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Database: PDB
Entry: 3WF3
LinkDB: 3WF3
Original site: 3WF3 
HEADER    HYDROLASE                               16-JUL-13   3WF3              
TITLE     CRYSTAL STRUCTURE OF HUMAN BETA-GALACTOSIDASE MUTANT I51T IN COMPLEX  
TITLE    2 WITH GALACTOSE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-GALACTOSIDASE;                                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ACID BETA-GALACTOSIDASE, LACTASE, ELASTIN RECEPTOR 1;       
COMPND   5 EC: 3.2.1.23;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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: ELNR1, GLB1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    GLYCOSYL HYDROLASE, TIM-BARREL DOMAIN, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.SUZUKI,U.OHTO,T.SHIMIZU                                             
REVDAT   3   08-NOV-23 3WF3    1       HETSYN                                   
REVDAT   2   29-JUL-20 3WF3    1       COMPND REMARK SEQADV HETNAM              
REVDAT   2 2                   1       LINK   SITE                              
REVDAT   1   23-APR-14 3WF3    0                                                
JRNL        AUTH   H.SUZUKI,U.OHTO,K.HIGAKI,T.MENA-BARRAGAN,M.AGUILAR-MONCAYO,  
JRNL        AUTH 2 C.ORTIZ MELLET,E.NANBA,J.M.GARCIA FERNANDEZ,Y.SUZUKI,        
JRNL        AUTH 3 T.SHIMIZU                                                    
JRNL        TITL   STRUCTURAL BASIS OF PHARMACOLOGICAL CHAPERONING FOR HUMAN    
JRNL        TITL 2 BETA-GALACTOSIDASE                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
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) : 27.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 158881                         
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7765                            
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) : 11376                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.56                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 562                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19202                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 348                                     
REMARK   3   SOLVENT ATOMS            : 1428                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.41                          
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): 0.243         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.200         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.144         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.538         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20234 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 18635 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27606 ; 1.700 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 42857 ; 1.345 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2410 ; 7.154 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   912 ;36.642 ;23.805       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3077 ;15.301 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    96 ;20.092 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2985 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 22684 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  4760 ; 0.001 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 3WF3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000096255.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 160267                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.15400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
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: 3THC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM SULFATE, HEPES, PH    
REMARK 280  7.5, VAPOR DIFFUSION, SITTINGDROP, TEMPERATURE 277K, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP                                             
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       57.94400            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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     GLU A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     TYR A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     ASP A    14                                                      
REMARK 465     TYR A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     ASP A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     ARG A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     ASP A   531                                                      
REMARK 465     SER A   532                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     HIS A   534                                                      
REMARK 465     HIS A   535                                                      
REMARK 465     ASP A   536                                                      
REMARK 465     GLU A   537                                                      
REMARK 465     ALA A   538                                                      
REMARK 465     TRP A   539                                                      
REMARK 465     ALA A   540                                                      
REMARK 465     HIS A   541                                                      
REMARK 465     ASN A   542                                                      
REMARK 465     SER A   543                                                      
REMARK 465     SER A   544                                                      
REMARK 465     VAL A   648                                                      
REMARK 465     THR A   649                                                      
REMARK 465     TYR A   650                                                      
REMARK 465     ASP A   651                                                      
REMARK 465     HIS A   652                                                      
REMARK 465     PRO A   653                                                      
REMARK 465     SER A   654                                                      
REMARK 465     LYS A   655                                                      
REMARK 465     PRO A   656                                                      
REMARK 465     VAL A   657                                                      
REMARK 465     GLU A   658                                                      
REMARK 465     LYS A   659                                                      
REMARK 465     ARG A   660                                                      
REMARK 465     LEU A   661                                                      
REMARK 465     MET A   662                                                      
REMARK 465     PRO A   663                                                      
REMARK 465     PRO A   664                                                      
REMARK 465     PRO A   665                                                      
REMARK 465     PRO A   666                                                      
REMARK 465     GLN A   667                                                      
REMARK 465     LYS A   668                                                      
REMARK 465     ASN A   669                                                      
REMARK 465     LYS A   670                                                      
REMARK 465     ASP A   671                                                      
REMARK 465     SER A   672                                                      
REMARK 465     TRP A   673                                                      
REMARK 465     LEU A   674                                                      
REMARK 465     ASP A   675                                                      
REMARK 465     HIS A   676                                                      
REMARK 465     VAL A   677                                                      
REMARK 465     GLU B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     TYR B     4                                                      
REMARK 465     VAL B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     PHE B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     HIS B    11                                                      
REMARK 465     HIS B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     ASP B    14                                                      
REMARK 465     TYR B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     ASP B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     ASP B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     ARG B    25                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     THR B    28                                                      
REMARK 465     ASP B   531                                                      
REMARK 465     SER B   532                                                      
REMARK 465     GLY B   533                                                      
REMARK 465     HIS B   534                                                      
REMARK 465     HIS B   535                                                      
REMARK 465     ASP B   536                                                      
REMARK 465     GLU B   537                                                      
REMARK 465     ALA B   538                                                      
REMARK 465     TRP B   539                                                      
REMARK 465     ALA B   540                                                      
REMARK 465     HIS B   541                                                      
REMARK 465     ASN B   542                                                      
