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Database: PDB
Entry: 3GXD
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Original site: 3GXD 
HEADER    HYDROLASE                               02-APR-09   3GXD              
TITLE     CRYSTAL STRUCTURE OF APO ACID-BETA-GLUCOSIDASE PH 4.5                 
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                            
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 3GXD    1       VERSN                                    
REVDAT   2   16-JUN-09 3GXD    1       JRNL                                     
REVDAT   1   05-MAY-09 3GXD    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.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 81268                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4342                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4168                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 61.37                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 222                          
REMARK   3   BIN FREE R VALUE                    : 0.3880                       
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          : 334                                     
REMARK   3   SOLVENT ATOMS            : 223                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08000                                              
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.545         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.327         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.235         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.774        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16502 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22538 ; 1.873 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1984 ; 7.851 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   720 ;38.923 ;23.444       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2516 ;19.519 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;23.621 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2420 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12540 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8184 ; 0.241 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 11041 ; 0.322 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   807 ; 0.184 ; 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):    46 ; 0.269 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.160 ; 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): 10140 ; 0.955 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.668 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7271 ; 2.223 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6466 ; 3.501 ; 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 3GXD 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 RCSB052424.                                      
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                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81268                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 142.000                            
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) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
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         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2NT0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M NA H2PO4, 0.8 M K H2PO4, 0.1 M     
REMARK 280  CITRATE PH 5.5 SOAKED WITH ACETATE BUFFER PH 4.5 AND 1.8 M LI2SO4   
REMARK 280  PRIOR TO FREEZING, VAPOR DIFFUSION, TEMPERATURE 298K                
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       45.85150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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 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   OH   TYR D   313     O    HOH D   552              1.98            
REMARK 500   CB   ASN C   370     CH2  TRP C   378              2.05            
REMARK 500   NZ   LYS B   155     O    HOH B   546              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A 378   CB    TRP A 378   CG     -0.140                       
REMARK 500    TRP C 378   CB    TRP C 378   CG     -0.142                       
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    ARG A 433   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU B 286   CA  -  CB  -  CG  ANGL. DEV. = -16.3 DEGREES          
REMARK 500    TRP C 378   CA  -  CB  -  CG  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG D 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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    SER A  12       -8.34    -58.62                                   
REMARK 500    ASN A  19     -156.71   -144.23                                   
REMARK 500    PRO A  28      121.83    -36.96                                   
REMARK 500    ALA A  33      152.74    -29.91                                   
REMARK 500    PHE A  75     -131.47   -123.25                                   
REMARK 500    ASN A 117       10.54   -144.68                                   
REMARK 500    ALA A 124     -159.33     79.20                                   
REMARK 500    CYS A 126     -156.86   -128.14                                   
REMARK 500    PHE A 128       33.36    -75.57                                   
REMARK 500    TYR A 133      149.41    174.12                                   
REMARK 500    ALA A 136       75.44   -150.34                                   
