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Database: PDB
Entry: 2V3F
LinkDB: 2V3F
Original site: 2V3F 
HEADER    HYDROLASE                               17-JUN-07   2V3F              
TITLE     ACID-BETA-GLUCOSIDASE PRODUCED IN CARROT                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID-BETA-GLUCOSIDASE,             
COMPND   5  D-GLUCOSYL-N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE,           
COMPND   6  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_TAXID: 4039                                        
KEYWDS    ALTERNATIVE INITIATION, SPHINGOLIPID METABOLISM, GAUCHER              
KEYWDS   2 DISEASE, DISEASE MUTATION, LIPID METABOLISM, POLYMORPHISM,           
KEYWDS   3 GLYCOPROTEIN, PHARMACEUTICAL, N-BUTYL-DEOXYNOJIRIMYCIN,              
KEYWDS   4 ALTERNATIVE SPLICING, ACID-BETA-GLUCOSIDASE, MEMBRANE,               
KEYWDS   5 LYSOSOME, HYDROLASE, GLYCOSIDASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SHAALTIEL,D.BARTFELD,S.HASHMUELI,G.BAUM,E.BRILL-ALMON,              
AUTHOR   2 G.GALILI,O.DYM,S.A.BOLDIN-ADAMSKY,I.SILMAN,J.L.SUSSMAN,              
AUTHOR   3 A.H.FUTERMAN,D.AVIEZER,                                              
AUTHOR   4 ISRAEL STRUCTURAL PROTEOMICS CENTER(ISPC)                            
REVDAT   3   24-FEB-09 2V3F    1       VERSN                                    
REVDAT   2   06-MAY-08 2V3F    1       AUTHOR                                   
REVDAT   1   08-APR-08 2V3F    0                                                
JRNL        AUTH   Y.SHAALTIEL,D.BARTFELD,S.HASHMUELI,G.BAUM,                   
JRNL        AUTH 2 E.BRILL-ALMON,G.GALILI,O.DYM,S.A.BOLDIN-ADAMSKY,             
JRNL        AUTH 3 I.SILMAN,J.L.SUSSMAN,A.H.FUTERMAN,D.AVIEZER                  
JRNL        TITL   PRODUCTION OF GLUCOCEREBROSIDASE WITH TERMINAL               
JRNL        TITL 2 MANNOSE GLYCANS FOR ENZYME REPLACEMENT THERAPY OF            
JRNL        TITL 3 GAUCHER'S DISEASE USING A PLANT CELL SYSTEM.                 
JRNL        REF    PLANT BIOTECHNOL.J.           V.   5   579 2007              
JRNL        REFN                   ISSN 1467-7644                               
JRNL        PMID   17524049                                                     
JRNL        DOI    10.1111/J.1467-7652.2007.00263.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 66326                          
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) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 7449                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4966                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1510                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 553                          
REMARK   3   BIN FREE R VALUE                    : 0.2170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7785                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 175                                     
REMARK   3   SOLVENT ATOMS            : 805                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.162         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.145         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.790         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8202 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11214 ; 1.371 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   992 ; 7.556 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   355 ;36.897 ;23.437       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1237 ;14.122 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;21.089 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1231 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6218 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3817 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5589 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   781 ; 0.174 ; 0.200       
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):    36 ; 0.160 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.133 ; 0.200       
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):  5078 ; 0.850 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7989 ; 1.313 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3596 ; 2.027 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3207 ; 3.057 ; 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 : NULL                              
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2V3F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUN-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-32937.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-05                          
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                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0723                             
REMARK 200  MONOCHROMATOR                  : C AND AL                           
REMARK 200  OPTICS                         : MIRRORD                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74750                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.95                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 4                                  
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.25                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.30                               
