK   3    11  2.1518 -  2.0845    0.99     5112   299  0.1935 0.2095        
REMARK   3    12  2.0845 -  2.0249    0.99     5086   262  0.1910 0.2290        
REMARK   3    13  2.0249 -  1.9716    0.99     5073   270  0.1990 0.2439        
REMARK   3    14  1.9716 -  1.9235    0.99     5160   256  0.1974 0.2232        
REMARK   3    15  1.9235 -  1.8798    1.00     5074   281  0.1920 0.2134        
REMARK   3    16  1.8798 -  1.8398    1.00     5195   244  0.2007 0.2489        
REMARK   3    17  1.8398 -  1.8030    1.00     5064   274  0.2065 0.2343        
REMARK   3    18  1.8030 -  1.7690    1.00     5143   256  0.2022 0.2475        
REMARK   3    19  1.7690 -  1.7374    1.00     5078   272  0.2160 0.2649        
REMARK   3    20  1.7374 -  1.7079    0.99     5120   276  0.2140 0.2659        
REMARK   3    21  1.7079 -  1.6804    0.99     5016   281  0.2105 0.2496        
REMARK   3    22  1.6804 -  1.6545    0.99     5112   263  0.2071 0.2284        
REMARK   3    23  1.6545 -  1.6302    0.99     4977   264  0.2200 0.2953        
REMARK   3    24  1.6302 -  1.6072    0.98     5067   281  0.2225 0.2551        
REMARK   3    25  1.6072 -  1.5855    0.99     5038   260  0.2305 0.2766        
REMARK   3    26  1.5855 -  1.5649    0.98     5060   262  0.2430 0.2652        
REMARK   3    27  1.5649 -  1.5453    0.98     5004   251  0.2422 0.2605        
REMARK   3    28  1.5453 -  1.5267    0.99     5002   252  0.2471 0.2609        
REMARK   3    29  1.5267 -  1.5090    0.97     5003   249  0.2475 0.2620        
REMARK   3    30  1.5090 -  1.4920    0.90     4587   259  0.2624 0.2845        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 45.55                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.870           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.85                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.81280                                              
REMARK   3    B22 (A**2) : -1.01710                                             
REMARK   3    B33 (A**2) : -1.79570                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.000           7630                                  
REMARK   3   ANGLE     :  1.220          10302                                  
REMARK   3   CHIRALITY :  0.110           1083                                  
REMARK   3   PLANARITY :  0.000           1343                                  
REMARK   3   DIHEDRAL  : 17.270           2825                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2W20 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-37899.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 159417                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.49                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.9                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG4K, 0.1 M MES PH6.0               
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       23.60000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      109.10000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      109.10000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.60000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.30000            
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 GENERATING THE BIOMOLECULE                                           
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     LYS A   791                                                      
REMARK 465     ALA B   321                                                      
REMARK 465     LYS B   791                                                      
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    ILE A 348       71.12     71.52                                   
REMARK 500    HIS A 369      176.07    178.88                                   
REMARK 500    ASP A 372       46.42    -80.00                                   
REMARK 500    ASP A 417      103.99     71.41                                   
REMARK 500    ARG A 476     -149.64   -112.49                                   
REMARK 500    LYS A 564      -87.70    -89.99                                   
REMARK 500    HIS A 597     -124.38     41.63                                   
REMARK 500    THR A 646     -119.10   -123.09                                   
REMARK 500    TYR A 695       68.28     73.46                                   
REMARK 500    LYS A 720     -158.49   -103.73                                   
REMARK 500    GLU A 733       50.36    -92.13                                   
REMARK 500    ALA A 751     -116.16   -132.84                                   
REMARK 500    ASN B 339     -169.34    -79.78                                   
REMARK 500    ILE B 348       68.92     70.25                                   
REMARK 500    HIS B 369      176.81    179.12                                   
REMARK 500    ASP B 372       45.13    -76.15                                   
REMARK 500    ASP B 417      103.00     71.14                                   
REMARK 500    ARG B 476     -152.13   -117.04                                   
REMARK 500    ASP B 533     -156.11   -128.66                                   
REMARK 500    LYS B 564      -86.15    -89.66                                   
REMARK 500    HIS B 597     -126.33     44.67                                   
REMARK 500    THR B 646     -117.83   -120.39                                   