REMARK 465     SER B   543                                                      
REMARK 465     SER B   544                                                      
REMARK 465     VAL B   648                                                      
REMARK 465     THR B   649                                                      
REMARK 465     TYR B   650                                                      
REMARK 465     ASP B   651                                                      
REMARK 465     HIS B   652                                                      
REMARK 465     PRO B   653                                                      
REMARK 465     SER B   654                                                      
REMARK 465     LYS B   655                                                      
REMARK 465     PRO B   656                                                      
REMARK 465     VAL B   657                                                      
REMARK 465     GLU B   658                                                      
REMARK 465     LYS B   659                                                      
REMARK 465     ARG B   660                                                      
REMARK 465     LEU B   661                                                      
REMARK 465     MET B   662                                                      
REMARK 465     PRO B   663                                                      
REMARK 465     PRO B   664                                                      
REMARK 465     PRO B   665                                                      
REMARK 465     PRO B   666                                                      
REMARK 465     GLN B   667                                                      
REMARK 465     LYS B   668                                                      
REMARK 465     ASN B   669                                                      
REMARK 465     LYS B   670                                                      
REMARK 465     ASP B   671                                                      
REMARK 465     SER B   672                                                      
REMARK 465     TRP B   673                                                      
REMARK 465     LEU B   674                                                      
REMARK 465     ASP B   675                                                      
REMARK 465     HIS B   676                                                      
REMARK 465     VAL B   677                                                      
REMARK 465     GLU C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     TYR C     4                                                      
REMARK 465     VAL C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     PHE C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     HIS C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     HIS C    13                                                      
REMARK 465     ASP C    14                                                      
REMARK 465     TYR C    15                                                      
REMARK 465     LYS C    16                                                      
REMARK 465     ASP C    17                                                      
REMARK 465     ASP C    18                                                      
REMARK 465     ASP C    19                                                      
REMARK 465     ASP C    20                                                      
REMARK 465     LYS C    21                                                      
REMARK 465     THR C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     ARG C    25                                                      
REMARK 465     ASN C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     THR C    28                                                      
REMARK 465     HIS C   529                                                      
REMARK 465     ARG C   530                                                      
REMARK 465     ASP C   531                                                      
REMARK 465     SER C   532                                                      
REMARK 465     GLY C   533                                                      
REMARK 465     HIS C   534                                                      
REMARK 465     HIS C   535                                                      
REMARK 465     ASP C   536                                                      
REMARK 465     GLU C   537                                                      
REMARK 465     ALA C   538                                                      
REMARK 465     TRP C   539                                                      
REMARK 465     ALA C   540                                                      
REMARK 465     HIS C   541                                                      
REMARK 465     ASN C   542                                                      
REMARK 465     SER C   543                                                      
REMARK 465     SER C   544                                                      
REMARK 465     VAL C   648                                                      
REMARK 465     THR C   649                                                      
REMARK 465     TYR C   650                                                      
REMARK 465     ASP C   651                                                      
REMARK 465     HIS C   652                                                      
REMARK 465     PRO C   653                                                      
REMARK 465     SER C   654                                                      
REMARK 465     LYS C   655                                                      
REMARK 465     PRO C   656                                                      
REMARK 465     VAL C   657                                                      
REMARK 465     GLU C   658                                                      
REMARK 465     LYS C   659                                                      
REMARK 465     ARG C   660                                                      
REMARK 465     LEU C   661                                                      
REMARK 465     MET C   662                                                      
REMARK 465     PRO C   663                                                      
REMARK 465     PRO C   664                                                      
REMARK 465     PRO C   665                                                      
REMARK 465     PRO C   666                                                      
REMARK 465     GLN C   667                                                      
REMARK 465     LYS C   668                                                      
REMARK 465     ASN C   669                                                      
REMARK 465     LYS C   670                                                      
REMARK 465     ASP C   671                                                      
REMARK 465     SER C   672                                                      
REMARK 465     TRP C   673                                                      
REMARK 465     LEU C   674                                                      
REMARK 465     ASP C   675                                                      
REMARK 465     HIS C   676                                                      
REMARK 465     VAL C   677                                                      
REMARK 465     GLU D     0                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     TYR D     4                                                      
REMARK 465     VAL D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     PHE D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     HIS D    10                                                      
REMARK 465     HIS D    11                                                      
REMARK 465     HIS D    12                                                      
REMARK 465     HIS D    13                                                      
REMARK 465     ASP D    14                                                      
REMARK 465     TYR D    15                                                      
REMARK 465     LYS D    16                                                      
REMARK 465     ASP D    17                                                      
REMARK 465     ASP D    18                                                      
REMARK 465     ASP D    19                                                      
REMARK 465     ASP D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     THR D    22                                                      
REMARK 465     SER D    23                                                      
REMARK 465     LEU D    24                                                      
REMARK 465     ARG D    25                                                      
REMARK 465     ASN D    26                                                      
REMARK 465     ALA D    27                                                      
REMARK 465     THR D    28                                                      
REMARK 465     HIS D   529                                                      
REMARK 465     ARG D   530                                                      
REMARK 465     ASP D   531                                                      
REMARK 465     SER D   532                                                      
REMARK 465     GLY D   533                                                      
REMARK 465     HIS D   534                                                      
