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Database: PDB
Entry: 1OGS
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Original site: 1OGS 
HEADER    HYDROLASE                               13-MAY-03   1OGS              
TITLE     HUMAN ACID-BETA-GLUCOSIDASE                                           
CAVEAT     1OGS    NAG A 1997 WRONG HAND AT C1                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GLUCOCEREBROSIDASE, BETA-GLUCOCEREBROSIDASE, ACID           
COMPND   5  BETA-GLUCOSIDASE, D-GLUCOSYL-N-ACYLSPHINGOSINE                      
COMPND   6  GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;                          
COMPND   7 EC: 3.2.1.45;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606;                                                
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO                                     
KEYWDS    HYDROLASE, GAUCHER DISEASE, GLUCOSIDASE,                              
KEYWDS   2 GLUCOCEREBROSIDASE, CEREZYME HYDROLASE, GLYCOSIDASE,                 
KEYWDS   3 SPHINGOLIPID METABOLISM, GLYCOPROTE LYSOSOME, MEMBRANE,              
KEYWDS   4 SIGNAL, DISEASE MUTATI POLYMORPHISM, ALTERNATIVE                     
KEYWDS   5 INITIATION, PHARMACEUTICAL, ISRAEL STRUCTURAL PROTEOMICS             
KEYWDS   6 CENTER, ISPC, STRUCTURAL GENOMICS                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.DVIR,M.HAREL,A.A.MCCARTHY,L.TOKER,I.SILMAN,A.H.FUTERMAN,            
AUTHOR   2 J.L.SUSSMAN                                                          
REVDAT   4   25-JAN-12 1OGS    1       CAVEAT REMARK VERSN  HET                 
REVDAT   4 2                           HETNAM FORMUL HETSYN LINK                
REVDAT   4 3                           SITE   HETATM                            
REVDAT   3   24-FEB-09 1OGS    1       VERSN                                    
REVDAT   2   21-OCT-03 1OGS    1       REMARK                                   
REVDAT   1   03-JUL-03 1OGS    0                                                
JRNL        AUTH   H.DVIR,M.HAREL,A.A.MCCARTHY,L.TOKER,I.SILMAN,                
JRNL        AUTH 2 A.H.FUTERMAN,J.L.SUSSMAN                                     
JRNL        TITL   X-RAY STRUCTURE OF HUMAN ACID-BETA-GLUCOSIDASE,              
JRNL        TITL 2 THE DEFECTIVE ENZYME IN GAUCHER DISEASE                      
JRNL        REF    EMBO REP.                     V.   4   704 2003              
JRNL        REFN                   ISSN 1469-3178                               
JRNL        PMID   12792654                                                     
JRNL        DOI    10.1038/SJ.EMBOR.EMBOR873                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.4                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 88501                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.3                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4690                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.9                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 12234                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.301                        
REMARK   3   BIN FREE R VALUE                    : 0.310                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.1                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 662                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7965                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 117                                     
REMARK   3   SOLVENT ATOMS            : 938                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.6                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.7                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 17.24                                                
REMARK   3    B22 (A**2) : -8.15                                                
REMARK   3    B33 (A**2) : -9.09                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.32                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.31                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.3                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.8                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.21  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.90  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.95  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.84  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.391893                                             
REMARK   3   BSOL        : 69.0691                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAY-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-12718.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0092, 1.0075, 1.0015, 0.8856     
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93248                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.230                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 57.5                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION AT ROOM TEMP            
REMARK 280  DROP CONTAINS 1.5 MICROLITER OF PROTEIN SOLUTION                    
REMARK 280 (10MG/ML) AND 1.5 MICROLITER OF MOTHER LIQUOR.                       
REMARK 280  MOTHER LIQUOR CONTAINS 1M AMMONIUM SULFATE,                         
REMARK 280  0.17M GUANIDINE HYDROCHLORIDE, 0.02M KCL,                           
REMARK 280  0.1M ACETATE PH 4.6.                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.83900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.83900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       53.86750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      142.61600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       53.86750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      142.61600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.83900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       53.86750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      142.61600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       45.83900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       53.86750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      142.61600            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B2013  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2209  LIES ON A SPECIAL POSITION.                          