REMARK 500    PHE A 142       -9.91    -53.71                                   
REMARK 500    LEU A 156      -61.42   -108.74                                   
REMARK 500    PRO A 182      136.11    -35.21                                   
REMARK 500    ASN A 192     -150.52   -140.79                                   
REMARK 500    GLU A 233      135.40    175.88                                   
REMARK 500    GLU A 235       72.43     17.85                                   
REMARK 500    LEU A 249      108.48   -168.76                                   
REMARK 500    LEU A 281      -78.57     68.66                                   
REMARK 500    TYR A 313      -78.09   -117.55                                   
REMARK 500    ASP A 315      -39.88   -141.60                                   
REMARK 500    THR A 323      -76.84   -124.32                                   
REMARK 500    SER A 345     -127.21    -60.99                                   
REMARK 500    LYS A 346       88.28     22.57                                   
REMARK 500    PHE A 347      -34.05    -39.20                                   
REMARK 500    LEU A 354      104.46    -58.19                                   
REMARK 500    HIS A 374        5.51     89.66                                   
REMARK 500    TRP A 381     -139.25    -72.97                                   
REMARK 500    VAL A 394      -65.93   -124.35                                   
REMARK 500    ARG A 395      147.32   -171.61                                   
REMARK 500    PHE A 397      -27.96     20.49                                   
REMARK 500    ASP A 409       37.59     39.44                                   
REMARK 500    LEU A 436      102.89   -164.37                                   
REMARK 500    ASP A 453        4.80    -63.91                                   
REMARK 500    ARG A 463       25.37    -72.85                                   
REMARK 500    MET B  49       42.18     38.90                                   
REMARK 500    GLN B  73       94.62    -59.94                                   
REMARK 500    PHE B  75     -150.67   -148.08                                   
REMARK 500    ALA B 124     -154.02     62.07                                   
REMARK 500    CYS B 126     -152.16   -108.47                                   
REMARK 500    PHE B 128       39.97    -96.11                                   
REMARK 500    ASN B 146       34.31    -94.06                                   
REMARK 500    LEU B 156      -75.43   -106.80                                   
REMARK 500    PRO B 182      148.53    -36.83                                   
REMARK 500    ASN B 192     -160.50   -123.46                                   
REMARK 500    GLU B 233      126.85    161.44                                   
REMARK 500    ASP B 263      -65.95   -137.54                                   
REMARK 500    LEU B 281      -80.16     73.00                                   
REMARK 500    GLN B 284      133.11    -37.88                                   
REMARK 500    THR B 297        5.86    -67.35                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     125 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 GLU B  349     GLN B  350                   49.71                    
REMARK 500 GLY C  344     SER C  345                  142.65                    
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 161        20.8      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 313        17.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 314        24.9      L          L   OUTSIDE RANGE           
REMARK 500    CYS A 342        23.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 397        22.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 343        23.8      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 397        22.4      L          L   OUTSIDE RANGE           
REMARK 500    TRP D 348        22.5      L          L   OUTSIDE RANGE           
REMARK 500    GLU D 349        21.0      L          L   OUTSIDE RANGE           
REMARK 500    PHE D 397        21.3      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 PO4 A 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 510                 
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                         
REMARK 900 RELATED ID: 3GXM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 4.5                         
DBREF  3GXD A    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3GXD B    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3GXD C    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3GXD D    1   497  UNP    P04062   GLCM_HUMAN      40    536             
SEQADV 3GXD HIS A  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3GXD HIS B  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3GXD HIS C  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3GXD 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 3GXD ASN A   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3GXD ASN B   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3GXD ASN C   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3GXD ASN D   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3GXD ASN B  146  ASN  GLYCOSYLATION SITE                                 
MODRES 3GXD ASN D  146  ASN  GLYCOSYLATION SITE                                 
HET    PO4  A 499       5                                                       
