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Database: PDB
Entry: 2XWD
LinkDB: 2XWD
Original site: 2XWD 
HEADER    HYDROLASE                               01-NOV-10   2XWD              
TITLE     X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6O-(N'-(N-           
TITLE    2 OCTYL)IMINO)NOJIRIMYCIN IN THE ACTIVE SITE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACID-BETA-GLUCOSIDASE, ALGLUCERASE,                         
COMPND   5  BETA-GLUCOCEREBROSIDASE, D-GLUCOSYL-N-ACYLSPHINGOSINE               
COMPND   6  GLUCOHYDROLASE, IMIGLUCERASE;                                       
COMPND   7 EC: 3.2.1.45;                                                        
COMPND   8 ENGINEERED: 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: DAUCUS CAROTA;                                    
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CARROT;                                    
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4039                                        
KEYWDS    GLUCOCEREBROSIDASE, HYDROLASE, GAUCHER DISEASE, SPHINGOLIPID          
KEYWDS   2 METABOLISM                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.BRUMSHTEIN,M.AGUILAR-MONCAYO,J.M.BENITO,C.ORTIZ MELLET,             
AUTHOR   2 J.M.GARCIA FERNANDEZ,I.SILMAN,Y.SHAALTIEL,J.L.SUSSMAN,A.H.FUTERMAN   
REVDAT   1   14-SEP-11 2XWD    0                                                
JRNL        AUTH   B.BRUMSHTEIN,M.AGUILAR-MONCAYO,J.M.BENITO,                   
JRNL        AUTH 2 J.M.GARCIA FERNANDEZ,I.SILMAN,Y.SHAALTIEL,D.AVIEZER,         
JRNL        AUTH 3 J.L.SUSSMAN,A.H.FUTERMAN,C.ORTIZ MELLET                      
JRNL        TITL   CYCLODEXTRIN-MEDIATED CRYSTALLIZATION OF ACID BETA-          
JRNL        TITL 2 GLUCOSIDASE IN COMPLEX WITH AMPHIPHILIC BICYCLIC             
JRNL        TITL 3 NOJIRIMYCIN ANALOGUES.                                       
JRNL        REF    ORG.BIOMOL.CHEM.              V.   9  4160 2011              
JRNL        REFN                   ISSN 1477-0520                               
JRNL        PMID   21483943                                                     
JRNL        DOI    10.1039/C1OB05200D                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.79                          
REMARK   3   NUMBER OF REFLECTIONS             : 28378                          
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 + TEST SET) : 0.15348                         
REMARK   3   R VALUE            (WORKING SET) : 0.15003                         
REMARK   3   FREE R VALUE                     : 0.21893                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1510                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.657                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.726                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1821                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.194                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.290                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7721                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 196                                     
REMARK   3   SOLVENT ATOMS            : 266                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.304                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03                                                 
REMARK   3    B22 (A**2) : -0.02                                                
REMARK   3    B33 (A**2) : -0.02                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.01                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.319         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.711         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8155 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11126 ; 1.581 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   981 ; 6.731 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   348 ;37.490 ;23.448       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1213 ;16.240 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;20.043 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1232 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6162 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4916 ; 0.689 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7926 ; 1.349 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3239 ; 2.110 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3200 ; 3.368 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 8                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     -1       A      25      3                      
REMARK   3           1     B     -1       B      25      3                      
REMARK   3           2     A     27       A      50      3                      
REMARK   3           2     B     27       B      50      3                      
REMARK   3           3     A     65       A     168      3                      
REMARK   3           3     B     65       B     168      3                      
REMARK   3           4     A    170       A     311      3                      
REMARK   3           4     B    170       B     311      3                      
REMARK   3           5     A    320       A     340      3                      
REMARK   3           5     B    320       B     340      3                      
REMARK   3           6     A    360       A     395      3                      
REMARK   3           6     B    360       B     395      3                      
REMARK   3           7     A    400       A     449      3                      
REMARK   3           7     B    400       B     449      3                      
REMARK   3           8     A    456       A     497      3                      