REMARK 465     HIS D   535                                                      
REMARK 465     ASP D   536                                                      
REMARK 465     GLU D   537                                                      
REMARK 465     ALA D   538                                                      
REMARK 465     TRP D   539                                                      
REMARK 465     ALA D   540                                                      
REMARK 465     HIS D   541                                                      
REMARK 465     ASN D   542                                                      
REMARK 465     SER D   543                                                      
REMARK 465     SER D   544                                                      
REMARK 465     VAL D   648                                                      
REMARK 465     THR D   649                                                      
REMARK 465     TYR D   650                                                      
REMARK 465     ASP D   651                                                      
REMARK 465     HIS D   652                                                      
REMARK 465     PRO D   653                                                      
REMARK 465     SER D   654                                                      
REMARK 465     LYS D   655                                                      
REMARK 465     PRO D   656                                                      
REMARK 465     VAL D   657                                                      
REMARK 465     GLU D   658                                                      
REMARK 465     LYS D   659                                                      
REMARK 465     ARG D   660                                                      
REMARK 465     LEU D   661                                                      
REMARK 465     MET D   662                                                      
REMARK 465     PRO D   663                                                      
REMARK 465     PRO D   664                                                      
REMARK 465     PRO D   665                                                      
REMARK 465     PRO D   666                                                      
REMARK 465     GLN D   667                                                      
REMARK 465     LYS D   668                                                      
REMARK 465     ASN D   669                                                      
REMARK 465     LYS D   670                                                      
REMARK 465     ASP D   671                                                      
REMARK 465     SER D   672                                                      
REMARK 465     TRP D   673                                                      
REMARK 465     LEU D   674                                                      
REMARK 465     ASP D   675                                                      
REMARK 465     HIS D   676                                                      
REMARK 465     VAL D   677                                                      
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   CB   ASN D   555     O5   NAG D   703              2.09            
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    ASP A 101   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 206   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    MET A 609   CA  -  CB  -  CG  ANGL. DEV. =  12.6 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    GLU A 100     -120.68     70.29                                   
REMARK 500    CYS A 127     -106.25     64.61                                   
REMARK 500    ASP A 151      121.86    -33.44                                   
REMARK 500    GLU A 186     -160.60     60.66                                   
REMARK 500    ALA A 315     -115.35     59.93                                   
REMARK 500    ASN A 458      -16.93     73.75                                   
REMARK 500    TYR A 488       41.04   -101.30                                   
REMARK 500    LYS A 493      155.24     93.57                                   
REMARK 500    SER A 503       -7.48     78.90                                   
REMARK 500    ASP A 508       78.32     79.04                                   
REMARK 500    THR A 577      -70.62   -134.10                                   
REMARK 500    TRP A 592       65.88   -162.53                                   
REMARK 500    SER A 611      -61.48     54.19                                   
REMARK 500    GLU A 622      -50.70   -124.65                                   
REMARK 500    CYS A 626       12.46   -143.00                                   
REMARK 500    SER A 628      168.65    -34.86                                   
REMARK 500    ASP A 629       42.67    -91.56                                   
REMARK 500    ASP B  44       49.69     39.57                                   
REMARK 500    GLU B 100     -123.50     57.80                                   
REMARK 500    CYS B 127     -100.60     65.38                                   
REMARK 500    GLU B 131      119.43    -35.91                                   
REMARK 500    MET B 132       28.24     47.90                                   
REMARK 500    GLU B 186     -163.82     60.45                                   
REMARK 500    HIS B 224      137.42   -170.75                                   
REMARK 500    GLU B 268       85.86   -152.58                                   
REMARK 500    ALA B 315     -118.91     59.91                                   
REMARK 500    TYR B 333       -0.30     76.08                                   
REMARK 500    LEU B 382      -60.00   -100.02                                   
REMARK 500    ASN B 458      -49.26     78.89                                   
REMARK 500    TYR B 488       43.14    -97.13                                   
REMARK 500    LYS B 493      155.99     78.51                                   
REMARK 500    ASP B 508       84.35     68.58                                   
REMARK 500    THR B 577      -67.37   -127.77                                   
REMARK 500    TRP B 592       65.89   -155.52                                   
REMARK 500    GLU C 100     -124.01     55.97                                   
REMARK 500    CYS C 127     -103.81     66.23                                   
REMARK 500    GLU C 131      117.55    -31.35                                   
REMARK 500    GLU C 186     -170.43     59.58                                   
REMARK 500    ALA C 315     -127.58     50.21                                   
REMARK 500    TYR C 333       -6.12     76.22                                   
REMARK 500    LEU C 382      -62.49   -101.47                                   
REMARK 500    ASP C 448       56.89     37.43                                   
REMARK 500    ASN C 459      -45.10   -151.48                                   
REMARK 500    VAL C 483      129.14    -34.75                                   
REMARK 500    TYR C 488       38.76    -98.34                                   
REMARK 500    LYS C 493      150.55     78.20                                   
REMARK 500    SER C 503       -8.32     62.77                                   
REMARK 500    ASP C 508       87.62     66.88                                   
REMARK 500    THR C 577      -64.49   -129.49                                   
REMARK 500    TRP C 592       69.05   -152.85                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WEZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WF0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WF1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WF2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WF4   RELATED DB: PDB                                   
DBREF  3WF3 A   24   677  UNP    P16278   BGAL_HUMAN      24    677             
DBREF  3WF3 B   24   677  UNP    P16278   BGAL_HUMAN      24    677             
DBREF  3WF3 C   24   677  UNP    P16278   BGAL_HUMAN      24    677             
DBREF  3WF3 D   24   677  UNP    P16278   BGAL_HUMAN      24    677             
SEQADV 3WF3 GLU A    0  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ALA A    1  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 GLU A    2  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ALA A    3  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 TYR A    4  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 VAL A    5  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 GLU A    6  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 PHE A    7  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS A    8  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS A    9  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS A   10  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS A   11  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS A   12  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS A   13  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP A   14  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 TYR A   15  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 LYS A   16  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP A   17  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP A   18  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP A   19  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP A   20  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 LYS A   21  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 THR A   22  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 SER A   23  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 THR A   51  UNP  P16278    ILE    51 ENGINEERED MUTATION            
