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Database: PDB
Entry: 1Y7V
LinkDB: 1Y7V
Original site: 1Y7V 
HEADER    HYDROLASE                               10-DEC-04   1Y7V              
TITLE     X-RAY STRUCTURE OF HUMAN ACID-BETA-GLUCOSIDASE COVALENTLY BOUND TO    
TITLE    2 CONDURITOL B EPOXIDE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL- 
COMPND   5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;         
COMPND   6 EC: 3.2.1.45;                                                        
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 GENE: GBA, GC;                                                       
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS                             
KEYWDS    GAUCHER DISEASE, GLUCOSIDASE, GLUCOCEREBROSIDASE, CEREZYME,           
KEYWDS   2 HYDROLASE, GLYCOSIDASE, SPHINGOLIPID METABOLISM, GLYCOPROTEIN,       
KEYWDS   3 LYSOSOME, MEMBRANE, DISEASE MUTATION, ALTERNATIVE INITIATION, ISRAEL 
KEYWDS   4 STRUCTURAL PROTEOMICS CENTER, ISPC, STRUCTURAL GENOMICS              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.PREMKUMAR,A.R.SAWKAR,S.BOLDIN-ADAMSKY,L.TOKER,I.SILMAN,J.W.KELLY,   
AUTHOR   2 A.H.FUTERMAN,J.L.SUSSMAN,ISRAEL STRUCTURAL PROTEOMICS CENTER (ISPC)  
REVDAT   5   13-JUL-11 1Y7V    1       VERSN                                    
REVDAT   4   24-FEB-09 1Y7V    1       VERSN                                    
REVDAT   3   26-JUL-05 1Y7V    1       JRNL                                     
REVDAT   2   26-APR-05 1Y7V    1       SOURCE                                   
REVDAT   1   12-APR-05 1Y7V    0                                                
JRNL        AUTH   L.PREMKUMAR,A.R.SAWKAR,S.BOLDIN-ADAMSKY,L.TOKER,I.SILMAN,    
JRNL        AUTH 2 J.W.KELLY,A.H.FUTERMAN,J.L.SUSSMAN                           
JRNL        TITL   X-RAY STRUCTURE OF HUMAN ACID-BETA-GLUCOSIDASE COVALENTLY    
JRNL        TITL 2 BOUND TO CONDURITOL-B-EPOXIDE. IMPLICATIONS FOR GAUCHER      
JRNL        TITL 3 DISEASE.                                                     
JRNL        REF    J.BIOL.CHEM.                  V. 280 23815 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15817452                                                     
JRNL        DOI    10.1074/JBC.M502799200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.82                          
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)   (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 53193                          
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) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2686                            
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            : 7860                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 143                                     
REMARK   3   SOLVENT ATOMS            : 286                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 28.23000                                             
REMARK   3    B22 (A**2) : -9.87000                                             
REMARK   3    B33 (A**2) : -18.37000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.65                            
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) : 0.43                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.69                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.10                            
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) : 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        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Y7V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB031226.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55401                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
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     (%) : 96.4                               
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  : 12.7500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
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         : 4.880                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200  TECHNIQUE                                                           
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1OGS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, GUANIDINE HCL, KCL,    
REMARK 280  ACETATE , PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       45.75500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.75500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       52.24500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      142.80500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       52.24500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      142.80500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.75500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       52.24500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      142.80500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       45.75500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       52.24500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      142.80500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13550 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 68140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -354.0 KCAL/MOL                       
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       45.75500            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       52.24500            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      142.80500            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000       45.75500            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000      -52.24500            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      142.80500            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 66110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -350.0 KCAL/MOL                       