REMARK   3           8     B    456       B     497      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1756 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1756 ;  0.05 ;  0.05           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1666 ;  0.07 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1666 ;  0.07 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1756 ;  0.12 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1756 ;  0.12 ;  0.50           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1666 ;  0.15 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1666 ;  0.15 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2XWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-46040.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : PT COATED SI MIRROR                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28378                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.66                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.90                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.7                                
REMARK 200  R MERGE                    (I) : 0.18                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.55                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2J25                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1 M TRIS PH            
REMARK 280  6.5, 25% W/V PEG3350                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       48.30850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A    -1                                                      
REMARK 465     ASP A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     THR A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     LEU A   498                                                      
REMARK 465     LEU A   499                                                      
REMARK 465     VAL A   500                                                      
REMARK 465     ASP A   501                                                      
REMARK 465     THR A   502                                                      
REMARK 465     MET A   503                                                      
REMARK 465     GLU B    -1                                                      
REMARK 465     ASP B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     THR B    30                                                      
REMARK 465     PHE B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     LEU B   498                                                      
REMARK 465     LEU B   499                                                      
REMARK 465     VAL B   500                                                      
REMARK 465     ASP B   501                                                      
REMARK 465     THR B   502                                                      
REMARK 465     MET B   503                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A  34    CG   CD1  CD2                                       
REMARK 470     GLN A 143    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 155    CE   NZ                                             
REMARK 470     ARG A 163    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 277    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 300    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 321    CE   NZ                                             
REMARK 470     LYS A 346    CE   NZ                                             
REMARK 470     PHE A 347    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     LYS A 441    CD   CE   NZ                                        
REMARK 470     LYS A 466    CE   NZ                                             
REMARK 470     GLN A 497    CG   CD   OE1  NE2                                  
REMARK 470     PHE B   0    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B  34    CG   CD1  CD2                                       
REMARK 470     GLU B 111    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 155    CG   CD   CE   NZ                                   
REMARK 470     LYS B 441    CD   CE   NZ                                        
REMARK 470     ARG B 463    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 466    CD   CE   NZ                                        
REMARK 470     GLN B 497    CG   CD   OE1  NE2                                  
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   O    HOH A  2029     O    HOH A  2081              1.84            
REMARK 500   O    HOH A  2107     O    HOH A  2108              2.00            
REMARK 500   O    HOH B  2036     O    HOH B  2117              2.05            
REMARK 500   OG   SER B    12     O3   SO4 B  1502              2.09            
REMARK 500   O    HOH A  2005     O    HOH A  2010              2.09            
REMARK 500   O    HOH B  2094     O    HOH B  2095              2.13            
REMARK 500   O    HOH B  2018     O    HOH B  2050              2.15            
REMARK 500   O4   NAG A  1498     O5   NAG A  1499              2.15            
REMARK 500   O    HOH B  2066     O    HOH B  2068              2.17            
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    GLU A 111   CB    GLU A 111   CG      0.136                       
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    ASP A 218   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 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    PHE A  75     -134.77   -122.92                                   
REMARK 500    ALA A 124     -161.96     69.04                                   
REMARK 500    ASN A 146       32.39    -95.55                                   
REMARK 500    LEU A 156      -72.35   -106.22                                   
REMARK 500    ASN A 192     -164.32   -115.78                                   
REMARK 500    GLU A 233      135.13    166.17                                   
REMARK 500    LEU A 249      109.00   -160.70                                   
REMARK 500    LEU A 281      -82.05     68.92                                   
