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Database: PDB
Entry: 3H73
LinkDB: 3H73
Original site: 3H73 
HEADER    HYDROLASE                               24-APR-09   3H73              
TITLE     CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE D39                     
TITLE    2 NEURAMINIDASE A PRECURSOR (NANA) IN COMPLEX WITH DANA                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE A;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 317-793;                                      
COMPND   5 SYNONYM: 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: 171101;                                              
SOURCE   4 STRAIN: R6;                                                          
SOURCE   5 GENE: NANA, SPR1536;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28A                                
KEYWDS    SIX-BLADED BETA-PROPELLER, CELL WALL, GLYCOSIDASE,                    
KEYWDS   2 HYDROLASE, PEPTIDOGLYCAN-ANCHOR, SECRETED                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.-S.HSIAO,L.TONG                                                     
REVDAT   1   12-MAY-09 3H73    0                                                
JRNL        AUTH   Y.-S.HSIAO,D.PARKER,A.J.RATNER,A.PRINCE,L.TONG               
JRNL        TITL   CRYSTAL STRUCTURES OF RESPIRATORY PATHOGEN                   
JRNL        TITL 2 NEURAMINIDASES                                               
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 380   467 2009              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   19284989                                                     
JRNL        DOI    10.1016/J.BBRC.2009.01.108                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 734818.060                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 93563                          
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 SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7032                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 13240                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050                       
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1074                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7518                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 1539                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.61000                                             
REMARK   3    B22 (A**2) : 0.85000                                              
REMARK   3    B33 (A**2) : 0.76000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.44000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.12                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.83                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.050 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.600 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.830 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.600 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 37.93                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : DAN.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : DAN.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3H73 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052774.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93762                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.5410                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 14.600                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: COMO                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 30% JEFFAMINE ED-          
REMARK 280  2001, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       79.17000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.17000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.70000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A   317                                                      
REMARK 465     PRO A   318                                                      
REMARK 465     GLU A   319                                                      
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   OG1  THR B   591     O    HOH B  1497              2.15            
REMARK 500   O    ASP A   417     O    HOH A  1159              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 348       73.76     59.34                                   
REMARK 500    HIS A 369     -177.79   -175.80                                   
REMARK 500    TRP A 373     -173.05   -172.13                                   
REMARK 500    ASP A 417      112.10     70.10                                   
REMARK 500    ARG A 476     -157.53   -113.04                                   
REMARK 500    LYS A 564      -81.22    -92.77                                   
REMARK 500    HIS A 597     -125.35     40.97                                   
REMARK 500    ARG A 605     -177.72   -172.15                                   
REMARK 500    THR A 646     -111.03   -113.76                                   
REMARK 500    TYR A 695       66.17     75.07                                   
REMARK 500    LYS A 720     -146.93   -105.63                                   
REMARK 500    ASN A 723       71.89     59.27                                   
REMARK 500    ALA A 751     -116.03   -131.96                                   
REMARK 500    LYS A 772       17.24     58.12                                   
REMARK 500    SER A 790      -83.65    -86.85                                   
REMARK 500    ILE B 348       70.24     59.25                                   
