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Database: PDB
Entry: 2VT0
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Original site: 2VT0 
HEADER    HYDROLASE                               03-MAY-08   2VT0              
TITLE     X-RAY STRUCTURE OF A CONJUGATE WITH CONDURITOL-BETA-EPOXIDE           
TITLE    2 OF ACID-BETA-GLUCOSIDASE OVEREXPRESSED IN CULTURED PLANT             
TITLE    3 CELLS                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: TIM BARREL GLUCOSIDASE, RESIDUES 40-536;                   
COMPND   5 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE,             
COMPND   6  D-GLUCOSYL-N-ACYLSPHINGOSINE GLUCOHYDROLASE, GLUCOSIDASE;           
COMPND   7 EC: 3.2.1.45;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: THE ENZYME IS COVALENTLY INHIBITED BY CBE             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: LYSOSOME;                                                     
SOURCE   6 EXPRESSION_SYSTEM: DAUCUS CAROTA;                                    
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4039                                        
KEYWDS    HYDROLASE, ALTERNATIVE INITIATION, SPHINGOLIPID METABOLISM,           
KEYWDS   2 ISRAEL STRUCTURAL PROTEOMICS CENTER, DISEASE MUTATION,               
KEYWDS   3 GLUCOCEREBROSIDASE, PHARMACEUTICAL, GAUCHER DISEASE, LIPID           
KEYWDS   4 METABOLISM, GLUCOSIDASE, GLYCOSIDASE, POLYMORPHISM,                  
KEYWDS   5 GLYCOPROTEIN, ISPC, MEMBRANE, CEREZYME, LYSOSOME,                    
KEYWDS   6 STRUCTURAL GENOMICS, ALTERNATIVE SPLICING                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.BRUMSHTEIN,H.M.GREENBLATT,Y.SHAALTIEL,D.AVIEZER,I.SILMAN,           
AUTHOR   2 A.H.FUTERMAN,J.L.SUSSMAN                                             
REVDAT   3   10-OCT-12 2VT0    1       JRNL   REMARK VERSN  FORMUL              
REVDAT   3 2                           SITE                                     
REVDAT   2   24-FEB-09 2VT0    1       VERSN                                    
REVDAT   1   23-SEP-08 2VT0    0                                                
JRNL        AUTH   Y.KACHER,B.BRUMSHTEIN,S.BOLDIN-ADAMSKY,L.TOKER,A.SHAINSKAYA, 
JRNL        AUTH 2 I.SILMAN,J.L.SUSSMAN,A.H.FUTERMAN                            
JRNL        TITL   ACID BETA-GLUCOSIDASE: INSIGHTS FROM STRUCTURAL ANALYSIS     
JRNL        TITL 2 AND RELEVANCE TO GAUCHER DISEASE THERAPY.                    
JRNL        REF    BIOL.CHEM.                    V. 389  1361 2008              
JRNL        REFN                   ISSN 1431-6730                               
JRNL        PMID   18783340                                                     
JRNL        DOI    10.1515/BC.2008.163                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0067                                      
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 53238                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2838                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3474                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 201                          
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7723                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 159                                     
REMARK   3   SOLVENT ATOMS            : 464                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.217         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.175         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.520         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8119 ; 0.025 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11089 ; 1.993 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   979 ; 7.228 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   349 ;36.583 ;23.381       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1218 ;14.264 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;23.574 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1226 ; 0.140 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6145 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4907 ; 1.011 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7912 ; 1.765 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3212 ; 3.000 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3177 ; 4.543 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     162      2                      
REMARK   3           1     B      1       B     162      2                      
REMARK   3           2     A    167       A     450      2                      
REMARK   3           2     B    167       B     450      2                      
REMARK   3           3     A    452       A     496      2                      
REMARK   3           3     B    452       B     496      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1936 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1936 ;  0.06 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1848 ;  0.10 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1848 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1936 ;  0.27 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1936 ;  0.27 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1848 ;  0.32 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1848 ;  0.32 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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          
REMARK   3  RIDING POSITIONS. RESIDUES 27-31 ON CHAIN A AND 27-33 ON CHAIN      
REMARK   3  B ARE NOT VISIBLE IN ELECTRON DENSITY, HENCE ARE MISSING            
REMARK   4                                                                      
REMARK   4 2VT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  07-MAY-08.                 