HET    PO4  A 500       5                                                       
HET    PO4  A 501       5                                                       
HET    PO4  A 502       5                                                       
HET    PO4  A 503       5                                                       
HET    PO4  A 498       5                                                       
HET    PO4  A 504       5                                                       
HET    PO4  A 505       5                                                       
HET    PO4  A 506       5                                                       
HET    PO4  A 507       5                                                       
HET    PO4  A 508       5                                                       
HET    PO4  A 509       5                                                       
HET    PO4  A 510       5                                                       
HET    PO4  A 511       5                                                       
HET    PO4  A 512       5                                                       
HET    NAG  A 513      14                                                       
HET    PO4  A 514       5                                                       
HET    PO4  B 500       5                                                       
HET    PO4  B 501       5                                                       
HET    PO4  B 502       5                                                       
HET    PO4  B 503       5                                                       
HET    PO4  B 504       5                                                       
HET    PO4  B 505       5                                                       
HET    PO4  B 498       5                                                       
HET    PO4  B 499       5                                                       
HET    PO4  B 506       5                                                       
HET    PO4  B 507       5                                                       
HET    NAG  B 508      14                                                       
HET    NAG  B 509      14                                                       
HET    PO4  C 499       5                                                       
HET    PO4  C 500       5                                                       
HET    PO4  C 501       5                                                       
HET    PO4  C 498       5                                                       
HET    PO4  C 502       5                                                       
HET    PO4  C 503       5                                                       
HET    PO4  C 504       5                                                       
HET    PO4  C 505       5                                                       
HET    PO4  C 506       5                                                       
HET    PO4  C 507       5                                                       
HET    PO4  C 508       5                                                       
HET    PO4  C 509       5                                                       
HET    NAG  C 510      14                                                       
HET    PO4  C 511       5                                                       
HET    PO4  D 499       5                                                       
HET    PO4  D 500       5                                                       
HET    PO4  D 501       5                                                       
HET    PO4  D 502       5                                                       
HET    PO4  D 498       5                                                       
HET    PO4  D 503       5                                                       
HET    PO4  D 504       5                                                       
HET    PO4  D 505       5                                                       
HET    PO4  D 506       5                                                       
HET    PO4  D 507       5                                                       
HET    PO4  D 508       5                                                       
HET    NAG  D 509      14                                                       
HET    NAG  D 510      14                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  PO4    50(O4 P 3-)                                                  
FORMUL  20  NAG    6(C8 H15 N O6)                                               
FORMUL  61  HOH   *223(H2 O)                                                    
HELIX    1   1 THR A   86  ALA A   95  1                                  10    
HELIX    2   2 SER A   97  SER A  110  1                                  14    
HELIX    3   3 PRO A  150  LYS A  155  1                                   6    
HELIX    4   4 LEU A  156  ALA A  168  1                                  13    
HELIX    5   5 PRO A  182  LYS A  186  5                                   5    
HELIX    6   6 ASP A  203  HIS A  223  1                                  21    
HELIX    7   7 GLU A  235  LEU A  241  5                                   7    
HELIX    8   8 THR A  252  ASP A  263  1                                  12    
HELIX    9   9 ASP A  263  ASN A  270  1                                   8    
HELIX   10  10 LEU A  286  LEU A  288  5                                   3    
HELIX   11  11 PRO A  289  THR A  297  1                                   9    
