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Database: PDB
Entry: 3PZ8
LinkDB: 3PZ8
Original site: 3PZ8 
HEADER    SIGNALING PROTEIN                       14-DEC-10   3PZ8              
TITLE     CRYSTAL STRUCTURE OF DVL1-DIX(Y17D) MUTANT                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-1;        
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: DIX DOMAIN;                                                
COMPND   5 SYNONYM: DISHEVELLED-1, DSH HOMOLOG 1;                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: DVL1, DVL;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    DIX DOMAIN, OLIGOMERIZATION, SIGNALING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.J.DAN,L.CHEN,Y.Y.ZHANG,Y.T.LIU,J.W.WU                               
REVDAT   2   02-FEB-11 3PZ8    1       TITLE                                    
REVDAT   1   29-DEC-10 3PZ8    0                                                
JRNL        AUTH   Y.T.LIU,Q.J.DAN,J.W.WANG,Y.G.FENG,L.CHEN,J.LIANG,Q.X.LI,     
JRNL        AUTH 2 S.C.LIN,Z.X.WANG,J.W.WU                                      
JRNL        TITL   MOLECULAR BASIS OF WNT ACTIVATION VIA THE DIX-DOMAIN PROTEIN 
JRNL        TITL 2 CCD1                                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30175                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1521                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.0188 -  6.3828    0.98     2771   134  0.2067 0.2204        
REMARK   3     2  6.3828 -  5.0692    1.00     2649   150  0.2037 0.2384        
REMARK   3     3  5.0692 -  4.4293    1.00     2629   150  0.1695 0.2091        
REMARK   3     4  4.4293 -  4.0247    1.00     2638   141  0.2048 0.2492        
REMARK   3     5  4.0247 -  3.7364    1.00     2636   132  0.2452 0.2849        
REMARK   3     6  3.7364 -  3.5163    1.00     2614   154  0.2549 0.3390        
REMARK   3     7  3.5163 -  3.3403    1.00     2598   133  0.2608 0.2992        
REMARK   3     8  3.3403 -  3.1949    1.00     2589   159  0.2739 0.2891        
REMARK   3     9  3.1949 -  3.0720    1.00     2609   128  0.2818 0.3312        
REMARK   3    10  3.0720 -  2.9660    1.00     2604   131  0.3211 0.3193        
REMARK   3    11  2.9660 -  2.8733    0.88     2317   109  0.3523 0.4329        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 72.92                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.590           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 85.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.06720                                              
REMARK   3    B22 (A**2) : -1.26950                                             
REMARK   3    B33 (A**2) : -0.79770                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           5503                                  
REMARK   3   ANGLE     :  1.193           7450                                  
REMARK   3   CHIRALITY :  0.078            826                                  
REMARK   3   PLANARITY :  0.004            954                                  
REMARK   3   DIHEDRAL  : 20.985           2008                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3PZ8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062994.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30176                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.873                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.015                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3PZ7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 10% ETHYLENE GLYCOL, 0.66M   
REMARK 280  SODIUM CITRATE, 0.3M SODIUM CHLORIDE, PH 7.2, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 298.0K                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
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       46.34350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      132.97850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.39000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      132.97850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.34350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.39000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       46.34350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.39000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      132.97850            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.39000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.34350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      132.97850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8                                  
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
