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Entry: 2SIM
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HEADER    HYDROLASE                               15-JUL-94   2SIM              
TITLE     THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE            
TITLE    2 AND ITS COMPLEX WITH A TRANSITION STATE ANALOGUE AT 1.6              
TITLE    3 ANGSTROMS RESOLUTION                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.18;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 602;                                                 
SOURCE   4 GENE: PSX62;                                                         
SOURCE   5 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;                            
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PSX62                                     
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.L.TAYLOR,S.J.CRENNELL,E.F.GARMAN,E.R.VIMR,W.G.LAVER                 
REVDAT   2   24-FEB-09 2SIM    1       VERSN                                    
REVDAT   1   30-NOV-94 2SIM    0                                                
SPRSDE     30-NOV-94 2SIM      1SIM                                             
JRNL        AUTH   S.J.CRENNELL,E.F.GARMAN,C.PHILIPPON,A.VASELLA,               
JRNL        AUTH 2 W.G.LAVER,E.R.VIMR,G.L.TAYLOR                                
JRNL        TITL   THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2                 
JRNL        TITL 2 NEURAMINIDASE AND ITS COMPLEXES WITH THREE                   
JRNL        TITL 3 INHIBITORS AT HIGH RESOLUTION.                               
JRNL        REF    J.MOL.BIOL.                   V. 259   264 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8656428                                                      
JRNL        DOI    10.1006/JMBI.1996.0318                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.J.CRENNELL,E.F.GARMAN,W.G.LAVER,E.R.VIMR,                  
REMARK   1  AUTH 2 G.L.TAYLOR                                                   
REMARK   1  TITL   CRYSTAL STRUCTURE OF A BACTERIAL SIALIDASE (FROM             
REMARK   1  TITL 2 SALMONELLA TYPHIMURIUM LT2) SHOWS THE SAME FOLD AS           
REMARK   1  TITL 3 AN INFLUENZA VIRUS NEURAMINIDASE                             
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  90  9852 1993              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.L.TAYLOR,E.R.VIMR,E.F.GARMAN,W.G.LAVER                     
REMARK   1  TITL   PURIFICATION, CRYSTALLISATION AND PRELIMINARY                
REMARK   1  TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM                 
REMARK   1  TITL 3 VIBRIO CHOLERAE AND SALMONELLA TYPHIMURIUM                   
REMARK   1  REF    J.MOL.BIOL.                   V. 226  1287 1992              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 41098                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2954                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 242                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.016 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 3.080 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2SIM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       23.80000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.95000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.95000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.80000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.25000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  57   NE2   HIS A  57   CD2    -0.088                       
REMARK 500    HIS A 162   NE2   HIS A 162   CD2    -0.068                       
REMARK 500    HIS A 297   NE2   HIS A 297   CD2    -0.079                       
REMARK 500    HIS A 317   NE2   HIS A 317   CD2    -0.069                       
REMARK 500    HIS A 374   NE2   HIS A 374   CD2    -0.069                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  37   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG A  37   NE  -  CZ  -  NH1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG A  37   NE  -  CZ  -  NH2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    TRP A  80   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    TRP A  80   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A  90   CG  -  CD  -  NE  ANGL. DEV. = -18.5 DEGREES          
REMARK 500    ARG A  90   NE  -  CZ  -  NH1 ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    TRP A 121   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    TRP A 121   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TRP A 128   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A 128   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TRP A 140   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    THR A 159   N   -  CA  -  CB  ANGL. DEV. = -17.3 DEGREES          
REMARK 500    LEU A 182   CA  -  CB  -  CG  ANGL. DEV. =  18.3 DEGREES          
REMARK 500    TRP A 218   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A 218   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A 251   CD  -  NE  -  CZ  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG A 251   NE  -  CZ  -  NH1 ANGL. DEV. =  13.5 DEGREES          