REMARK 500    TRP B 373     -173.72   -173.75                                   
REMARK 500    ASP B 417      111.37     62.30                                   
REMARK 500    VAL B 421      146.04   -170.34                                   
REMARK 500    ARG B 476     -156.14   -106.74                                   
REMARK 500    LYS B 564      -83.81    -93.07                                   
REMARK 500    HIS B 597     -123.54     38.07                                   
REMARK 500    ARG B 605     -175.19   -175.23                                   
REMARK 500    ASN B 639       68.98   -153.49                                   
REMARK 500    THR B 646     -114.00   -110.68                                   
REMARK 500    ASP B 684      101.27     63.51                                   
REMARK 500    TYR B 695       66.42     69.71                                   
REMARK 500    LYS B 720     -156.80   -102.00                                   
REMARK 500    ASN B 723       70.55     53.65                                   
REMARK 500    HIS B 742       46.19   -144.20                                   
REMARK 500    ALA B 751     -115.62   -132.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A 900                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3H6J   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A PUTATIVE NEURAMINIDASE FROM                   
REMARK 900 PSEUDOMONAS AERUGINOSA                                               
REMARK 900 RELATED ID: 3H71   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE D39                    
REMARK 900 NEURAMINIDASE A PRECURSOR (NANA), FREE ENZYME                        
REMARK 900 RELATED ID: 3H72   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE D39                    
REMARK 900 NEURAMINIDASE A PRECURSOR (NANA) IN COMPLEX WITH NANA                
DBREF  3H73 A  317   793  UNP    P62576   NANA_STRR6     317    793             
DBREF  3H73 B  317   793  UNP    P62576   NANA_STRR6     317    793             
SEQRES   1 A  477  LEU PRO GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE          
SEQRES   2 A  477  PHE GLU SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY          
SEQRES   3 A  477  ILE LYS SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP          
SEQRES   4 A  477  LYS GLY THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU          
SEQRES   5 A  477  HIS SER SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG          
SEQRES   6 A  477  ARG SER GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL          
SEQRES   7 A  477  THR ILE THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP          
SEQRES   8 A  477  PRO SER ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU          
SEQRES   9 A  477  VAL GLN ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR          
SEQRES  10 A  477  ASP MET PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER          
SEQRES  11 A  477  SER GLN LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS          
SEQRES  12 A  477  THR TYR GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA          
SEQRES  13 A  477  TYR THR ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP          
SEQRES  14 A  477  GLY LYS ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL          
SEQRES  15 A  477  LYS PRO ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY          
SEQRES  16 A  477  ASN GLN LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS          
SEQRES  17 A  477  THR SER PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP          
SEQRES  18 A  477  MET SER TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA          
SEQRES  19 A  477  PRO GLN ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET          
SEQRES  20 A  477  LYS PHE LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU          
SEQRES  21 A  477  ARG ASN GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL          
SEQRES  22 A  477  TYR THR THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN          
SEQRES  23 A  477  SER SER ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR          
SEQRES  24 A  477  TRP HIS ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL          
SEQRES  25 A  477  ASP GLY GLN LYS ILE HIS SER SER THR MET ASN ASN ARG          
SEQRES  26 A  477  ARG ALA GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN          
SEQRES  27 A  477  ASN GLY ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY          
SEQRES  28 A  477  ASP LEU GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR          
SEQRES  29 A  477  TRP GLU LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP          
SEQRES  30 A  477  VAL TYR VAL GLN MET SER ALA ILE HIS THR MET HIS GLU          
SEQRES  31 A  477  GLY LYS GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO          
SEQRES  32 A  477  LYS ARG GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU          
SEQRES  33 A  477  GLU ASN GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE          
SEQRES  34 A  477  GLN LYS GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU          
SEQRES  35 A  477  GLY ASN GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU          
SEQRES  36 A  477  LYS GLY GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE          
SEQRES  37 A  477  ASN TRP ASP PHE LEU SER LYS ASP LEU                          
SEQRES   1 B  477  LEU PRO GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE          
SEQRES   2 B  477  PHE GLU SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY          
SEQRES   3 B  477  ILE LYS SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP          