REMARK 500    TYR B 695       70.33     71.33                                   
REMARK 500    LYS B 720     -152.53   -107.00                                   
REMARK 500    GLU B 733     -120.25     30.10                                   
REMARK 500    ALA B 751     -120.88   -133.86                                   
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 MES A1791                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B1791                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1792                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1792                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1793                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1793                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1794                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1795                 
DBREF  2W20 A  321   791  UNP    P62576   NANA_STRR6     321    791             
DBREF  2W20 B  321   791  UNP    P62576   NANA_STRR6     321    791             
SEQRES   1 A  471  ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU SER GLY          
SEQRES   2 A  471  ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS SER TYR          
SEQRES   3 A  471  ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY THR LEU          
SEQRES   4 A  471  ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER SER ASP          
SEQRES   5 A  471  TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER GLU ASP          
SEQRES   6 A  471  ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE THR ASN          
SEQRES   7 A  471  LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER ILE GLY          
SEQRES   8 A  471  SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN ASP PRO          
SEQRES   9 A  471  GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET PHE PRO          
SEQRES  10 A  471  GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN LYS GLU          
SEQRES  11 A  471  GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR GLN ILE          
SEQRES  12 A  471  LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR ILE ARG          
SEQRES  13 A  471  GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS ALA THR          
SEQRES  14 A  471  ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO ALA TYR          
SEQRES  15 A  471  SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN LEU LEU          
SEQRES  16 A  471  GLY ASN ILE TYR PHE THR THR ASN LYS THR SER PRO PHE          
SEQRES  17 A  471  ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER TYR SER          
SEQRES  18 A  471  ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN ASP ILE          
SEQRES  19 A  471  THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE LEU GLY          
SEQRES  20 A  471  VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN GLY PRO          
SEQRES  21 A  471  HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR THR ASN          
SEQRES  22 A  471  ASN VAL SER HIS LEU ASN GLY SER GLN SER SER ARG ILE          
SEQRES  23 A  471  ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS ALA GLY          
SEQRES  24 A  471  GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY GLN LYS          
SEQRES  25 A  471  ILE HIS SER SER THR MET ASN ASN ARG ARG ALA GLN ASN          
SEQRES  26 A  471  THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY ASP VAL          
SEQRES  27 A  471  LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU GLN VAL          
SEQRES  28 A  471  ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU LYS ASP          
SEQRES  29 A  471  ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR VAL GLN          
SEQRES  30 A  471  MET SER ALA ILE HIS THR MET HIS GLU GLY LYS GLU TYR          
SEQRES  31 A  471  ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG GLU ASN          
SEQRES  32 A  471  GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN GLY GLU          
SEQRES  33 A  471  LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS GLY GLU          
SEQRES  34 A  471  PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN GLY GLU          
SEQRES  35 A  471  TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY GLN ASN          
SEQRES  36 A  471  ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP ASP PHE          
SEQRES  37 A  471  LEU SER LYS                                                  
SEQRES   1 B  471  ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU SER GLY          
SEQRES   2 B  471  ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS SER TYR          
SEQRES   3 B  471  ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY THR LEU          
SEQRES   4 B  471  ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER SER ASP          
SEQRES   5 B  471  TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER GLU ASP          
SEQRES   6 B  471  ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE THR ASN          
SEQRES   7 B  471  LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER ILE GLY          
SEQRES   8 B  471  SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN ASP PRO          
SEQRES   9 B  471  GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET PHE PRO          
SEQRES  10 B  471  GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN LYS GLU          