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -45.75500            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       52.24500            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      142.80500            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000      -45.75500            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000      -52.24500            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      142.80500            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -166.0 KCAL/MOL                       
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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -52.24500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      142.80500            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL                       
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       45.75500            
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   OE2  GLU B   235     OH   TYR B   313              2.12            
REMARK 500   OD2  ASP B   127     O4   INS B   506              2.16            
REMARK 500   OE2  GLU A   235     OH   TYR A   313              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    CYS A 342   CB    CYS A 342   SG     -0.128                       
REMARK 500    CYS B 342   CB    CYS B 342   SG     -0.112                       
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    PRO A 245   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A 353   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A 353   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 353   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    PRO B 245   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG B 353   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG B 353   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    THR A  63       32.97   -142.30                                   
REMARK 500    PHE A  75     -142.77   -128.28                                   
REMARK 500    ALA A 124     -148.42     84.43                                   
REMARK 500    PHE A 128       55.24   -100.27                                   
REMARK 500    TYR A 133      159.36    177.09                                   
REMARK 500    ALA A 136       72.31   -154.12                                   
REMARK 500    LEU A 156      -64.38   -100.96                                   
REMARK 500    ASN A 192     -153.85   -116.99                                   
REMARK 500    SER A 196     -162.65   -126.64                                   
REMARK 500    ASP A 203     -166.81    -76.64                                   
REMARK 500    GLU A 233      139.92    173.28                                   
REMARK 500    GLU A 235       63.23     34.41                                   
REMARK 500    GLN A 247      118.53    -39.90                                   
REMARK 500    LEU A 249       96.38   -168.28                                   
REMARK 500    LEU A 281      -82.61     66.14                                   
REMARK 500    ALA A 318       69.90   -172.85                                   
REMARK 500    PRO A 319      125.50    -32.80                                   
REMARK 500    THR A 323      -76.55   -110.48                                   
REMARK 500    LEU A 354      107.59    -48.79                                   
REMARK 500    HIS A 374       -3.70     78.04                                   
REMARK 500    TRP A 381     -128.36    -79.55                                   
REMARK 500    ASN A 396       55.00    -98.00                                   
REMARK 500    ASP A 409       46.75     38.21                                   
REMARK 500    LEU A 436       96.04   -165.92                                   
REMARK 500    THR B  63      -35.75    130.16                                   
REMARK 500    PRO B  71      -30.79    -37.91                                   
REMARK 500    PHE B  75     -142.92   -129.06                                   
REMARK 500    ALA B 124     -148.78     84.72                                   
REMARK 500    PHE B 128       58.96   -102.11                                   
REMARK 500    TYR B 133      158.96    175.12                                   
REMARK 500    ALA B 136       71.95   -156.12                                   
REMARK 500    ASN B 146       31.37    -98.21                                   
REMARK 500    ASP B 153      -60.29    -90.68                                   
REMARK 500    LEU B 156      -65.82   -101.56                                   
REMARK 500    ASN B 192     -155.08   -116.03                                   
REMARK 500    SER B 196     -163.24   -126.14                                   
REMARK 500    ASP B 203     -166.50    -77.95                                   
REMARK 500    GLU B 233      138.27    174.75                                   
REMARK 500    GLU B 235       62.92     34.73                                   
REMARK 500    LEU B 249       95.57   -167.10                                   
REMARK 500    LEU B 281      -79.84     64.40                                   
REMARK 500    ALA B 318       67.71   -173.39                                   
REMARK 500    PRO B 319      127.11    -31.51                                   
REMARK 500    THR B 323      -77.50   -110.34                                   
REMARK 500    PRO B 332      -19.54    -49.68                                   
REMARK 500    LEU B 354      108.24    -51.41                                   
REMARK 500    HIS B 374       -6.20     77.08                                   