SEQRES   4 B  477  LYS GLY THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU          
SEQRES   5 B  477  HIS SER SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG          
SEQRES   6 B  477  ARG SER GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL          
SEQRES   7 B  477  THR ILE THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP          
SEQRES   8 B  477  PRO SER ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU          
SEQRES   9 B  477  VAL GLN ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR          
SEQRES  10 B  477  ASP MET PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER          
SEQRES  11 B  477  SER GLN LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS          
SEQRES  12 B  477  THR TYR GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA          
SEQRES  13 B  477  TYR THR ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP          
SEQRES  14 B  477  GLY LYS ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL          
SEQRES  15 B  477  LYS PRO ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY          
SEQRES  16 B  477  ASN GLN LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS          
SEQRES  17 B  477  THR SER PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP          
SEQRES  18 B  477  MET SER TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA          
SEQRES  19 B  477  PRO GLN ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET          
SEQRES  20 B  477  LYS PHE LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU          
SEQRES  21 B  477  ARG ASN GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL          
SEQRES  22 B  477  TYR THR THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN          
SEQRES  23 B  477  SER SER ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR          
SEQRES  24 B  477  TRP HIS ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL          
SEQRES  25 B  477  ASP GLY GLN LYS ILE HIS SER SER THR MET ASN ASN ARG          
SEQRES  26 B  477  ARG ALA GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN          
SEQRES  27 B  477  ASN GLY ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY          
SEQRES  28 B  477  ASP LEU GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR          
SEQRES  29 B  477  TRP GLU LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP          
SEQRES  30 B  477  VAL TYR VAL GLN MET SER ALA ILE HIS THR MET HIS GLU          
SEQRES  31 B  477  GLY LYS GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO          
SEQRES  32 B  477  LYS ARG GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU          
SEQRES  33 B  477  GLU ASN GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE          
SEQRES  34 B  477  GLN LYS GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU          
SEQRES  35 B  477  GLY ASN GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU          
SEQRES  36 B  477  LYS GLY GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE          
SEQRES  37 B  477  ASN TRP ASP PHE LEU SER LYS ASP LEU                          
HET    DAN  A 900      20                                                       
HET    DAN  B 901      20                                                       
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID                     
FORMUL   3  DAN    2(C11 H17 N O8)                                              
FORMUL   5  HOH   *1539(H2 O)                                                   
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 TRP B  786  LYS B  791  1                                   6    
SHEET    1   A 4 THR A 327  PHE A 330  0                                        
SHEET    2   A 4 THR A 778  ASN A 785 -1  O  PHE A 781   N  THR A 327           
SHEET    3   A 4 GLU A 762  HIS A 769 -1  N  TYR A 763   O  PHE A 784           
SHEET    4   A 4 ASN A 753  GLY A 759 -1  N  GLN A 756   O  GLY A 764           
SHEET    1   B 4 SER A 345  LYS A 353  0                                        
SHEET    2   B 4 LEU A 359  ARG A 366 -1  O  ASP A 364   N  ARG A 347           
SHEET    3   B 4 ILE A 376  SER A 383 -1  O  GLY A 377   N  GLU A 365           
SHEET    4   B 4 VAL A 394  THR A 397 -1  O  ILE A 396   N  MET A 378           
SHEET    1   C 5 GLN A 552  ASP A 553  0                                        
SHEET    2   C 5 TYR A 535  SER A 541 -1  N  MET A 538   O  GLN A 552           
SHEET    3   C 5 ILE A 429  PHE A 436 -1  N  TYR A 433   O  TRP A 537           
SHEET    4   C 5 VAL A 414  GLN A 422 -1  N  VAL A 421   O  PHE A 430           
SHEET    5   C 5 GLY A 571  THR A 572  1  O  GLY A 571   N  LEU A 420           
SHEET    1   D 7 TYR A 453  LYS A 455  0                                        
SHEET    2   D 7 THR A 460  LEU A 464 -1  O  TYR A 461   N  LYS A 454           
SHEET    3   D 7 TYR A 473  ILE A 475 -1  O  TYR A 473   N  LEU A 464           
SHEET    4   D 7 THR A 480  TYR A 482 -1  O  TYR A 482   N  THR A 474           
SHEET    5   D 7 ALA A 488  VAL A 493 -1  O  TYR A 491   N  VAL A 481           
SHEET    6   D 7 ASP A 507  LYS A 510 -1  O  TYR A 509   N  ARG A 492           
SHEET    7   D 7 GLN A 513  ASN A 517 -1  O  LEU A 515   N  LEU A 508           
SHEET    1   E 3 LEU A 566  VAL A 568  0                                        
SHEET    2   E 3 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567           
SHEET    3   E 3 ILE A 574  VAL A 575 -1  N  ILE A 574   O  LEU A 586           
SHEET    1   F 4 LEU A 566  VAL A 568  0                                        
SHEET    2   F 4 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567           