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: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
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     GLY A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     GLU A    85                                                      
REMARK 465     GLY A    86                                                      
REMARK 465     ALA A    87                                                      
REMARK 465     HIS A    88                                                      
REMARK 465     SER A    89                                                      
REMARK 465     ASP A    90                                                      
REMARK 465     ALA A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     GLN A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     THR A    96                                                      
REMARK 465     ASP A    97                                                      
REMARK 465     SER A    98                                                      
REMARK 465     HIS A    99                                                      
REMARK 465     THR A   100                                                      
REMARK 465     ASP A   101                                                      
REMARK 465     LEU A   102                                                      
REMARK 465     PRO A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     GLY B    86                                                      
REMARK 465     ALA B    87                                                      
REMARK 465     HIS B    88                                                      
REMARK 465     SER B    89                                                      
REMARK 465     ASP B    90                                                      
REMARK 465     ALA B    91                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     SER B    93                                                      
REMARK 465     GLN B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 465     THR B    96                                                      
REMARK 465     ASP B    97                                                      
REMARK 465     SER B    98                                                      
REMARK 465     HIS B    99                                                      
REMARK 465     THR B   100                                                      
REMARK 465     ASP B   101                                                      
REMARK 465     LEU B   102                                                      
REMARK 465     PRO B   103                                                      
REMARK 465     PRO B   104                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     PRO C     0                                                      
REMARK 465     HIS C     1                                                      
REMARK 465     MET C     2                                                      
REMARK 465     GLU C    12                                                      
REMARK 465     GLU C    85                                                      
REMARK 465     GLY C    86                                                      
REMARK 465     ALA C    87                                                      
REMARK 465     HIS C    88                                                      
REMARK 465     SER C    89                                                      
REMARK 465     ASP C    90                                                      
REMARK 465     ALA C    91                                                      
REMARK 465     GLY C    92                                                      
REMARK 465     SER C    93                                                      
REMARK 465     GLN C    94                                                      
REMARK 465     GLY C    95                                                      
REMARK 465     THR C    96                                                      
REMARK 465     ASP C    97                                                      
REMARK 465     SER C    98                                                      
REMARK 465     HIS C    99                                                      
REMARK 465     THR C   100                                                      
REMARK 465     ASP C   101                                                      
REMARK 465     LEU C   102                                                      
REMARK 465     PRO C   103                                                      
REMARK 465     PRO C   104                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     PRO D     0                                                      
