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Database: PDB
Entry: 2F29
LinkDB: 2F29
Original site: 2F29 
HEADER    HYDROLASE                               15-NOV-05   2F29              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN SIALIDASE NEU2 Q116E MUTANT            
TITLE    2 IN COMPLEX WITH DANA INHIBITOR                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE 2;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NEU2, CYTOSOLIC SIALIDASE, N-ACETYL-ALPHA-                  
COMPND   5 NEURAMINIDASE 2;                                                     
COMPND   6 EC: 3.2.1.18;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    SIALIDASE, NEURAMINIDASE, GANGLIOSIDE, DRUG DESIGN,                   
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.M.G.CHAVAS,R.KATO,P.FUSI,C.TRINGALI,B.VENERANDO,                    
AUTHOR   2 G.TETTAMANTI,E.MONTI,S.WAKATSUKI                                     
REVDAT   2   24-FEB-09 2F29    1       VERSN                                    
REVDAT   1   21-NOV-06 2F29    0                                                
JRNL        AUTH   L.M.G.CHAVAS,R.KATO,P.FUSI,C.TRINGALI,B.VENERANDO,           
JRNL        AUTH 2 G.TETTAMANTI,E.MONTI,S.WAKATSUKI                             
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN SIALIDASE NEU2                
JRNL        TITL 2 Q116E MUTANT IN COMPLEX WITH DANA INHIBITOR                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.92 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 19087                          
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) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 980                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5830                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.32600                                             
REMARK   3    B22 (A**2) : -19.10600                                            
REMARK   3    B33 (A**2) : 7.78100                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.25300                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.45                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 43.96                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : DANA_HEPES_REP.PARAM                           
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2F29 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035362.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9744                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19087                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.060                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SNT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-METHYL-2,4-PENTANEDIOL, GUANIDINE      
REMARK 280  HYDROCHLORIDE, 2-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID, PH      
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                
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       78.64500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.99000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.64500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.99000            
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER. THERE ARE 2 BIOLOGICAL     
REMARK 300 UNITS IN THE ASYMMETRIC UNIT (CHAIN A AND CHAIN B)                   
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     THR A   226                                                      
REMARK 465     GLY A   227                                                      
REMARK 465     GLU A   228                                                      
REMARK 465     SER A   284                                                      
REMARK 465     GLY A   285                                                      
REMARK 465     PRO A   286                                                      
REMARK 465     GLY A   287                                                      