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   NE2  GLN A   226     O    HOH A  2238              2.14            
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    MET A  49       53.20     37.42                                   
REMARK 500    PHE A  75     -139.79   -126.44                                   
REMARK 500    ALA A 124     -153.88     79.85                                   
REMARK 500    PHE A 128       56.49    -90.73                                   
REMARK 500    TYR A 133      155.56    175.74                                   
REMARK 500    ASP A 140       71.74     31.85                                   
REMARK 500    LEU A 156      -69.66   -104.16                                   
REMARK 500    ASN A 192     -157.29   -128.36                                   
REMARK 500    GLU A 233      144.68    162.37                                   
REMARK 500    GLU A 235       68.26     37.52                                   
REMARK 500    ASP A 263      -70.34   -119.01                                   
REMARK 500    LEU A 281      -81.85     71.18                                   
REMARK 500    ALA A 318      118.48   -160.11                                   
REMARK 500    THR A 323      -74.78   -103.27                                   
REMARK 500    HIS A 374       -1.56     72.18                                   
REMARK 500    TRP A 381     -139.37    -84.82                                   
REMARK 500    ARG A 395      141.68    179.28                                   
REMARK 500    PHE A 397       -8.79   -151.89                                   
REMARK 500    PHE B  75     -139.05   -124.03                                   
REMARK 500    ALA B 124     -155.97     80.87                                   
REMARK 500    LEU B 156      -70.87   -116.20                                   
REMARK 500    ASN B 192     -167.48   -117.62                                   
REMARK 500    GLU B 233      139.97    166.77                                   
REMARK 500    GLU B 235       66.54     34.43                                   
REMARK 500    ASP B 263      -71.23   -114.50                                   
REMARK 500    LEU B 281      -76.15     67.75                                   
REMARK 500    THR B 323      -76.46   -103.60                                   
REMARK 500    HIS B 374       -5.84     76.46                                   
REMARK 500    TRP B 381     -138.35    -82.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "BC" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1997 BOUND TO ASN A  19                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B  19 RESIDUES 1503 TO 1504                                    
DBREF  1OGS A    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  1OGS B    1   497  UNP    P04062   GLCM_HUMAN      40    536             
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                                                  
HET    NAG  B1503      14                                                       
HET    NAG  B1504      14                                                       
HET    NAG  A1997      14                                                       
HET    SO4  A1498       5                                                       
HET    SO4  A1499       5                                                       
HET    SO4  A1500       5                                                       
HET    SO4  A1501       5                                                       
HET    SO4  A1502       5                                                       
HET    SO4  A1503       5                                                       
HET    SO4  A1504       5                                                       
HET    SO4  A1505       5                                                       
HET    SO4  A1506       5                                                       
HET    SO4  A1507       5                                                       
HET    SO4  B1498       5                                                       
HET    SO4  B1499       5                                                       
HET    SO4  B1500       5                                                       
HET    SO4  B1501       5                                                       
HET    SO4  B1502       5                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   4  SO4    15(O4 S 2-)                                                  
FORMUL   5  HOH   *938(H2 O)                                                    
HELIX    1   1 THR A   86  LEU A   94  1                                   9    