REMARK 465     HIS D     1                                                      
REMARK 465     GLU D    85                                                      
REMARK 465     GLY D    86                                                      
REMARK 465     ALA D    87                                                      
REMARK 465     HIS D    88                                                      
REMARK 465     SER D    89                                                      
REMARK 465     ASP D    90                                                      
REMARK 465     ALA D    91                                                      
REMARK 465     GLY D    92                                                      
REMARK 465     SER D    93                                                      
REMARK 465     GLN D    94                                                      
REMARK 465     GLY D    95                                                      
REMARK 465     THR D    96                                                      
REMARK 465     ASP D    97                                                      
REMARK 465     SER D    98                                                      
REMARK 465     HIS D    99                                                      
REMARK 465     THR D   100                                                      
REMARK 465     ASP D   101                                                      
REMARK 465     LEU D   102                                                      
REMARK 465     PRO D   103                                                      
REMARK 465     PRO D   104                                                      
REMARK 465     GLY E    -1                                                      
REMARK 465     PRO E     0                                                      
REMARK 465     HIS E     1                                                      
REMARK 465     GLU E    85                                                      
REMARK 465     GLY E    86                                                      
REMARK 465     ALA E    87                                                      
REMARK 465     HIS E    88                                                      
REMARK 465     SER E    89                                                      
REMARK 465     ASP E    90                                                      
REMARK 465     ALA E    91                                                      
REMARK 465     GLY E    92                                                      
REMARK 465     SER E    93                                                      
REMARK 465     GLN E    94                                                      
REMARK 465     GLY E    95                                                      
REMARK 465     THR E    96                                                      
REMARK 465     ASP E    97                                                      
REMARK 465     SER E    98                                                      
REMARK 465     HIS E    99                                                      
REMARK 465     THR E   100                                                      
REMARK 465     ASP E   101                                                      
REMARK 465     LEU E   102                                                      
REMARK 465     PRO E   103                                                      
REMARK 465     PRO E   104                                                      
REMARK 465     GLY F    -1                                                      
REMARK 465     GLU F    85                                                      
REMARK 465     GLY F    86                                                      
REMARK 465     ALA F    87                                                      
REMARK 465     HIS F    88                                                      
REMARK 465     SER F    89                                                      
REMARK 465     ASP F    90                                                      
REMARK 465     ALA F    91                                                      
REMARK 465     GLY F    92                                                      
REMARK 465     SER F    93                                                      
REMARK 465     GLN F    94                                                      
REMARK 465     GLY F    95                                                      
REMARK 465     THR F    96                                                      
REMARK 465     ASP F    97                                                      