REMARK 465     LEU A   378                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     GLN A   380                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     THR B   226                                                      
REMARK 465     GLY B   227                                                      
REMARK 465     GLU B   228                                                      
REMARK 465     SER B   284                                                      
REMARK 465     GLY B   285                                                      
REMARK 465     PRO B   286                                                      
REMARK 465     GLY B   287                                                      
REMARK 465     LEU B   378                                                      
REMARK 465     PRO B   379                                                      
REMARK 465     GLN B   380                                                      
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    GLN A   8      135.25   -172.00                                   
REMARK 500    ILE A  22       72.89     52.32                                   
REMARK 500    GLU A  47      -10.11    -46.12                                   
REMARK 500    GLU A  50      -70.89   -138.47                                   
REMARK 500    ASN A  86       90.26     66.63                                   
REMARK 500    ASP A 131       52.13   -118.13                                   
REMARK 500    ILE A 147      -98.00   -118.46                                   
REMARK 500    CYS A 164     -157.83    -88.05                                   
REMARK 500    ARG A 170       -3.38    -53.89                                   
REMARK 500    ALA A 171       19.15   -146.08                                   
REMARK 500    ARG A 172       79.16     36.44                                   
REMARK 500    ALA A 207      140.91   -175.22                                   
REMARK 500    VAL A 212     -163.03   -113.29                                   
REMARK 500    ASP A 215       44.55     71.88                                   
REMARK 500    LEU A 217     -137.83   -113.87                                   
REMARK 500    ALA A 242     -157.41   -131.08                                   
REMARK 500    GLU A 257       21.92     46.79                                   
REMARK 500    VAL A 265      174.85    -56.84                                   
REMARK 500    PRO A 268      -74.18    -21.77                                   
REMARK 500    PRO A 269      -93.55    -48.61                                   
REMARK 500    ASP A 306       80.36     52.31                                   
REMARK 500    ALA A 333     -138.54   -140.26                                   
REMARK 500    TYR A 334      137.06    -38.90                                   
REMARK 500    GLU A 376       32.54    -69.03                                   
REMARK 500    ILE B  22       67.77     64.15                                   
REMARK 500    GLU B  50      -69.39   -135.48                                   
REMARK 500    ARG B  78      174.16    169.92                                   
REMARK 500    ASP B  80      106.01    -16.85                                   
REMARK 500    ASN B  86       72.33     59.34                                   
REMARK 500    ASP B 131       52.21   -117.27                                   
REMARK 500    HIS B 132       19.04     48.29                                   
REMARK 500    THR B 156      159.06    179.75                                   
REMARK 500    ASN B 168       39.98    -99.44                                   
REMARK 500    PHE B 195      177.32    171.00                                   
REMARK 500    ALA B 213      130.87    -22.59                                   
REMARK 500    GLN B 214      158.02    -31.93                                   
REMARK 500    LEU B 217     -144.16   -105.61                                   
REMARK 500    VAL B 265      178.08    -53.85                                   
REMARK 500    PRO B 268      -58.43    -27.18                                   
REMARK 500    PRO B 269      -88.11    -58.92                                   