REMARK 500    ARG A 251   NE  -  CZ  -  NH2 ANGL. DEV. = -14.9 DEGREES          
REMARK 500    TRP A 263   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A 263   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    VAL A 280   CB  -  CA  -  C   ANGL. DEV. = -15.5 DEGREES          
REMARK 500    VAL A 280   CG1 -  CB  -  CG2 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    TYR A 331   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    TYR A 347   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 348   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    VAL A 358   CB  -  CA  -  C   ANGL. DEV. = -17.5 DEGREES          
REMARK 500    VAL A 358   N   -  CA  -  CB  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    VAL A 358   CG1 -  CB  -  CG2 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    VAL A 359   CG1 -  CB  -  CG2 ANGL. DEV. =  12.5 DEGREES          
REMARK 500    ARG A 373   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG A 373   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
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  38       70.26     58.98                                   
REMARK 500    ASP A 100       69.40     63.47                                   
REMARK 500    VAL A 178      127.90     82.53                                   
REMARK 500    SER A 208     -155.46   -166.86                                   
REMARK 500    PHE A 228     -122.58     48.64                                   
REMARK 500    SER A 230      -28.58     43.61                                   
REMARK 500    ALA A 239       38.84     36.05                                   
REMARK 500    ARG A 276     -152.36     59.48                                   
REMARK 500    HIS A 278      -30.61     74.93                                   
REMARK 500    ASP A 306     -158.93   -160.77                                   
REMARK 500    VAL A 351     -101.84     55.29                                   
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 ALA A  239     SER A  240                  143.35                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  90         0.11    SIDE_CHAIN                              
REMARK 500    ARG A 251         0.10    SIDE_CHAIN                              
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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 580        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH A 621        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A 640        DISTANCE =  5.05 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 RESIDUE DAN IS THE INHIBITOR, 2,3-DEHYDRO-2-DEOXY-N-ACETYL           
REMARK 600 NEURAMINIC ACID.                                                     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A 800                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE ADVISORY NOTICE                                             
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: NANH_SALTY                               
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999                                                                      
REMARK 999        NAME   NUMBER         NAME   CHAIN  SEQ/INSERT CODE           
REMARK 999        ALA      328          ASP            329                      
DBREF  2SIM A    2   382  UNP    P29768   NANH_SALTY       1    381             
SEQADV 2SIM ASP A  329  UNP  P29768    ALA   328 CONFLICT                       
SEQRES   1 A  381  THR VAL GLU LYS SER VAL VAL PHE LYS ALA GLU GLY GLU          
SEQRES   2 A  381  HIS PHE THR ASP GLN LYS GLY ASN THR ILE VAL GLY SER          
SEQRES   3 A  381  GLY SER GLY GLY THR THR LYS TYR PHE ARG ILE PRO ALA          
SEQRES   4 A  381  MET CYS THR THR SER LYS GLY THR ILE VAL VAL PHE ALA          
SEQRES   5 A  381  ASP ALA ARG HIS ASN THR ALA SER ASP GLN SER PHE ILE          
SEQRES   6 A  381  ASP THR ALA ALA ALA ARG SER THR ASP GLY GLY LYS THR          
SEQRES   7 A  381  TRP ASN LYS LYS ILE ALA ILE TYR ASN ASP ARG VAL ASN          
SEQRES   8 A  381  SER LYS LEU SER ARG VAL MET ASP PRO THR CYS ILE VAL          
SEQRES   9 A  381  ALA ASN ILE GLN GLY ARG GLU THR ILE LEU VAL MET VAL          
SEQRES  10 A  381  GLY LYS TRP ASN ASN ASN ASP LYS THR TRP GLY ALA TYR          
SEQRES  11 A  381  ARG ASP LYS ALA PRO ASP THR ASP TRP ASP LEU VAL LEU          
SEQRES  12 A  381  TYR LYS SER THR ASP ASP GLY VAL THR PHE SER LYS VAL          
SEQRES  13 A  381  GLU THR ASN ILE HIS ASP ILE VAL THR LYS ASN GLY THR          
SEQRES  14 A  381  ILE SER ALA MET LEU GLY GLY VAL GLY SER GLY LEU GLN          
SEQRES  15 A  381  LEU ASN ASP GLY LYS LEU VAL PHE PRO VAL GLN MET VAL          
SEQRES  16 A  381  ARG THR LYS ASN ILE THR THR VAL LEU ASN THR SER PHE          
SEQRES  17 A  381  ILE TYR SER THR ASP GLY ILE THR TRP SER LEU PRO SER          
SEQRES  18 A  381  GLY TYR CYS GLU GLY PHE GLY SER GLU ASN ASN ILE ILE          
SEQRES  19 A  381  GLU PHE ASN ALA SER LEU VAL ASN ASN ILE ARG ASN SER          
SEQRES  20 A  381  GLY LEU ARG ARG SER PHE GLU THR LYS ASP PHE GLY LYS          