SEQADV 3WF3 GLU B    0  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ALA B    1  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 GLU B    2  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ALA B    3  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 TYR B    4  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 VAL B    5  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 GLU B    6  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 PHE B    7  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS B    8  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS B    9  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS B   10  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS B   11  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS B   12  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS B   13  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP B   14  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 TYR B   15  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 LYS B   16  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP B   17  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP B   18  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP B   19  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP B   20  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 LYS B   21  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 THR B   22  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 SER B   23  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 THR B   51  UNP  P16278    ILE    51 ENGINEERED MUTATION            
SEQADV 3WF3 GLU C    0  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ALA C    1  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 GLU C    2  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ALA C    3  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 TYR C    4  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 VAL C    5  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 GLU C    6  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 PHE C    7  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS C    8  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS C    9  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS C   10  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS C   11  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS C   12  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS C   13  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP C   14  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 TYR C   15  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 LYS C   16  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP C   17  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP C   18  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP C   19  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP C   20  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 LYS C   21  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 THR C   22  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 SER C   23  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 THR C   51  UNP  P16278    ILE    51 ENGINEERED MUTATION            
SEQADV 3WF3 GLU D    0  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ALA D    1  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 GLU D    2  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ALA D    3  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 TYR D    4  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 VAL D    5  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 GLU D    6  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 PHE D    7  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS D    8  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS D    9  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS D   10  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS D   11  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS D   12  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 HIS D   13  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP D   14  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 TYR D   15  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 LYS D   16  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP D   17  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP D   18  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP D   19  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 ASP D   20  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 LYS D   21  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 THR D   22  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 SER D   23  UNP  P16278              EXPRESSION TAG                 
SEQADV 3WF3 THR D   51  UNP  P16278    ILE    51 ENGINEERED MUTATION            
SEQRES   1 A  678  GLU ALA GLU ALA TYR VAL GLU PHE HIS HIS HIS HIS HIS          
SEQRES   2 A  678  HIS ASP TYR LYS ASP ASP ASP ASP LYS THR SER LEU ARG          
SEQRES   3 A  678  ASN ALA THR GLN ARG MET PHE GLU ILE ASP TYR SER ARG          
SEQRES   4 A  678  ASP SER PHE LEU LYS ASP GLY GLN PRO PHE ARG TYR THR          
SEQRES   5 A  678  SER GLY SER ILE HIS TYR SER ARG VAL PRO ARG PHE TYR          
SEQRES   6 A  678  TRP LYS ASP ARG LEU LEU LYS MET LYS MET ALA GLY LEU          
SEQRES   7 A  678  ASN ALA ILE GLN THR TYR VAL PRO TRP ASN PHE HIS GLU          
SEQRES   8 A  678  PRO TRP PRO GLY GLN TYR GLN PHE SER GLU ASP HIS ASP          
SEQRES   9 A  678  VAL GLU TYR PHE LEU ARG LEU ALA HIS GLU LEU GLY LEU          
SEQRES  10 A  678  LEU VAL ILE LEU ARG PRO GLY PRO TYR ILE CYS ALA GLU          
SEQRES  11 A  678  TRP GLU MET GLY GLY LEU PRO ALA TRP LEU LEU GLU LYS          
SEQRES  12 A  678  GLU SER ILE LEU LEU ARG SER SER ASP PRO ASP TYR LEU          
SEQRES  13 A  678  ALA ALA VAL ASP LYS TRP LEU GLY VAL LEU LEU PRO LYS          
SEQRES  14 A  678  MET LYS PRO LEU LEU TYR GLN ASN GLY GLY PRO VAL ILE          
SEQRES  15 A  678  THR VAL GLN VAL GLU ASN GLU TYR GLY SER TYR PHE ALA          
SEQRES  16 A  678  CYS ASP PHE ASP TYR LEU ARG PHE LEU GLN LYS ARG PHE          
SEQRES  17 A  678  ARG HIS HIS LEU GLY ASP ASP VAL VAL LEU PHE THR THR          
SEQRES  18 A  678  ASP GLY ALA HIS LYS THR PHE LEU LYS CYS GLY ALA LEU          
SEQRES  19 A  678  GLN GLY LEU TYR THR THR VAL ASP PHE GLY THR GLY SER          
SEQRES  20 A  678  ASN ILE THR ASP ALA PHE LEU SER GLN ARG LYS CYS GLU          
SEQRES  21 A  678  PRO LYS GLY PRO LEU ILE ASN SER GLU PHE TYR THR GLY          
SEQRES  22 A  678  TRP LEU ASP HIS TRP GLY GLN PRO HIS SER THR ILE LYS          
SEQRES  23 A  678  THR GLU ALA VAL ALA SER SER LEU TYR ASP ILE LEU ALA          
SEQRES  24 A  678  ARG GLY ALA SER VAL ASN LEU TYR MET PHE ILE GLY GLY          
SEQRES  25 A  678  THR ASN PHE ALA TYR TRP ASN GLY ALA ASN SER PRO TYR          
SEQRES  26 A  678  ALA ALA GLN PRO THR SER TYR ASP TYR ASP ALA PRO LEU          
SEQRES  27 A  678  SER GLU ALA GLY ASP LEU THR GLU LYS TYR PHE ALA LEU          
SEQRES  28 A  678  ARG ASN ILE ILE GLN LYS PHE GLU LYS VAL PRO GLU GLY          
SEQRES  29 A  678  PRO ILE PRO PRO SER THR PRO LYS PHE ALA TYR GLY LYS          
SEQRES  30 A  678  VAL THR LEU GLU LYS LEU LYS THR VAL GLY ALA ALA LEU          
SEQRES  31 A  678  ASP ILE LEU CYS PRO SER GLY PRO ILE LYS SER LEU TYR          
SEQRES  32 A  678  PRO LEU THR PHE ILE GLN VAL LYS GLN HIS TYR GLY PHE          
SEQRES  33 A  678  VAL LEU TYR ARG THR THR LEU PRO GLN ASP CYS SER ASN          
SEQRES  34 A  678  PRO ALA PRO LEU SER SER PRO LEU ASN GLY VAL HIS ASP          
SEQRES  35 A  678  ARG ALA TYR VAL ALA VAL ASP GLY ILE PRO GLN GLY VAL          
SEQRES  36 A  678  LEU GLU ARG ASN ASN VAL ILE THR LEU ASN ILE THR GLY          
SEQRES  37 A  678  LYS ALA GLY ALA THR LEU ASP LEU LEU VAL GLU ASN MET          
SEQRES  38 A  678  GLY ARG VAL ASN TYR GLY ALA TYR ILE ASN ASP PHE LYS          
SEQRES  39 A  678  GLY LEU VAL SER ASN LEU THR LEU SER SER ASN ILE LEU          
SEQRES  40 A  678  THR ASP TRP THR ILE PHE PRO LEU ASP THR GLU ASP ALA          
SEQRES  41 A  678  VAL ARG SER HIS LEU GLY GLY TRP GLY HIS ARG ASP SER          
SEQRES  42 A  678  GLY HIS HIS ASP GLU ALA TRP ALA HIS ASN SER SER ASN          
SEQRES  43 A  678  TYR THR LEU PRO ALA PHE TYR MET GLY ASN PHE SER ILE          
SEQRES  44 A  678  PRO SER GLY ILE PRO ASP LEU PRO GLN ASP THR PHE ILE          
SEQRES  45 A  678  GLN PHE PRO GLY TRP THR LYS GLY GLN VAL TRP ILE ASN          
SEQRES  46 A  678  GLY PHE ASN LEU GLY ARG TYR TRP PRO ALA ARG GLY PRO          
SEQRES  47 A  678  GLN LEU THR LEU PHE VAL PRO GLN HIS ILE LEU MET THR          
SEQRES  48 A  678  SER ALA PRO ASN THR ILE THR VAL LEU GLU LEU GLU TRP          
SEQRES  49 A  678  ALA PRO CYS SER SER ASP ASP PRO GLU LEU CYS ALA VAL          
SEQRES  50 A  678  THR PHE VAL ASP ARG PRO VAL ILE GLY SER SER VAL THR          
SEQRES  51 A  678  TYR ASP HIS PRO SER LYS PRO VAL GLU LYS ARG LEU MET          
SEQRES  52 A  678  PRO PRO PRO PRO GLN LYS ASN LYS ASP SER TRP LEU ASP          
SEQRES  53 A  678  HIS VAL                                                      
SEQRES   1 B  678  GLU ALA GLU ALA TYR VAL GLU PHE HIS HIS HIS HIS HIS          
SEQRES   2 B  678  HIS ASP TYR LYS ASP ASP ASP ASP LYS THR SER LEU ARG          
SEQRES   3 B  678  ASN ALA THR GLN ARG MET PHE GLU ILE ASP TYR SER ARG          
SEQRES   4 B  678  ASP SER PHE LEU LYS ASP GLY GLN PRO PHE ARG TYR THR          
SEQRES   5 B  678  SER GLY SER ILE HIS TYR SER ARG VAL PRO ARG PHE TYR          
SEQRES   6 B  678  TRP LYS ASP ARG LEU LEU LYS MET LYS MET ALA GLY LEU          
SEQRES   7 B  678  ASN ALA ILE GLN THR TYR VAL PRO TRP ASN PHE HIS GLU          
SEQRES   8 B  678  PRO TRP PRO GLY GLN TYR GLN PHE SER GLU ASP HIS ASP          