REMARK 500    ASP B 306       76.85     56.66                                   
REMARK 500    PRO B 316       48.37   -103.40                                   
REMARK 500    SER B 331      109.74    -46.13                                   
REMARK 500    ALA B 333     -126.80   -126.77                                   
REMARK 500    ASN B 357       76.16     43.98                                   
REMARK 500    GLU B 361      149.68   -179.07                                   
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 407        DISTANCE =  5.11 ANGSTROMS                       
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 381                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 382                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 383                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B 381                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 382                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 383                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SNT   RELATED DB: PDB                                   
REMARK 900 HUMAN NEU2 APO-FORM                                                  
REMARK 900 RELATED ID: 1SO7   RELATED DB: PDB                                   
REMARK 900 HUMAN NEU2 SUGAR-INDUCED FORM                                        
REMARK 900 RELATED ID: 1VCU   RELATED DB: PDB                                   
REMARK 900 HUMAN NEU2-DANA COMPLEX                                              
REMARK 900 RELATED ID: 2F0Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F10   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F11   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F12   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F13   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F24   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F25   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F26   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F27   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2F28   RELATED DB: PDB                                   
DBREF  2F29 A    1   380  UNP    Q9Y3R4   NEUR2_HUMAN      1    380             
DBREF  2F29 B    1   380  UNP    Q9Y3R4   NEUR2_HUMAN      1    380             
SEQADV 2F29 GLY A   -1  UNP  Q9Y3R4              CLONING ARTIFACT               
SEQADV 2F29 SER A    0  UNP  Q9Y3R4              CLONING ARTIFACT               
SEQADV 2F29 GLU A  116  UNP  Q9Y3R4    GLN   116 ENGINEERED                     
SEQADV 2F29 GLY B   -1  UNP  Q9Y3R4              CLONING ARTIFACT               
SEQADV 2F29 SER B    0  UNP  Q9Y3R4              CLONING ARTIFACT               
SEQADV 2F29 GLU B  116  UNP  Q9Y3R4    GLN   116 ENGINEERED                     
SEQRES   1 A  382  GLY SER MET ALA SER LEU PRO VAL LEU GLN LYS GLU SER          
SEQRES   2 A  382  VAL PHE GLN SER GLY ALA HIS ALA TYR ARG ILE PRO ALA          
SEQRES   3 A  382  LEU LEU TYR LEU PRO GLY GLN GLN SER LEU LEU ALA PHE          
SEQRES   4 A  382  ALA GLU GLN ARG ALA SER LYS LYS ASP GLU HIS ALA GLU          
SEQRES   5 A  382  LEU ILE VAL LEU ARG ARG GLY ASP TYR ASP ALA PRO THR          
SEQRES   6 A  382  HIS GLN VAL GLN TRP GLN ALA GLN GLU VAL VAL ALA GLN          
SEQRES   7 A  382  ALA ARG LEU ASP GLY HIS ARG SER MET ASN PRO CYS PRO          
SEQRES   8 A  382  LEU TYR ASP ALA GLN THR GLY THR LEU PHE LEU PHE PHE          
SEQRES   9 A  382  ILE ALA ILE PRO GLY GLN VAL THR GLU GLN GLN GLN LEU          
SEQRES  10 A  382  GLU THR ARG ALA ASN VAL THR ARG LEU CYS GLN VAL THR          
SEQRES  11 A  382  SER THR ASP HIS GLY ARG THR TRP SER SER PRO ARG ASP          
SEQRES  12 A  382  LEU THR ASP ALA ALA ILE GLY PRO ALA TYR ARG GLU TRP          
SEQRES  13 A  382  SER THR PHE ALA VAL GLY PRO GLY HIS CYS LEU GLN LEU          
SEQRES  14 A  382  ASN ASP ARG ALA ARG SER LEU VAL VAL PRO ALA TYR ALA          
SEQRES  15 A  382  TYR ARG LYS LEU HIS PRO ILE GLN ARG PRO ILE PRO SER          
SEQRES  16 A  382  ALA PHE CYS PHE LEU SER HIS ASP HIS GLY ARG THR TRP          