HELIX   12  12 ASP A  298  LYS A  303  1                                   6    
HELIX   13  13 THR A  323  PHE A  331  1                                   9    
HELIX   14  14 SER A  356  TYR A  373  1                                  18    
HELIX   15  15 ILE A  406  ASP A  409  5                                   4    
HELIX   16  16 GLN A  414  LYS A  425  1                                  12    
HELIX   17  17 THR B   86  ALA B   95  1                                  10    
HELIX   18  18 SER B   97  SER B  110  1                                  14    
HELIX   19  19 PRO B  150  LYS B  155  1                                   6    
HELIX   20  20 LEU B  156  ALA B  168  1                                  13    
HELIX   21  21 PRO B  182  LYS B  186  5                                   5    
HELIX   22  22 ASP B  203  GLU B  222  1                                  20    
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  TYR B  373  1                                  18    
HELIX   31  31 ILE B  406  ASP B  409  5                                   4    
HELIX   32  32 GLN B  414  LYS B  425  1                                  12    
HELIX   33  33 THR C   86  LEU C   94  1                                   9    
HELIX   34  34 SER C   97  SER C  110  1                                  14    
HELIX   35  35 PRO C  150  LYS C  155  1                                   6    
HELIX   36  36 LEU C  156  ALA C  168  1                                  13    
HELIX   37  37 PRO C  182  LYS C  186  5                                   5    
HELIX   38  38 ASP C  203  HIS C  223  1                                  21    
HELIX   39  39 SER C  237  LEU C  241  5                                   5    
HELIX   40  40 THR C  252  ASP C  263  1                                  12    
HELIX   41  41 ASP C  263  ASN C  270  1                                   8    
HELIX   42  42 LEU C  286  LEU C  288  5                                   3    
HELIX   43  43 PRO C  289  THR C  297  1                                   9    
HELIX   44  44 ASP C  298  LYS C  303  1                                   6    
HELIX   45  45 PRO C  319  PHE C  331  1                                  13    
HELIX   46  46 SER C  356  TYR C  373  1                                  18    
HELIX   47  47 ILE C  406  ASP C  409  5                                   4    
HELIX   48  48 GLN C  414  LYS C  425  1                                  12    
HELIX   49  49 THR D   86  ALA D   95  1                                  10    
HELIX   50  50 SER D   97  SER D  110  1                                  14    
HELIX   51  51 PRO D  150  LYS D  155  1                                   6    
HELIX   52  52 LEU D  156  ALA D  168  1                                  13    
HELIX   53  53 PRO D  182  LYS D  186  5                                   5    
HELIX   54  54 ASP D  203  HIS D  223  1                                  21    
HELIX   55  55 SER D  237  LEU D  241  5                                   5    
HELIX   56  56 THR D  252  ASP D  263  1                                  12    
HELIX   57  57 ASP D  263  SER D  271  1                                   9    
HELIX   58  58 LEU D  286  LEU D  288  5                                   3    
HELIX   59  59 PRO D  289  THR D  297  1                                   9    
HELIX   60  60 ASP D  298  LYS D  303  1                                   6    
HELIX   61  61 THR D  323  PHE D  331  1                                   9    
HELIX   62  62 SER D  356  TYR D  373  1                                  18    
HELIX   63  63 ILE D  406  ASP D  409  5                                   4    
HELIX   64  64 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  ILE A 403   O  TYR A 412           
SHEET    1   B 9 GLU A  50  PRO A  55  0                                        
SHEET    2   B 9 THR A  36  THR A  43 -1  N  GLU A  41   O  GLU A  50           
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 460   O  HIS A 490           
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  SER A 484   N  VAL A 468           
SHEET    1   C 9 GLY A  80  ALA A  84  0                                        
SHEET    2   C 9 ILE A 118  MET A 123  1  O  ARG A 120   N  GLY A  83           
SHEET    3   C 9 SER A 173  PRO A 178  1  O  LEU A 175   N  ILE A 119           
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  TRP A 312  1  O  GLY A 307   N  MET A 280           
SHEET    7   C 9 MET A 335  ALA A 341  1  O  PHE A 337   N  VAL A 310           
SHEET    8   C 9 VAL A 375  ASN A 382  1  O  VAL A 376   N  LEU A 336           
SHEET    9   C 9 GLY A  80  ALA A  84  1  N  GLY A  82   O  ASP A 380           
SHEET    1   D 4 PRO B   6  LYS B   7  0                                        
SHEET    2   D 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7           
SHEET    3   D 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18           
SHEET    4   D 4 ILE B 402  ASP B 405 -1  N  ILE B 403   O  TYR B 412           
SHEET    1   E 9 GLU B  50  PRO B  55  0                                        
SHEET    2   E 9 THR B  36  THR B  43 -1  N  ARG B  39   O  SER B  52           
SHEET    3   E 9 SER B 488  TRP B 494 -1  O  LEU B 493   N  SER B  38           
SHEET    4   E 9 ALA B 456  ASN B 462 -1  N  VAL B 460   O  HIS B 490           
SHEET    5   E 9 ASP B 445  MET B 450 -1  N  ASP B 445   O  LEU B 461           
SHEET    6   E 9 GLN B 432  ALA B 438 -1  N  GLN B 432   O  MET B 450           
