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Database: PDB
Entry: 3KEH
LinkDB: 3KEH
Original site: 3KEH 
HEADER    HYDROLASE                               26-OCT-09   3KEH              
TITLE     CRYSTAL STRUCTURE OF N370S GLUCOCEREBROSIDASE MUTANT AT PH 7.4        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOCEREBROSIDASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL- 
COMPND   5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;         
COMPND   6 EC: 3.2.1.45;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GBA, GC, GLUC;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GLUCOCEREBROSIDASE, ACID-BETA-GLUCOSIDASE, N370S, GLUCOSYCEREMIDASE,  
KEYWDS   2 TIM BARREL, ALTERNATIVE INITIATION, DISEASE MUTATION, DISULFIDE      
KEYWDS   3 BOND, GAUCHER DISEASE, GLYCOPROTEIN, GLYCOSIDASE, HYDROLASE,         
KEYWDS   4 ICHTHYOSIS, LIPID METABOLISM, LYSOSOME, MEMBRANE, SPHINGOLIPID       
KEYWDS   5 METABOLISM                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.R.WEI,S.BOUCHER,C.Q.PAN,T.EDMUNDS                                   
REVDAT   1   27-OCT-10 3KEH    0                                                
JRNL        AUTH   R.R.WEI,S.BOUCHER,H.HUGHES,N.GUZIEWICA,S.VANPATTEN,C.Q.PAN,  
JRNL        AUTH 2 T.EDMUNDS                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF GLUCOCEREBROSIDASE CONTAINING THE N370S 
JRNL        TITL 2 MUTATION: IMPLICATION ON CHAPERON THERAPY                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 31773                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1698                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2249                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.36                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 104                          
REMARK   3   BIN FREE R VALUE                    : 0.4080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7857                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 109                                     
REMARK   3   SOLVENT ATOMS            : 42                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.68000                                              
REMARK   3    B22 (A**2) : -1.67000                                             
REMARK   3    B33 (A**2) : -4.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.399         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.303         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.352        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.853                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8202 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11189 ; 1.605 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   992 ; 7.050 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   358 ;36.124 ;23.352       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1262 ;18.394 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;19.315 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1215 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6274 ; 0.007 ; 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):  4971 ; 0.625 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8037 ; 1.195 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3231 ; 1.747 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3152 ; 2.915 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3KEH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055890.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765                             
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL, CYLINDRICALLY      
REMARK 200                                   BENT, SI(220)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31773                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.15800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: !OGS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7M POTASSIUM PHOSPHATE/0.7M SODIUM     
REMARK 280  PHOSPHATE/0.1M HEPES, PH7.4, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 294K                                                    
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       46.00000            
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       46.00000            
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       53.91500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      142.96000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       53.91500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      142.96000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       46.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       53.91500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      142.96000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       46.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       53.91500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      142.96000            