REMARK 500    TRP B 381     -129.65    -76.68                                   
REMARK 500    TRP B 393       -8.16    -58.20                                   
REMARK 500    ASN B 396       55.02    -96.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
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 B 642        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B 648        DISTANCE =  5.64 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     INS A  507                                                       
REMARK 610     INS B  506                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INS A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INS B 506                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OGS   RELATED DB: PDB                                   
REMARK 900 NATIVE HUMAN ACID-BETA-GLUCOSIDASE                                   
REMARK 900 RELATED ID: W00572   RELATED DB: TARGETDB                            
DBREF  1Y7V A    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  1Y7V B    1   497  UNP    P04062   GLCM_HUMAN      40    536             
SEQADV 1Y7V HIS A  495  UNP  P04062    ARG   534 ENGINEERED                     
SEQADV 1Y7V HIS B  495  UNP  P04062    ARG   534 ENGINEERED                     
SEQRES   1 A  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 A  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 A  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 A  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 A  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 A  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 A  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 A  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 A  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 A  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 A  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 A  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 A  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 A  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 A  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 A  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 A  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 A  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 A  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 A  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 A  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 A  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 A  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 A  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 A  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 A  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 A  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 A  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 A  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 A  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 A  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 A  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 A  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 A  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 A  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 A  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 A  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 A  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 A  497  HIS ARG GLN                                                  
SEQRES   1 B  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 B  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 B  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 B  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 B  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 B  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 B  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 B  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 B  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 B  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 B  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 B  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 B  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 B  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 B  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 B  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 B  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 B  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 B  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 B  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 B  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 B  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 B  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 B  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 B  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 B  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 B  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 B  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 B  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 B  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 B  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 B  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 B  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 B  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 B  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 B  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 B  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 B  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 B  497  HIS ARG GLN                                                  
MODRES 1Y7V ASN A   19  ASN  GLYCOSYLATION SITE                                 
