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Database: PDB
Entry: 3GXM
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Original site: 3GXM 
HEADER    HYDROLASE                               02-APR-09   3GXM              
TITLE     CRYSTAL STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 4.5, PHOSPHATE       
TITLE    2 CRYSTALLIZATION CONDITION                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;                                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL- 
COMPND   5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;         
COMPND   6 EC: 3.2.1.45;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GBA, GC, GLUC;                                                 
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    HYDROLASE, ALTERNATIVE INITIATION, DISEASE MUTATION, DISULFIDE BOND,  
KEYWDS   2 GAUCHER DISEASE, GLYCOPROTEIN, GLYCOSIDASE, ICHTHYOSIS, LIPID        
KEYWDS   3 METABOLISM, LYSOSOME, MEMBRANE, SPHINGOLIPID METABOLISM              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.L.LIEBERMAN                                                         
REVDAT   3   13-JUL-11 3GXM    1       VERSN                                    
REVDAT   2   16-JUN-09 3GXM    1       JRNL                                     
REVDAT   1   05-MAY-09 3GXM    0                                                
JRNL        AUTH   R.L.LIEBERMAN,J.A.D'AQUINO,D.RINGE,G.A.PETSKO                
JRNL        TITL   EFFECTS OF PH AND IMINOSUGAR PHARMACOLOGICAL CHAPERONES ON   
JRNL        TITL 2 LYSOSOMAL GLYCOSIDASE STRUCTURE AND STABILITY.               
JRNL        REF    BIOCHEMISTRY                  V.  48  4816 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19374450                                                     
JRNL        DOI    10.1021/BI9002265                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 138784                         
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) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6970                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8760                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 504                          
REMARK   3   BIN FREE R VALUE                    : 0.4710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15720                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 196                                     
REMARK   3   SOLVENT ATOMS            : 1144                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
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): 0.259         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.226         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.196         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.245         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.873                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16384 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22368 ; 1.682 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1984 ; 7.689 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   720 ;37.157 ;23.444       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2516 ;17.716 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;21.807 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2440 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12532 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8004 ; 0.216 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10770 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1245 ; 0.312 ; 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):    76 ; 0.192 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.217 ; 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): 10168 ; 0.823 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.394 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7140 ; 2.053 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6296 ; 3.084 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3GXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052433.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 138784                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION                          
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       45.88950            
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, 3, 4                                              
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 67860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -386.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 70180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -378.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       91.77900            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -194.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -174.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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    LEU D   149     O    HOH D   665              2.08            
REMARK 500   O    HOH B   580     O    HOH B  1179              2.08            