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, 3                                                 
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
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 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -53.91500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      142.96000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 68460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -239.0 KCAL/MOL                       
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       46.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       53.91500            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      142.96000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000       46.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000      -53.91500            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      142.96000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A   363     OD1  ASP A   380              2.06            
REMARK 500   O    LEU B   281     O    ALA B   309              2.08            
REMARK 500   OH   TYR B   363     OD1  ASP B   380              2.15            
REMARK 500   O    PRO B     3     OH   TYR B    22              2.18            
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    CYS A  23   CB    CYS A  23   SG      0.116                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B 167   CA  -  CB  -  CG  ANGL. DEV. =  14.7 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    ASN A  19     -157.66   -110.80                                   
REMARK 500    ALA A  33      132.48    -32.38                                   
REMARK 500    PHE A  75     -146.57   -120.53                                   
REMARK 500    ALA A 124     -169.34     85.18                                   
REMARK 500    PHE A 128       53.62    -92.32                                   
REMARK 500    ALA A 136       83.15   -159.49                                   
REMARK 500    LEU A 144       69.93     60.18                                   
REMARK 500    LEU A 156      -62.76   -104.76                                   
REMARK 500    LYS A 194       97.20    -54.12                                   
REMARK 500    LYS A 224       60.44     68.92                                   
REMARK 500    LEU A 281       59.75     38.81                                   
REMARK 500    ALA A 318       98.15   -168.92                                   
REMARK 500    THR A 323      -79.18    -98.24                                   
REMARK 500    LYS A 346      119.27    -32.13                                   
REMARK 500    TRP A 381     -100.85    -82.78                                   
REMARK 500    ARG A 395      142.92   -175.09                                   
REMARK 500    PHE A 397       -1.68   -141.38                                   
REMARK 500    ASP A 399     -179.47    -69.36                                   
REMARK 500    ASP A 409       23.32     41.61                                   
REMARK 500    PHE A 423      -63.34   -102.25                                   
REMARK 500    LEU A 436      108.74   -161.96                                   
REMARK 500    HIS A 451      162.64    -49.06                                   
REMARK 500    ASN B  19     -158.07   -137.81                                   
REMARK 500    PHE B  75     -147.93   -122.64                                   
REMARK 500    ALA B 124     -160.27     90.22                                   
REMARK 500    CYS B 126     -163.76   -110.13                                   
REMARK 500    PHE B 128       54.71    -93.02                                   
REMARK 500    LEU B 156      -72.13   -118.08                                   
REMARK 500    GLU B 233      146.34   -178.26                                   
REMARK 500    GLU B 235       55.83     32.12                                   
REMARK 500    LEU B 249      113.16   -175.94                                   
REMARK 500    ASP B 263      -74.08   -120.81                                   
REMARK 500    HIS B 274      -36.70    -38.92                                   
REMARK 500    LEU B 281       71.97     37.84                                   
REMARK 500    THR B 323      -82.48    -95.90                                   
REMARK 500    TRP B 381     -119.42    -79.43                                   
REMARK 500    ASN B 396       44.03    -91.55                                   
REMARK 500    PHE B 423      -63.35   -105.88                                   
REMARK 500    GLN B 440      154.23    178.37                                   
REMARK 500    ASN B 442      154.22    175.72                                   
REMARK 500    VAL B 477      -32.65   -130.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NDG A 1997                                                       