SEQRES  17 A  382  ALA ARG GLY HIS PHE VAL ALA GLN ASP THR LEU GLU CYS          
SEQRES  18 A  382  GLN VAL ALA GLU VAL GLU THR GLY GLU GLN ARG VAL VAL          
SEQRES  19 A  382  THR LEU ASN ALA ARG SER HIS LEU ARG ALA ARG VAL GLN          
SEQRES  20 A  382  ALA GLN SER THR ASN ASP GLY LEU ASP PHE GLN GLU SER          
SEQRES  21 A  382  GLN LEU VAL LYS LYS LEU VAL GLU PRO PRO PRO GLN GLY          
SEQRES  22 A  382  CYS GLN GLY SER VAL ILE SER PHE PRO SER PRO ARG SER          
SEQRES  23 A  382  GLY PRO GLY SER PRO ALA GLN TRP LEU LEU TYR THR HIS          
SEQRES  24 A  382  PRO THR HIS SER TRP GLN ARG ALA ASP LEU GLY ALA TYR          
SEQRES  25 A  382  LEU ASN PRO ARG PRO PRO ALA PRO GLU ALA TRP SER GLU          
SEQRES  26 A  382  PRO VAL LEU LEU ALA LYS GLY SER CYS ALA TYR SER ASP          
SEQRES  27 A  382  LEU GLN SER MET GLY THR GLY PRO ASP GLY SER PRO LEU          
SEQRES  28 A  382  PHE GLY CYS LEU TYR GLU ALA ASN ASP TYR GLU GLU ILE          
SEQRES  29 A  382  VAL PHE LEU MET PHE THR LEU LYS GLN ALA PHE PRO ALA          
SEQRES  30 A  382  GLU TYR LEU PRO GLN                                          
SEQRES   1 B  382  GLY SER MET ALA SER LEU PRO VAL LEU GLN LYS GLU SER          
SEQRES   2 B  382  VAL PHE GLN SER GLY ALA HIS ALA TYR ARG ILE PRO ALA          
SEQRES   3 B  382  LEU LEU TYR LEU PRO GLY GLN GLN SER LEU LEU ALA PHE          
SEQRES   4 B  382  ALA GLU GLN ARG ALA SER LYS LYS ASP GLU HIS ALA GLU          
SEQRES   5 B  382  LEU ILE VAL LEU ARG ARG GLY ASP TYR ASP ALA PRO THR          
SEQRES   6 B  382  HIS GLN VAL GLN TRP GLN ALA GLN GLU VAL VAL ALA GLN          
SEQRES   7 B  382  ALA ARG LEU ASP GLY HIS ARG SER MET ASN PRO CYS PRO          
SEQRES   8 B  382  LEU TYR ASP ALA GLN THR GLY THR LEU PHE LEU PHE PHE          
SEQRES   9 B  382  ILE ALA ILE PRO GLY GLN VAL THR GLU GLN GLN GLN LEU          
SEQRES  10 B  382  GLU THR ARG ALA ASN VAL THR ARG LEU CYS GLN VAL THR          
SEQRES  11 B  382  SER THR ASP HIS GLY ARG THR TRP SER SER PRO ARG ASP          
SEQRES  12 B  382  LEU THR ASP ALA ALA ILE GLY PRO ALA TYR ARG GLU TRP          
SEQRES  13 B  382  SER THR PHE ALA VAL GLY PRO GLY HIS CYS LEU GLN LEU          
SEQRES  14 B  382  ASN ASP ARG ALA ARG SER LEU VAL VAL PRO ALA TYR ALA          
SEQRES  15 B  382  TYR ARG LYS LEU HIS PRO ILE GLN ARG PRO ILE PRO SER          
SEQRES  16 B  382  ALA PHE CYS PHE LEU SER HIS ASP HIS GLY ARG THR TRP          
SEQRES  17 B  382  ALA ARG GLY HIS PHE VAL ALA GLN ASP THR LEU GLU CYS          
SEQRES  18 B  382  GLN VAL ALA GLU VAL GLU THR GLY GLU GLN ARG VAL VAL          
SEQRES  19 B  382  THR LEU ASN ALA ARG SER HIS LEU ARG ALA ARG VAL GLN          
SEQRES  20 B  382  ALA GLN SER THR ASN ASP GLY LEU ASP PHE GLN GLU SER          
SEQRES  21 B  382  GLN LEU VAL LYS LYS LEU VAL GLU PRO PRO PRO GLN GLY          
SEQRES  22 B  382  CYS GLN GLY SER VAL ILE SER PHE PRO SER PRO ARG SER          
SEQRES  23 B  382  GLY PRO GLY SER PRO ALA GLN TRP LEU LEU TYR THR HIS          
SEQRES  24 B  382  PRO THR HIS SER TRP GLN ARG ALA ASP LEU GLY ALA TYR          
SEQRES  25 B  382  LEU ASN PRO ARG PRO PRO ALA PRO GLU ALA TRP SER GLU          
SEQRES  26 B  382  PRO VAL LEU LEU ALA LYS GLY SER CYS ALA TYR SER ASP          
SEQRES  27 B  382  LEU GLN SER MET GLY THR GLY PRO ASP GLY SER PRO LEU          
SEQRES  28 B  382  PHE GLY CYS LEU TYR GLU ALA ASN ASP TYR GLU GLU ILE          
SEQRES  29 B  382  VAL PHE LEU MET PHE THR LEU LYS GLN ALA PHE PRO ALA          
SEQRES  30 B  382  GLU TYR LEU PRO GLN                                          
HET    DAN  A 381      20                                                       
HET    EPE  A 382      15                                                       
HET    EPE  A 383      15                                                       
HET    DAN  B 381      20                                                       
HET    EPE  B 382      15                                                       
HET    EPE  B 383      15                                                       
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID                     