REMARK 465     SER F    98                                                      
REMARK 465     HIS F    99                                                      
REMARK 465     THR F   100                                                      
REMARK 465     ASP F   101                                                      
REMARK 465     LEU F   102                                                      
REMARK 465     PRO F   103                                                      
REMARK 465     PRO F   104                                                      
REMARK 465     GLY G    -1                                                      
REMARK 465     PRO G     0                                                      
REMARK 465     HIS G     1                                                      
REMARK 465     MET G     2                                                      
REMARK 465     VAL G    42                                                      
REMARK 465     ALA G    84                                                      
REMARK 465     GLU G    85                                                      
REMARK 465     GLY G    86                                                      
REMARK 465     ALA G    87                                                      
REMARK 465     HIS G    88                                                      
REMARK 465     SER G    89                                                      
REMARK 465     ASP G    90                                                      
REMARK 465     ALA G    91                                                      
REMARK 465     GLY G    92                                                      
REMARK 465     SER G    93                                                      
REMARK 465     GLN G    94                                                      
REMARK 465     GLY G    95                                                      
REMARK 465     THR G    96                                                      
REMARK 465     ASP G    97                                                      
REMARK 465     SER G    98                                                      
REMARK 465     HIS G    99                                                      
REMARK 465     THR G   100                                                      
REMARK 465     ASP G   101                                                      
REMARK 465     LEU G   102                                                      
REMARK 465     PRO G   103                                                      
REMARK 465     PRO G   104                                                      
REMARK 465     GLY H    -1                                                      
REMARK 465     PRO H     0                                                      
REMARK 465     HIS H     1                                                      
REMARK 465     MET H     2                                                      
REMARK 465     GLU H    12                                                      
REMARK 465     GLU H    13                                                      
REMARK 465     ASP H    65                                                      
REMARK 465     ALA H    87                                                      
REMARK 465     HIS H    88                                                      
REMARK 465     SER H    89                                                      
REMARK 465     ASP H    90                                                      
REMARK 465     ALA H    91                                                      
REMARK 465     GLY H    92                                                      
REMARK 465     SER H    93                                                      
REMARK 465     GLN H    94                                                      
REMARK 465     GLY H    95                                                      
REMARK 465     THR H    96                                                      
REMARK 465     ASP H    97                                                      
REMARK 465     SER H    98                                                      
REMARK 465     HIS H    99                                                      
REMARK 465     THR H   100                                                      
REMARK 465     ASP H   101                                                      
REMARK 465     LEU H   102                                                      
REMARK 465     PRO H   103                                                      
REMARK 465     PRO H   104                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP C  11    CG   OD1  OD2                                       