REMARK 500   O    HOH D   535     O    HOH D  1169              2.09            
REMARK 500   O    HOH B   522     O    HOH B  1115              2.11            
REMARK 500   O    HOH D   524     O    HOH D  1142              2.14            
REMARK 500   O    HOH C   521     O    HOH C  1128              2.17            
REMARK 500   OE2  GLU A   254     O    HOH A   579              2.17            
REMARK 500   OD2  ASP A   405     O    HOH A   953              2.19            
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    TRP A 378   CB    TRP A 378   CG     -0.114                       
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    LEU A 165   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    PRO A 319   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    LEU B 286   CA  -  CB  -  CG  ANGL. DEV. =  19.8 DEGREES          
REMARK 500    LEU B 480   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ASN C  92   N   -  CA  -  C   ANGL. DEV. = -22.6 DEGREES          
REMARK 500    LEU D 480   CA  -  CB  -  CG  ANGL. DEV. =  17.2 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    TYR A  11     -166.39   -101.00                                   
REMARK 500    SER A  13     -157.30   -133.92                                   
REMARK 500    ASN A  19     -155.62   -155.59                                   
REMARK 500    ALA A  33      158.85    -49.03                                   
REMARK 500    MET A  49       44.29     38.70                                   
REMARK 500    PHE A  75     -137.70   -115.82                                   
REMARK 500    ALA A 124     -153.69     74.07                                   
REMARK 500    TYR A 133      150.64    163.70                                   
REMARK 500    PRO A 150     -165.53    -72.93                                   
REMARK 500    LEU A 156      -77.89    -99.39                                   
REMARK 500    ASN A 188        1.67    -67.91                                   
REMARK 500    ASN A 192     -163.93   -120.05                                   
REMARK 500    SER A 196     -167.56   -122.66                                   
REMARK 500    ASP A 203     -173.09    -67.90                                   
REMARK 500    GLU A 233      144.85   -178.11                                   
REMARK 500    ASP A 263      -64.14   -122.63                                   
REMARK 500    HIS A 273       45.67   -102.78                                   
REMARK 500    LEU A 281      -88.02     63.84                                   
REMARK 500    TYR A 313      -64.49    -25.05                                   
REMARK 500    LEU A 314       45.74    -98.47                                   
REMARK 500    THR A 323      -71.32   -113.69                                   
REMARK 500    VAL A 343      -93.11    -79.97                                   
REMARK 500    SER A 345      -90.19    -76.85                                   
REMARK 500    TRP A 381     -144.01    -75.20                                   
REMARK 500    ARG A 395      130.77    179.60                                   
REMARK 500    THR B  63      -56.36     90.37                                   
REMARK 500    PHE B  75     -134.74   -113.01                                   
REMARK 500    ALA B 124     -151.32     77.26                                   
REMARK 500    PHE B 128       57.47    -93.02                                   
REMARK 500    LEU B 156      -68.95   -106.64                                   
REMARK 500    PRO B 182      141.68    -36.82                                   
REMARK 500    GLU B 233      133.62    158.89                                   
REMARK 500    LEU B 281      -82.76     78.56                                   
REMARK 500    PHE B 316       67.67   -116.15                                   
REMARK 500    LEU B 317      100.21    -52.78                                   
REMARK 500    ALA B 320      -80.31    151.05                                   
REMARK 500    THR B 323      -70.25   -119.54                                   
REMARK 500    LYS B 346       85.51     -2.84                                   
REMARK 500    GLN B 350      175.77    -59.28                                   
REMARK 500    TRP B 381     -139.69    -73.92                                   
REMARK 500    ASN C  19     -153.69   -140.81                                   
REMARK 500    PHE C  75     -135.03   -121.26                                   
REMARK 500    ASN C  92      -52.22   -129.15                                   
REMARK 500    ALA C 124     -157.74     67.18                                   
REMARK 500    TYR C 133      149.94    177.31                                   
REMARK 500    ASP C 141       71.73   -100.89                                   
REMARK 500    PRO C 150     -169.57    -76.67                                   
REMARK 500    LEU C 156      -62.56   -104.78                                   
REMARK 500    PRO C 182      139.81    -39.20                                   
REMARK 500    LEU C 281      -87.34     71.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      72 RAMACHANDRAN OUTLIERS.                        