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     EPE HEPES                                                            
FORMUL   3  DAN    2(C11 H17 N O8)                                              
FORMUL   4  EPE    4(C8 H18 N2 O4 S)                                            
FORMUL   9  HOH   *75(H2 O)                                                     
HELIX    1   1 LYS A   45  ALA A   49  5                                   5    
HELIX    2   2 THR A  110  THR A  117  1                                   8    
HELIX    3   3 LEU A  142  ILE A  147  1                                   6    
HELIX    4   4 ALA A  317  TRP A  321  5                                   5    
HELIX    5   5 LEU A  369  PHE A  373  1                                   5    
HELIX    6   6 PRO A  374  TYR A  377  5                                   4    
HELIX    7   7 LYS B   45  GLU B   47  5                                   3    
HELIX    8   8 THR B  110  THR B  117  1                                   8    
HELIX    9   9 LEU B  142  ILE B  147  1                                   6    
HELIX   10  10 GLY B  148  ARG B  152  5                                   5    
HELIX   11  11 ALA B  317  TRP B  321  5                                   5    
HELIX   12  12 LEU B  369  PHE B  373  1                                   5    
HELIX   13  13 PRO B  374  TYR B  377  5                                   4    
SHEET    1   A14 SER A 275  PRO A 280  0                                        
SHEET    2   A14 GLN A 291  PRO A 298 -1  O  THR A 296   N  SER A 275           
SHEET    3   A14 ALA A 305  ASN A 312 -1  O  GLY A 308   N  HIS A 297           
SHEET    4   A14 VAL A 325  THR A 342 -1  O  LEU A 327   N  LEU A 307           
SHEET    5   A14 PRO A 348  ALA A 356 -1  O  LEU A 349   N  GLY A 341           
SHEET    6   A14 GLU A 361  THR A 368 -1  O  LEU A 365   N  CYS A 352           
SHEET    7   A14 GLN A   8  GLN A  14 -1  N  GLU A  10   O  PHE A 364           
SHEET    8   A14 GLN B   8  GLN B  14 -1  O  LYS B   9   N  SER A  11           
SHEET    9   A14 GLU B 361  THR B 368 -1  O  ILE B 362   N  VAL B  12           
SHEET   10   A14 PRO B 348  ALA B 356 -1  N  CYS B 352   O  LEU B 365           
SHEET   11   A14 VAL B 325  THR B 342 -1  N  GLY B 341   O  LEU B 349           
SHEET   12   A14 ALA B 305  ASN B 312 -1  N  LEU B 307   O  LEU B 327           
SHEET   13   A14 GLN B 291  PRO B 298 -1  N  HIS B 297   O  GLY B 308           
SHEET   14   A14 SER B 275  PRO B 280 -1  N  SER B 275   O  THR B 296           
SHEET    1   B 4 ALA A  19  TYR A  27  0                                        
SHEET    2   B 4 SER A  33  ARG A  41 -1  O  GLU A  39   N  ARG A  21           
SHEET    3   B 4 LEU A  51  ASP A  60 -1  O  LEU A  51   N  GLN A  40           
SHEET    4   B 4 GLN A  65  TRP A  68 -1  O  GLN A  65   N  ASP A  60           
SHEET    1   C 4 ALA A  19  TYR A  27  0                                        
SHEET    2   C 4 SER A  33  ARG A  41 -1  O  GLU A  39   N  ARG A  21           
SHEET    3   C 4 LEU A  51  ASP A  60 -1  O  LEU A  51   N  GLN A  40           
SHEET    4   C 4 GLU A  72  VAL A  73 -1  O  GLU A  72   N  LEU A  54           
SHEET    1   D 4 HIS A  82  ASP A  92  0                                        
SHEET    2   D 4 THR A  97  PRO A 106 -1  O  PHE A  99   N  LEU A  90           
SHEET    3   D 4 ARG A 123  SER A 129 -1  O  SER A 129   N  LEU A  98           
SHEET    4   D 4 ARG A 140  ASP A 141 -1  O  ARG A 140   N  GLN A 126           
SHEET    1   E 3 TRP A 154  VAL A 159  0                                        
SHEET    2   E 3 LEU A 174  ARG A 182 -1  O  TYR A 181   N  SER A 155           
SHEET    3   E 3 LEU A 165  GLN A 166 -1  N  LEU A 165   O  VAL A 175           
SHEET    1   F 3 TRP A 154  VAL A 159  0                                        
SHEET    2   F 3 LEU A 174  ARG A 182 -1  O  TYR A 181   N  SER A 155           
SHEET    3   F 3 ILE A 191  SER A 199 -1  O  PHE A 195   N  ALA A 178           
SHEET    1   G 4 THR A 216  VAL A 224  0                                        
SHEET    2   G 4 VAL A 231  SER A 238 -1  O  ARG A 237   N  LEU A 217           