REMARK 100 THE PDBE ID CODE IS EBI-35997.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000ONE                         
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59355                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 3.6                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.40                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.41                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.73                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2V3F                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE; 0.1M              
REMARK 280  TRIS PH 6.5; 25% W/V PEG 3350; CRYSTALLIZATION UNDER OIL            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       48.44200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     THR A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     LEU A   499                                                      
REMARK 465     VAL A   500                                                      
REMARK 465     ASP A   501                                                      
REMARK 465     THR A   502                                                      
REMARK 465     MET A   503                                                      
REMARK 465     GLU B    -1                                                      
REMARK 465     PHE B     0                                                      
REMARK 465     ASP B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     THR B    30                                                      
REMARK 465     PHE B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     ALA B    33                                                      
REMARK 465     GLN B   497                                                      
REMARK 465     LEU B   498                                                      
REMARK 465     LEU B   499                                                      
REMARK 465     VAL B   500                                                      
REMARK 465     ASP B   501                                                      
REMARK 465     THR B   502                                                      
REMARK 465     MET B   503                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  -1    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  34    CG   CD1  CD2                                       
REMARK 470     GLN A 169    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 224    CE   NZ                                             
REMARK 470     GLU A 300    CD   OE1  OE2                                       
REMARK 470     LYS A 441    CG   CD   CE   NZ                                   
REMARK 470     LYS A 466    CG   CD   CE   NZ                                   
REMARK 470     LEU A 498    CA   C    O    CB   CG   CD1  CD2                   
REMARK 470     ARG B   2    CZ   NH1  NH2                                       
REMARK 470     LEU B  34    CG   CD1  CD2                                       
REMARK 470     ASN B  59    CG   OD1  ND2                                       
REMARK 470     GLU B 111    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 112    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 303    NZ                                                  
REMARK 470     LYS B 441    CD   CE   NZ                                        
REMARK 470     LYS B 466    CG   CD   CE   NZ                                   
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   OD2  ASP A   298     O    HOH A  2128              2.16            
REMARK 500   O    HOH A  2102     O    HOH A  2122              1.89            
REMARK 500   O    HOH A  2153     O    HOH A  2159              1.98            
REMARK 500   O    HOH B  2013     O    HOH B  2014              2.12            
REMARK 500   O    HOH B  2021     O    HOH B  2221              2.09            
REMARK 500   O    HOH B  2049     O    HOH B  2126              1.77            
REMARK 500   O    HOH B  2076     O    HOH B  2206              2.19            
REMARK 500   O    HOH B  2089     O    HOH B  2092              2.12            
REMARK 500   O    HOH B  2164     O    HOH B  2165              2.10            
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    TYR A 212   CD1   TYR A 212   CE1     0.096                       
REMARK 500    ARG A 353   CZ    ARG A 353   NH2    -0.080                       
REMARK 500    TYR A 487   C     TYR A 487   O       0.136                       
REMARK 500    TRP B 184   CB    TRP B 184   CG      0.117                       
REMARK 500    ALA B 384   CA    ALA B 384   CB      0.130                       
REMARK 500    VAL B 394   CB    VAL B 394   CG1    -0.132                       
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 131   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 163   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 353   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A 433   NE  -  CZ  -  NH1 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG A 433   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    ARG A 463   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B  39   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    LEU B 317   CA  -  CB  -  CG  ANGL. DEV. =  17.5 DEGREES          