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 CYS A  342     VAL A  343                 -147.70                    
REMARK 500 GLY B  344     SER B  345                  145.48                    
REMARK 500 LEU C   91     ASN C   92                 -118.84                    
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    ILE A 114        24.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 343        25.0      L          L   OUTSIDE RANGE           
REMARK 500    THR B  63        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 114        25.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU C  91        23.1      L          L   OUTSIDE RANGE           
REMARK 500    TYR C 313        18.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 314        19.3      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 343        19.6      L          L   OUTSIDE RANGE           
REMARK 500    TRP D 312        22.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GXF   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH ISOFAGOMINE AT               
REMARK 900 NEUTRAL PH                                                           
REMARK 900 RELATED ID: 3GXI   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 5.5                         
DBREF  3GXM A    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3GXM B    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3GXM C    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3GXM D    1   497  UNP    P04062   GLCM_HUMAN      40    536             
SEQADV 3GXM HIS A  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3GXM HIS B  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3GXM HIS C  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3GXM HIS D  495  UNP  P04062    ARG   534 VARIANT                        
SEQRES   1 A  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 A  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 A  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 A  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 A  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 A  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 A  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 A  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 A  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 A  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 A  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 A  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 A  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 A  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 A  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 A  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 A  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 A  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 A  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 A  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 A  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 A  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 A  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 A  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 A  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 A  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 A  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 A  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 A  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 A  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 A  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 A  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 A  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 A  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 A  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 A  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 A  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 A  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 A  497  HIS ARG GLN                                                  
SEQRES   1 B  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 B  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 B  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 B  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 B  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 B  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 B  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 B  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 B  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 B  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 B  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 B  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 B  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 B  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 B  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 B  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 B  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 B  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 B  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 B  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 B  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 B  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 B  