SHEET    3   G 4 ALA A 242  SER A 248 -1  O  ALA A 246   N  LEU A 234           
SHEET    4   G 4 GLN A 256  VAL A 265 -1  O  GLN A 256   N  GLN A 247           
SHEET    1   H 4 ALA B  19  TYR B  27  0                                        
SHEET    2   H 4 SER B  33  ARG B  41 -1  O  ARG B  41   N  ALA B  19           
SHEET    3   H 4 ALA B  49  ASP B  60 -1  O  LEU B  51   N  GLN B  40           
SHEET    4   H 4 GLN B  65  TRP B  68 -1  O  GLN B  65   N  ASP B  60           
SHEET    1   I 4 ALA B  19  TYR B  27  0                                        
SHEET    2   I 4 SER B  33  ARG B  41 -1  O  ARG B  41   N  ALA B  19           
SHEET    3   I 4 ALA B  49  ASP B  60 -1  O  LEU B  51   N  GLN B  40           
SHEET    4   I 4 GLU B  72  VAL B  73 -1  O  GLU B  72   N  LEU B  54           
SHEET    1   J 4 HIS B  82  TYR B  91  0                                        
SHEET    2   J 4 LEU B  98  PRO B 106 -1  O  ILE B 105   N  ARG B  83           
SHEET    3   J 4 ARG B 123  SER B 129 -1  O  SER B 129   N  LEU B  98           
SHEET    4   J 4 ARG B 140  ASP B 141 -1  O  ARG B 140   N  GLN B 126           
SHEET    1   K 3 TRP B 154  VAL B 159  0                                        
SHEET    2   K 3 LEU B 174  ARG B 182 -1  O  TYR B 181   N  THR B 156           
SHEET    3   K 3 LEU B 165  GLN B 166 -1  N  LEU B 165   O  VAL B 175           
SHEET    1   L 3 TRP B 154  VAL B 159  0                                        
SHEET    2   L 3 LEU B 174  ARG B 182 -1  O  TYR B 181   N  THR B 156           
SHEET    3   L 3 ILE B 191  SER B 199 -1  O  PHE B 195   N  ALA B 178           
SHEET    1   M 4 VAL B 221  VAL B 224  0                                        
SHEET    2   M 4 VAL B 231  ALA B 236 -1  O  VAL B 231   N  VAL B 224           
SHEET    3   M 4 ALA B 242  SER B 248 -1  O  ALA B 246   N  LEU B 234           
SHEET    4   M 4 GLU B 257  VAL B 265 -1  O  GLN B 259   N  GLN B 245           
CISPEP   1 GLY A  160    PRO A  161          0         0.05                     
CISPEP   2 PRO A  315    PRO A  316          0        -0.10                     
CISPEP   3 GLY B  160    PRO B  161          0         0.07                     
CISPEP   4 PRO B  315    PRO B  316          0         0.11                     
SITE     1 AC1 13 ARG A  21  ARG A  41  ASP A  46  MET A  85                    
SITE     2 AC1 13 GLU A 111  TYR A 179  TYR A 181  LEU A 217                    
SITE     3 AC1 13 GLU A 218  ARG A 237  ARG A 304  TYR A 334                    
SITE     4 AC1 13 EPE A 383                                                     
SITE     1 AC2  9 SER A  11  GLN A  14  GLY A  16  ALA A  17                    
SITE     2 AC2  9 HIS A  18  TYR A  20  GLN A  71  VAL B   6                    
SITE     3 AC2  9 LEU B   7                                                     
SITE     1 AC3  8 ARG A  21  ARG A  41  LYS A  44  ARG A 237                    
SITE     2 AC3  8 PRO A 269  GLN A 270  TYR A 359  DAN A 381                    
SITE     1 AC4 15 ARG B  21  ILE B  22  ARG B  41  ASP B  46                    
SITE     2 AC4 15 MET B  85  ASN B  86  GLU B 111  TYR B 179                    
SITE     3 AC4 15 TYR B 181  LEU B 217  GLU B 218  ARG B 237                    
SITE     4 AC4 15 ARG B 304  TYR B 334  EPE B 383                               
SITE     1 AC5 10 VAL A   6  SER B  11  VAL B  12  PHE B  13                    
SITE     2 AC5 10 GLN B  14  GLY B  16  ALA B  17  HIS B  18                    
SITE     3 AC5 10 TYR B  20  ARG B  55                                          
SITE     1 AC6  8 ARG B  21  LYS B  44  ARG B 237  PRO B 269                    
SITE     2 AC6  8 GLN B 270  ARG B 304  TYR B 359  DAN B 381                    
CRYST1  157.290   73.980   77.180  90.00  93.14  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      0.006358  0.000000  0.000349        0.00000                         
SCALE2      0.000000  0.013517  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012976        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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