REMARK 500    THR A 323      -73.39   -118.01                                   
REMARK 500    SER A 356      108.49    -57.60                                   
REMARK 500    TRP A 381     -141.65    -79.18                                   
REMARK 500    ASN A 382      126.81    -39.85                                   
REMARK 500    VAL A 477      -35.84   -141.45                                   
REMARK 500    TYR A 487      -12.46     68.37                                   
REMARK 500    ASN B  19     -158.45   -140.31                                   
REMARK 500    PHE B  75     -130.12   -123.09                                   
REMARK 500    ALA B 124     -166.50     67.78                                   
REMARK 500    ASN B 146       30.87    -93.65                                   
REMARK 500    LEU B 156      -73.31   -108.74                                   
REMARK 500    ASN B 192     -163.87   -120.94                                   
REMARK 500    SER B 196     -169.75   -129.04                                   
REMARK 500    GLU B 233      130.91    170.54                                   
REMARK 500    TYR B 244      125.85    -38.60                                   
REMARK 500    LEU B 249      112.24   -161.08                                   
REMARK 500    LEU B 281      -77.51     68.04                                   
REMARK 500    ALA B 318       86.00   -151.65                                   
REMARK 500    THR B 323      -75.88   -114.51                                   
REMARK 500    HIS B 374        0.38     81.19                                   
REMARK 500    TRP B 381     -142.97    -85.02                                   
REMARK 500    ASN B 382      121.01    -35.44                                   
REMARK 500    VAL B 477      -36.33   -139.97                                   
REMARK 500    TYR B 487      -12.41     74.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE B  26        21.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     LGS A 1510                                                       
REMARK 610     LGS B 1510                                                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BC" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LGS A1510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LGS B1510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF                        
REMARK 800  SUGAR BOUND TO ASN A  19 RESIDUES 1498 TO 1501                      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF                        
REMARK 800  SUGAR BOUND TO ASN B  19 RESIDUES 1498 TO 1501                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Y7V   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN ACID-BETA-GLUCOSIDASE                      
REMARK 900  COVALENTLYBOUND TO CONDURITOL B EPOXIDE                             
REMARK 900 RELATED ID: 2F61   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PARTIALLY DEGLYCOSYLATED ACID BETA-            
REMARK 900  GLUCOSIDASE                                                         
REMARK 900 RELATED ID: 2V3F   RELATED DB: PDB                                   
REMARK 900  ACID-BETA-GLUCOSIDASE PRODUCED IN CARROT                            
REMARK 900 RELATED ID: 2J25   RELATED DB: PDB                                   
REMARK 900  PARTIALLY DEGLYCOSYLATED GLUCOCERAMIDASE                            
REMARK 900 RELATED ID: 2V3E   RELATED DB: PDB                                   
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-NONYL-DEOXYNOJIRIMYCIN                 
REMARK 900 RELATED ID: 2WKL   RELATED DB: PDB                                   
REMARK 900  VELAGLUCERASE ALFA                                                  
REMARK 900 RELATED ID: 2V3D   RELATED DB: PDB                                   
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-BUTYL-DEOXYNOJIRIMYCIN                 
REMARK 900 RELATED ID: 1OGS   RELATED DB: PDB                                   
REMARK 900  HUMAN ACID-BETA-GLUCOSIDASE                                         
REMARK 900 RELATED ID: 2XWE   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6S                 
REMARK 900  -(N'-(N-OCTYL)IMINO)-6-THIONOJIRIMYCIN IN THE ACTIVE                
REMARK 900   SITE                                                               
REMARK 900 RELATED ID: 2WCG   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH N-                    
REMARK 900  OCTYL(CYCLIC GUANIDINE)-NOJIRIMYCIN IN THE ACTIVE SITE              
DBREF  2XWD A    1   497  UNP    P04062   GLCM_HUMAN      20    516             
DBREF  2XWD B    1   497  UNP    P04062   GLCM_HUMAN      20    516             
SEQADV 2XWD GLU A   -1  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD PHE A    0  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD HIS A  495  UNP  P04062    ARG   514 VARIANT                        
SEQADV 2XWD LEU A  498  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD LEU A  499  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD VAL A  500  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD ASP A  501  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD THR A  502  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD MET A  503  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD GLU B   -1  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD PHE B    0  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD HIS B  495  UNP  P04062    ARG   514 VARIANT                        
SEQADV 2XWD LEU B  498  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD LEU B  499  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD VAL B  500  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD ASP B  501  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD THR B  502  UNP  P04062              EXPRESSION TAG                 
SEQADV 2XWD MET B  503  UNP  P04062              EXPRESSION TAG                 