SEQRES   9 B  678  VAL GLU TYR PHE LEU ARG LEU ALA HIS GLU LEU GLY LEU          
SEQRES  10 B  678  LEU VAL ILE LEU ARG PRO GLY PRO TYR ILE CYS ALA GLU          
SEQRES  11 B  678  TRP GLU MET GLY GLY LEU PRO ALA TRP LEU LEU GLU LYS          
SEQRES  12 B  678  GLU SER ILE LEU LEU ARG SER SER ASP PRO ASP TYR LEU          
SEQRES  13 B  678  ALA ALA VAL ASP LYS TRP LEU GLY VAL LEU LEU PRO LYS          
SEQRES  14 B  678  MET LYS PRO LEU LEU TYR GLN ASN GLY GLY PRO VAL ILE          
SEQRES  15 B  678  THR VAL GLN VAL GLU ASN GLU TYR GLY SER TYR PHE ALA          
SEQRES  16 B  678  CYS ASP PHE ASP TYR LEU ARG PHE LEU GLN LYS ARG PHE          
SEQRES  17 B  678  ARG HIS HIS LEU GLY ASP ASP VAL VAL LEU PHE THR THR          
SEQRES  18 B  678  ASP GLY ALA HIS LYS THR PHE LEU LYS CYS GLY ALA LEU          
SEQRES  19 B  678  GLN GLY LEU TYR THR THR VAL ASP PHE GLY THR GLY SER          
SEQRES  20 B  678  ASN ILE THR ASP ALA PHE LEU SER GLN ARG LYS CYS GLU          
SEQRES  21 B  678  PRO LYS GLY PRO LEU ILE ASN SER GLU PHE TYR THR GLY          
SEQRES  22 B  678  TRP LEU ASP HIS TRP GLY GLN PRO HIS SER THR ILE LYS          
SEQRES  23 B  678  THR GLU ALA VAL ALA SER SER LEU TYR ASP ILE LEU ALA          
SEQRES  24 B  678  ARG GLY ALA SER VAL ASN LEU TYR MET PHE ILE GLY GLY          
SEQRES  25 B  678  THR ASN PHE ALA TYR TRP ASN GLY ALA ASN SER PRO TYR          
SEQRES  26 B  678  ALA ALA GLN PRO THR SER TYR ASP TYR ASP ALA PRO LEU          
SEQRES  27 B  678  SER GLU ALA GLY ASP LEU THR GLU LYS TYR PHE ALA LEU          
SEQRES  28 B  678  ARG ASN ILE ILE GLN LYS PHE GLU LYS VAL PRO GLU GLY          
SEQRES  29 B  678  PRO ILE PRO PRO SER THR PRO LYS PHE ALA TYR GLY LYS          
SEQRES  30 B  678  VAL THR LEU GLU LYS LEU LYS THR VAL GLY ALA ALA LEU          
SEQRES  31 B  678  ASP ILE LEU CYS PRO SER GLY PRO ILE LYS SER LEU TYR          
SEQRES  32 B  678  PRO LEU THR PHE ILE GLN VAL LYS GLN HIS TYR GLY PHE          
SEQRES  33 B  678  VAL LEU TYR ARG THR THR LEU PRO GLN ASP CYS SER ASN          
SEQRES  34 B  678  PRO ALA PRO LEU SER SER PRO LEU ASN GLY VAL HIS ASP          
SEQRES  35 B  678  ARG ALA TYR VAL ALA VAL ASP GLY ILE PRO GLN GLY VAL          
SEQRES  36 B  678  LEU GLU ARG ASN ASN VAL ILE THR LEU ASN ILE THR GLY          
SEQRES  37 B  678  LYS ALA GLY ALA THR LEU ASP LEU LEU VAL GLU ASN MET          
SEQRES  38 B  678  GLY ARG VAL ASN TYR GLY ALA TYR ILE ASN ASP PHE LYS          
SEQRES  39 B  678  GLY LEU VAL SER ASN LEU THR LEU SER SER ASN ILE LEU          
SEQRES  40 B  678  THR ASP TRP THR ILE PHE PRO LEU ASP THR GLU ASP ALA          
SEQRES  41 B  678  VAL ARG SER HIS LEU GLY GLY TRP GLY HIS ARG ASP SER          
SEQRES  42 B  678  GLY HIS HIS ASP GLU ALA TRP ALA HIS ASN SER SER ASN          
SEQRES  43 B  678  TYR THR LEU PRO ALA PHE TYR MET GLY ASN PHE SER ILE          
SEQRES  44 B  678  PRO SER GLY ILE PRO ASP LEU PRO GLN ASP THR PHE ILE          
SEQRES  45 B  678  GLN PHE PRO GLY TRP THR LYS GLY GLN VAL TRP ILE ASN          
SEQRES  46 B  678  GLY PHE ASN LEU GLY ARG TYR TRP PRO ALA ARG GLY PRO          
SEQRES  47 B  678  GLN LEU THR LEU PHE VAL PRO GLN HIS ILE LEU MET THR          
SEQRES  48 B  678  SER ALA PRO ASN THR ILE THR VAL LEU GLU LEU GLU TRP          
SEQRES  49 B  678  ALA PRO CYS SER SER ASP ASP PRO GLU LEU CYS ALA VAL          
SEQRES  50 B  678  THR PHE VAL ASP ARG PRO VAL ILE GLY SER SER VAL THR          
SEQRES  51 B  678  TYR ASP HIS PRO SER LYS PRO VAL GLU LYS ARG LEU MET          
SEQRES  52 B  678  PRO PRO PRO PRO GLN LYS ASN LYS ASP SER TRP LEU ASP          
SEQRES  53 B  678  HIS VAL                                                      
SEQRES   1 C  678  GLU ALA GLU ALA TYR VAL GLU PHE HIS HIS HIS HIS HIS          
SEQRES   2 C  678  HIS ASP TYR LYS ASP ASP ASP ASP LYS THR SER LEU ARG          
SEQRES   3 C  678  ASN ALA THR GLN ARG MET PHE GLU ILE ASP TYR SER ARG          
SEQRES   4 C  678  ASP SER PHE LEU LYS ASP GLY GLN PRO PHE ARG TYR THR          
SEQRES   5 C  678  SER GLY SER ILE HIS TYR SER ARG VAL PRO ARG PHE TYR          
SEQRES   6 C  678  TRP LYS ASP ARG LEU LEU LYS MET LYS MET ALA GLY LEU          
SEQRES   7 C  678  ASN ALA ILE GLN THR TYR VAL PRO TRP ASN PHE HIS GLU          
SEQRES   8 C  678  PRO TRP PRO GLY GLN TYR GLN PHE SER GLU ASP HIS ASP          
SEQRES   9 C  678  VAL GLU TYR PHE LEU ARG LEU ALA HIS GLU LEU GLY LEU          
SEQRES  10 C  678  LEU VAL ILE LEU ARG PRO GLY PRO TYR ILE CYS ALA GLU          
SEQRES  11 C  678  TRP GLU MET GLY GLY LEU PRO ALA TRP LEU LEU GLU LYS          
SEQRES  12 C  678  GLU SER ILE LEU LEU ARG SER SER ASP PRO ASP TYR LEU          
SEQRES  13 C  678  ALA ALA VAL ASP LYS TRP LEU GLY VAL LEU LEU PRO LYS          
SEQRES  14 C  678  MET LYS PRO LEU LEU TYR GLN ASN GLY GLY PRO VAL ILE          
SEQRES  15 C  678  THR VAL GLN VAL GLU ASN GLU TYR GLY SER TYR PHE ALA          
SEQRES  16 C  678  CYS ASP PHE ASP TYR LEU ARG PHE LEU GLN LYS ARG PHE          
SEQRES  17 C  678  ARG HIS HIS LEU GLY ASP ASP VAL VAL LEU PHE THR THR          
SEQRES  18 C  678  ASP GLY ALA HIS LYS THR PHE LEU LYS CYS GLY ALA LEU          
SEQRES  19 C  678  GLN GLY LEU TYR THR THR VAL ASP PHE GLY THR GLY SER          
SEQRES  20 C  678  ASN ILE THR ASP ALA PHE LEU SER GLN ARG LYS CYS GLU          
SEQRES  21 C  678  PRO LYS GLY PRO LEU ILE ASN SER GLU PHE TYR THR GLY          
SEQRES  22 C  678  TRP LEU ASP HIS TRP GLY GLN PRO HIS SER THR ILE LYS          
SEQRES  23 C  678  THR GLU ALA VAL ALA SER SER LEU TYR ASP ILE LEU ALA          
SEQRES  24 C  678  ARG GLY ALA SER VAL ASN LEU TYR MET PHE ILE GLY GLY          
SEQRES  25 C  678  THR ASN PHE ALA TYR TRP ASN GLY ALA ASN SER PRO TYR          
SEQRES  26 C  678  ALA ALA GLN PRO THR SER TYR ASP TYR ASP ALA PRO LEU          
SEQRES  27 C  678  SER GLU ALA GLY ASP LEU THR GLU LYS TYR PHE ALA LEU          
SEQRES  28 C  678  ARG ASN ILE ILE GLN LYS PHE GLU LYS VAL PRO GLU GLY          
SEQRES  29 C  678  PRO ILE PRO PRO SER THR PRO LYS PHE ALA TYR GLY LYS          
SEQRES  30 C  678  VAL THR LEU GLU LYS LEU LYS THR VAL GLY ALA ALA LEU          
SEQRES  31 C  678  ASP ILE LEU CYS PRO SER GLY PRO ILE LYS SER LEU TYR          
SEQRES  32 C  678  PRO LEU THR PHE ILE GLN VAL LYS GLN HIS TYR GLY PHE          
SEQRES  33 C  678  VAL LEU TYR ARG THR THR LEU PRO GLN ASP CYS SER ASN          
SEQRES  34 C  678  PRO ALA PRO LEU SER SER PRO LEU ASN GLY VAL HIS ASP          
SEQRES  35 C  678  ARG ALA TYR VAL ALA VAL ASP GLY ILE PRO GLN GLY VAL          
SEQRES  36 C  678  LEU GLU ARG ASN ASN VAL ILE THR LEU ASN ILE THR GLY          
SEQRES  37 C  678  LYS ALA GLY ALA THR LEU ASP LEU LEU VAL GLU ASN MET          
SEQRES  38 C  678  GLY ARG VAL ASN TYR GLY ALA TYR ILE ASN ASP PHE LYS          
SEQRES  39 C  678  GLY LEU VAL SER ASN LEU THR LEU SER SER ASN ILE LEU          
SEQRES  40 C  678  THR ASP TRP THR ILE PHE PRO LEU ASP THR GLU ASP ALA          
SEQRES  41 C  678  VAL ARG SER HIS LEU GLY GLY TRP GLY HIS ARG ASP SER          
SEQRES  42 C  678  GLY HIS HIS ASP GLU ALA TRP ALA HIS ASN SER SER ASN          
SEQRES  43 C  678  TYR THR LEU PRO ALA PHE TYR MET GLY ASN PHE SER ILE          
SEQRES  44 C  678  PRO SER GLY ILE PRO ASP LEU PRO GLN ASP THR PHE ILE          
SEQRES  45 C  678  GLN PHE PRO GLY TRP THR LYS GLY GLN VAL TRP ILE ASN          
SEQRES  46 C  678  GLY PHE ASN LEU GLY ARG TYR TRP PRO ALA ARG GLY PRO          
SEQRES  47 C  678  GLN LEU THR LEU PHE VAL PRO GLN HIS ILE LEU MET THR          
SEQRES  48 C  678  SER ALA PRO ASN THR ILE THR VAL LEU GLU LEU GLU TRP          
SEQRES  49 C  678  ALA PRO CYS SER SER ASP ASP PRO GLU LEU CYS ALA VAL          
SEQRES  50 C  678  THR PHE VAL ASP ARG PRO VAL ILE GLY SER SER VAL THR          
SEQRES  51 C  678  TYR ASP HIS PRO SER LYS PRO VAL GLU LYS ARG LEU MET          
SEQRES  52 C  678  PRO PRO PRO PRO GLN LYS ASN LYS ASP SER TRP LEU ASP          
SEQRES  53 C  678  HIS VAL                                                      
SEQRES   1 D  678  GLU ALA GLU ALA TYR VAL GLU PHE HIS HIS HIS HIS HIS          
SEQRES   2 D  678  HIS ASP TYR LYS ASP ASP ASP ASP LYS THR SER LEU ARG          
SEQRES   3 D  678  ASN ALA THR GLN ARG MET PHE GLU ILE ASP TYR SER ARG          
SEQRES   4 D  678  ASP SER PHE LEU LYS ASP GLY GLN PRO PHE ARG TYR THR          
SEQRES   5 D  678  SER GLY SER ILE HIS TYR SER ARG VAL PRO ARG PHE TYR          
SEQRES   6 D  678  TRP LYS ASP ARG LEU LEU LYS MET LYS MET ALA GLY LEU          
SEQRES   7 D  678  ASN ALA ILE GLN THR TYR VAL PRO TRP ASN PHE HIS GLU          
SEQRES   8 D  678  PRO TRP PRO GLY GLN TYR GLN PHE SER GLU ASP HIS ASP          
SEQRES   9 D  678  VAL GLU TYR PHE LEU ARG LEU ALA HIS GLU LEU GLY LEU          
SEQRES  10 D  678  LEU VAL ILE LEU ARG PRO GLY PRO TYR ILE CYS ALA GLU          
SEQRES  11 D  678  TRP GLU MET GLY GLY LEU PRO ALA TRP LEU LEU GLU LYS          
SEQRES  12 D  678  GLU SER ILE LEU LEU ARG SER SER ASP PRO ASP TYR LEU          
SEQRES  13 D  678  ALA ALA VAL ASP LYS TRP LEU GLY VAL LEU LEU PRO LYS          
SEQRES  14 D  678  MET LYS PRO LEU LEU TYR GLN ASN GLY GLY PRO VAL ILE          
SEQRES  15 D  678  THR VAL GLN VAL GLU ASN GLU TYR GLY SER TYR PHE ALA          
SEQRES  16 D  678  CYS ASP PHE ASP TYR LEU ARG PHE LEU GLN LYS ARG PHE          
SEQRES  17 D  678  ARG HIS HIS LEU GLY ASP ASP VAL VAL LEU PHE THR THR          
SEQRES  18 D  678  ASP GLY ALA HIS LYS THR PHE LEU LYS CYS GLY ALA LEU          
SEQRES  19 D  678  GLN GLY LEU TYR THR THR VAL ASP PHE GLY THR GLY SER          
SEQRES  20 D  678  ASN ILE THR ASP ALA PHE LEU SER GLN ARG LYS CYS GLU          
SEQRES  21 D  678  PRO LYS GLY PRO LEU ILE ASN SER GLU PHE TYR THR GLY          
SEQRES  22 D  678  TRP LEU ASP HIS TRP GLY GLN PRO HIS SER THR ILE LYS          
SEQRES  23 D  678  THR GLU ALA VAL ALA SER SER LEU TYR ASP ILE LEU ALA          
SEQRES  24 D  678  ARG GLY ALA SER VAL ASN LEU TYR MET PHE ILE GLY GLY          