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  THR B  68   O  VAL B 437           
SHEET    8   E 9 VAL B 468  ASP B 474  1  O  LYS B 473   N  LEU B  67           
SHEET    9   E 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474           
SHEET    1   F 9 GLY B  80  ALA B  84  0                                        
SHEET    2   F 9 ILE B 118  MET B 123  1  O  ARG B 120   N  GLY B  83           
SHEET    3   F 9 SER B 173  PRO B 178  1  O  LEU B 175   N  ILE B 119           
SHEET    4   F 9 ALA B 229  THR B 231  1  O  THR B 231   N  ALA B 176           
SHEET    5   F 9 ARG B 277  GLN B 284  1  O  ARG B 277   N  VAL B 230           
SHEET    6   F 9 GLY B 307  TYR B 313  1  O  ALA B 309   N  MET B 280           
SHEET    7   F 9 MET B 335  CYS B 342  1  O  PHE B 337   N  VAL B 310           
SHEET    8   F 9 GLY B 377  ASN B 382  1  O  THR B 379   N  ALA B 338           
SHEET    9   F 9 GLY B  80  ALA B  84  1  N  ALA B  84   O  TRP B 381           
SHEET    1   G 4 PRO C   6  LYS C   7  0                                        
SHEET    2   G 4 VAL C  15  CYS C  18 -1  O  VAL C  15   N  LYS C   7           
SHEET    3   G 4 THR C 410  LYS C 413 -1  O  PHE C 411   N  CYS C  18           
SHEET    4   G 4 ILE C 402  ASP C 405 -1  N  ILE C 403   O  TYR C 412           
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  LEU C 449   O  VAL C 457           
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  LYS C 473   N  LEU C  69           
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  ARG C 277   N  VAL C 230           
SHEET    6   I 9 VAL C 305  HIS C 311  1  O  ALA C 309   N  MET C 280           
SHEET    7   I 9 MET C 335  ALA C 341  1  O  PHE C 337   N  VAL C 310           
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  ALA C  84   O  TRP C 381           
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  ILE D 403   O  TYR D 412           
SHEET    1   K10 THR D  36  THR D  43  0                                        
SHEET    2   K10 ARG D  48  GLN D  57 -1  O  SER D  52   N  ARG D  39           
SHEET    3   K10 GLY D 478  SER D 484 -1  O  PHE D 479   N  GLN D  57           
SHEET    4   K10 VAL D 468  ASP D 474 -1  N  ASP D 474   O  GLY D 478           
SHEET    5   K10 LEU D  65  LYS D  77  1  N  LEU D  69   O  LYS D 473           
SHEET    6   K10 GLN D 432  ALA D 438 -1  O  VAL D 437   N  THR D  68           
SHEET    7   K10 ASP D 445  MET D 450 -1  O  MET D 450   N  GLN D 432           
SHEET    8   K10 ALA D 456  ASN D 462 -1  O  VAL D 459   N  VAL D 447           
SHEET    9   K10 SER D 488  TRP D 494 -1  O  HIS D 490   N  VAL D 460           
SHEET   10   K10 THR D  36  THR D  43 -1  N  SER D  38   O  LEU D 493           
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  PHE D 337   N  VAL D 310           
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  80   O  TRP D 378           
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.08  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.16  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.13  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.16  
SSBOND   5 CYS C    4    CYS C   16                          1555   1555  2.09  
SSBOND   6 CYS C   18    CYS C   23                          1555   1555  2.14  
SSBOND   7 CYS D    4    CYS D   16                          1555   1555  2.11  
SSBOND   8 CYS D   18    CYS D   23                          1555   1555  2.15  
LINK         ND2 ASN A  19                 C1  NAG A 513     1555   1555  1.45  
LINK         ND2 ASN B  19                 C1  NAG B 509     1555   1555  1.47  
LINK         ND2 ASN C  19                 C1  NAG C 510     1555   1555  1.45  
LINK         ND2 ASN D  19                 C1  NAG D 510     1555   1555  1.44  
LINK         ND2 ASN B 146                 C1  NAG B 508     1555   1555  1.35  
LINK         ND2 ASN D 146                 C1  NAG D 509     1555   1555  1.34  
CISPEP   1 LEU A  288    PRO A  289          0         8.11                     
CISPEP   2 TYR A  313    LEU A  314          0        26.71                     
CISPEP   3 GLY A  390    PRO A  391          0         5.75                     
CISPEP   4 GLY B   62    THR B   63          0         5.60                     
CISPEP   5 LEU B  288    PRO B  289          0         4.75                     
CISPEP   6 GLY B  344    SER B  345          0         3.81                     
CISPEP   7 LYS B  346    PHE B  347          0         3.14                     
CISPEP   8 GLY B  390    PRO B  391          0         4.97                     
CISPEP   9 LEU C  288    PRO C  289          0         7.24                     
CISPEP  10 ALA C  318    PRO C  319          0        20.08                     
CISPEP  11 GLY C  390    PRO C  391          0         0.77                     
CISPEP  12 LEU D  288    PRO D  289          0         5.85                     
CISPEP  13 TRP D  348    GLU D  349          0         2.85                     
CISPEP  14 GLY D  390    PRO D  391          0         1.47                     
SITE     1 AC1  6 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 AC1  6 TRP A 357  ASP A 358                                          
SITE     1 AC2  3 ARG A  44  SER A  45  HOH A 559                               
SITE     1 AC3  5 THR A  63  GLY A  64  GLN A 440  HOH A 572                    
SITE     2 AC3  5 LYS C 473                                                     
SITE     1 AC4  4 LYS A  79  TRP A 228  ARG A 277  HIS A 306                    