REMARK 500    ARG B 353   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    VAL B 457   CG1 -  CB  -  CG2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG B 463   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 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    ALA A  33      151.31    -48.94                                   
REMARK 500    MET A  49       49.77     39.78                                   
REMARK 500    PHE A  75     -129.33   -122.82                                   
REMARK 500    ALA A 124     -152.54     68.60                                   
REMARK 500    PHE A 128       48.15    -81.90                                   
REMARK 500    LEU A 156      -69.20   -107.93                                   
REMARK 500    ASN A 192     -169.83   -120.58                                   
REMARK 500    GLU A 233      139.96    177.11                                   
REMARK 500    LEU A 249      108.46   -162.35                                   
REMARK 500    LEU A 281      -84.94     71.82                                   
REMARK 500    THR A 323      -74.16   -109.08                                   
REMARK 500    HIS A 374        1.14     84.55                                   
REMARK 500    TRP A 381     -132.70    -90.95                                   
REMARK 500    ASN A 392      115.89   -166.76                                   
REMARK 500    PHE B  75     -124.34   -115.97                                   
REMARK 500    ALA B 124     -156.08     76.37                                   
REMARK 500    LEU B 156      -68.90   -100.19                                   
REMARK 500    ASN B 192     -163.39   -124.69                                   
REMARK 500    GLU B 233      134.52    171.05                                   
REMARK 500    LEU B 281      -81.64     68.30                                   
REMARK 500    THR B 323      -75.17   -116.62                                   
REMARK 500    HIS B 374       -0.88     87.09                                   
REMARK 500    TRP B 381     -138.13    -88.23                                   
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 LEU A   34     GLY A   35                  -47.38                    
REMARK 500 ALA A  476     VAL A  477                 -142.94                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 CBU IS THE COVALENTLY BOUND FORM OF CONDURITOL-BETA-EPOXIDE,         
REMARK 600  ONLY STEREOISOMER WAS EXPERIMENTALLY OBSERVED IN THE STRUCTURE      
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AC", "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 CBU A1499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBU B1497                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A  19 RESIDUES 1500 TO 1509                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B  19 RESIDUES 1498 TO 1504                                    
DBREF  2VT0 A   -1     0  PDB    2VT0     2VT0            -1      0             
DBREF  2VT0 A    1   497  UNP    Q9BDT0   GLCM_PANTR      40    536             
DBREF  2VT0 A  498   503  PDB    2VT0     2VT0           498    503             
DBREF  2VT0 B   -1     0  PDB    2VT0     2VT0            -1      0             
DBREF  2VT0 B    1   497  UNP    Q9BDT0   GLCM_PANTR      40    536             
DBREF  2VT0 B  498   503  PDB    2VT0     2VT0           498    503             
SEQADV 2VT0 PRO A   55  UNP  Q9BDT0    THR    94 CONFLICT                       
SEQADV 2VT0 HIS A  495  UNP  Q9BDT0    ARG   534 CONFLICT                       
SEQADV 2VT0 PRO B   55  UNP  Q9BDT0    THR    94 CONFLICT                       
SEQADV 2VT0 HIS B  495  UNP  Q9BDT0    ARG   534 CONFLICT                       
SEQRES   1 A  505  GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR          
SEQRES   2 A  505  SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP          
SEQRES   3 A  505  SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE          
SEQRES   4 A  505  SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU          
SEQRES   5 A  505  LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR          
SEQRES   6 A  505  GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN          
SEQRES   7 A  505  LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA          
SEQRES   8 A  505  ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN          
SEQRES   9 A  505  LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY          
SEQRES  10 A  505  TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE          
SEQRES  11 A  505  SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP          
SEQRES  12 A  505  PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR          
SEQRES  13 A  505  LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU          
SEQRES  14 A  505  ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR          
SEQRES  15 A  505  SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY          