REMARK 610     NAG A 1998                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 1997                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1509                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1499                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 498                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KE0   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN CRYSTALLIZED AT PH5.4                               
DBREF  3KEH A    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3KEH B    1   497  UNP    P04062   GLCM_HUMAN      40    536             
SEQADV 3KEH SER A  370  UNP  P04062    ASN   409 ENGINEERED                     
SEQADV 3KEH SER B  370  UNP  P04062    ASN   409 ENGINEERED                     
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 SER 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  ARG 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 SER 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  ARG ARG GLN                                                  
MODRES 3KEH ASN B   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3KEH ASN B  146  ASN  GLYCOSYLATION SITE                                 
HET    NDG  A1997      14                                                       
HET    SO4  A1501       5                                                       
HET    SO4  A1502       5                                                       
HET    SO4  A1504       5                                                       
HET    SO4  A1506       5                                                       
HET    SO4  A1507       5                                                       
HET    GOL  A1509       6                                                       
HET    NAG  A1998       1                                                       
HET    NAG  B1503      14                                                       
HET    NAG  B1504      14                                                       
HET    SO4  B1499       5                                                       
HET    SO4  B1500       5                                                       
HET    SO4  B1502       5                                                       
HET    NAG  B1505      14                                                       
HET    GOL  B 498       6                                                       
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NDG    C8 H15 N O6                                                  
FORMUL   4  SO4    8(O4 S 2-)                                                   
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  10  NAG    4(C8 H15 N O6)                                               
FORMUL  17  HOH   *42(H2 O)                                                     
HELIX    1   1 THR A   86  LEU A   96  1                                  11    
HELIX    2   2 SER A   97  SER A  110  1                                  14    
HELIX    3   3 PRO A  150  LEU A  156  1                                   7    
HELIX    4   4 LEU A  156  ALA A  168  1                                  13    
HELIX    5   5 PRO A  182  LYS A  186  5                                   5    
HELIX    6   6 ASP A  203  HIS A  223  1                                  21    
HELIX    7   7 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  ASP A  409  5                                   4    
HELIX   16  16 GLN A  414  LYS A  425  1                                  12    
HELIX   17  17 THR B   86  ALA B   95  1                                  10    
HELIX   18  18 SER B   97  SER B  110  1                                  14    
HELIX   19  19 PRO B  150  LYS B  155  1                                   6    
HELIX   20  20 LEU B  156  ALA B  168  1                                  13    
HELIX   21  21 PRO B  182  LYS B  186  5                                   5    
HELIX   22  22 ASP B  203  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   A 5 PRO A   6  LYS A   7  0                                        
SHEET    2   A 5 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7           
SHEET    3   A 5 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18           
SHEET    4   A 5 ILE A 402  ASP A 405 -1  N  ILE A 403   O  TYR A 412           
SHEET    5   A 5 ALA A 384  LEU A 385  1  N  LEU A 385   O  VAL A 404           
SHEET    1   B 9 ARG A  48  PRO A  55  0                                        
SHEET    2   B 9 THR A  36  THR A  43 -1  N  ARG A  39   O  SER A  52           
SHEET    3   B 9 SER A 488  TRP A 494 -1  O  LEU A 493   N  SER A  38           
SHEET    4   B 9 ALA A 456  ASN A 462 -1  N  VAL A 460   O  HIS A 490           
SHEET    5   B 9 LEU A 444  MET A 450 -1  N  ASP A 445   O  LEU A 461           
SHEET    6   B 9 GLN A 432  ALA A 438 -1  N  GLN A 432   O  MET A 450           
SHEET    7   B 9 LEU A  65  LYS A  77 -1  N  PHE A  75   O  ARG A 433           
SHEET    8   B 9 VAL A 468  ASP A 474  1  O  THR A 471   N  LEU A  67           
SHEET    9   B 9 GLY A 478  SER A 484 -1  O  SER A 484   N  VAL A 468           
SHEET    1   C 9 GLY A  80  ALA A  84  0                                        