SEQRES  25 D  678  THR ASN PHE ALA TYR TRP ASN GLY ALA ASN SER PRO TYR          
SEQRES  26 D  678  ALA ALA GLN PRO THR SER TYR ASP TYR ASP ALA PRO LEU          
SEQRES  27 D  678  SER GLU ALA GLY ASP LEU THR GLU LYS TYR PHE ALA LEU          
SEQRES  28 D  678  ARG ASN ILE ILE GLN LYS PHE GLU LYS VAL PRO GLU GLY          
SEQRES  29 D  678  PRO ILE PRO PRO SER THR PRO LYS PHE ALA TYR GLY LYS          
SEQRES  30 D  678  VAL THR LEU GLU LYS LEU LYS THR VAL GLY ALA ALA LEU          
SEQRES  31 D  678  ASP ILE LEU CYS PRO SER GLY PRO ILE LYS SER LEU TYR          
SEQRES  32 D  678  PRO LEU THR PHE ILE GLN VAL LYS GLN HIS TYR GLY PHE          
SEQRES  33 D  678  VAL LEU TYR ARG THR THR LEU PRO GLN ASP CYS SER ASN          
SEQRES  34 D  678  PRO ALA PRO LEU SER SER PRO LEU ASN GLY VAL HIS ASP          
SEQRES  35 D  678  ARG ALA TYR VAL ALA VAL ASP GLY ILE PRO GLN GLY VAL          
SEQRES  36 D  678  LEU GLU ARG ASN ASN VAL ILE THR LEU ASN ILE THR GLY          
SEQRES  37 D  678  LYS ALA GLY ALA THR LEU ASP LEU LEU VAL GLU ASN MET          
SEQRES  38 D  678  GLY ARG VAL ASN TYR GLY ALA TYR ILE ASN ASP PHE LYS          
SEQRES  39 D  678  GLY LEU VAL SER ASN LEU THR LEU SER SER ASN ILE LEU          
SEQRES  40 D  678  THR ASP TRP THR ILE PHE PRO LEU ASP THR GLU ASP ALA          
SEQRES  41 D  678  VAL ARG SER HIS LEU GLY GLY TRP GLY HIS ARG ASP SER          
SEQRES  42 D  678  GLY HIS HIS ASP GLU ALA TRP ALA HIS ASN SER SER ASN          
SEQRES  43 D  678  TYR THR LEU PRO ALA PHE TYR MET GLY ASN PHE SER ILE          
SEQRES  44 D  678  PRO SER GLY ILE PRO ASP LEU PRO GLN ASP THR PHE ILE          
SEQRES  45 D  678  GLN PHE PRO GLY TRP THR LYS GLY GLN VAL TRP ILE ASN          
SEQRES  46 D  678  GLY PHE ASN LEU GLY ARG TYR TRP PRO ALA ARG GLY PRO          
SEQRES  47 D  678  GLN LEU THR LEU PHE VAL PRO GLN HIS ILE LEU MET THR          
SEQRES  48 D  678  SER ALA PRO ASN THR ILE THR VAL LEU GLU LEU GLU TRP          
SEQRES  49 D  678  ALA PRO CYS SER SER ASP ASP PRO GLU LEU CYS ALA VAL          
SEQRES  50 D  678  THR PHE VAL ASP ARG PRO VAL ILE GLY SER SER VAL THR          
SEQRES  51 D  678  TYR ASP HIS PRO SER LYS PRO VAL GLU LYS ARG LEU MET          
SEQRES  52 D  678  PRO PRO PRO PRO GLN LYS ASN LYS ASP SER TRP LEU ASP          
SEQRES  53 D  678  HIS VAL                                                      
MODRES 3WF3 ASN A  464  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN B  498  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN A  247  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN A  498  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN B  247  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN D  247  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN C  498  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN C  464  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN C  247  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN B  464  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN C  555  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN D  498  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN A  555  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN D  464  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN B  555  ASN  GLYCOSYLATION SITE                                 
MODRES 3WF3 ASN D  555  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 701      14                                                       
HET    NAG  A 702      14                                                       
HET    NAG  A 703      14                                                       
HET    NAG  A 704      14                                                       
HET    GAL  A 705      12                                                       
HET     CL  A 706       1                                                       
HET    SO4  A 707       5                                                       
HET    SO4  A 708       5                                                       
HET    EDO  A 709       4                                                       
HET    EDO  A 710       4                                                       
HET    NAG  B 701      14                                                       
HET    NAG  B 702      14                                                       
HET    NAG  B 703      14                                                       
HET    NAG  B 704      14                                                       
HET     CL  B 705       1                                                       
HET    SO4  B 706       5                                                       
HET    SO4  B 707       5                                                       
HET    EDO  B 708       4                                                       
HET    EDO  B 709       4                                                       
HET    GAL  B 710      12                                                       
HET    NAG  C 701      14                                                       
HET    NAG  C 702      14                                                       
HET    NAG  C 703      14                                                       
HET    NAG  C 704      14                                                       
HET     CL  C 705       1                                                       
HET    GAL  C 706      12                                                       
HET    SO4  C 707       5                                                       
HET    SO4  C 708       5                                                       
HET    EDO  C 709       4                                                       
HET    EDO  C 710       4                                                       
HET    NAG  D 701      14                                                       
HET    NAG  D 702      14                                                       
HET    NAG  D 703      14                                                       
HET    NAG  D 704      14                                                       
HET     CL  D 705       1                                                       
HET    GAL  D 706      12                                                       
HET    SO4  D 707       5                                                       
HET    SO4  D 708       5                                                       
HET    EDO  D 709       4                                                       
HET    EDO  D 710       4                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GAL BETA-D-GALACTOPYRANOSE                                           
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  NAG    16(C8 H15 N O6)                                              
FORMUL   9  GAL    4(C6 H12 O6)                                                 
FORMUL  10   CL    4(CL 1-)                                                     
FORMUL  11  SO4    8(O4 S 2-)                                                   
FORMUL  13  EDO    8(C2 H6 O2)                                                  
FORMUL  45  HOH   *1428(H2 O)                                                   
HELIX    1   1 TYR A   57  VAL A   60  5                                   4    
HELIX    2   2 PRO A   61  PHE A   63  5                                   3    
HELIX    3   3 TYR A   64  ALA A   75  1                                  12    
HELIX    4   4 PRO A   85  GLU A   90  1                                   6    
HELIX    5   5 SER A   99  HIS A  102  5                                   4    
HELIX    6   6 ASP A  103  LEU A  114  1                                  12    
HELIX    7   7 TRP A  130  LEU A  135  5                                   6    
HELIX    8   8 PRO A  136  LYS A  142  5                                   7    
HELIX    9   9 ASP A  151  LYS A  170  1                                  20    
HELIX   10  10 PRO A  171  GLY A  177  5                                   7    
HELIX   11  11 GLU A  188  TYR A  192  5                                   5    
HELIX   12  12 ASP A  196  GLY A  212  1                                  17    
HELIX   13  13 HIS A  224  ALA A  232  1                                   9    
HELIX   14  14 ASN A  247  GLU A  259  1                                  13    
HELIX   15  15 LYS A  285  ARG A  299  1                                  15    
HELIX   16  16 THR A  344  LYS A  356  1                                  13    
HELIX   17  17 ALA A  388  CYS A  393  1                                   6    
HELIX   18  18 PHE A  406  LYS A  410  5                                   5    
HELIX   19  19 ASP A  515  SER A  522  1                                   8    
HELIX   20  20 PRO A  604  LEU A  608  5                                   5    
HELIX   21  21 ASP A  630  LEU A  633  5                                   4    
HELIX   22  22 HIS B   56  VAL B   60  5                                   5    
HELIX   23  23 PRO B   61  PHE B   63  5                                   3    
HELIX   24  24 TYR B   64  ALA B   75  1                                  12    
HELIX   25  25 PRO B   85  GLU B   90  1                                   6    
HELIX   26  26 SER B   99  HIS B  102  5                                   4    
HELIX   27  27 ASP B  103  LEU B  114  1                                  12    
HELIX   28  28 TRP B  130  LEU B  135  5                                   6    
HELIX   29  29 PRO B  136  LYS B  142  5                                   7    
HELIX   30  30 ASP B  151  LYS B  170  1                                  20    
HELIX   31  31 PRO B  171  GLY B  177  5                                   7    
HELIX   32  32 GLU B  188  TYR B  192  5                                   5    
HELIX   33  33 ASP B  196  GLY B  212  1                                  17    