SEQRES  21 A  381  THR TRP THR GLU PHE PRO PRO MET ASP LYS LYS VAL ASP          
SEQRES  22 A  381  ASN ARG ASN HIS GLY VAL GLN GLY SER THR ILE THR ILE          
SEQRES  23 A  381  PRO SER GLY ASN LYS LEU VAL ALA ALA HIS SER SER ALA          
SEQRES  24 A  381  GLN ASN LYS ASN ASN ASP TYR THR ARG SER ASP ILE SER          
SEQRES  25 A  381  LEU TYR ALA HIS ASN LEU TYR SER GLY GLU VAL LYS LEU          
SEQRES  26 A  381  ILE ASP ASP PHE TYR PRO LYS VAL GLY ASN ALA SER GLY          
SEQRES  27 A  381  ALA GLY TYR SER CYS LEU SER TYR ARG LYS ASN VAL ASP          
SEQRES  28 A  381  LYS GLU THR LEU TYR VAL VAL TYR GLU ALA ASN GLY SER          
SEQRES  29 A  381  ILE GLU PHE GLN ASP LEU SER ARG HIS LEU PRO VAL ILE          
SEQRES  30 A  381  LYS SER TYR ASN                                              
HET    DAN  A 800      20                                                       
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID                     
FORMUL   2  DAN    C11 H17 N O8                                                 
FORMUL   3  HOH   *242(H2 O)                                                    
HELIX    1   1 SER A   29  GLY A   31  5                                   3    
HELIX    2   2 THR A  127  TYR A  131  5                                   5    
HELIX    3   3 ASN A  160  GLY A  169  1                                  10    
HELIX    4   4 HIS A  374  SER A  380  1                                   7    
SHEET    1   A 4 LYS A   5  PHE A   9  0                                        
SHEET    2   A 4 SER A 365  ASP A 370 -1  O  ILE A 366   N  VAL A   8           
SHEET    3   A 4 LYS A 353  ALA A 362 -1  O  VAL A 358   N  GLN A 369           
SHEET    4   A 4 SER A 343  ASN A 350 -1  N  CYS A 344   O  VAL A 359           
SHEET    1   B 2 PHE A  16  THR A  17  0                                        
SHEET    2   B 2 THR A  23  ILE A  24 -1  N  ILE A  24   O  PHE A  16           
SHEET    1   C 4 TYR A  35  THR A  43  0                                        
SHEET    2   C 4 ILE A  49  ARG A  56 -1  N  VAL A  50   O  CYS A  42           
SHEET    3   C 4 ILE A  66  SER A  73 -1  O  ASP A  67   N  ALA A  55           
SHEET    4   C 4 ASN A  81  ILE A  86 -1  N  ASN A  81   O  ARG A  72           
SHEET    1   D 5 SER A 155  LYS A 156  0                                        
SHEET    2   D 5 ASP A 141  SER A 147 -1  N  LYS A 146   O  SER A 155           
SHEET    3   D 5 ARG A 111  TRP A 121 -1  N  ILE A 114   O  SER A 147           
SHEET    4   D 5 ARG A  97  ILE A 108 -1  N  ARG A  97   O  TRP A 121           
SHEET    5   D 5 GLY A 179  SER A 180  1  O  GLY A 179   N  CYS A 103           
SHEET    1   E 4 CYS A 225  GLU A 226  0                                        
SHEET    2   E 4 LEU A 205  SER A 212 -1  O  THR A 207   N  CYS A 225           
SHEET    3   E 4 LEU A 189  ARG A 197 -1  N  LEU A 189   O  SER A 212           
SHEET    4   E 4 ILE A 171  GLY A 176 -1  N  SER A 172   O  VAL A 196           
SHEET    1   F 4 CYS A 225  GLU A 226  0                                        
SHEET    2   F 4 LEU A 205  SER A 212 -1  O  THR A 207   N  CYS A 225           
SHEET    3   F 4 LEU A 189  ARG A 197 -1  N  LEU A 189   O  SER A 212           
SHEET    4   F 4 LEU A 182  GLN A 183 -1  O  LEU A 182   N  VAL A 190           
SHEET    1   G 4 ASN A 232  PHE A 237  0                                        
SHEET    2   G 4 SER A 240  ILE A 245 -1  O  SER A 240   N  PHE A 237           
SHEET    3   G 4 PHE A 254  THR A 256 -1  O  PHE A 254   N  ASN A 243           
SHEET    4   G 4 THR A 264  GLU A 265 -1  O  THR A 264   N  GLU A 255           
SHEET    1   H 4 SER A 283  SER A 289  0                                        
SHEET    2   H 4 LYS A 292  ALA A 300 -1  O  LYS A 292   N  SER A 289           
SHEET    3   H 4 ILE A 312  HIS A 317 -1  N  SER A 313   O  SER A 299           
SHEET    4   H 4 VAL A 324  TYR A 331 -1  O  LYS A 325   N  ALA A 316           
SSBOND   1 CYS A   42    CYS A  103                          1555   1555  2.06  
CISPEP   1 ALA A  135    PRO A  136          0        -6.67                     
SITE     1 ACT 13 ARG A  37  ARG A  56  ASP A  62  MET A  99                    
SITE     2 ACT 13 ASP A 100  TRP A 121  TRP A 128  LEU A 175                    
SITE     3 ACT 13 GLU A 231  ARG A 246  ARG A 309  TYR A 342                    
SITE     4 ACT 13 GLU A 361                                                     
SITE     1 AC1 19 ARG A  37  ILE A  38  ARG A  56  ASP A  62                    
SITE     2 AC1 19 MET A  99  ASP A 100  THR A 127  TRP A 128                    
SITE     3 AC1 19 ARG A 246  ARG A 309  TYR A 342  HOH A 664                    
SITE     4 AC1 19 HOH A 688  HOH A 689  HOH A 690  HOH A 692                    
SITE     5 AC1 19 HOH A 694  HOH A 695  HOH A 696                               
CRYST1   47.600   82.500   91.900  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021008  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012121  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010881        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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