REMARK 470     MET D   2    CG   SD   CE                                        
REMARK 470     ASP D  11    CG   OD1  OD2                                       
REMARK 470     GLU G  26    CG   CD   OE1  OE2                                  
REMARK 470     ASP H  66    CG   OD1  OD2                                       
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  12       50.03   -103.54                                   
REMARK 500    ARG A  27      -11.48     66.38                                   
REMARK 500    LEU A  37       51.43   -116.78                                   
REMARK 500    VAL A  42      -43.09    -28.21                                   
REMARK 500    PHE A  47       95.03     77.23                                   
REMARK 500    PRO B  22       38.04    -85.37                                   
REMARK 500    GLU B  26       -8.01    -56.91                                   
REMARK 500    LEU B  30      -36.26    -37.85                                   
REMARK 500    VAL B  42      -49.92    -28.78                                   
REMARK 500    ASP B  53       68.00   -159.00                                   
REMARK 500    PHE B  73       90.35    -60.08                                   
REMARK 500    ASN B  74       43.44     74.73                                   
REMARK 500    ARG C  27       -9.27     71.88                                   
REMARK 500    LEU C  37       51.10   -113.95                                   
REMARK 500    PRO C  41       64.80    -69.01                                   
REMARK 500    HIS C  43        0.75    -58.27                                   
REMARK 500    ASP C  65      106.79    -53.47                                   
REMARK 500    ASP C  66      -15.72    -47.38                                   
REMARK 500    ARG C  76      126.16   -172.84                                   
REMARK 500    VAL D  23      164.06    -29.06                                   
REMARK 500    ARG D  27      -31.25   -141.75                                   
REMARK 500    VAL D  36       -0.65    -58.88                                   
REMARK 500    LEU D  37       42.24   -102.99                                   
REMARK 500    ALA D  44       32.69    -82.41                                   
REMARK 500    ASP D  66       -2.38    -50.50                                   
REMARK 500    LEU D  83     -169.61   -113.44                                   
REMARK 500    PRO E  22       -8.46    -59.77                                   
REMARK 500    PRO E  25      -73.09    -43.92                                   
REMARK 500    ARG E  27       -0.89    107.51                                   
REMARK 500    LEU E  30      -49.67    -29.67                                   
REMARK 500    ASN E  67       -2.25     89.40                                   
REMARK 500    CYS E  72       85.36   -152.99                                   
REMARK 500    ASN E  74       63.78     38.66                                   
REMARK 500    LEU E  83      -77.24    -84.01                                   
REMARK 500    PRO F  22       37.95    -72.98                                   
REMARK 500    VAL F  36      -18.51    -46.39                                   
REMARK 500    VAL F  42     -138.89     42.92                                   
REMARK 500    SER F  51      147.63   -171.85                                   
REMARK 500    PHE F  64      -18.81   -141.80                                   
REMARK 500    GLU G  14      -72.69    -64.02                                   
REMARK 500    ALA G  24     -143.32     51.24                                   
REMARK 500    THR G  29      141.42   -170.29                                   
REMARK 500    ASN G  35       24.57    -75.36                                   
REMARK 500    LEU G  37       41.30   -100.67                                   
REMARK 500    PHE G  64       -7.11   -142.41                                   
REMARK 500    LYS G  69      155.10    -46.46                                   
REMARK 500    MET H  10      -55.58   -151.35                                   
REMARK 500    VAL H  23      123.39    -27.30                                   
REMARK 500    ALA H  24     -178.50    -57.98                                   
REMARK 500    GLU H  26     -159.55    -73.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H 143        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH E 145        DISTANCE = 11.51 ANGSTROMS                       
REMARK 525    HOH E 146        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH F 144        DISTANCE =  6.72 ANGSTROMS                       
DBREF  3PZ8 A    3   104  UNP    P51141   DVL1_MOUSE       3    104             