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 B  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 B  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 B  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 B  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 B  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 B  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 B  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 B  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 B  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 B  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 B  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 B  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 B  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 B  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 B  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 B  497  HIS ARG GLN                                                  
SEQRES   1 C  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 C  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 C  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 C  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 C  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 C  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 C  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 C  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 C  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 C  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 C  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 C  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 C  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 C  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 C  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 C  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 C  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 C  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 C  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 C  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 C  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 C  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 C  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 C  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 C  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 C  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 C  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 C  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 C  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 C  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 C  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 C  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 C  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 C  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 C  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 C  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 C  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 C  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 C  497  HIS ARG GLN                                                  
SEQRES   1 D  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 D  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 D  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 D  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 D  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 D  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 D  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 D  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 D  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 D  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 D  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 D  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 D  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 D  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 D  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 D  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 D  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 D  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 D  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 D  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 D  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 D  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 D  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 D  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 D  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 D  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 D  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 D  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 D  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 D  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 D  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 D  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 D  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 D  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 D  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 D  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 D  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 D  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 D  497  HIS ARG GLN                                                  
MODRES 3GXM ASN A   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3GXM ASN B   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3GXM ASN C   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3GXM ASN D   19  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 498      14                                                       
HET    SO4  A 499       5                                                       
HET    SO4  A 500       5                                                       
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    SO4  A 506       5                                                       
HET    NAG  B 498      14                                                       
HET    SO4  B 499       5                                                       
HET    SO4  B 500       5                                                       
HET    SO4  B 501       5                                                       
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HET    SO4  B 504       5                                                       
HET    SO4  B 505       5                                                       
HET    NAG  C 498      14                                                       
HET    SO4  C 499       5                                                       
HET    SO4  C 500       5                                                       
HET    SO4  C 501       5                                                       
HET    SO4  C 502       5                                                       
HET    SO4  C 503       5                                                       
HET    SO4  C 504       5                                                       
HET    SO4  C 505       5                                                       
HET    NAG  D 498      14                                                       
HET    SO4  D 499       5                                                       
HET    SO4  D 500       5                                                       
HET    SO4  D 501       5                                                       
HET    SO4  D 502       5                                                       
HET    SO4  D 503       5                                                       
HET    SO4  D 504       5                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  NAG    4(C8 H15 N O6)                                               
FORMUL   6  SO4    28(O4 S 2-)                                                  
FORMUL  37  HOH   *1144(H2 O)                                                   
HELIX    1   1 THR A   86  LEU A   94  1                                   9    
HELIX    2   2 SER A   97  SER A  110  1                                  14    
HELIX    3   3 PRO A  150  LYS A  155  1                                   6    
HELIX    4   4 LEU A  156  ALA A  168  1                                  13    
HELIX    5   5 PRO A  182  LYS A  186  5                                   5    
HELIX    6   6 ASP A  203  HIS A  223  1                                  21    
HELIX    7   7 GLU A  235  LEU A  241  5                                   7    
HELIX    8   8 THR A  252  ASP A  263  1                                  12    
HELIX    9   9 ASP A  263  ASN A  270  1                                   8    
HELIX   10  10 LEU A  286  LEU A  288  5                                   3    
HELIX   11  11 PRO A  289  THR A  297  1                                   9    
HELIX   12  12 ASP A  298  LYS A  303  1                                   6    
HELIX   13  13 PRO A  319  PHE A  331  1                                  13    
HELIX   14  14 SER A  356  TYR A  373  1                                  18    
HELIX   15  15 ILE A  406  ASP A  409  5                                   4    
HELIX   16  16 GLN A  414  LYS A  425  1                                  12    
HELIX   17  17 THR B   86  LEU B   94  1                                   9    
HELIX   18  18 SER B   97  SER B  110  1                                  14    
HELIX   19  19 PRO B  150  LYS B  155  1                                   6    
HELIX   20  20 LEU B  156  ALA B  168  1                                  13    
HELIX   21  21 PRO B  182  LYS B  186  5                                   5    
HELIX   22  22 ASP B  203  HIS B  223  1                                  21    
HELIX   23  23 GLU B  235  LEU B  241  5                                   7    
HELIX   24  24 THR B  252  ASP B  263  1                                  12    
HELIX   25  25 ASP B  263  SER B  271  1                                   9    
HELIX   26  26 LEU B  286  LEU B  288  5                                   3    
HELIX   27  27 PRO B  289  THR B  297  1                                   9    
HELIX   28  28 ASP B  298  LYS B  303  1                                   6    
HELIX   29  29 THR B  323  PHE B  331  1                                   9    
HELIX   30  30 SER B  356  LEU B  372  1                                  17    
HELIX   31  31 GLN B  414  LYS B  425  1                                  12    
HELIX   32  32 THR C   86  LEU C   94  1                                   9    
HELIX   33  33 SER C   97  SER C  110  1                                  14    