SHEET    2   C 9 ILE A 118  MET A 123  1  O  ILE A 118   N  GLY A  83           
SHEET    3   C 9 SER A 173  PRO A 178  1  O  LEU A 175   N  VAL A 121           
SHEET    4   C 9 ALA A 229  THR A 231  1  O  THR A 231   N  ALA A 176           
SHEET    5   C 9 ARG A 277  GLN A 284  1  O  ARG A 277   N  VAL A 230           
SHEET    6   C 9 VAL A 305  TYR A 313  1  O  ALA A 309   N  MET A 280           
SHEET    7   C 9 MET A 335  CYS A 342  1  O  MET A 335   N  ILE A 308           
SHEET    8   C 9 VAL A 375  ASN A 382  1  O  VAL A 376   N  LEU A 336           
SHEET    9   C 9 GLY A  80  ALA A  84  1  N  GLY A  82   O  ASP A 380           
SHEET    1   D 5 PRO B   6  LYS B   7  0                                        
SHEET    2   D 5 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7           
SHEET    3   D 5 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18           
SHEET    4   D 5 ILE B 402  ASP B 405 -1  N  ILE B 403   O  TYR B 412           
SHEET    5   D 5 ALA B 384  LEU B 385  1  N  LEU B 385   O  VAL B 404           
SHEET    1   E 9 GLU B  50  PRO B  55  0                                        
SHEET    2   E 9 THR B  36  THR B  43 -1  N  ARG B  39   O  SER B  52           
SHEET    3   E 9 SER B 488  TRP B 494 -1  O  LEU B 493   N  SER B  38           
SHEET    4   E 9 ALA B 456  ASN B 462 -1  N  VAL B 460   O  HIS B 490           
SHEET    5   E 9 LEU B 444  MET B 450 -1  N  ASP B 445   O  LEU B 461           
SHEET    6   E 9 GLN B 432  VAL B 437 -1  N  VAL B 434   O  ALA B 448           
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  THR B  68   O  VAL B 437           
SHEET    8   E 9 VAL B 468  ASP B 474  1  O  LYS B 473   N  LEU B  69           
SHEET    9   E 9 GLY B 478  SER B 484 -1  O  SER B 484   N  VAL B 468           
SHEET    1   F 9 GLY B  80  ALA B  84  0                                        
SHEET    2   F 9 ILE B 118  MET B 123  1  O  ILE B 118   N  GLY B  83           
SHEET    3   F 9 SER B 173  PRO B 178  1  O  LEU B 175   N  VAL B 121           
SHEET    4   F 9 ALA B 229  THR B 231  1  O  THR B 231   N  ALA B 176           
SHEET    5   F 9 ARG B 277  GLN B 284  1  O  LEU B 279   N  VAL B 230           
SHEET    6   F 9 GLY B 307  TYR B 313  1  O  ALA B 309   N  MET B 280           
SHEET    7   F 9 MET B 335  CYS B 342  1  O  PHE B 337   N  VAL B 310           
SHEET    8   F 9 VAL B 375  ASN B 382  1  O  VAL B 376   N  LEU B 336           
SHEET    9   F 9 GLY B  80  ALA B  84  1  N  GLY B  82   O  ASP B 380           
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.08  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.09  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.10  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.13  
LINK         ND2 ASN B  19                 C1  NAG B1503     1555   1555  1.46  
LINK         ND2 ASN B 146                 C1  NAG B1505     1555   1555  1.47  
LINK         O4  NAG B1503                 C1  NAG B1504     1555   1555  1.47  
CISPEP   1 LEU A  288    PRO A  289          0        -4.27                     
CISPEP   2 GLY A  390    PRO A  391          0        11.30                     
CISPEP   3 LEU B  288    PRO B  289          0         2.97                     
CISPEP   4 GLY B  390    PRO B  391          0         4.63                     
SITE     1 AC1  2 ASN A  19  THR A  21                                          
SITE     1 AC2  3 GLU A 254  ARG A 257  VAL A 294                               
SITE     1 AC3  3 GLN A 169  ARG A 170  PRO A 428                               
SITE     1 AC4  7 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 AC4  7 TRP A 357  ASP A 358  HOH A 509                               
SITE     1 AC5  4 LYS A  79  TRP A 228  ARG A 277  HIS A 306                    
SITE     1 AC6  4 ARG A 329  LEU A 330  LYS B 321  ARG B 329                    
SITE     1 AC7  6 ASP A  24  SER A  25  PHE A  26  ARG A  48                    
SITE     2 AC7  6 MET A  49  TYR A 418                                          
SITE     1 AC8  2 ASN B  19  NAG B1504                                          
SITE     1 AC9  1 NAG B1503                                                     
SITE     1 BC1  4 LYS B  79  TRP B 228  ARG B 277  HIS B 306                    
SITE     1 BC2  7 SER A 242  TYR B  11  SER B  12  ARG B 353                    
SITE     2 BC2  7 SER B 356  TRP B 357  ASP B 358                               
SITE     1 BC3  3 ARG B  44  SER B 465  TYR B 487                               
SITE     1 BC4  2 HOH A 506  ASN B 146                                          
SITE     1 BC5  9 ASP B 127  PHE B 128  TRP B 179  ASN B 234                    
SITE     2 BC5  9 GLU B 235  PHE B 246  GLU B 340  TRP B 381                    
SITE     3 BC5  9 ASN B 396                                                     
CRYST1  107.830  285.920   92.000  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      0.009274  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010870        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system