SEQRES  11 B  471  GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR GLN ILE          
SEQRES  12 B  471  LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR ILE ARG          
SEQRES  13 B  471  GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS ALA THR          
SEQRES  14 B  471  ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO ALA TYR          
SEQRES  15 B  471  SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN LEU LEU          
SEQRES  16 B  471  GLY ASN ILE TYR PHE THR THR ASN LYS THR SER PRO PHE          
SEQRES  17 B  471  ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER TYR SER          
SEQRES  18 B  471  ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN ASP ILE          
SEQRES  19 B  471  THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE LEU GLY          
SEQRES  20 B  471  VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN GLY PRO          
SEQRES  21 B  471  HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR THR ASN          
SEQRES  22 B  471  ASN VAL SER HIS LEU ASN GLY SER GLN SER SER ARG ILE          
SEQRES  23 B  471  ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS ALA GLY          
SEQRES  24 B  471  GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY GLN LYS          
SEQRES  25 B  471  ILE HIS SER SER THR MET ASN ASN ARG ARG ALA GLN ASN          
SEQRES  26 B  471  THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY ASP VAL          
SEQRES  27 B  471  LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU GLN VAL          
SEQRES  28 B  471  ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU LYS ASP          
SEQRES  29 B  471  ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR VAL GLN          
SEQRES  30 B  471  MET SER ALA ILE HIS THR MET HIS GLU GLY LYS GLU TYR          
SEQRES  31 B  471  ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG GLU ASN          
SEQRES  32 B  471  GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN GLY GLU          
SEQRES  33 B  471  LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS GLY GLU          
SEQRES  34 B  471  PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN GLY GLU          
SEQRES  35 B  471  TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY GLN ASN          
SEQRES  36 B  471  ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP ASP PHE          
SEQRES  37 B  471  LEU SER LYS                                                  
HET    MES  A1791      12                                                       
HET    MES  B1791      12                                                       
HET     CL  B1792       1                                                       
HET     CL  A1792       1                                                       
HET     CL  A1793       1                                                       
HET    GOL  B1793       6                                                       
HET    GOL  A1794       6                                                       
HET    GOL  A1795       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   3  GOL    3(C3 H8 O3)                                                  
FORMUL   4   CL    3(CL 1-)                                                     
FORMUL   5  MES    2(C6 H13 N O4 S)                                             
FORMUL   6  HOH   *1025(H2 O1)                                                  
HELIX    1   1 ASP A  407  GLY A  411  5                                   5    
HELIX    2   2 LYS A  440  MET A  445  5                                   6    
HELIX    3   3 LYS A  499  SER A  503  5                                   5    
HELIX    4   4 ILE A  554  LYS A  559  1                                   6    
HELIX    5   5 SER A  596  SER A  601  1                                   6    
HELIX    6   6 ASN A  640  GLN A  644  5                                   5    
HELIX    7   7 TRP A  786  SER A  790  1                                   5    
HELIX    8   8 ASP B  407  GLY B  411  5                                   5    
HELIX    9   9 LYS B  440  MET B  445  5                                   6    
HELIX   10  10 LYS B  499  SER B  503  5                                   5    
HELIX   11  11 ILE B  554  LYS B  559  1                                   6    
HELIX   12  12 SER B  596  SER B  601  1                                   6    
HELIX   13  13 ASN B  640  GLN B  644  5                                   5    
HELIX   14  14 TRP B  786  SER B  790  1                                   5    
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 4 SER A 345  LYS A 353  0                                        
SHEET    2  AB 4 LEU A 359  ARG A 366 -1  O  ILE A 360   N  LEU A 352           
SHEET    3  AB 4 ILE A 376  SER A 383 -1  O  GLY A 377   N  GLU A 365           
SHEET    4  AB 4 VAL A 394  THR A 397 -1  O  VAL A 394   N  ILE A 380           
SHEET    1  AC 5 GLN A 552  ASP A 553  0                                        
SHEET    2  AC 5 TYR A 535  SER A 541 -1  O  MET A 538   N  GLN A 552           
SHEET    3  AC 5 ILE A 429  PHE A 436 -1  O  ILE A 429   N  SER A 541           
SHEET    4  AC 5 VAL A 414  GLN A 422 -1  O  VAL A 414   N  PHE A 436           
SHEET    5  AC 5 GLY A 571  THR A 572  1  O  GLY A 571   N  LEU A 420           
SHEET    1  AD 7 TYR A 453  ILE A 456  0                                        
SHEET    2  AD 7 LYS A 459  ARG A 466 -1  O  LYS A 459   N  ILE A 456           