HELIX   34  34 HIS B  224  ALA B  232  1                                   9    
HELIX   35  35 ASN B  247  GLU B  259  1                                  13    
HELIX   36  36 LYS B  285  ARG B  299  1                                  15    
HELIX   37  37 THR B  344  LYS B  356  1                                  13    
HELIX   38  38 ALA B  388  CYS B  393  1                                   6    
HELIX   39  39 PHE B  406  LYS B  410  5                                   5    
HELIX   40  40 ASP B  515  SER B  522  1                                   8    
HELIX   41  41 HIS B  523  GLY B  526  5                                   4    
HELIX   42  42 PRO B  604  LEU B  608  5                                   5    
HELIX   43  43 ASP B  630  LEU B  633  5                                   4    
HELIX   44  44 TYR C   36  ASP C   39  5                                   4    
HELIX   45  45 HIS C   56  VAL C   60  5                                   5    
HELIX   46  46 PRO C   61  PHE C   63  5                                   3    
HELIX   47  47 TYR C   64  ALA C   75  1                                  12    
HELIX   48  48 PRO C   85  GLU C   90  1                                   6    
HELIX   49  49 SER C   99  HIS C  102  5                                   4    
HELIX   50  50 ASP C  103  LEU C  114  1                                  12    
HELIX   51  51 TRP C  130  LEU C  135  5                                   6    
HELIX   52  52 PRO C  136  LYS C  142  5                                   7    
HELIX   53  53 ASP C  151  LYS C  170  1                                  20    
HELIX   54  54 PRO C  171  GLY C  177  5                                   7    
HELIX   55  55 GLU C  188  TYR C  192  5                                   5    
HELIX   56  56 ASP C  196  GLY C  212  1                                  17    
HELIX   57  57 HIS C  224  ALA C  232  1                                   9    
HELIX   58  58 ASN C  247  GLU C  259  1                                  13    
HELIX   59  59 LYS C  285  ARG C  299  1                                  15    
HELIX   60  60 THR C  344  GLU C  358  1                                  15    
HELIX   61  61 ALA C  388  CYS C  393  1                                   6    
HELIX   62  62 ASP C  515  SER C  522  1                                   8    
HELIX   63  63 PRO C  604  LEU C  608  5                                   5    
HELIX   64  64 ASP C  630  LEU C  633  5                                   4    
HELIX   65  65 TYR D   36  ASP D   39  5                                   4    
HELIX   66  66 HIS D   56  VAL D   60  5                                   5    
HELIX   67  67 PRO D   61  PHE D   63  5                                   3    
HELIX   68  68 TYR D   64  ALA D   75  1                                  12    
HELIX   69  69 PRO D   85  GLU D   90  1                                   6    
HELIX   70  70 SER D   99  HIS D  102  5                                   4    
HELIX   71  71 ASP D  103  LEU D  114  1                                  12    
HELIX   72  72 TRP D  130  LEU D  135  5                                   6    
HELIX   73  73 PRO D  136  LYS D  142  5                                   7    
HELIX   74  74 ASP D  151  LYS D  170  1                                  20    
HELIX   75  75 PRO D  171  GLY D  177  5                                   7    
HELIX   76  76 GLU D  188  TYR D  192  5                                   5    
HELIX   77  77 ASP D  196  GLY D  212  1                                  17    
HELIX   78  78 HIS D  224  ALA D  232  1                                   9    
HELIX   79  79 ASN D  247  GLU D  259  1                                  13    
HELIX   80  80 LYS D  285  ARG D  299  1                                  15    
HELIX   81  81 THR D  344  GLN D  355  1                                  12    
HELIX   82  82 ALA D  388  CYS D  393  1                                   6    
HELIX   83  83 ASP D  515  SER D  522  1                                   8    
HELIX   84  84 PRO D  604  LEU D  608  5                                   5    
HELIX   85  85 ASP D  630  LEU D  633  5                                   4    
SHEET    1   A 3 PHE A  32  ASP A  35  0                                        
SHEET    2   A 3 SER A  40  LYS A  43 -1  O  SER A  40   N  ASP A  35           
SHEET    3   A 3 GLN A  46  PHE A  48 -1  O  GLN A  46   N  LYS A  43           
SHEET    1   B 9 THR A  51  ILE A  55  0                                        
SHEET    2   B 9 ALA A  79  TYR A  83  1  O  GLN A  81   N  ILE A  55           
SHEET    3   B 9 LEU A 117  ARG A 121  1  O  ILE A 119   N  ILE A  80           
SHEET    4   B 9 VAL A 180  GLN A 184  1  O  GLN A 184   N  LEU A 120           
SHEET    5   B 9 VAL A 216  GLY A 222  1  O  VAL A 216   N  VAL A 183           
SHEET    6   B 9 TYR A 237  ASP A 241  1  O  TYR A 237   N  THR A 219           
SHEET    7   B 9 ILE A 265  TYR A 270  1  O  SER A 267   N  VAL A 240           
SHEET    8   B 9 SER A 302  ILE A 309  1  O  ASN A 304   N  PHE A 269           
SHEET    9   B 9 THR A  51  ILE A  55  1  N  SER A  52   O  VAL A 303           
SHEET    1   C 2 ALA A 320  ASN A 321  0                                        
SHEET    2   C 2 ALA A 325  ALA A 326 -1  O  ALA A 325   N  ASN A 321           
SHEET    1   D 4 GLY A 375  THR A 378  0                                        
SHEET    2   D 4 ALA A 635  VAL A 639 -1  O  PHE A 638   N  GLY A 375           
SHEET    3   D 4 THR A 569  GLN A 572 -1  N  PHE A 570   O  VAL A 639           
SHEET    4   D 4 LEU A 601  VAL A 603 -1  O  VAL A 603   N  THR A 569           
SHEET    1   E 5 GLU A 380  THR A 384  0                                        
SHEET    2   E 5 ALA A 550  PHE A 556 -1  O  MET A 553   N  GLU A 380           
SHEET    3   E 5 ASN A 614  GLU A 620 -1  O  ILE A 616   N  GLY A 554           
SHEET    4   E 5 GLY A 579  ILE A 583 -1  N  GLN A 580   O  LEU A 619           
SHEET    5   E 5 PHE A 586  TYR A 591 -1  O  PHE A 586   N  ILE A 583           
SHEET    1   F 6 ILE A 398  SER A 400  0                                        
SHEET    2   F 6 TRP A 509  PRO A 513 -1  O  TRP A 509   N  SER A 400           
SHEET    3   F 6 PHE A 415  THR A 421 -1  N  ARG A 419   O  THR A 510           
SHEET    4   F 6 THR A 472  GLU A 478 -1  O  LEU A 475   N  TYR A 418           
SHEET    5   F 6 ARG A 442  VAL A 447 -1  N  ALA A 446   O  ASP A 474           
SHEET    6   F 6 ILE A 450  GLU A 456 -1  O  GLN A 452   N  VAL A 445           
SHEET    1   G 4 THR A 462  GLY A 467  0                                        
SHEET    2   G 4 CYS A 426  SER A 433 -1  N  ALA A 430   O  ILE A 465           
SHEET    3   G 4 THR A 500  LEU A 501 -1  O  THR A 500   N  SER A 433           
SHEET    4   G 4 ASN A 504  ILE A 505 -1  O  ASN A 504   N  LEU A 501           
SHEET    1   H 2 VAL A 439  HIS A 440  0                                        
SHEET    2   H 2 GLY A 494  LEU A 495 -1  O  GLY A 494   N  HIS A 440           
SHEET    1   I 3 PHE B  32  ASP B  35  0                                        
SHEET    2   I 3 SER B  40  LYS B  43 -1  O  LEU B  42   N  GLU B  33           
SHEET    3   I 3 GLN B  46  PHE B  48 -1  O  GLN B  46   N  LYS B  43           
SHEET    1   J 9 THR B  51  SER B  54  0                                        
SHEET    2   J 9 ALA B  79  TYR B  83  1  O  GLN B  81   N  GLY B  53           
SHEET    3   J 9 LEU B 117  ARG B 121  1  O  ILE B 119   N  ILE B  80           
SHEET    4   J 9 VAL B 180  GLN B 184  1  O  THR B 182   N  LEU B 120           
SHEET    5   J 9 VAL B 216  GLY B 222  1  O  VAL B 216   N  VAL B 183           
SHEET    6   J 9 TYR B 237  ASP B 241  1  O  TYR B 237   N  LEU B 217           
SHEET    7   J 9 ILE B 265  TYR B 270  1  O  SER B 267   N  VAL B 240           
SHEET    8   J 9 SER B 302  TYR B 306  1  O  ASN B 304   N  PHE B 269           
SHEET    9   J 9 THR B  51  SER B  54  1  N  SER B  52   O  VAL B 303           
SHEET    1   K 2 ALA B 320  ASN B 321  0                                        
SHEET    2   K 2 ALA B 325  ALA B 326 -1  O  ALA B 325   N  ASN B 321           
SHEET    1   L 4 GLY B 375  THR B 378  0                                        
SHEET    2   L 4 ALA B 635  VAL B 639 -1  O  VAL B 636   N  VAL B 377           
SHEET    3   L 4 THR B 569  GLN B 572 -1  N  GLN B 572   O  THR B 637           
SHEET    4   L 4 LEU B 601  VAL B 603 -1  O  LEU B 601   N  ILE B 571           
SHEET    1   M 5 GLU B 380  THR B 384  0                                        
SHEET    2   M 5 ALA B 550  PHE B 556 -1  O  MET B 553   N  GLU B 380           
SHEET    3   M 5 ASN B 614  GLU B 620 -1  O  ILE B 616   N  GLY B 554           
SHEET    4   M 5 GLY B 579  ILE B 583 -1  N  TRP B 582   O  THR B 617           
SHEET    5   M 5 PHE B 586  TYR B 591 -1  O  PHE B 586   N  ILE B 583           
SHEET    1   N 6 ILE B 398  SER B 400  0                                        
SHEET    2   N 6 TRP B 509  PRO B 513 -1  O  TRP B 509   N  SER B 400           
SHEET    3   N 6 PHE B 415  THR B 421 -1  N  ARG B 419   O  THR B 510           
SHEET    4   N 6 THR B 472  GLU B 478 -1  O  LEU B 475   N  TYR B 418           
SHEET    5   N 6 ARG B 442  VAL B 447 -1  N  ALA B 446   O  ASP B 474           
SHEET    6   N 6 ILE B 450  GLU B 456 -1  O  GLN B 452   N  VAL B 445           
SHEET    1   O 4 THR B 462  GLY B 467  0                                        
SHEET    2   O 4 CYS B 426  SER B 433 -1  N  LEU B 432   O  LEU B 463           
SHEET    3   O 4 THR B 500  LEU B 501 -1  O  THR B 500   N  SER B 433           
SHEET    4   O 4 ASN B 504  ILE B 505 -1  O  ASN B 504   N  LEU B 501           
SHEET    1   P 2 VAL B 439  HIS B 440  0                                        
SHEET    2   P 2 GLY B 494  LEU B 495 -1  O  GLY B 494   N  HIS B 440           