MODRES 1Y7V ASN B   19  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 498      14                                                       
HET    NAG  A 499      14                                                       
HET    NAG  B 498      14                                                       
HET    NAG  B 499      14                                                       
HET    SO4  A 500       5                                                       
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  B 500       5                                                       
HET    SO4  A 505       5                                                       
HET    SO4  B 501       5                                                       
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HET    SO4  A 506       5                                                       
HET    SO4  B 504       5                                                       
HET    SO4  B 505       5                                                       
HET    INS  A 507      11                                                       
HET    INS  B 506      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     INS 1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE                              
HETSYN     INS MYO-INOSITOL                                                     
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   5  SO4    13(O4 S 2-)                                                  
FORMUL  18  INS    2(C6 H12 O6)                                                 
FORMUL  20  HOH   *286(H2 O)                                                    
HELIX    1   1 THR A   86  LEU A   94  1                                   9    
HELIX    2   2 SER A   97  SER A  110  1                                  14    
HELIX    3   3 PRO A  150  LYS A  155  1                                   6    
HELIX    4   4 LEU A  156  ALA A  168  1                                  13    
HELIX    5   5 PRO A  182  LYS A  186  5                                   5    
HELIX    6   6 ASP A  203  HIS A  223  1                                  21    
HELIX    7   7 GLU A  235  LEU A  241  5                                   7    
HELIX    8   8 THR A  252  ASP A  263  1                                  12    
HELIX    9   9 ASP A  263  ASN A  270  1                                   8    
HELIX   10  10 LEU A  286  LEU A  288  5                                   3    
HELIX   11  11 PRO A  289  THR A  297  1                                   9    
HELIX   12  12 ASP A  298  LYS A  303  1                                   6    
HELIX   13  13 THR A  323  PHE A  331  1                                   9    
HELIX   14  14 SER A  356  TYR A  373  1                                  18    
HELIX   15  15 ILE A  406  LYS A  408  5                                   3    
HELIX   16  16 GLN A  414  LYS A  425  1                                  12    
HELIX   17  17 THR B   86  ALA B   95  1                                  10    
HELIX   18  18 SER B   97  SER B  110  1                                  14    
HELIX   19  19 PRO B  150  LYS B  155  1                                   6    
HELIX   20  20 LEU B  156  ALA B  168  1                                  13    
HELIX   21  21 PRO B  182  LYS B  186  5                                   5    
HELIX   22  22 ASP B  203  HIS B  223  1                                  21    
HELIX   23  23 GLU B  235  LEU B  241  5                                   7    
HELIX   24  24 THR B  252  ASP B  263  1                                  12    
HELIX   25  25 ASP B  263  ASN B  270  1                                   8    
HELIX   26  26 LEU B  286  LEU B  288  5                                   3    
HELIX   27  27 PRO B  289  THR B  297  1                                   9    
HELIX   28  28 ASP B  298  LYS B  303  1                                   6    
HELIX   29  29 THR B  323  PHE B  331  1                                   9    
HELIX   30  30 SER B  356  TYR B  373  1                                  18    
HELIX   31  31 ILE B  406  LYS B  408  5                                   3    
HELIX   32  32 GLN B  414  LYS B  425  1                                  12    
SHEET    1   A 4 PRO A   6  LYS A   7  0                                        
SHEET    2   A 4 VAL A  15  ASN A  19 -1  O  VAL A  15   N  LYS A   7           
SHEET    3   A 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18           
SHEET    4   A 4 ILE A 402  ASP A 405 -1  N  ILE A 403   O  TYR A 412           
SHEET    1   B 9 GLU A  50  PRO A  55  0                                        
SHEET    2   B 9 THR A  36  THR A  43 -1  N  ARG A  39   O  SER A  52           
SHEET    3   B 9 SER A 488  TRP A 494 -1  O  LEU A 493   N  SER A  38           
SHEET    4   B 9 ALA A 456  ASN A 462 -1  N  VAL A 458   O  TYR A 492           
SHEET    5   B 9 LEU A 444  MET A 450 -1  N  ASP A 445   O  LEU A 461           
SHEET    6   B 9 GLN A 432  ALA A 438 -1  N  GLN A 432   O  MET A 450           
SHEET    7   B 9 LEU A  66  LYS A  77 -1  N  THR A  68   O  VAL A 437           
SHEET    8   B 9 VAL A 468  ASP A 474  1  O  LYS A 473   N  LEU A  67           
SHEET    9   B 9 GLY A 478  SER A 484 -1  O  SER A 484   N  VAL A 468           
SHEET    1   C 9 GLY A  80  ALA A  84  0                                        
SHEET    2   C 9 ILE A 118  MET A 123  1  O  ARG A 120   N  GLY A  83           
SHEET    3   C 9 SER A 173  PRO A 178  1  O  SER A 177   N  MET A 123           
SHEET    4   C 9 ALA A 229  THR A 231  1  O  THR A 231   N  ALA A 176           
SHEET    5   C 9 ARG A 277  GLN A 284  1  O  ARG A 277   N  VAL A 230           
SHEET    6   C 9 GLY A 307  TYR A 313  1  O  GLY A 307   N  MET A 280           
SHEET    7   C 9 MET A 335  CYS A 342  1  O  PHE A 337   N  VAL A 310           