SHEET    3  AD 7 TYR A 473  ILE A 475 -1  O  TYR A 473   N  LEU A 464           
SHEET    4  AD 7 THR A 480  TYR A 482 -1  O  TYR A 482   N  THR A 474           
SHEET    5  AD 7 ALA A 488  VAL A 493 -1  N  THR A 489   O  VAL A 481           
SHEET    6  AD 7 ASP A 507  LYS A 510 -1  O  TYR A 509   N  ARG A 492           
SHEET    7  AD 7 GLN A 513  ASN A 517 -1  O  GLN A 513   N  LYS A 510           
SHEET    1  AE 3 TYR A 453  ILE A 456  0                                        
SHEET    2  AE 3 LYS A 459  ARG A 466 -1  O  LYS A 459   N  ILE A 456           
SHEET    3  AE 3 PHE A 528  ARG A 529 -1  O  ARG A 529   N  TYR A 465           
SHEET    1  AF 3 LEU A 566  VAL A 568  0                                        
SHEET    2  AF 3 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567           
SHEET    3  AF 3 ILE A 574  VAL A 575 -1  O  ILE A 574   N  LEU A 586           
SHEET    1  AG 4 LEU A 566  VAL A 568  0                                        
SHEET    2  AG 4 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567           
SHEET    3  AG 4 SER A 603  SER A 609 -1  O  SER A 603   N  THR A 591           
SHEET    4  AG 4 HIS A 617  ALA A 618 -1  O  HIS A 617   N  TYR A 608           
SHEET    1  AH 2 ARG A 626  VAL A 628  0                                        
SHEET    2  AH 2 GLN A 631  ILE A 633 -1  O  GLN A 631   N  VAL A 628           
SHEET    1  AI 4 SER A 648  GLN A 652  0                                        
SHEET    2  AI 4 VAL A 658  MET A 662 -1  O  LYS A 659   N  VAL A 651           
SHEET    3  AI 4 ASP A 668  SER A 674 -1  O  GLN A 670   N  MET A 662           
SHEET    4  AI 4 LYS A 686  LYS A 692 -1  O  LYS A 686   N  VAL A 671           
SHEET    1  AJ 4 SER A 699  HIS A 705  0                                        
SHEET    2  AJ 4 LYS A 708  ALA A 716 -1  O  LYS A 708   N  HIS A 705           
SHEET    3  AJ 4 GLU A 722  VAL A 731 -1  O  MET A 725   N  ASN A 715           
SHEET    4  AJ 4 LEU A 737  GLU A 749 -1  O  THR A 738   N  ARG A 730           
SHEET    1  BA 4 THR B 327  PHE B 330  0                                        
SHEET    2  BA 4 THR B 778  ASN B 785 -1  O  LEU B 779   N  ILE B 329           
SHEET    3  BA 4 GLU B 762  HIS B 769 -1  O  TYR B 763   N  PHE B 784           
SHEET    4  BA 4 ASN B 753  GLY B 759 -1  O  SER B 754   N  LEU B 766           
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  ILE B 456  0                                        
SHEET    2  BD 7 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456           
SHEET    3  BD 7 TYR B 473  ILE B 475 -1  O  TYR B 473   N  LEU B 464           
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 493 -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  ARG B 492           
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  ILE B 456  0                                        
SHEET    2  BE 3 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456           
SHEET    3  BE 3 PHE B 528  ARG B 529 -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           
SHEET    1  BI 4 SER B 699  HIS B 705  0                                        
SHEET    2  BI 4 LYS B 708  ALA B 716 -1  O  LYS B 708   N  HIS B 705           
SHEET    3  BI 4 GLU B 722  VAL B 731 -1  O  MET B 725   N  ASN B 715           
SHEET    4  BI 4 LEU B 737  GLU B 749 -1  O  THR B 738   N  ARG B 730           
CISPEP   1 GLY A  718    PRO A  719          0         6.25                     
CISPEP   2 ASN A  734    GLY A  735          0         0.36                     
CISPEP   3 ALA A  776    TYR A  777          0       -12.76                     
CISPEP   4 GLY B  718    PRO B  719          0         5.75                     
CISPEP   5 ALA B  776    TYR B  777          0        -6.02                     
SITE     1 AC1 10 TYR A 465  ARG A 466  GLU A 467  GLY A 468                    
SITE     2 AC1 10 GLU A 469  ARG A 529  HOH A2559  HOH A2560                    
SITE     3 AC1 10 ASN B 625  LYS B 632                                          
SITE     1 AC2 12 ASN A 625  LYS A 632  GLU B 450  TYR B 465                    
SITE     2 AC2 12 ARG B 466  GLU B 467  GLY B 468  GLU B 469                    
SITE     3 AC2 12 LYS B 470  ARG B 529  GOL B1793  HOH B2465                    
SITE     1 AC3  4 ASN B 517  LYS B 524  THR B 525  SER B 526                    
SITE     1 AC4  5 GLY A 516  ASN A 517  LYS A 524  THR A 525                    
SITE     2 AC4  5 SER A 526                                                     
SITE     1 AC5  4 VAL A 628  GLN A 631  HOH A2396  HOH A2403                    
SITE     1 AC6  6 GLN A 627  LYS A 632  LYS A 683  GLU B 469                    
SITE     2 AC6  6 LYS B 470  MES B1791                                          
SITE     1 AC7  7 ASP A 385  ASN A 386  GLU A 762  LYS A 783                    
SITE     2 AC7  7 HOH A2057  ASP B 490  LYS B 510                               
SITE     1 AC8  6 SER A 371  TRP A 373  SER A 409  ILE A 410                    
SITE     2 AC8  6 GLU A 425  HIS A 612                                          
CRYST1   47.200   96.600  218.200  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      0.021186  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010352  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004583        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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