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 1OGS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMSO4 0.2M, BIS-TRIS PH6.5, PEG          
REMARK 280  3350 25%, HEXAMINECOCL                                              
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       48.55200            
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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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: PQS                                                   
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     PRO A    29                                                      
REMARK 465     THR A    30                                                      
REMARK 465     PHE A    31                                                      
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     PHE B     0                                                      
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     GLU A  72    CD   OE1  OE2                                       
REMARK 470     ASN A 146    OD1  ND2                                            
REMARK 470     LYS A 155    CE   NZ                                             
REMARK 470     ARG A 211    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 222    CD   OE1  OE2                                       
REMARK 470     LYS A 224    CE   NZ                                             
REMARK 470     LYS A 408    CE   NZ                                             
REMARK 470     LYS A 441    CG   CD   CE   NZ                                   
REMARK 470     LYS A 466    CG   CD   CE   NZ                                   
REMARK 470     LEU A 498    CA   C    O    CB   CG   CD1  CD2                   
REMARK 470     GLU B 111    CD   OE1  OE2                                       
REMARK 470     LYS B 155    CD   CE   NZ                                        
REMARK 470     ARG B 211    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 441    CD   CE   NZ                                        
REMARK 470     GLN B 497    CA   C    O    CB   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  2021  -  O    HOH A  2054              2.18            
REMARK 500   O    HOH A  2023  -  O    HOH A  2054              2.08            
REMARK 500   O    HOH A  2038  -  O    HOH A  2044              2.19            
REMARK 500   O    HOH A  2139  -  O    HOH A  2153              2.10            
REMARK 500   O    HOH A  2221  -  O    HOH A  2251              1.73            
REMARK 500   O    HOH A  2269  -  O    HOH A  2316              1.92            
REMARK 500   O    HOH B  2016  -  O    HOH B  2019              2.17            
REMARK 500   O    HOH B  2230  -  O    HOH B  2295              2.09            
REMARK 500   O    HOH B  2248  -  O    HOH B  2295              1.75            
REMARK 500   O    HOH B  2279  -  O    HOH B  2282              2.07            
REMARK 500   O    HOH B  2296  -  O    HOH B  2336              2.19            
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 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    TYR A  11     -165.38   -100.07                                   
REMARK 500    ALA A  33      156.08    -43.94                                   
REMARK 500    GLN A  70       78.96   -119.90                                   
REMARK 500    PHE A  75     -132.70   -118.33                                   
REMARK 500    ALA A 124     -151.30     66.46                                   
REMARK 500    LEU A 156      -67.66   -107.39                                   
REMARK 500    GLU A 233      137.84    175.30                                   
REMARK 500    GLU A 235       66.11     36.76                                   
REMARK 500    ASP A 263      -70.25   -122.28                                   
REMARK 500    LEU A 281      -87.20     71.44                                   
REMARK 500    THR A 323      -72.83   -113.49                                   
REMARK 500    HIS A 374        3.57     83.39                                   
REMARK 500    TRP A 381     -134.28    -87.21                                   
REMARK 500    ALA A 476       -0.72     62.50                                   
REMARK 500    TYR A 487       -3.08     76.19                                   
REMARK 500    ASN B  19     -157.81   -146.07                                   
REMARK 500    PHE B  75     -133.03   -117.25                                   
REMARK 500    ALA B 124     -151.32     67.90                                   
REMARK 500    CYS B 126     -163.62   -129.07                                   
REMARK 500    LEU B 156      -67.34   -101.70                                   
REMARK 500    GLU B 233      137.86    174.12                                   
REMARK 500    GLU B 235       64.76     38.34                                   
REMARK 500    ASP B 263      -63.98   -121.08                                   
REMARK 500    LEU B 281      -84.82     76.04                                   
REMARK 500    THR B 323      -74.20   -115.75                                   
REMARK 500    HIS B 374       -1.48     84.61                                   
REMARK 500    TRP B 381     -134.74    -88.30                                   
REMARK 500    TYR B 487       -8.98     77.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A   26     ASP A   27                  148.88                    