HELIX   34  34 PRO C  150  LYS C  155  1                                   6    
HELIX   35  35 LEU C  156  ALA C  168  1                                  13    
HELIX   36  36 PRO C  182  LYS C  186  5                                   5    
HELIX   37  37 ASP C  203  HIS C  223  1                                  21    
HELIX   38  38 GLU C  235  LEU C  241  5                                   7    
HELIX   39  39 THR C  252  ASP C  263  1                                  12    
HELIX   40  40 ASP C  263  ASN C  270  1                                   8    
HELIX   41  41 LEU C  286  LEU C  288  5                                   3    
HELIX   42  42 PRO C  289  THR C  297  1                                   9    
HELIX   43  43 ASP C  298  LYS C  303  1                                   6    
HELIX   44  44 PRO C  319  PHE C  331  1                                  13    
HELIX   45  45 SER C  356  TYR C  373  1                                  18    
HELIX   46  46 ILE C  406  ASP C  409  5                                   4    
HELIX   47  47 GLN C  414  LYS C  425  1                                  12    
HELIX   48  48 THR D   86  LEU D   94  1                                   9    
HELIX   49  49 SER D   97  SER D  110  1                                  14    
HELIX   50  50 PRO D  150  LYS D  155  1                                   6    
HELIX   51  51 LEU D  156  ALA D  168  1                                  13    
HELIX   52  52 PRO D  182  LYS D  186  5                                   5    
HELIX   53  53 ASP D  203  GLU D  222  1                                  20    
HELIX   54  54 GLU D  235  LEU D  241  5                                   7    
HELIX   55  55 THR D  252  ASP D  263  1                                  12    
HELIX   56  56 ASP D  263  ASN D  270  1                                   8    
HELIX   57  57 LEU D  286  LEU D  288  5                                   3    
HELIX   58  58 PRO D  289  THR D  297  1                                   9    
HELIX   59  59 ASP D  298  LYS D  303  1                                   6    
HELIX   60  60 THR D  323  PHE D  331  1                                   9    
HELIX   61  61 SER D  356  TYR D  373  1                                  18    
HELIX   62  62 ILE D  406  ASP D  409  5                                   4    
HELIX   63  63 GLN D  414  LYS D  425  1                                  12    
SHEET    1   A 4 PRO A   6  LYS A   7  0                                        
SHEET    2   A 4 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7           
SHEET    3   A 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18           
SHEET    4   A 4 ILE A 402  ASP A 405 -1  N  ASP A 405   O  THR A 410           
SHEET    1   B 9 GLU A  50  PRO A  55  0                                        
SHEET    2   B 9 THR A  36  THR A  43 -1  N  ARG A  39   O  SER A  52           
SHEET    3   B 9 SER A 488  TRP A 494 -1  O  LEU A 493   N  SER A  38           
SHEET    4   B 9 ALA A 456  ASN A 462 -1  N  VAL A 458   O  TYR A 492           
SHEET    5   B 9 ASP A 445  MET A 450 -1  N  ASP A 445   O  LEU A 461           
SHEET    6   B 9 GLN A 432  ALA A 438 -1  N  GLN A 432   O  MET A 450           
SHEET    7   B 9 LEU A  65  LYS A  77 -1  N  PHE A  75   O  ARG A 433           
SHEET    8   B 9 VAL A 468  ASP A 474  1  O  LYS A 473   N  LEU A  69           
SHEET    9   B 9 GLY A 478  SER A 484 -1  O  THR A 482   N  LEU A 470           
SHEET    1   C 9 GLY A  80  ALA A  84  0                                        
SHEET    2   C 9 ILE A 118  MET A 123  1  O  ARG A 120   N  GLY A  83           
SHEET    3   C 9 SER A 173  PRO A 178  1  O  LEU A 175   N  VAL A 121           
SHEET    4   C 9 ALA A 229  THR A 231  1  O  THR A 231   N  ALA A 176           
SHEET    5   C 9 ARG A 277  GLN A 284  1  O  LEU A 279   N  VAL A 230           
SHEET    6   C 9 GLY A 307  HIS A 311  1  O  ALA A 309   N  MET A 280           
SHEET    7   C 9 MET A 335  ALA A 341  1  O  MET A 335   N  ILE A 308           
SHEET    8   C 9 VAL A 375  ASN A 382  1  O  THR A 379   N  ALA A 341           
SHEET    9   C 9 GLY A  80  ALA A  84  1  N  GLY A  82   O  ASP A 380           
SHEET    1   D 5 PRO B   6  LYS B   7  0                                        
SHEET    2   D 5 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7           
SHEET    3   D 5 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18           
SHEET    4   D 5 ILE B 402  ASP B 405 -1  N  ASP B 405   O  THR B 410           
SHEET    5   D 5 ALA B 384  LEU B 385  1  N  LEU B 385   O  VAL B 404           
SHEET    1   E 9 GLU B  50  PRO B  55  0                                        
SHEET    2   E 9 THR B  36  THR B  43 -1  N  ARG B  39   O  SER B  52           
SHEET    3   E 9 SER B 488  TRP B 494 -1  O  LEU B 493   N  SER B  38           
SHEET    4   E 9 ALA B 456  ASN B 462 -1  N  VAL B 460   O  HIS B 490           
SHEET    5   E 9 LEU B 444  MET B 450 -1  N  ASP B 445   O  LEU B 461           
SHEET    6   E 9 GLN B 432  ALA B 438 -1  N  GLN B 432   O  MET B 450           
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  THR B  68   O  VAL B 437           
SHEET    8   E 9 VAL B 468  ASP B 474  1  O  LYS B 473   N  LEU B  69           
SHEET    9   E 9 GLY B 478  SER B 484 -1  O  SER B 484   N  VAL B 468           