SEQRES  16 A  505  LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS          
SEQRES  17 A  505  GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA          
SEQRES  18 A  505  TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA          
SEQRES  19 A  505  GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO          
SEQRES  20 A  505  PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP          
SEQRES  21 A  505  PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER          
SEQRES  22 A  505  THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN          
SEQRES  23 A  505  ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR          
SEQRES  24 A  505  ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL          
SEQRES  25 A  505  HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR          
SEQRES  26 A  505  LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU          
SEQRES  27 A  505  PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU          
SEQRES  28 A  505  GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN          
SEQRES  29 A  505  TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL          
SEQRES  30 A  505  VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU          
SEQRES  31 A  505  GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO          
SEQRES  32 A  505  ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN          
SEQRES  33 A  505  PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE          
SEQRES  34 A  505  PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN          
SEQRES  35 A  505  LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP          
SEQRES  36 A  505  GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS          
SEQRES  37 A  505  ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE          
SEQRES  38 A  505  LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR          
SEQRES  39 A  505  LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET                  
SEQRES   1 B  505  GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR          
SEQRES   2 B  505  SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP          
SEQRES   3 B  505  SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE          
SEQRES   4 B  505  SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU          
SEQRES   5 B  505  LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR          
SEQRES   6 B  505  GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN          
SEQRES   7 B  505  LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA          
SEQRES   8 B  505  ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN          
SEQRES   9 B  505  LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY          
SEQRES  10 B  505  TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE          
SEQRES  11 B  505  SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP          
SEQRES  12 B  505  PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR          
SEQRES  13 B  505  LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU          
SEQRES  14 B  505  ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR          
SEQRES  15 B  505  SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY          
SEQRES  16 B  505  LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS          
SEQRES  17 B  505  GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA          
SEQRES  18 B  505  TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA          
SEQRES  19 B  505  GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO          
SEQRES  20 B  505  PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP          
SEQRES  21 B  505  PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER          
SEQRES  22 B  505  THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN          
SEQRES  23 B  505  ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR          
SEQRES  24 B  505  ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL          
SEQRES  25 B  505  HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR          
SEQRES  26 B  505  LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU          
SEQRES  27 B  505  PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU          
SEQRES  28 B  505  GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN          
SEQRES  29 B  505  TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL          
SEQRES  30 B  505  VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU          
SEQRES  31 B  505  GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO          
SEQRES  32 B  505  ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN          
SEQRES  33 B  505  PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE          
SEQRES  34 B  505  PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN          
SEQRES  35 B  505  LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP          
SEQRES  36 B  505  GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS          
SEQRES  37 B  505  ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE          
SEQRES  38 B  505  LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR          