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 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                                                                      
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 MAN A1500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B1500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B1508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1506                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OGS   RELATED DB: PDB                                   
REMARK 900  HUMAN ACID-BETA-GLUCOSIDASE                                         
REMARK 900 RELATED ID: 1Y7V   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN ACID-BETA-                                 
REMARK 900  GLUCOSIDASE COVALENTLYBOUND TO CONDURITOL B                         
REMARK 900  EPOXIDE                                                             
REMARK 900 RELATED ID: 2F61   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PARTIALLY DEGLYCOSYLATED                       
REMARK 900  ACID BETA-GLUCOSIDASE                                               
REMARK 900 RELATED ID: 2J25   RELATED DB: PDB                                   
REMARK 900  PARTIALLY DEGLYCOSYLATED GLUCOCERAMIDASE                            
REMARK 900 RELATED ID: 2V3D   RELATED DB: PDB                                   
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-BUTYL-                                 
REMARK 900  DEOXYNOJIRIMYCIN                                                    
REMARK 900 RELATED ID: 2V3E   RELATED DB: PDB                                   
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-NONYL-                                 
REMARK 900  DEOXYNOJIRIMYCIN                                                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 IN ADDITION TO THE NATIVE SEQUENCE OF HUMAN ACID-BETA-GLUCOSIDASE,   
REMARK 999 THE MOLECULE HAS 2 AMINO ACIDS AT THE N-TERMINAL, AND 6 AMINO ACIDS  
REMARK 999 AT THE C-TERMINAL                                                    
DBREF  2V3F A   -1     0  PDB    2V3F     2V3F            -1      0             
DBREF  2V3F A    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  2V3F A  498   503  PDB    2V3F     2V3F           498    503             
DBREF  2V3F B   -1     0  PDB    2V3F     2V3F            -1      0             
DBREF  2V3F B    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  2V3F B  498   503  PDB    2V3F     2V3F           498    503             
SEQADV 2V3F HIS A  495  UNP  P04062    ARG   534 CONFLICT                       
SEQADV 2V3F HIS B  495  UNP  P04062    ARG   534 CONFLICT                       
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    MAN  A1500      11                                                       
HET    FUC  A1508      10                                                       
HET    NAG  A1498      14                                                       
HET    NAG  A1499      14                                                       
HET    BTB  B1500      14                                                       
HET    NAG  B1498      14                                                       
HET    NAG  B1499      14                                                       
HET    BTB  A1501      14                                                       
HET    FUC  B1508      10                                                       
HET    SO4  B1501       5                                                       
HET    SO4  A1502       5                                                       
HET    SO4  A1503       5                                                       
HET    SO4  A1504       5                                                       
HET    SO4  A1505       5                                                       
HET    SO4  B1502       5                                                       
HET    SO4  B1503       5                                                       
HET    SO4  B1504       5                                                       
HET    SO4  B1505       5                                                       
HET    SO4  B1506       5                                                       
HET    SO4  B1507       5                                                       
HET    SO4  A1506       5                                                       
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-                               
HETNAM   2 BTB  HYDROXYMETHYL-PROPANE-1,3-DIOL                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     MXY 2-O-METHYL FUCOSE                                                
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     BTB BIS-TRIS BUFFER                                                  
HETSYN     NAG NAG                                                              
FORMUL   3  BTB    2(C8 H19 N O5)                                               
FORMUL   4  SO4    12(O4 S 2-)                                                  
FORMUL   5  FUC    2(C6 H12 O5)                                                 
FORMUL   6  MXY    C7 H14 O5                                                    
FORMUL   7  NAG    4(C8 H15 N O6)                                               
FORMUL   8  MAN    C6 H12 O6                                                    
FORMUL   9  HOH   *805(H2 O1)                                                   