HELIX    2   2 SER A   97  SER A  110  1                                  14    
HELIX    3   3 PRO A  150  LYS A  155  1                                   6    
HELIX    4   4 LEU A  156  ALA A  168  1                                  13    
HELIX    5   5 PRO A  182  LEU A  185  5                                   4    
HELIX    6   6 ASP A  203  HIS A  223  1                                  21    
HELIX    7   7 SER A  237  LEU A  241  5                                   5    
HELIX    8   8 THR A  252  ASP A  263  1                                  12    
HELIX    9   9 ASP A  263  ASN A  270  1                                   8    
HELIX   10  10 LEU A  286  LEU A  288  5                                   3    
HELIX   11  11 PRO A  289  THR A  297  1                                   9    
HELIX   12  12 ASP A  298  LYS A  303  1                                   6    
HELIX   13  13 PRO A  319  PHE A  331  1                                  13    
HELIX   14  14 SER A  356  TYR A  373  1                                  18    
HELIX   15  15 ILE A  406  LYS A  408  5                                   3    
HELIX   16  16 GLN A  414  LYS A  425  1                                  12    
HELIX   17  17 THR B   86  ALA B   95  1                                  10    
HELIX   18  18 SER B   97  SER B  110  1                                  14    
HELIX   19  19 PRO B  150  LYS B  155  1                                   6    
HELIX   20  20 LEU B  156  ALA B  168  1                                  13    
HELIX   21  21 PRO B  182  LEU B  185  5                                   4    
HELIX   22  22 ASP B  203  HIS B  223  1                                  21    
HELIX   23  23 GLU B  235  LEU B  241  5                                   7    
HELIX   24  24 THR B  252  ASP B  263  1                                  12    
HELIX   25  25 ASP B  263  ASN B  270  1                                   8    
HELIX   26  26 LEU B  286  LEU B  288  5                                   3    
HELIX   27  27 PRO B  289  THR B  297  1                                   9    
HELIX   28  28 ASP B  298  LYS B  303  1                                   6    
HELIX   29  29 PRO B  319  PHE B  331  1                                  13    
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    
SHEET    1  AA 4 PRO A   6  LYS A   7  0                                        
SHEET    2  AA 4 VAL A  15  ASN A  19 -1  O  VAL A  15   N  LYS A   7           
SHEET    3  AA 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18           
SHEET    4  AA 4 ILE A 402  ASP A 405 -1  O  ILE A 403   N  TYR A 412           
SHEET    1  AB 9 GLU A  50  PRO A  55  0                                        
SHEET    2  AB 9 THR A  36  THR A  43 -1  O  PHE A  37   N  GLY A  54           
SHEET    3  AB 9 SER A 488  TRP A 494 -1  O  ILE A 489   N  SER A  42           
SHEET    4  AB 9 ALA A 456  ASN A 462 -1  O  ALA A 456   N  TRP A 494           
SHEET    5  AB 9 LEU A 444  MET A 450 -1  O  ASP A 445   N  LEU A 461           
SHEET    6  AB 9 GLN A 432  ALA A 438 -1  O  GLN A 432   N  MET A 450           
SHEET    7  AB 9 LEU A  65  LYS A  77 -1  O  THR A  68   N  VAL A 437           
SHEET    8  AB 9 VAL A 468  ASP A 474  1  O  PRO A 469   N  LEU A  65           
SHEET    9  AB 9 GLY A 478  SER A 484 -1  O  GLY A 478   N  ASP A 474           
SHEET    1  AC 9 GLY A  80  ALA A  84  0                                        
SHEET    2  AC 9 VAL A 375  ASN A 382  1  O  TRP A 378   N  GLY A  82           
SHEET    3  AC 9 MET A 335  CYS A 342  1  O  LEU A 336   N  VAL A 376           
SHEET    4  AC 9 GLY A 307  TYR A 313  1  O  ILE A 308   N  PHE A 337           
SHEET    5  AC 9 ARG A 277  GLN A 284  1  O  MET A 280   N  ALA A 309           
SHEET    6  AC 9 ALA A 229  THR A 231  1  O  VAL A 230   N  LEU A 279           
SHEET    7  AC 9 SER A 173  PRO A 178  1  O  ALA A 176   N  THR A 231           
SHEET    8  AC 9 ILE A 118  MET A 123  1  O  ILE A 119   N  LEU A 175           
SHEET    9  AC 9 GLY A  80  ALA A  84  1  O  GLY A  83   N  ARG A 120           
SHEET    1  BA 4 PRO B   6  LYS B   7  0                                        
SHEET    2  BA 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7           
SHEET    3  BA 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18           
SHEET    4  BA 4 ILE B 402  ASP B 405 -1  O  ILE B 403   N  TYR B 412           
SHEET    1  BB 9 GLU B  50  PRO B  55  0                                        
SHEET    2  BB 9 THR B  36  THR B  43 -1  O  PHE B  37   N  GLY B  54           
SHEET    3  BB 9 SER B 488  TRP B 494 -1  O  ILE B 489   N  SER B  42           