SHEET    1   F 9 GLY B  80  ALA B  84  0                                        
SHEET    2   F 9 ILE B 118  MET B 123  1  O  ARG B 120   N  GLY B  83           
SHEET    3   F 9 SER B 173  PRO B 178  1  O  LEU B 175   N  VAL B 121           
SHEET    4   F 9 ALA B 229  THR B 231  1  O  THR B 231   N  ALA B 176           
SHEET    5   F 9 ARG B 277  GLN B 284  1  O  LEU B 279   N  VAL B 230           
SHEET    6   F 9 GLY B 307  TYR B 313  1  O  ALA B 309   N  MET B 280           
SHEET    7   F 9 MET B 335  CYS B 342  1  O  MET B 335   N  ILE B 308           
SHEET    8   F 9 VAL B 375  ASN B 382  1  O  VAL B 376   N  LEU B 336           
SHEET    9   F 9 GLY B  80  ALA B  84  1  N  ALA B  84   O  TRP B 381           
SHEET    1   G 5 PRO C   6  LYS C   7  0                                        
SHEET    2   G 5 VAL C  15  CYS C  18 -1  O  VAL C  15   N  LYS C   7           
SHEET    3   G 5 THR C 410  LYS C 413 -1  O  PHE C 411   N  CYS C  18           
SHEET    4   G 5 ILE C 402  ASP C 405 -1  N  ILE C 403   O  TYR C 412           
SHEET    5   G 5 ALA C 384  LEU C 385  1  N  LEU C 385   O  VAL C 404           
SHEET    1   H 9 GLU C  50  PRO C  55  0                                        
SHEET    2   H 9 THR C  36  THR C  43 -1  N  GLU C  41   O  GLU C  50           
SHEET    3   H 9 SER C 488  TRP C 494 -1  O  LEU C 493   N  SER C  38           
SHEET    4   H 9 ALA C 456  ASN C 462 -1  N  VAL C 458   O  TYR C 492           
SHEET    5   H 9 ASP C 445  MET C 450 -1  N  ASP C 445   O  LEU C 461           
SHEET    6   H 9 GLN C 432  ALA C 438 -1  N  GLN C 432   O  MET C 450           
SHEET    7   H 9 LEU C  65  LYS C  77 -1  N  PHE C  75   O  ARG C 433           
SHEET    8   H 9 VAL C 468  ASP C 474  1  O  THR C 471   N  LEU C  67           
SHEET    9   H 9 GLY C 478  SER C 484 -1  O  SER C 484   N  VAL C 468           
SHEET    1   I 9 GLY C  80  ALA C  84  0                                        
SHEET    2   I 9 ILE C 118  MET C 123  1  O  ARG C 120   N  GLY C  83           
SHEET    3   I 9 SER C 173  PRO C 178  1  O  LEU C 175   N  VAL C 121           
SHEET    4   I 9 ALA C 229  THR C 231  1  O  THR C 231   N  ALA C 176           
SHEET    5   I 9 ARG C 277  GLN C 284  1  O  LEU C 279   N  VAL C 230           
SHEET    6   I 9 GLY C 307  HIS C 311  1  O  ALA C 309   N  MET C 280           
SHEET    7   I 9 MET C 335  GLU C 340  1  O  MET C 335   N  ILE C 308           
SHEET    8   I 9 VAL C 375  ASN C 382  1  O  VAL C 376   N  LEU C 336           
SHEET    9   I 9 GLY C  80  ALA C  84  1  N  GLY C  82   O  ASP C 380           
SHEET    1   J 4 PRO D   6  LYS D   7  0                                        
SHEET    2   J 4 VAL D  15  CYS D  18 -1  O  VAL D  15   N  LYS D   7           
SHEET    3   J 4 THR D 410  LYS D 413 -1  O  PHE D 411   N  CYS D  18           
SHEET    4   J 4 ILE D 402  ASP D 405 -1  N  ASP D 405   O  THR D 410           
SHEET    1   K 9 GLU D  50  PRO D  55  0                                        
SHEET    2   K 9 THR D  36  THR D  43 -1  N  GLU D  41   O  GLU D  50           
SHEET    3   K 9 SER D 488  TRP D 494 -1  O  LEU D 493   N  SER D  38           
SHEET    4   K 9 ALA D 456  ASN D 462 -1  N  VAL D 460   O  HIS D 490           
SHEET    5   K 9 LEU D 444  MET D 450 -1  N  ASP D 445   O  LEU D 461           
SHEET    6   K 9 GLN D 432  ALA D 438 -1  N  GLN D 432   O  MET D 450           
SHEET    7   K 9 LEU D  65  LYS D  77 -1  N  PHE D  75   O  ARG D 433           
SHEET    8   K 9 VAL D 468  ASP D 474  1  O  LYS D 473   N  LEU D  69           
SHEET    9   K 9 GLY D 478  SER D 484 -1  O  SER D 484   N  VAL D 468           
SHEET    1   L 9 GLY D  80  ALA D  84  0                                        
SHEET    2   L 9 ILE D 118  MET D 123  1  O  ARG D 120   N  GLY D  83           
SHEET    3   L 9 SER D 173  PRO D 178  1  O  LEU D 175   N  VAL D 121           
SHEET    4   L 9 ALA D 229  THR D 231  1  O  THR D 231   N  ALA D 176           
SHEET    5   L 9 ARG D 277  GLN D 284  1  O  LEU D 279   N  VAL D 230           
SHEET    6   L 9 GLY D 307  TYR D 313  1  O  ALA D 309   N  MET D 280           
SHEET    7   L 9 MET D 335  CYS D 342  1  O  MET D 335   N  ILE D 308           
SHEET    8   L 9 VAL D 375  ASN D 382  1  O  VAL D 376   N  LEU D 336           
SHEET    9   L 9 GLY D  80  ALA D  84  1  N  GLY D  82   O  ASP D 380           
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.06  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.10  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.12  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.13  
SSBOND   5 CYS C    4    CYS C   16                          1555   1555  2.06  
SSBOND   6 CYS C   18    CYS C   23                          1555   1555  2.13  
SSBOND   7 CYS D    4    CYS D   16                          1555   1555  2.12  
SSBOND   8 CYS D   18    CYS D   23                          1555   1555  2.14  
LINK         ND2 ASN A  19                 C1  NAG A 498     1555   1555  1.45  
LINK         ND2 ASN B  19                 C1  NAG B 498     1555   1555  1.47  
LINK         ND2 ASN C  19                 C1  NAG C 498     1555   1555  1.45  
LINK         ND2 ASN D  19                 C1  NAG D 498     1555   1555  1.46  
CISPEP   1 LEU A  288    PRO A  289          0         2.69                     