SEQRES  39 B  505  LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET                  
HET    CBU  A1499      11                                                       
HET    CBU  B1497      11                                                       
HET    FUC  A1509      10                                                       
HET    NAG  A1500      14                                                       
HET    NAG  A1501      14                                                       
HET    MAN  A1502      11                                                       
HET    FUC  B1504      10                                                       
HET    NAG  B1498      14                                                       
HET    NAG  B1499      14                                                       
HET    SO4  A1503       5                                                       
HET    SO4  B1500       5                                                       
HET    SO4  B1501       5                                                       
HET    SO4  A1504       5                                                       
HET    SO4  A1505       5                                                       
HET    SO4  B1502       5                                                       
HET    SO4  A1506       5                                                       
HET    SO4  B1503       5                                                       
HET    SO4  A1507       5                                                       
HET    SO4  A1508       5                                                       
HETNAM     CBU (1R,2R,3S,4S,5S,6S)-CYCLOHEXANE-1,2,3,4,5,6-                     
HETNAM   2 CBU  HEXOL                                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  CBU    2(C6 H12 O6)                                                 
FORMUL   4  SO4    10(O4 S 2-)                                                  
FORMUL   5  MAN    C6 H12 O6                                                    
FORMUL   6  FUC    2(C6 H12 O5)                                                 
FORMUL   7  NAG    4(C8 H15 N O6)                                               
FORMUL   8  HOH   *464(H2 O)                                                    
HELIX    1   1 THR A   86  ALA A   95  1                                  10    
HELIX    2   2 SER A   97  SER A  110  1                                  14    
HELIX    3   3 PRO A  150  LYS A  155  1                                   6    
HELIX    4   4 LEU A  156  ALA A  168  1                                  13    
HELIX    5   5 PRO A  182  LEU A  185  5                                   4    
HELIX    6   6 ASP A  203  GLU A  222  1                                  20    
HELIX    7   7 GLU A  235  LEU A  241  5                                   7    
HELIX    8   8 THR A  252  ASP A  263  1                                  12    
HELIX    9   9 ASP A  263  ASN A  270  1                                   8    
HELIX   10  10 LEU A  286  LEU A  288  5                                   3    
HELIX   11  11 PRO A  289  THR A  297  1                                   9    
HELIX   12  12 ASP A  298  LYS A  303  1                                   6    
HELIX   13  13 LEU A  314  ALA A  318  5                                   5    
HELIX   14  14 PRO A  319  PHE A  331  1                                  13    
HELIX   15  15 SER A  356  TYR A  373  1                                  18    
HELIX   16  16 ILE A  406  ASP A  409  5                                   4    
HELIX   17  17 GLN A  414  LYS A  425  1                                  12    
HELIX   18  18 THR B   86  ALA B   95  1                                  10    
HELIX   19  19 SER B   97  SER B  110  1                                  14    
HELIX   20  20 PRO B  150  LYS B  155  1                                   6    
HELIX   21  21 LEU B  156  ALA B  168  1                                  13    
HELIX   22  22 PRO B  182  LEU B  185  5                                   4    
HELIX   23  23 ASP B  203  HIS B  223  1                                  21    
HELIX   24  24 GLU B  235  LEU B  241  5                                   7    
HELIX   25  25 THR B  252  ASP B  263  1                                  12    
HELIX   26  26 ASP B  263  ASN B  270  1                                   8    
HELIX   27  27 LEU B  286  LEU B  288  5                                   3    
HELIX   28  28 PRO B  289  THR B  297  1                                   9    
HELIX   29  29 ASP B  298  LYS B  303  1                                   6    
HELIX   30  30 LEU B  314  ALA B  318  5                                   5    
HELIX   31  31 THR B  323  PHE B  331  1                                   9    
HELIX   32  32 SER B  356  TYR B  373  1                                  18    
HELIX   33  33 ILE B  406  ASP B  409  5                                   4    
HELIX   34  34 GLN B  414  LYS B  425  1                                  12    
SHEET    1  AA 4 PRO A   6  LYS A   7  0                                        
SHEET    2  AA 4 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7           