SHEET    4  BB 9 ALA B 456  ASN B 462 -1  O  ALA B 456   N  TRP B 494           
SHEET    5  BB 9 LEU B 444  MET B 450 -1  O  ASP B 445   N  LEU B 461           
SHEET    6  BB 9 GLN B 432  ALA B 438 -1  O  GLN B 432   N  MET B 450           
SHEET    7  BB 9 LEU B  65  LYS B  77 -1  O  THR B  68   N  VAL B 437           
SHEET    8  BB 9 VAL B 468  ASP B 474  1  O  PRO B 469   N  LEU B  65           
SHEET    9  BB 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474           
SHEET    1  BC 9 GLY B  80  ALA B  84  0                                        
SHEET    2  BC 9 VAL B 375  ASN B 382  1  O  TRP B 378   N  GLY B  82           
SHEET    3  BC 9 MET B 335  CYS B 342  1  O  LEU B 336   N  VAL B 376           
SHEET    4  BC 9 GLY B 307  TYR B 313  1  O  ILE B 308   N  PHE B 337           
SHEET    5  BC 9 ARG B 277  GLN B 284  1  O  MET B 280   N  ALA B 309           
SHEET    6  BC 9 ALA B 229  THR B 231  1  O  VAL B 230   N  LEU B 279           
SHEET    7  BC 9 SER B 173  PRO B 178  1  O  ALA B 176   N  THR B 231           
SHEET    8  BC 9 ILE B 118  MET B 123  1  O  ILE B 119   N  LEU B 175           
SHEET    9  BC 9 GLY B  80  ALA B  84  1  O  GLY B  83   N  ARG B 120           
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.04  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.04  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.05  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.05  
LINK         ND2 ASN A  19                 C1  NAG A1997     1555   1555  1.46  
LINK         ND2 ASN B  19                 C1  NAG B1503     1555   1555  1.45  
LINK         O4  NAG B1503                 C1  NAG B1504     1555   1555  1.38  
CISPEP   1 LEU A  288    PRO A  289          0         0.35                     
CISPEP   2 GLY A  390    PRO A  391          0         0.08                     
CISPEP   3 LEU B  288    PRO B  289          0         0.05                     
CISPEP   4 GLY B  390    PRO B  391          0         0.25                     
SITE     1 AC1  9 ASP A 127  PHE A 128  TRP A 179  PHE A 246                    
SITE     2 AC1  9 TYR A 313  GLU A 340  TRP A 381  PHE A 397                    
SITE     3 AC1  9 HOH A2424                                                     
SITE     1 AC2  7 ARG A   2  ASP A  24  SER A  25  PHE A  26                    
SITE     2 AC2  7 ARG A  48  MET A  49  HOH A2425                               
SITE     1 AC3  2 ARG A  44  TYR A 487                                          
SITE     1 AC4  2 GLU A 254  ARG A 257                                          
SITE     1 AC5  5 GLN A 169  ARG A 170  PRO A 428  HOH A2427                    
SITE     2 AC5  5 HOH A2428                                                     
SITE     1 AC6  2 ARG A  44  SER A  45                                          
SITE     1 AC7  7 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 AC7  7 TRP A 357  ASP A 358  HOH A2322                               
SITE     1 AC8  6 THR A  63  GLY A  64  GLN A 440  LYS A 473                    
SITE     2 AC8  6 HOH A2430  HOH A2431                                          
SITE     1 AC9  6 LYS A  79  TRP A 228  ARG A 277  HIS A 306                    
SITE     2 AC9  6 HOH A2432  HOH A2433                                          
SITE     1 BC1  3 ARG A 329  LYS B 321  ARG B 329                               
SITE     1 BC2  7 GLY B 193  LYS B 194  SER B 242  GLY B 243                    
SITE     2 BC2  7 HOH B2259  HOH B2489  HOH B2490                               
SITE     1 BC3  6 LYS B  79  TRP B 228  ARG B 277  HIS B 306                    
SITE     2 BC3  6 HOH B2438  HOH B2491                                          
SITE     1 BC4  7 SER A 242  TYR B  11  SER B  12  ARG B 353                    
SITE     2 BC4  7 SER B 356  TRP B 357  ASP B 358                               
SITE     1 BC5  3 ARG B  44  SER B  45  HOH B2493                               
SITE     1 BC6  3 ARG B  44  SER B 465  TYR B 487                               
SITE     1 BC7  8 ASN A  19  THR A  21  TYR A  22  HOH A2422                    
SITE     2 BC7  8 HOH A2434  HOH A2435  HOH A2436  HOH A2437                    
SITE     1 BC8  6 ASN B  19  HOH B2022  HOH B2494  HOH B2497                    
SITE     2 BC8  6 HOH B2499  HOH B2500                                          
CRYST1  107.735  285.232   91.678  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009282  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003506  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010908        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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