CISPEP   2 GLY A  344    SER A  345          0       -19.60                     
CISPEP   3 GLY A  390    PRO A  391          0        -0.93                     
CISPEP   4 GLY B   62    THR B   63          0        13.87                     
CISPEP   5 LEU B  288    PRO B  289          0        -0.39                     
CISPEP   6 PRO B  319    ALA B  320          0        -3.85                     
CISPEP   7 GLY B  390    PRO B  391          0         4.82                     
CISPEP   8 LEU C  288    PRO C  289          0         2.58                     
CISPEP   9 TYR C  313    LEU C  314          0        24.98                     
CISPEP  10 VAL C  343    GLY C  344          0         0.87                     
CISPEP  11 GLY C  390    PRO C  391          0        -1.81                     
CISPEP  12 LEU D  288    PRO D  289          0         1.43                     
CISPEP  13 GLY D  390    PRO D  391          0         6.20                     
SITE     1 AC1  5 ASN A  19  HOH A 575  HOH A 602  HOH A 998                    
SITE     2 AC1  5 HOH A1075                                                     
SITE     1 AC2  7 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 AC2  7 TRP A 357  ASP A 358  HOH A 577                               
SITE     1 AC3  6 THR A  63  GLY A  64  GLN A 440  HOH A 651                    
SITE     2 AC3  6 LYS C 473  HOH C 677                                          
SITE     1 AC4  5 LYS A  79  TRP A 228  ARG A 277  HIS A 306                    
SITE     2 AC4  5 HOH A1017                                                     
SITE     1 AC5  5 TYR A  11  TRP A 348  GLU A 349  GLN A 350                    
SITE     2 AC5  5 ARG A 353                                                     
SITE     1 AC6  4 ARG A  44  SER A 465  TYR A 487  HOH A 839                    
SITE     1 AC7  3 GLU A 254  ARG A 257  LYS B 441                               
SITE     1 AC8  2 HIS A 290  LYS A 293                                          
SITE     1 AC9  4 ARG A  44  SER A  45  HOH A 762  HOH A1014                    
SITE     1 BC1  4 ILE B   5  ASN B  19  HOH B 863  HOH B1088                    
SITE     1 BC2  7 SER A 242  TYR B  11  SER B  12  ARG B 353                    
SITE     2 BC2  7 SER B 356  TRP B 357  ASP B 358                               
SITE     1 BC3  5 GLY B 193  LYS B 194  SER B 242  GLY B 243                    
SITE     2 BC3  5 HOH B 524                                                     
SITE     1 BC4  5 LYS B  79  TRP B 228  ARG B 277  HIS B 306                    
SITE     2 BC4  5 HOH B 528                                                     
SITE     1 BC5  6 GLN B 226  THR B 272  HIS B 273  HOH B 555                    
SITE     2 BC5  6 HOH B 568  HOH B 598                                          
SITE     1 BC6  3 ARG B  44  SER B  45  HOH B 575                               
SITE     1 BC7  3 ARG B  44  SER B 465  TYR B 487                               
SITE     1 BC8  3 ARG B 277  VAL B 305  HIS B 306                               
SITE     1 BC9  4 ASN C  19  THR C  21  TYR C  22  HOH C 897                    
SITE     1 CC1  9 LYS A 473  HOH A 956  THR C  63  GLY C  64                    
SITE     2 CC1  9 GLN C 440  HOH C 562  HOH C 800  HOH C 954                    
SITE     3 CC1  9 HOH C1160                                                     
SITE     1 CC2  7 TYR C  11  SER C  12  ARG C 353  SER C 356                    
SITE     2 CC2  7 TRP C 357  ASP C 358  HOH C 613                               
SITE     1 CC3  5 LYS C  79  TRP C 228  ARG C 277  HIS C 306                    
SITE     2 CC3  5 HOH C1048                                                     
SITE     1 CC4  5 TYR C  11  GLU C 349  GLN C 350  ARG C 353                    
SITE     2 CC4  5 HOH C 591                                                     
SITE     1 CC5  3 GLU C 254  ARG C 257  HOH C1016                               
SITE     1 CC6  2 ARG C  44  SER C  45                                          
SITE     1 CC7  4 ARG C  44  TYR C 487  HOH C 861  HOH C1002                    
SITE     1 CC8  3 ILE D   5  ASN D  19  TYR D  22                               
SITE     1 CC9  9 SER C 242  TYR D  11  SER D  12  ARG D 353                    
SITE     2 CC9  9 SER D 356  TRP D 357  ASP D 358  HOH D 910                    
SITE     3 CC9  9 HOH D 917                                                     
SITE     1 DC1  7 GLY D 193  LYS D 194  SER D 242  GLY D 243                    
SITE     2 DC1  7 HOH D 569  HOH D 586  HOH D 630                               
SITE     1 DC2  8 LYS D  79  TRP D 228  ARG D 277  HIS D 306                    
SITE     2 DC2  8 HOH D 531  HOH D 591  HOH D 621  HOH D 635                    
SITE     1 DC3  4 ARG D  44  SER D  45  HOH D 606  HOH D 965                    
SITE     1 DC4  8 GLN D 226  THR D 272  HIS D 273  VAL D 276                    
SITE     2 DC4  8 HOH D 536  HOH D 824  HOH D 962  HOH D1085                    
SITE     1 DC5  3 ARG D  44  SER D 465  TYR D 487                               
CRYST1  110.505   91.779  152.751  90.00 111.24  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009049  0.000000  0.003517        0.00000                         
SCALE2      0.000000  0.010896  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007024        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system