SHEET    3   F 4 SER A 603  SER A 609 -1  O  ARG A 605   N  VAL A 589           
SHEET    4   F 4 HIS A 617  ALA A 618 -1  O  HIS A 617   N  TYR A 608           
SHEET    1   G 2 ARG A 626  VAL A 628  0                                        
SHEET    2   G 2 GLN A 631  ILE A 633 -1  O  GLN A 631   N  VAL A 628           
SHEET    1   H 4 SER A 648  GLN A 652  0                                        
SHEET    2   H 4 VAL A 658  MET A 662 -1  O  LYS A 659   N  VAL A 651           
SHEET    3   H 4 ASP A 668  SER A 674 -1  O  SER A 674   N  VAL A 658           
SHEET    4   H 4 LYS A 686  LYS A 692 -1  O  LYS A 686   N  VAL A 671           
SHEET    1   I 4 SER A 699  HIS A 705  0                                        
SHEET    2   I 4 LYS A 708  ALA A 716 -1  O  TYR A 710   N  THR A 703           
SHEET    3   I 4 GLU A 722  VAL A 731 -1  O  HIS A 727   N  LEU A 713           
SHEET    4   I 4 LEU A 737  GLU A 749 -1  O  THR A 738   N  ARG A 730           
SHEET    1   J 4 THR B 327  PHE B 330  0                                        
SHEET    2   J 4 THR B 778  ASN B 785 -1  O  PHE B 781   N  THR B 327           
SHEET    3   J 4 GLU B 762  HIS B 769 -1  N  TYR B 763   O  PHE B 784           
SHEET    4   J 4 ASN B 753  GLY B 759 -1  N  GLN B 756   O  GLY B 764           
SHEET    1   K 4 SER B 345  LYS B 353  0                                        
SHEET    2   K 4 LEU B 359  ARG B 366 -1  O  ASP B 364   N  ARG B 347           
SHEET    3   K 4 ILE B 376  SER B 383 -1  O  GLY B 377   N  GLU B 365           
SHEET    4   K 4 VAL B 394  THR B 397 -1  O  ILE B 396   N  MET B 378           
SHEET    1   L 5 GLN B 552  ASP B 553  0                                        
SHEET    2   L 5 TYR B 535  SER B 541 -1  N  MET B 538   O  GLN B 552           
SHEET    3   L 5 ILE B 429  PHE B 436 -1  N  TYR B 433   O  TRP B 537           
SHEET    4   L 5 VAL B 414  GLN B 422 -1  N  VAL B 421   O  PHE B 430           
SHEET    5   L 5 GLY B 571  THR B 572  1  O  GLY B 571   N  LEU B 420           
SHEET    1   M 7 TYR B 453  ILE B 456  0                                        
SHEET    2   M 7 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456           
SHEET    3   M 7 TYR B 473  ILE B 475 -1  O  TYR B 473   N  LEU B 464           
SHEET    4   M 7 THR B 480  TYR B 482 -1  O  TYR B 482   N  THR B 474           
SHEET    5   M 7 ALA B 488  VAL B 493 -1  O  TYR B 491   N  VAL B 481           
SHEET    6   M 7 ASP B 507  LYS B 510 -1  O  TYR B 509   N  ARG B 492           
SHEET    7   M 7 GLN B 513  ASN B 517 -1  O  GLY B 516   N  LEU B 508           
SHEET    1   N 3 TYR B 453  ILE B 456  0                                        
SHEET    2   N 3 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456           
SHEET    3   N 3 PHE B 528  ARG B 529 -1  O  ARG B 529   N  TYR B 465           
SHEET    1   O 3 LEU B 566  VAL B 568  0                                        
SHEET    2   O 3 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567           
SHEET    3   O 3 ILE B 574  VAL B 575 -1  N  ILE B 574   O  LEU B 586           
SHEET    1   P 4 LEU B 566  VAL B 568  0                                        
SHEET    2   P 4 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567           
SHEET    3   P 4 SER B 603  SER B 609 -1  O  ARG B 605   N  VAL B 589           
SHEET    4   P 4 HIS B 617  ALA B 618 -1  O  HIS B 617   N  TYR B 608           
SHEET    1   Q 2 GLN B 627  VAL B 628  0                                        
SHEET    2   Q 2 GLN B 631  LYS B 632 -1  O  GLN B 631   N  VAL B 628           
SHEET    1   R 4 SER B 648  GLN B 652  0                                        
SHEET    2   R 4 VAL B 658  MET B 662 -1  O  LYS B 659   N  VAL B 651           
SHEET    3   R 4 ASP B 668  SER B 674 -1  O  SER B 674   N  VAL B 658           
SHEET    4   R 4 LYS B 686  LYS B 692 -1  O  LYS B 686   N  VAL B 671           
SHEET    1   S 4 SER B 699  HIS B 705  0                                        
SHEET    2   S 4 LYS B 708  ALA B 716 -1  O  TYR B 710   N  THR B 703           
SHEET    3   S 4 GLU B 722  VAL B 731 -1  O  VAL B 731   N  GLU B 709           
SHEET    4   S 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         0.41                     
CISPEP   2 ALA A  776    TYR A  777          0        -1.54                     
CISPEP   3 GLY B  718    PRO B  719          0         0.32                     
CISPEP   4 ALA B  776    TYR B  777          0        -1.50                     
SITE     1 AC1 18 HOH A  27  HOH A  52  ARG A 347  ILE A 348                    
SITE     2 AC1 18 ARG A 366  ASP A 372  ILE A 416  ASP A 417                    
SITE     3 AC1 18 ASP A 434  ILE A 442  PHE A 443  TYR A 590                    
SITE     4 AC1 18 GLN A 602  ARG A 663  ARG A 721  TYR A 752                    
SITE     5 AC1 18 HOH A 995  HOH A1066                                          
SITE     1 AC2 19 HOH B  45  HOH B  79  HOH B 188  ARG B 347                    
SITE     2 AC2 19 ILE B 348  ARG B 366  ASP B 372  ILE B 416                    
SITE     3 AC2 19 ASP B 417  ASP B 434  ILE B 442  PHE B 443                    
SITE     4 AC2 19 TYR B 590  GLN B 602  ARG B 663  ARG B 721                    
SITE     5 AC2 19 TYR B 752  HOH B1027  HOH B1062                               
CRYST1  158.340   47.400  137.320  90.00 116.45  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006316  0.000000  0.003142        0.00000                         
SCALE2      0.000000  0.021097  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008134        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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