DBREF  3PZ8 B    3   104  UNP    P51141   DVL1_MOUSE       3    104             
DBREF  3PZ8 C    3   104  UNP    P51141   DVL1_MOUSE       3    104             
DBREF  3PZ8 D    3   104  UNP    P51141   DVL1_MOUSE       3    104             
DBREF  3PZ8 E    3   104  UNP    P51141   DVL1_MOUSE       3    104             
DBREF  3PZ8 F    3   104  UNP    P51141   DVL1_MOUSE       3    104             
DBREF  3PZ8 G    3   104  UNP    P51141   DVL1_MOUSE       3    104             
DBREF  3PZ8 H    3   104  UNP    P51141   DVL1_MOUSE       3    104             
SEQADV 3PZ8 GLY A   -1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 PRO A    0  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 HIS A    1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 MET A    2  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 ASP A    3  UNP  P51141    GLU     3 ENGINEERED MUTATION            
SEQADV 3PZ8 ASP A   17  UNP  P51141    TYR    17 ENGINEERED MUTATION            
SEQADV 3PZ8 GLY B   -1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 PRO B    0  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 HIS B    1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 MET B    2  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 ASP B    3  UNP  P51141    GLU     3 ENGINEERED MUTATION            
SEQADV 3PZ8 ASP B   17  UNP  P51141    TYR    17 ENGINEERED MUTATION            
SEQADV 3PZ8 GLY C   -1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 PRO C    0  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 HIS C    1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 MET C    2  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 ASP C    3  UNP  P51141    GLU     3 ENGINEERED MUTATION            
SEQADV 3PZ8 ASP C   17  UNP  P51141    TYR    17 ENGINEERED MUTATION            
SEQADV 3PZ8 GLY D   -1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 PRO D    0  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 HIS D    1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 MET D    2  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 ASP D    3  UNP  P51141    GLU     3 ENGINEERED MUTATION            
SEQADV 3PZ8 ASP D   17  UNP  P51141    TYR    17 ENGINEERED MUTATION            
SEQADV 3PZ8 GLY E   -1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 PRO E    0  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 HIS E    1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 MET E    2  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 ASP E    3  UNP  P51141    GLU     3 ENGINEERED MUTATION            
SEQADV 3PZ8 ASP E   17  UNP  P51141    TYR    17 EXPRESSION TAG                 
SEQADV 3PZ8 GLY F   -1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 PRO F    0  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 HIS F    1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 MET F    2  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 ASP F    3  UNP  P51141    GLU     3 ENGINEERED MUTATION            
SEQADV 3PZ8 ASP F   17  UNP  P51141    TYR    17 ENGINEERED MUTATION            
SEQADV 3PZ8 GLY G   -1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 PRO G    0  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 HIS G    1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 MET G    2  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 ASP G    3  UNP  P51141    GLU     3 ENGINEERED MUTATION            
SEQADV 3PZ8 ASP G   17  UNP  P51141    TYR    17 ENGINEERED MUTATION            
SEQADV 3PZ8 GLY H   -1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 PRO H    0  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 HIS H    1  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 MET H    2  UNP  P51141              EXPRESSION TAG                 
SEQADV 3PZ8 ASP H    3  UNP  P51141    GLU     3 ENGINEERED MUTATION            
SEQADV 3PZ8 ASP H   17  UNP  P51141    TYR    17 ENGINEERED MUTATION            
SEQRES   1 A  106  GLY PRO HIS MET ASP THR LYS ILE ILE TYR HIS MET ASP          
SEQRES   2 A  106  GLU GLU GLU THR PRO ASP LEU VAL LYS LEU PRO VAL ALA          
SEQRES   3 A  106  PRO GLU ARG VAL THR LEU ALA ASP PHE LYS ASN VAL LEU          
SEQRES   4 A  106  SER ASN ARG PRO VAL HIS ALA TYR LYS PHE PHE PHE LYS          
SEQRES   5 A  106  SER MET ASP GLN ASP PHE GLY VAL VAL LYS GLU GLU ILE          
SEQRES   6 A  106  PHE ASP ASP ASN ALA LYS LEU PRO CYS PHE ASN GLY ARG          
SEQRES   7 A  106  VAL VAL SER TRP LEU VAL LEU ALA GLU GLY ALA HIS SER          
SEQRES   8 A  106  ASP ALA GLY SER GLN GLY THR ASP SER HIS THR ASP LEU          
SEQRES   9 A  106  PRO PRO                                                      
SEQRES   1 B  106  GLY PRO HIS MET ASP THR LYS ILE ILE TYR HIS MET ASP          