SITE     1 AC5  4 LYS A 473  THR C  63  GLY C  64  GLN C 440                    
SITE     1 AC6  3 ARG A  44  SER A 465  TYR A 487                               
SITE     1 AC7  2 THR A 272  HIS A 273                                          
SITE     1 AC8  4 HIS A 290  LYS A 293  HOH A 523  HOH A 526                    
SITE     1 AC9  2 GLU A 254  ARG A 257                                          
SITE     1 BC1  3 ARG A 277  HIS A 306  HOH A 563                               
SITE     1 BC2  2 SER A  45  ARG A  47                                          
SITE     1 BC3  3 GLU A  72  GLU D 254  ARG D 257                               
SITE     1 BC4  2 ARG A 170  PRO A 428                                          
SITE     1 BC5  4 ARG A 395  ASN D 392  TRP D 393  ARG D 395                    
SITE     1 BC6  3 THR A 187  LYS A 198  GLY A 199                               
SITE     1 BC7  3 ILE A   5  ASN A  19  THR A  21                               
SITE     1 BC8  5 TYR A  11  TRP A 348  GLU A 349  GLN A 350                    
SITE     2 BC8  5 ARG A 353                                                     
SITE     1 BC9  6 TYR B  11  SER B  12  ARG B 353  SER B 356                    
SITE     2 BC9  6 TRP B 357  ASP B 358                                          
SITE     1 CC1  2 ARG B  44  SER B  45                                          
SITE     1 CC2  4 LYS B  79  TRP B 228  HIS B 306  HOH B 534                    
SITE     1 CC3  5 GLY B 193  LYS B 194  SER B 242  GLY B 243                    
SITE     2 CC3  5 HOH B 524                                                     
SITE     1 CC4  4 LYS B 321  ARG B 329  ARG C 329  LEU C 330                    
SITE     1 CC5  3 ARG B  44  SER B 465  TYR B 487                               
SITE     1 CC6  3 ARG B 277  VAL B 305  HIS B 306                               
SITE     1 CC7  3 ILE B 158  PRO B 159  HIS B 162                               
SITE     1 CC8  3 GLN B 226  HIS B 273  ASN B 275                               
SITE     1 CC9  4 ALA B   1  ARG B   2  SER B  25  HOH B 518                    
SITE     1 DC1  4 ASN B 146  HOH B 545  HOH B 548  LEU C  96                    
SITE     1 DC2  2 ILE B   5  ASN B  19                                          
SITE     1 DC3  4 LYS C  79  TRP C 228  ARG C 277  HIS C 306                    
SITE     1 DC4  6 TYR C  11  SER C  12  ARG C 353  SER C 356                    
SITE     2 DC4  6 TRP C 357  ASP C 358                                          
SITE     1 DC5  3 ARG C  44  SER C  45  HOH C 552                               
SITE     1 DC6  3 ARG C 257  HOH C 534  HOH C 535                               
SITE     1 DC7  5 GLN C 226  PHE C 227  THR C 272  HIS C 273                    
SITE     2 DC7  5 VAL C 276                                                     
SITE     1 DC8  3 ARG C  44  TYR C 487  HOH C 556                               
SITE     1 DC9  3 ARG C 277  HIS C 306  HOH C 561                               
SITE     1 EC1  5 HIS C 290  LYS C 293  HOH C 523  HOH C 562                    
SITE     2 EC1  5 HOH C 569                                                     
SITE     1 EC2  4 ALA C 438  ASN C 442  HOH C 545  HOH C 547                    
SITE     1 EC3  5 ILE C 158  PRO C 159  HIS C 162  HOH C 516                    
SITE     2 EC3  5 HOH C 559                                                     
SITE     1 EC4  3 PHE C  75  HIS C 328  HIS C 374                               
SITE     1 EC5  2 ARG C 170  PRO C 428                                          
SITE     1 EC6  3 ILE C   5  ASN C  19  THR C  21                               
SITE     1 EC7  5 TYR C  11  TRP C 348  GLU C 349  GLN C 350                    
SITE     2 EC7  5 ARG C 353                                                     
SITE     1 EC8  6 TYR D  11  SER D  12  ARG D 353  SER D 356                    
SITE     2 EC8  6 TRP D 357  ASP D 358                                          
SITE     1 EC9  2 ARG D  44  SER D  45                                          
SITE     1 FC1  5 LYS D  79  TRP D 228  ARG D 277  HIS D 306                    
SITE     2 FC1  5 HOH D 560                                                     
SITE     1 FC2  5 GLY D 193  LYS D 194  SER D 242  GLY D 243                    
SITE     2 FC2  5 HOH D 531                                                     
SITE     1 FC3  3 GLN D 226  HIS D 273  ASN D 275                               
SITE     1 FC4  2 ARG D  44  TYR D 487                                          
SITE     1 FC5  4 ARG D 277  VAL D 305  HIS D 306  HOH D 554                    
SITE     1 FC6  4 ILE D 158  PRO D 159  HIS D 162  HOH D 541                    
SITE     1 FC7  1 ARG D 262                                                     
SITE     1 FC8  3 ARG A 329  LYS D 321  ARG D 329                               
SITE     1 FC9  5 THR D 187  LYS D 198  GLY D 199  HOH D 533                    
SITE     2 FC9  5 HOH D 542                                                     
SITE     1 GC1  4 LEU A  96  ASN D 146  HOH D 517  HOH D 545                    
SITE     1 GC2  3 ASN D  19  TYR D  22  HOH D 561                               
CRYST1  109.442   91.703  152.491  90.00 111.04  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      0.009137  0.000000  0.003515        0.00000                         
SCALE2      0.000000  0.010905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007026        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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