SEQRES   1 A  505  GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR          
SEQRES   2 A  505  SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP          
SEQRES   3 A  505  SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE          
SEQRES   4 A  505  SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU          
SEQRES   5 A  505  LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR          
SEQRES   6 A  505  GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN          
SEQRES   7 A  505  LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA          
SEQRES   8 A  505  ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN          
SEQRES   9 A  505  LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY          
SEQRES  10 A  505  TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE          
SEQRES  11 A  505  SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP          
SEQRES  12 A  505  PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR          
SEQRES  13 A  505  LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU          
SEQRES  14 A  505  ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR          
SEQRES  15 A  505  SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY          
SEQRES  16 A  505  LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS          
SEQRES  17 A  505  GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA          
SEQRES  18 A  505  TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA          
SEQRES  19 A  505  GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO          
SEQRES  20 A  505  PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP          
SEQRES  21 A  505  PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER          
SEQRES  22 A  505  THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN          
SEQRES  23 A  505  ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR          
SEQRES  24 A  505  ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL          
SEQRES  25 A  505  HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR          
SEQRES  26 A  505  LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU          
SEQRES  27 A  505  PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU          
SEQRES  28 A  505  GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN          
SEQRES  29 A  505  TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL          
SEQRES  30 A  505  VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU          
SEQRES  31 A  505  GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO          
SEQRES  32 A  505  ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN          
SEQRES  33 A  505  PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE          
SEQRES  34 A  505  PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN          
SEQRES  35 A  505  LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP          
SEQRES  36 A  505  GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS          
SEQRES  37 A  505  ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE          
SEQRES  38 A  505  LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR          
SEQRES  39 A  505  LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET                  
SEQRES   1 B  505  GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR          
SEQRES   2 B  505  SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP          
SEQRES   3 B  505  SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE          
SEQRES   4 B  505  SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU          
SEQRES   5 B  505  LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR          
SEQRES   6 B  505  GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN          
SEQRES   7 B  505  LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA          
SEQRES   8 B  505  ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN          
SEQRES   9 B  505  LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY          
SEQRES  10 B  505  TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE          
SEQRES  11 B  505  SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP          
SEQRES  12 B  505  PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR          
SEQRES  13 B  505  LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU          
SEQRES  14 B  505  ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR          
SEQRES  15 B  505  SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY          
SEQRES  16 B  505  LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS          
SEQRES  17 B  505  GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA          
SEQRES  18 B  505  TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA          
SEQRES  19 B  505  GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO          
SEQRES  20 B  505  PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP          
SEQRES  21 B  505  PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER          
SEQRES  22 B  505  THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN          
SEQRES  23 B  505  ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR          
SEQRES  24 B  505  ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL          
SEQRES  25 B  505  HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR          
SEQRES  26 B  505  LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU          
SEQRES  27 B  505  PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU          
SEQRES  28 B  505  GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN          
SEQRES  29 B  505  TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL          
SEQRES  30 B  505  VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU          
SEQRES  31 B  505  GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO          
SEQRES  32 B  505  ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN          