SEQRES   2 B  106  GLU GLU GLU THR PRO ASP LEU VAL LYS LEU PRO VAL ALA          
SEQRES   3 B  106  PRO GLU ARG VAL THR LEU ALA ASP PHE LYS ASN VAL LEU          
SEQRES   4 B  106  SER ASN ARG PRO VAL HIS ALA TYR LYS PHE PHE PHE LYS          
SEQRES   5 B  106  SER MET ASP GLN ASP PHE GLY VAL VAL LYS GLU GLU ILE          
SEQRES   6 B  106  PHE ASP ASP ASN ALA LYS LEU PRO CYS PHE ASN GLY ARG          
SEQRES   7 B  106  VAL VAL SER TRP LEU VAL LEU ALA GLU GLY ALA HIS SER          
SEQRES   8 B  106  ASP ALA GLY SER GLN GLY THR ASP SER HIS THR ASP LEU          
SEQRES   9 B  106  PRO PRO                                                      
SEQRES   1 C  106  GLY PRO HIS MET ASP THR LYS ILE ILE TYR HIS MET ASP          
SEQRES   2 C  106  GLU GLU GLU THR PRO ASP LEU VAL LYS LEU PRO VAL ALA          
SEQRES   3 C  106  PRO GLU ARG VAL THR LEU ALA ASP PHE LYS ASN VAL LEU          
SEQRES   4 C  106  SER ASN ARG PRO VAL HIS ALA TYR LYS PHE PHE PHE LYS          
SEQRES   5 C  106  SER MET ASP GLN ASP PHE GLY VAL VAL LYS GLU GLU ILE          
SEQRES   6 C  106  PHE ASP ASP ASN ALA LYS LEU PRO CYS PHE ASN GLY ARG          
SEQRES   7 C  106  VAL VAL SER TRP LEU VAL LEU ALA GLU GLY ALA HIS SER          
SEQRES   8 C  106  ASP ALA GLY SER GLN GLY THR ASP SER HIS THR ASP LEU          
SEQRES   9 C  106  PRO PRO                                                      
SEQRES   1 D  106  GLY PRO HIS MET ASP THR LYS ILE ILE TYR HIS MET ASP          
SEQRES   2 D  106  GLU GLU GLU THR PRO ASP LEU VAL LYS LEU PRO VAL ALA          
SEQRES   3 D  106  PRO GLU ARG VAL THR LEU ALA ASP PHE LYS ASN VAL LEU          
SEQRES   4 D  106  SER ASN ARG PRO VAL HIS ALA TYR LYS PHE PHE PHE LYS          
SEQRES   5 D  106  SER MET ASP GLN ASP PHE GLY VAL VAL LYS GLU GLU ILE          
SEQRES   6 D  106  PHE ASP ASP ASN ALA LYS LEU PRO CYS PHE ASN GLY ARG          
SEQRES   7 D  106  VAL VAL SER TRP LEU VAL LEU ALA GLU GLY ALA HIS SER          
SEQRES   8 D  106  ASP ALA GLY SER GLN GLY THR ASP SER HIS THR ASP LEU          
SEQRES   9 D  106  PRO PRO                                                      
SEQRES   1 E  106  GLY PRO HIS MET ASP THR LYS ILE ILE TYR HIS MET ASP          
SEQRES   2 E  106  GLU GLU GLU THR PRO ASP LEU VAL LYS LEU PRO VAL ALA          
SEQRES   3 E  106  PRO GLU ARG VAL THR LEU ALA ASP PHE LYS ASN VAL LEU          
SEQRES   4 E  106  SER ASN ARG PRO VAL HIS ALA TYR LYS PHE PHE PHE LYS          
SEQRES   5 E  106  SER MET ASP GLN ASP PHE GLY VAL VAL LYS GLU GLU ILE          
SEQRES   6 E  106  PHE ASP ASP ASN ALA LYS LEU PRO CYS PHE ASN GLY ARG          
SEQRES   7 E  106  VAL VAL SER TRP LEU VAL LEU ALA GLU GLY ALA HIS SER          
SEQRES   8 E  106  ASP ALA GLY SER GLN GLY THR ASP SER HIS THR ASP LEU          
SEQRES   9 E  106  PRO PRO                                                      
SEQRES   1 F  106  GLY PRO HIS MET ASP THR LYS ILE ILE TYR HIS MET ASP          
SEQRES   2 F  106  GLU GLU GLU THR PRO ASP LEU VAL LYS LEU PRO VAL ALA          
SEQRES   3 F  106  PRO GLU ARG VAL THR LEU ALA ASP PHE LYS ASN VAL LEU          
SEQRES   4 F  106  SER ASN ARG PRO VAL HIS ALA TYR LYS PHE PHE PHE LYS          
SEQRES   5 F  106  SER MET ASP GLN ASP PHE GLY VAL VAL LYS GLU GLU ILE          
SEQRES   6 F  106  PHE ASP ASP ASN ALA LYS LEU PRO CYS PHE ASN GLY ARG          
SEQRES   7 F  106  VAL VAL SER TRP LEU VAL LEU ALA GLU GLY ALA HIS SER          
SEQRES   8 F  106  ASP ALA GLY SER GLN GLY THR ASP SER HIS THR ASP LEU          
SEQRES   9 F  106  PRO PRO                                                      
SEQRES   1 G  106  GLY PRO HIS MET ASP THR LYS ILE ILE TYR HIS MET ASP          
SEQRES   2 G  106  GLU GLU GLU THR PRO ASP LEU VAL LYS LEU PRO VAL ALA          
SEQRES   3 G  106  PRO GLU ARG VAL THR LEU ALA ASP PHE LYS ASN VAL LEU          
SEQRES   4 G  106  SER ASN ARG PRO VAL HIS ALA TYR LYS PHE PHE PHE LYS          
SEQRES   5 G  106  SER MET ASP GLN ASP PHE GLY VAL VAL LYS GLU GLU ILE          
SEQRES   6 G  106  PHE ASP ASP ASN ALA LYS LEU PRO CYS PHE ASN GLY ARG          
SEQRES   7 G  106  VAL VAL SER TRP LEU VAL LEU ALA GLU GLY ALA HIS SER          
SEQRES   8 G  106  ASP ALA GLY SER GLN GLY THR ASP SER HIS THR ASP LEU          
SEQRES   9 G  106  PRO PRO                                                      
SEQRES   1 H  106  GLY PRO HIS MET ASP THR LYS ILE ILE TYR HIS MET ASP          
SEQRES   2 H  106  GLU GLU GLU THR PRO ASP LEU VAL LYS LEU PRO VAL ALA          
SEQRES   3 H  106  PRO GLU ARG VAL THR LEU ALA ASP PHE LYS ASN VAL LEU          
SEQRES   4 H  106  SER ASN ARG PRO VAL HIS ALA TYR LYS PHE PHE PHE LYS          
SEQRES   5 H  106  SER MET ASP GLN ASP PHE GLY VAL VAL LYS GLU GLU ILE          
SEQRES   6 H  106  PHE ASP ASP ASN ALA LYS LEU PRO CYS PHE ASN GLY ARG          