SHEET    8   C 9 VAL A 375  ASN A 382  1  O  VAL A 376   N  LEU A 336           
SHEET    9   C 9 GLY A  80  ALA A  84  1  N  ALA A  84   O  TRP A 381           
SHEET    1   D 4 PRO B   6  LYS B   7  0                                        
SHEET    2   D 4 VAL B  15  ASN B  19 -1  O  VAL B  15   N  LYS B   7           
SHEET    3   D 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18           
SHEET    4   D 4 ILE B 402  ASP B 405 -1  N  ILE B 403   O  TYR B 412           
SHEET    1   E 9 GLU B  50  PRO B  55  0                                        
SHEET    2   E 9 THR B  36  THR B  43 -1  N  ARG B  39   O  SER B  52           
SHEET    3   E 9 SER B 488  TRP B 494 -1  O  LEU B 493   N  SER B  38           
SHEET    4   E 9 ALA B 456  ASN B 462 -1  N  VAL B 458   O  TYR B 492           
SHEET    5   E 9 LEU B 444  MET B 450 -1  N  ASP B 445   O  LEU B 461           
SHEET    6   E 9 GLN B 432  ALA B 438 -1  N  GLN B 432   O  MET B 450           
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  THR B  68   O  VAL B 437           
SHEET    8   E 9 VAL B 468  ASP B 474  1  O  LYS B 473   N  LEU B  67           
SHEET    9   E 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474           
SHEET    1   F 9 GLY B  80  ALA B  84  0                                        
SHEET    2   F 9 ILE B 118  MET B 123  1  O  ARG B 120   N  GLY B  83           
SHEET    3   F 9 SER B 173  PRO B 178  1  O  SER B 177   N  MET B 123           
SHEET    4   F 9 ALA B 229  THR B 231  1  O  THR B 231   N  ALA B 176           
SHEET    5   F 9 ARG B 277  GLN B 284  1  O  ARG B 277   N  VAL B 230           
SHEET    6   F 9 GLY B 307  TYR B 313  1  O  GLY B 307   N  MET B 280           
SHEET    7   F 9 MET B 335  CYS B 342  1  O  PHE B 337   N  VAL B 310           
SHEET    8   F 9 VAL B 375  ASN B 382  1  O  VAL B 376   N  LEU B 336           
SHEET    9   F 9 GLY B  80  ALA B  84  1  N  ALA B  84   O  TRP B 381           
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.06  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.04  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.06  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.05  
LINK         ND2 ASN A  19                 C1  NAG A 498     1555   1555  1.46  
LINK         ND2 ASN B  19                 C1  NAG B 498     1555   1555  1.45  
LINK         O4  NAG A 498                 C1  NAG A 499     1555   1555  1.39  
LINK         O4  NAG B 498                 C1  NAG B 499     1555   1555  1.39  
LINK         C1  INS A 507                 OE2 GLU A 340     1555   1555  1.43  
LINK         C1  INS B 506                 OE2 GLU B 340     1555   1555  1.43  
CISPEP   1 LEU A  288    PRO A  289          0         0.32                     
CISPEP   2 GLY A  390    PRO A  391          0         0.17                     
CISPEP   3 LEU B  288    PRO B  289          0         0.09                     
CISPEP   4 GLY B  390    PRO B  391          0         0.23                     
SITE     1 AC1  5 ASN A  19  THR A  21  GLN A 497  NAG A 499                    
SITE     2 AC1  5 HOH A 599                                                     
SITE     1 AC2  2 NAG A 498  HOH A 601                                          
SITE     1 AC3  3 ASN B  19  THR B  21  NAG B 499                               
SITE     1 AC4  1 NAG B 498                                                     
SITE     1 AC5  3 GLU A 254  ARG A 257  HOH A 598                               
SITE     1 AC6  2 ARG A  44  SER A  45                                          
SITE     1 AC7  6 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 AC7  6 TRP A 357  ASP A 358                                          
SITE     1 AC8  5 THR A  63  GLY A  64  GLN A 440  LYS A 473                    
SITE     2 AC8  5 HOH A 633                                                     
SITE     1 AC9  5 LYS A  79  TRP A 228  ARG A 277  HIS A 306                    
SITE     2 AC9  5 HOH A 625                                                     
SITE     1 BC1  6 ARG B 285  TRP B 312  LEU B 314  HIS B 365                    
SITE     2 BC1  6 SER B 366  THR B 369                                          
SITE     1 BC2  2 HIS A 290  LYS A 293                                          
SITE     1 BC3  6 LYS B  79  TRP B 228  ARG B 277  HIS B 306                    
SITE     2 BC3  6 HOH B 591  HOH B 592                                          
SITE     1 BC4  6 CYS B   4  GLY B  46  ARG B  47  ARG B  48                    
SITE     2 BC4  6 GLU B  50  GLN B  57                                          
SITE     1 BC5  3 ARG B  44  SER B  45  HOH B 599                               
SITE     1 BC6  3 ARG A 329  LYS B 321  ARG B 329                               
SITE     1 BC7  4 GLY B 193  LYS B 194  SER B 242  GLY B 243                    
SITE     1 BC8  6 TYR B  11  SER B  12  ARG B 353  SER B 356                    
SITE     2 BC8  6 TRP B 357  ASP B 358                                          
SITE     1 BC9  9 ASP A 127  PHE A 128  TRP A 179  ASN A 234                    
SITE     2 BC9  9 TYR A 313  GLU A 340  CYS A 342  TRP A 381                    
SITE     3 BC9  9 ASN A 396                                                     
SITE     1 CC1  9 ASP B 127  PHE B 128  TRP B 179  ASN B 234                    
SITE     2 CC1  9 TYR B 313  GLU B 340  CYS B 342  TRP B 381                    
SITE     3 CC1  9 ASN B 396                                                     
CRYST1  104.490  285.610   91.510  90.00  90.00  90.00 C 2 2 21     16          
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      0.009570  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003501  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010928        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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