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 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 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 GLU B  235  LEU B  241  5                                   7    
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  TYR B  373  1                                  18    
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 GLY A 307  HIS A 311  1  O  ILE A 308   N  PHE A 337           
SHEET    5  AC 9 ARG A 277  GLN A 284  1  O  MET A 280   N  ALA A 309           
SHEET    6  AC 9 ALA A 229  THR A 231  1  O  VAL A 230   N  LEU A 279           
SHEET    7  AC 9 SER A 173  PRO A 178  1  O  ALA A 176   N  THR A 231           
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  ALA B 176   N  THR B 231           
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  2.09  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.11  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.07  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.12  
LINK         ND2 ASN A  19                 C1  NAG A1498     1555   1555  1.45  
LINK         O3  NAG A1498                 C1  FUC A1508     1555   1555  1.45  
LINK         O4  NAG A1498                 C1  NAG A1499     1555   1555  1.44  
LINK         O4  NAG A1499                 C1  MAN A1500     1555   1555  1.44  
LINK         ND2 ASN B  19                 C1  NAG B1498     1555   1555  1.43  
LINK         O3  NAG B1498                 C1  FUC B1508     1555   1555  1.46  
LINK         O4  NAG B1498                 C1  NAG B1499     1555   1555  1.44  
CISPEP   1 LEU A  288    PRO A  289          0         2.90                     
CISPEP   2 GLY A  390    PRO A  391          0         7.79                     
CISPEP   3 LEU B  288    PRO B  289          0         3.50                     
CISPEP   4 GLY B  390    PRO B  391          0         7.49                     
SITE     1 AC1  2 NAG A1499  HOH A2402                                          
SITE     1 AC2  3 NAG A1498  NAG A1499  HOH A2412                               
SITE     1 AC3  6 ILE A   5  ASN A  19  NAG A1499  FUC A1508                    
SITE     2 AC3  6 HOH A2015  HOH A2400                                          
SITE     1 AC4  4 NAG A1498  MAN A1500  FUC A1508  HOH A2401                    
SITE     1 AC5 16 ASP B 127  PHE B 128  TRP B 179  ASN B 234                    
SITE     2 AC5 16 GLU B 235  TYR B 244  PHE B 246  TYR B 313                    
SITE     3 AC5 16 GLU B 340  CYS B 342  SER B 345  TRP B 381                    
SITE     4 AC5 16 VAL B 398  HOH B2204  HOH B2316  HOH B2380                    
SITE     1 AC6  7 ASN B  19  TYR B  22  NAG B1499  FUC B1508                    
SITE     2 AC6  7 HOH B2376  HOH B2377  HOH B2393                               
SITE     1 AC7  4 NAG B1498  FUC B1508  HOH B2378  HOH B2379                    
SITE     1 AC8 14 ASP A 127  PHE A 128  TRP A 179  ASN A 234                    
SITE     2 AC8 14 GLU A 235  TYR A 244  PHE A 246  TYR A 313                    
SITE     3 AC8 14 GLU A 340  CYS A 342  TRP A 381  ASN A 396                    
SITE     4 AC8 14 VAL A 398  HOH A2403                                          
SITE     1 AC9  4 NAG B1498  NAG B1499  HOH B2392  HOH B2393                    
SITE     1 BC1  3 ARG B  44  SER B  45  HOH B2381                               
SITE     1 BC2  3 ARG A  44  SER A  45  HOH A2404                               
SITE     1 BC3  6 GLY A 193  LYS A 194  SER A 242  GLY A 243                    
SITE     2 BC3  6 HOH A2186  HOH A2190                                          
SITE     1 BC4  4 LYS A  79  TRP A 228  ARG A 277  HOH A2406                    
SITE     1 BC5  6 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 BC5  6 ASP A 358  HOH A2407                                          
SITE     1 BC6  6 GLY B 193  LYS B 194  GLY B 243  HOH B2168                    
SITE     2 BC6  6 HOH B2383  HOH B2384                                          
SITE     1 BC7  6 LYS B  79  TRP B 228  ARG B 277  HIS B 306                    
SITE     2 BC7  6 HOH B2328  HOH B2385                                          
SITE     1 BC8  7 TYR B  11  SER B  12  ARG B 353  SER B 356                    
SITE     2 BC8  7 ASP B 358  HOH B2386  HOH B2387                               
SITE     1 BC9  7 PRO B   3  CYS B   4  GLY B  46  ARG B  47                    
SITE     2 BC9  7 ARG B  48  GLU B  50  HOH B2039                               
SITE     1 CC1  5 ARG B 285  HIS B 365  HOH B2388  HOH B2389                    
SITE     2 CC1  5 HOH B2390                                                     
SITE     1 CC2  9 GLY B 265  LEU B 268  ALA B 269  HIS B 274                    
SITE     2 CC2  9 VAL B 276  TYR B 304  HOH B2226  HOH B2242                    
SITE     3 CC2  9 HOH B2391                                                     
SITE     1 CC3  6 ARG A 285  HIS A 365  THR A 369  HOH A2409                    
SITE     2 CC3  6 HOH A2410  HOH A2411                                          
CRYST1   68.088   97.104   82.932  90.00 104.43  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      0.014687  0.000000  0.003779        0.00000                         
SCALE2      0.000000  0.010298  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012451        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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