SHEET    1   Q 3 PHE C  32  ASP C  35  0                                        
SHEET    2   Q 3 SER C  40  LYS C  43 -1  O  SER C  40   N  ASP C  35           
SHEET    3   Q 3 GLN C  46  PHE C  48 -1  O  GLN C  46   N  LYS C  43           
SHEET    1   R 9 THR C  51  SER C  54  0                                        
SHEET    2   R 9 ALA C  79  TYR C  83  1  O  GLN C  81   N  GLY C  53           
SHEET    3   R 9 LEU C 117  ARG C 121  1  O  LEU C 117   N  ILE C  80           
SHEET    4   R 9 VAL C 180  GLN C 184  1  O  ILE C 181   N  VAL C 118           
SHEET    5   R 9 VAL C 216  GLY C 222  1  O  VAL C 216   N  VAL C 183           
SHEET    6   R 9 TYR C 237  ASP C 241  1  O  TYR C 237   N  THR C 219           
SHEET    7   R 9 ILE C 265  TYR C 270  1  O  SER C 267   N  VAL C 240           
SHEET    8   R 9 SER C 302  TYR C 306  1  O  ASN C 304   N  PHE C 269           
SHEET    9   R 9 THR C  51  SER C  54  1  N  SER C  54   O  LEU C 305           
SHEET    1   S 2 ALA C 320  ASN C 321  0                                        
SHEET    2   S 2 ALA C 325  ALA C 326 -1  O  ALA C 325   N  ASN C 321           
SHEET    1   T 4 GLY C 375  THR C 378  0                                        
SHEET    2   T 4 ALA C 635  VAL C 639 -1  O  VAL C 636   N  VAL C 377           
SHEET    3   T 4 THR C 569  GLN C 572 -1  N  PHE C 570   O  VAL C 639           
SHEET    4   T 4 LEU C 601  VAL C 603 -1  O  VAL C 603   N  THR C 569           
SHEET    1   U 5 GLU C 380  THR C 384  0                                        
SHEET    2   U 5 ALA C 550  PHE C 556 -1  O  PHE C 551   N  LEU C 382           
SHEET    3   U 5 ASN C 614  GLU C 620 -1  O  ASN C 614   N  PHE C 556           
SHEET    4   U 5 GLY C 579  ILE C 583 -1  N  TRP C 582   O  THR C 617           
SHEET    5   U 5 PHE C 586  TYR C 591 -1  O  TYR C 591   N  GLY C 579           
SHEET    1   V 6 ILE C 398  SER C 400  0                                        
SHEET    2   V 6 TRP C 509  PRO C 513 -1  O  TRP C 509   N  SER C 400           
SHEET    3   V 6 GLY C 414  THR C 421 -1  N  ARG C 419   O  THR C 510           
SHEET    4   V 6 THR C 472  ASN C 479 -1  O  ASN C 479   N  GLY C 414           
SHEET    5   V 6 ARG C 442  VAL C 447 -1  N  ALA C 446   O  ASP C 474           
SHEET    6   V 6 ILE C 450  GLU C 456 -1  O  ILE C 450   N  VAL C 447           
SHEET    1   W 4 THR C 462  GLY C 467  0                                        
SHEET    2   W 4 CYS C 426  SER C 433 -1  N  LEU C 432   O  LEU C 463           
SHEET    3   W 4 THR C 500  LEU C 501 -1  O  THR C 500   N  SER C 433           
SHEET    4   W 4 ASN C 504  ILE C 505 -1  O  ASN C 504   N  LEU C 501           
SHEET    1   X 2 VAL C 439  HIS C 440  0                                        
SHEET    2   X 2 GLY C 494  LEU C 495 -1  O  GLY C 494   N  HIS C 440           
SHEET    1   Y 3 PHE D  32  ASP D  35  0                                        
SHEET    2   Y 3 SER D  40  LYS D  43 -1  O  SER D  40   N  ASP D  35           
SHEET    3   Y 3 GLN D  46  PHE D  48 -1  O  GLN D  46   N  LYS D  43           
SHEET    1   Z 9 THR D  51  SER D  54  0                                        
SHEET    2   Z 9 ALA D  79  TYR D  83  1  O  GLN D  81   N  GLY D  53           
SHEET    3   Z 9 LEU D 117  ARG D 121  1  O  ILE D 119   N  ILE D  80           
SHEET    4   Z 9 VAL D 180  GLN D 184  1  O  ILE D 181   N  VAL D 118           
SHEET    5   Z 9 VAL D 216  GLY D 222  1  O  PHE D 218   N  VAL D 183           
SHEET    6   Z 9 TYR D 237  ASP D 241  1  O  TYR D 237   N  THR D 219           
SHEET    7   Z 9 ILE D 265  TYR D 270  1  O  SER D 267   N  VAL D 240           
SHEET    8   Z 9 SER D 302  TYR D 306  1  O  ASN D 304   N  PHE D 269           
SHEET    9   Z 9 THR D  51  SER D  54  1  N  SER D  52   O  VAL D 303           
SHEET    1  AA 2 ALA D 320  ASN D 321  0                                        
SHEET    2  AA 2 ALA D 325  ALA D 326 -1  O  ALA D 325   N  ASN D 321           
SHEET    1  AB 4 GLY D 375  THR D 378  0                                        
SHEET    2  AB 4 ALA D 635  VAL D 639 -1  O  PHE D 638   N  GLY D 375           
SHEET    3  AB 4 THR D 569  GLN D 572 -1  N  GLN D 572   O  THR D 637           
SHEET    4  AB 4 LEU D 601  VAL D 603 -1  O  LEU D 601   N  ILE D 571           
SHEET    1  AC 5 GLU D 380  THR D 384  0                                        
SHEET    2  AC 5 ALA D 550  PHE D 556 -1  O  PHE D 551   N  LEU D 382           
SHEET    3  AC 5 ASN D 614  GLU D 620 -1  O  VAL D 618   N  TYR D 552           
SHEET    4  AC 5 GLY D 579  ILE D 583 -1  N  TRP D 582   O  THR D 617           
SHEET    5  AC 5 PHE D 586  TYR D 591 -1  O  TYR D 591   N  GLY D 579           
SHEET    1  AD 6 ILE D 398  SER D 400  0                                        
SHEET    2  AD 6 TRP D 509  PRO D 513 -1  O  TRP D 509   N  SER D 400           
SHEET    3  AD 6 GLY D 414  THR D 421 -1  N  LEU D 417   O  PHE D 512           
SHEET    4  AD 6 THR D 472  ASN D 479 -1  O  LEU D 473   N  THR D 420           
SHEET    5  AD 6 ARG D 442  VAL D 447 -1  N  ALA D 446   O  ASP D 474           
SHEET    6  AD 6 ILE D 450  GLU D 456 -1  O  GLN D 452   N  VAL D 445           
SHEET    1  AE 4 THR D 462  GLY D 467  0                                        
SHEET    2  AE 4 CYS D 426  SER D 433 -1  N  ALA D 430   O  ILE D 465           
SHEET    3  AE 4 THR D 500  LEU D 501 -1  O  THR D 500   N  SER D 433           
SHEET    4  AE 4 ASN D 504  ILE D 505 -1  O  ASN D 504   N  LEU D 501           
SHEET    1  AF 2 VAL D 439  HIS D 440  0                                        
SHEET    2  AF 2 GLY D 494  LEU D 495 -1  O  GLY D 494   N  HIS D 440           
SSBOND   1 CYS A  195    CYS A  230                          1555   1555  2.09  
SSBOND   2 CYS A  626    CYS A  634                          1555   1555  2.08  
SSBOND   3 CYS B  195    CYS B  230                          1555   1555  2.05  
SSBOND   4 CYS B  626    CYS B  634                          1555   1555  2.03  
SSBOND   5 CYS C  195    CYS C  230                          1555   1555  2.08  
SSBOND   6 CYS C  626    CYS C  634                          1555   1555  2.08  
SSBOND   7 CYS D  195    CYS D  230                          1555   1555  2.06  
SSBOND   8 CYS D  626    CYS D  634                          1555   1555  2.06  
LINK         ND2 ASN A 247                 C1  NAG A 704     1555   1555  1.43  
LINK         ND2 ASN A 464                 C1  NAG A 701     1555   1555  1.43  
LINK         ND2 ASN A 498                 C1  NAG A 702     1555   1555  1.45  
LINK         ND2 ASN A 555                 C1  NAG A 703     1555   1555  1.47  
LINK         ND2 ASN B 247                 C1  NAG B 704     1555   1555  1.45  
LINK         ND2 ASN B 464                 C1  NAG B 701     1555   1555  1.46  
LINK         ND2 ASN B 498                 C1  NAG B 702     1555   1555  1.43  
LINK         ND2 ASN B 555                 C1  NAG B 703     1555   1555  1.47  
LINK         ND2 ASN C 247                 C1  NAG C 704     1555   1555  1.46  
LINK         ND2 ASN C 464                 C1  NAG C 701     1555   1555  1.46  
LINK         ND2 ASN C 498                 C1  NAG C 702     1555   1555  1.45  
LINK         ND2 ASN C 555                 C1  NAG C 703     1555   1555  1.46  
LINK         ND2 ASN D 247                 C1  NAG D 704     1555   1555  1.45  
LINK         ND2 ASN D 464                 C1  NAG D 701     1555   1555  1.47  
LINK         ND2 ASN D 498                 C1  NAG D 702     1555   1555  1.46  
LINK         ND2 ASN D 555                 C1  NAG D 703     1555   1555  1.55  
CISPEP   1 GLY A  123    PRO A  124          0        20.16                     
CISPEP   2 TYR A  306    MET A  307          0       -11.35                     
CISPEP   3 SER A  322    PRO A  323          0         3.25                     
CISPEP   4 HIS A  440    ASP A  441          0        18.55                     
CISPEP   5 LEU A  565    PRO A  566          0         3.50                     
CISPEP   6 GLY A  596    PRO A  597          0         6.95                     
CISPEP   7 GLY B  123    PRO B  124          0        10.88                     
CISPEP   8 TYR B  306    MET B  307          0        -8.21                     
CISPEP   9 SER B  322    PRO B  323          0         4.85                     
CISPEP  10 HIS B  440    ASP B  441          0        16.72                     
CISPEP  11 LEU B  565    PRO B  566          0         4.10                     
CISPEP  12 GLY B  596    PRO B  597          0         2.11                     
CISPEP  13 GLY C  123    PRO C  124          0        10.58                     
CISPEP  14 TYR C  306    MET C  307          0       -11.38                     
CISPEP  15 SER C  322    PRO C  323          0        -2.42                     
CISPEP  16 HIS C  440    ASP C  441          0        12.40                     
CISPEP  17 LEU C  565    PRO C  566          0         3.44                     
CISPEP  18 GLY C  596    PRO C  597          0         7.26                     
CISPEP  19 GLY D  123    PRO D  124          0        14.50                     
CISPEP  20 TYR D  306    MET D  307          0       -15.47                     
CISPEP  21 SER D  322    PRO D  323          0         3.29                     
CISPEP  22 HIS D  440    ASP D  441          0        20.42                     
CISPEP  23 LEU D  565    PRO D  566          0         0.86                     
CISPEP  24 GLY D  596    PRO D  597          0        -1.10                     
CRYST1   94.960  115.888  140.284  90.00  92.23  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010531  0.000000  0.000410        0.00000                         
SCALE2      0.000000  0.008629  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007134        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system