SHEET    3  AA 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18           
SHEET    4  AA 4 ILE A 402  ASP A 405 -1  O  ILE A 403   N  TYR A 412           
SHEET    1  AB 9 GLU A  50  PRO A  55  0                                        
SHEET    2  AB 9 THR A  36  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 GLY A 377  ASN A 382  1  O  TRP A 378   N  GLY A  82           
SHEET    3  AC 9 MET A 335  GLU A 340  1  O  ALA A 338   N  THR A 379           
SHEET    4  AC 9 GLY A 307  HIS A 311  1  O  ILE A 308   N  PHE A 337           
SHEET    5  AC 9 ARG A 277  GLN A 284  1  O  MET A 280   N  ALA A 309           
SHEET    6  AC 9 ALA A 229  THR A 231  1  O  VAL A 230   N  LEU A 279           
SHEET    7  AC 9 SER A 173  PRO A 178  1  O  ALA A 176   N  THR A 231           
SHEET    8  AC 9 ILE A 118  MET A 123  1  O  ILE A 119   N  LEU A 175           
SHEET    9  AC 9 GLY A  80  ALA A  84  1  O  GLY A  83   N  ARG A 120           
SHEET    1  BA 4 PRO B   6  LYS B   7  0                                        
SHEET    2  BA 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7           
SHEET    3  BA 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18           
SHEET    4  BA 4 ILE B 402  ASP B 405 -1  O  ILE B 403   N  TYR B 412           
SHEET    1  BB 9 GLU B  50  PRO B  55  0                                        
SHEET    2  BB 9 THR B  36  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  GLU B 340  1  O  LEU B 336   N  VAL B 376           
SHEET    4  BC 9 GLY B 307  HIS B 311  1  O  ILE B 308   N  PHE B 337           
SHEET    5  BC 9 ARG B 277  GLN B 284  1  O  MET B 280   N  ALA B 309           
SHEET    6  BC 9 ALA B 229  THR B 231  1  O  VAL B 230   N  LEU B 279           
SHEET    7  BC 9 SER B 173  PRO B 178  1  O  ALA B 176   N  THR B 231           
SHEET    8  BC 9 ILE B 118  MET B 123  1  O  ILE B 119   N  LEU B 175           
SHEET    9  BC 9 GLY B  80  ALA B  84  1  O  GLY B  83   N  ARG B 120           
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.19  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.21  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.12  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.23  
LINK         ND2 ASN A  19                 C1  NAG A1500     1555   1555  1.47  
LINK         OE2 GLU A 340                 C5  CBU A1499     1555   1555  1.47  
LINK         O3  NAG A1500                 C1  FUC A1509     1555   1555  1.49  
LINK         O4  NAG A1500                 C1  NAG A1501     1555   1555  1.43  
LINK         O4  NAG A1501                 C1  MAN A1502     1555   1555  1.45  
LINK         ND2 ASN B  19                 C1  NAG B1498     1555   1555  1.45  
LINK         OE2 GLU B 340                 C5  CBU B1497     1555   1555  1.48  
LINK         O3  NAG B1498                 C1  FUC B1504     1555   1555  1.47  
LINK         O4  NAG B1498                 C1  NAG B1499     1555   1555  1.44  
CISPEP   1 LEU A  288    PRO A  289          0         3.70                     
CISPEP   2 GLY A  390    PRO A  391          0         3.15                     
CISPEP   3 LEU B  288    PRO B  289          0         0.99                     
CISPEP   4 GLY B  390    PRO B  391          0         3.50                     
SITE     1 AC1 12 ASP A 127  PHE A 128  TRP A 179  ASN A 234                    
SITE     2 AC1 12 GLU A 235  PHE A 246  TYR A 313  GLU A 340                    
SITE     3 AC1 12 TRP A 381  ASN A 396  HOH A2224  HOH A2225                    
SITE     1 AC2 12 ASP B 127  PHE B 128  TRP B 179  ASN B 234                    
SITE     2 AC2 12 GLU B 235  PHE B 246  TYR B 313  GLU B 340                    
SITE     3 AC2 12 TRP B 381  ASN B 396  HOH B2226  HOH B2227                    
SITE     1 AC3 27 TYR A  11  SER A  12  ASN A  19  ARG A  44                    
SITE     2 AC3 27 SER A  45  LYS A  79  GLY A 193  LYS A 194                    
SITE     3 AC3 27 TRP A 228  SER A 242  GLY A 243  GLU A 254                    
SITE     4 AC3 27 ARG A 257  ARG A 277  HIS A 306  ARG A 353                    
SITE     5 AC3 27 SER A 356  TRP A 357  ASP A 358  TYR A 487                    
SITE     6 AC3 27 HOH A2012  HOH A2113  HOH A2226  HOH A2227                    
SITE     7 AC3 27 HOH A2228  HOH A2229  HOH A2230                               
SITE     1 AC4 26 TYR B  11  SER B  12  ASN B  19  TYR B  22                    
SITE     2 AC4 26 LYS B  79  GLY B 193  LYS B 194  TRP B 228                    
SITE     3 AC4 26 SER B 242  GLY B 243  GLU B 254  ARG B 257                    
SITE     4 AC4 26 ARG B 277  HIS B 306  ARG B 353  SER B 356                    
SITE     5 AC4 26 TRP B 357  ASP B 358  HOH B2009  HOH B2228                    
SITE     6 AC4 26 HOH B2229  HOH B2230  HOH B2231  HOH B2232                    
SITE     7 AC4 26 HOH B2233  HOH B2234                                          
CRYST1   68.184   96.884   83.171  90.00 103.73  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014666  0.000000  0.003583        0.00000                         
SCALE2      0.000000  0.010322  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012377        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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