SEQRES  33 B  505  PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE          
SEQRES  34 B  505  PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN          
SEQRES  35 B  505  LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP          
SEQRES  36 B  505  GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS          
SEQRES  37 B  505  ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE          
SEQRES  38 B  505  LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR          
SEQRES  39 B  505  LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET                  
HET    NAG  A1498      14                                                       
HET    NAG  A1499      14                                                       
HET    MAN  A1500      11                                                       
HET    FUC  A1501      10                                                       
HET    SO4  A1502       5                                                       
HET    SO4  A1503       5                                                       
HET    SO4  A1504       5                                                       
HET    SO4  A1505       5                                                       
HET    SO4  A1506       5                                                       
HET    LGS  A1510      16                                                       
HET    NAG  B1498      14                                                       
HET    NAG  B1499      14                                                       
HET    BMA  B1500      11                                                       
HET    FUC  B1501      10                                                       
HET    SO4  B1502       5                                                       
HET    SO4  B1503       5                                                       
HET    SO4  B1504       5                                                       
HET    SO4  B1505       5                                                       
HET    SO4  B1506       5                                                       
HET    LGS  B1510      32                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM     LGS (3Z,5S,6R,7S,8R,8AR)-3-(OCTYLIMINO)HEXAHYDRO                     
HETNAM   2 LGS  [1,3]OXAZOLO[3,4-A]PYRIDINE-5,6,7,8-TETROL                      
HETNAM     BMA BETA-D-MANNOSE                                                   
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   4  MAN    C6 H12 O6                                                    
FORMUL   5  FUC    2(C6 H12 O5)                                                 
FORMUL   6  SO4    10(O4 S 2-)                                                  
FORMUL   7  LGS    2(C15 H28 N2 O5)                                             
FORMUL   8  BMA    C6 H12 O6                                                    
FORMUL   9  HOH   *266(H2 O)                                                    
HELIX    1   1 THR A   86  ALA A   95  1                                  10    
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  LEU A  185  5                                   4    
HELIX    6   6 ASP A  203  HIS A  223  1                                  21    
HELIX    7   7 SER A  237  LEU A  241  5                                   5    
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 LEU A  314  ALA A  318  5                                   5    
HELIX   14  14 PRO A  319  PHE A  331  1                                  13    
HELIX   15  15 SER A  356  TYR A  373  1                                  18    
HELIX   16  16 ILE A  406  ASP A  409  5                                   4    
HELIX   17  17 GLN A  414  LYS A  425  1                                  12    
HELIX   18  18 THR B   86  ALA B   95  1                                  10    
HELIX   19  19 SER B   97  SER B  110  1                                  14    
HELIX   20  20 PRO B  150  LYS B  155  1                                   6    
HELIX   21  21 LEU B  156  ALA B  168  1                                  13    
HELIX   22  22 PRO B  182  LEU B  185  5                                   4    
HELIX   23  23 ASP B  203  HIS B  223  1                                  21    
HELIX   24  24 SER B  237  LEU B  241  5                                   5    
HELIX   25  25 THR B  252  ASP B  263  1                                  12    
HELIX   26  26 ASP B  263  ASN B  270  1                                   8    
HELIX   27  27 LEU B  286  LEU B  288  5                                   3    
HELIX   28  28 PRO B  289  THR B  297  1                                   9    
HELIX   29  29 ASP B  298  LYS B  303  1                                   6    
HELIX   30  30 LEU B  314  ALA B  318  5                                   5    
HELIX   31  31 THR B  323  PHE B  331  1                                   9    
HELIX   32  32 SER B  356  LEU B  372  1                                  17    
HELIX   33  33 ILE B  406  ASP B  409  5                                   4    
HELIX   34  34 GLN B  414  LYS B  425  1                                  12    
SHEET    1  AA 4 PRO A   6  LYS A   7  0                                        
SHEET    2  AA 4 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7           
SHEET    3  AA 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18           
SHEET    4  AA 4 ILE A 402  ASP A 405 -1  O  ILE A 403   N  TYR A 412           
SHEET    1  AB 9 GLU A  50  PRO A  55  0                                        
SHEET    2  AB 9 THR A  36  SER A  42 -1  O  PHE A  37   N  GLY A  54           
SHEET    3  AB 9 ILE A 489  TRP A 494 -1  O  ILE A 489   N  SER A  42           
SHEET    4  AB 9 ALA A 456  ASN A 462 -1  O  ALA A 456   N  TRP A 494           
SHEET    5  AB 9 LEU A 444  MET A 450 -1  O  ASP A 445   N  LEU A 461           
SHEET    6  AB 9 GLN A 432  ALA A 438 -1  O  GLN A 432   N  MET A 450           
SHEET    7  AB 9 LEU A  65  LYS A  77 -1  O  THR A  68   N  VAL A 437           
SHEET    8  AB 9 VAL A 468  ASP A 474  1  O  PRO A 469   N  LEU A  65           
SHEET    9  AB 9 GLY A 478  SER A 484 -1  O  GLY A 478   N  ASP A 474           
SHEET    1  AC 9 GLY A  80  ALA A  84  0                                        
SHEET    2  AC 9 VAL A 375  ASN A 382  1  O  TRP A 378   N  GLY A  82           
SHEET    3  AC 9 MET A 335  GLU A 340  1  O  LEU A 336   N  VAL A 376           
SHEET    4  AC 9 VAL A 305  HIS A 311  1  O  HIS A 306   N  MET A 335           
SHEET    5  AC 9 ARG A 277  GLN A 284  1  O  LEU A 278   N  HIS A 306           
SHEET    6  AC 9 PHE A 227  THR A 231  1  O  TRP A 228   N  ARG A 277           
SHEET    7  AC 9 SER A 173  PRO A 178  1  O  LEU A 174   N  TRP A 228           
SHEET    8  AC 9 ILE A 118  MET A 123  1  O  ILE A 119   N  LEU A 175           
SHEET    9  AC 9 GLY A  80  ALA A  84  1  O  GLY A  83   N  ARG A 120           
SHEET    1  BA 4 PRO B   6  LYS B   7  0                                        
SHEET    2  BA 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7           
SHEET    3  BA 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18           
SHEET    4  BA 4 ILE B 402  ASP B 405 -1  O  ILE B 403   N  TYR B 412           
SHEET    1  BB 9 GLU B  50  PRO B  55  0                                        
SHEET    2  BB 9 THR B  36  SER B  42 -1  O  PHE B  37   N  GLY B  54           
SHEET    3  BB 9 ILE B 489  TRP B 494 -1  O  ILE B 489   N  SER B  42           
SHEET    4  BB 9 ALA B 456  ASN B 462 -1  O  ALA B 456   N  TRP B 494           
SHEET    5  BB 9 LEU B 444  MET B 450 -1  O  ASP B 445   N  LEU B 461           
SHEET    6  BB 9 GLN B 432  ALA B 438 -1  O  GLN B 432   N  MET B 450           
SHEET    7  BB 9 LEU B  65  LYS B  77 -1  O  THR B  68   N  VAL B 437           
SHEET    8  BB 9 VAL B 468  ASP B 474  1  O  PRO B 469   N  LEU B  65           
SHEET    9  BB 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474           
SHEET    1  BC 9 GLY B  80  ALA B  84  0                                        
SHEET    2  BC 9 VAL B 375  ASN B 382  1  O  TRP B 378   N  GLY B  82           
SHEET    3  BC 9 MET B 335  GLU B 340  1  O  LEU B 336   N  VAL B 376           
SHEET    4  BC 9 GLY B 307  HIS B 311  1  O  ILE B 308   N  PHE B 337           
SHEET    5  BC 9 ARG B 277  GLN B 284  1  O  MET B 280   N  ALA B 309           
SHEET    6  BC 9 ALA B 229  THR B 231  1  O  VAL B 230   N  LEU B 279           
SHEET    7  BC 9 SER B 173  PRO B 178  1  O  LEU B 174   N  ALA B 229           
SHEET    8  BC 9 ILE B 118  MET B 123  1  O  ILE B 119   N  LEU B 175           
SHEET    9  BC 9 GLY B  80  ALA B  84  1  O  GLY B  83   N  ARG B 120           
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.12  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.17  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.06  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.14  
LINK         ND2 ASN A  19                 C1  NAG A1498     1555   1555  1.40  
LINK         O3  NAG A1498                 C1  FUC A1501     1555   1555  1.45  
LINK         O4  NAG A1498                 C1  NAG A1499     1555   1555  1.40  
LINK         O4  NAG A1499                 C1  MAN A1500     1555   1555  1.41  
LINK         ND2 ASN B  19                 C1  NAG B1498     1555   1555  1.40  
LINK         O4  NAG B1498                 C1  NAG B1499     1555   1555  1.41  
LINK         O3  NAG B1498                 C1  FUC B1501     1555   1555  1.43  
LINK         O4  NAG B1499                 C1  BMA B1500     1555   1555  1.41  
CISPEP   1 LEU A  288    PRO A  289          0         1.93                     
CISPEP   2 GLY A  390    PRO A  391          0         1.97                     
CISPEP   3 LEU B  288    PRO B  289          0        -0.61                     
CISPEP   4 GLY B  390    PRO B  391          0         5.55                     
SITE     1 AC1  2 GLU A 254  ARG A 257                                          
SITE     1 AC2  5 GLY A 193  LYS A 194  SER A 242  GLY A 243                    
SITE     2 AC2  5 HOH A2048                                                     
SITE     1 AC3  4 LYS A  79  TRP A 228  HIS A 306  HOH A2137                    
SITE     1 AC4  7 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 AC4  7 TRP A 357  ASP A 358  HOH A2136                               
SITE     1 AC5  3 ARG A  44  SER A  45  HOH A2013                               
SITE     1 AC6 10 ASP A 127  PHE A 128  TRP A 179  ASN A 234                    
SITE     2 AC6 10 GLU A 235  PHE A 246  TYR A 313  GLU A 340                    
SITE     3 AC6 10 SER A 345  TRP A 381                                          
SITE     1 AC7  6 TYR B  11  SER B  12  ARG B 353  SER B 356                    
SITE     2 AC7  6 TRP B 357  ASP B 358                                          
SITE     1 AC8  5 LYS B  79  TRP B 228  ARG B 277  HIS B 306                    
SITE     2 AC8  5 HOH B2127                                                     
SITE     1 AC9  3 ARG B  44  SER B  45  HOH B2007                               
SITE     1 BC1  4 GLY B 193  LYS B 194  SER B 242  GLY B 243                    
SITE     1 BC2  2 GLU B 254  ARG B 257                                          
SITE     1 BC3 12 ASP B 127  PHE B 128  TRP B 179  ASN B 234                    
SITE     2 BC3 12 GLU B 235  TYR B 244  PHE B 246  TYR B 313                    
SITE     3 BC3 12 GLU B 340  SER B 345  TRP B 381  ASN B 396                    
SITE     1 BC4  1 ASN A  19                                                     
SITE     1 BC5  2 ASN B  19  HOH B2128                                          
CRYST1   68.036   96.617   83.164  90.00 103.69  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014698  0.000000  0.003580        0.00000                         
SCALE2      0.000000  0.010350  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012376        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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