SEQRES   7 H  106  VAL VAL SER TRP LEU VAL LEU ALA GLU GLY ALA HIS SER          
SEQRES   8 H  106  ASP ALA GLY SER GLN GLY THR ASP SER HIS THR ASP LEU          
SEQRES   9 H  106  PRO PRO                                                      
FORMUL   9  HOH   *41(H2 O)                                                     
HELIX    1   1 THR A   29  VAL A   36  1                                   8    
HELIX    2   2 PRO A   41  TYR A   45  5                                   5    
HELIX    3   3 ALA B   24  VAL B   28  5                                   5    
HELIX    4   4 THR B   29  ASN B   35  1                                   7    
HELIX    5   5 PRO B   41  HIS B   43  5                                   3    
HELIX    6   6 CYS B   72  ARG B   76  5                                   5    
HELIX    7   7 THR C   29  VAL C   36  1                                   8    
HELIX    8   8 PRO C   41  HIS C   43  5                                   3    
HELIX    9   9 THR D   29  LEU D   37  1                                   9    
HELIX   10  10 THR E   29  VAL E   36  1                                   8    
HELIX   11  11 PRO E   41  TYR E   45  5                                   5    
HELIX   12  12 ALA F   24  VAL F   28  5                                   5    
HELIX   13  13 THR F   29  LEU F   37  1                                   9    
HELIX   14  14 THR G   29  ASN G   35  1                                   7    
HELIX   15  15 CYS G   72  ARG G   76  5                                   5    
HELIX   16  16 LYS H   34  SER H   38  5                                   5    
SHEET    1   A20 PHE B  56  ILE B  63  0                                        
SHEET    2   A20 TYR B  45  ASP B  53 -1  N  ASP B  53   O  PHE B  56           
SHEET    3   A20 VAL B  77  LEU B  83 -1  O  VAL B  82   N  LYS B  46           
SHEET    4   A20 THR B   4  HIS B   9  1  N  HIS B   9   O  SER B  79           
SHEET    5   A20 ASP B  17  LEU B  21 -1  O  ASP B  17   N  TYR B   8           
SHEET    6   A20 GLY A  57  GLU A  62  1  N  GLU A  62   O  LEU B  18           
SHEET    7   A20 PHE A  48  ASP A  53 -1  N  ASP A  53   O  GLY A  57           
SHEET    8   A20 VAL A  77  TRP A  80 -1  O  VAL A  78   N  LYS A  50           
SHEET    9   A20 THR A   4  HIS A   9  1  N  ILE A   7   O  SER A  79           
SHEET   10   A20 ASP A  17  LEU A  21 -1  O  LEU A  21   N  THR A   4           
SHEET   11   A20 GLY H  57  GLU H  61  1  O  LYS H  60   N  LEU A  18           
SHEET   12   A20 TYR H  45  ASP H  53 -1  N  ASP H  53   O  GLY H  57           
SHEET   13   A20 ARG H  76  LEU H  83 -1  O  VAL H  82   N  LYS H  46           
SHEET   14   A20 THR H   4  TYR H   8  1  N  LYS H   5   O  VAL H  77           
SHEET   15   A20 ASP H  17  LEU H  21 -1  O  ASP H  17   N  TYR H   8           
SHEET   16   A20 GLY G  57  ILE G  63  1  N  LYS G  60   O  LEU H  18           
SHEET   17   A20 LYS G  46  ASP G  53 -1  N  ASP G  53   O  GLY G  57           
SHEET   18   A20 VAL G  77  VAL G  82 -1  O  VAL G  82   N  LYS G  46           
SHEET   19   A20 THR G   4  MET G  10  1  N  HIS G   9   O  LEU G  81           
SHEET   20   A20 ASP G  17  LEU G  21 -1  O  LEU G  21   N  THR G   4           
SHEET    1   B20 ASP C  17  LEU C  21  0                                        
SHEET    2   B20 THR C   4  HIS C   9 -1  N  ILE C   6   O  VAL C  19           
SHEET    3   B20 VAL C  77  LEU C  83  1  O  SER C  79   N  HIS C   9           
SHEET    4   B20 TYR C  45  ASP C  53 -1  N  LYS C  46   O  VAL C  82           
SHEET    5   B20 GLY C  57  GLU C  62 -1  O  VAL C  59   N  SER C  51           
SHEET    6   B20 ASP D  17  LEU D  21  1  O  LEU D  18   N  GLU C  62           
SHEET    7   B20 THR D   4  MET D  10 -1  N  THR D   4   O  LEU D  21           
SHEET    8   B20 VAL D  77  VAL D  82  1  O  SER D  79   N  HIS D   9           
SHEET    9   B20 LYS D  46  ASP D  53 -1  N  LYS D  46   O  VAL D  82           
SHEET   10   B20 GLY D  57  ILE D  63 -1  O  GLY D  57   N  ASP D  53           
SHEET   11   B20 ASP E  17  LEU E  21  1  O  LEU E  18   N  LYS D  60           
SHEET   12   B20 THR E   4  MET E  10 -1  N  TYR E   8   O  ASP E  17           
SHEET   13   B20 ARG E  76  VAL E  82  1  O  SER E  79   N  ILE E   7           
SHEET   14   B20 LYS E  46  ASP E  53 -1  N  LYS E  46   O  VAL E  82           
SHEET   15   B20 GLY E  57  ILE E  63 -1  O  VAL E  59   N  SER E  51           
SHEET   16   B20 ASP F  17  LEU F  21  1  O  LEU F  18   N  LYS E  60           
SHEET   17   B20 THR F   4  MET F  10 -1  N  ILE F   6   O  VAL F  19           
SHEET   18   B20 VAL F  77  LEU F  83  1  O  VAL F  77   N  ILE F   7           
SHEET   19   B20 TYR F  45  ASP F  53 -1  N  LYS F  46   O  VAL F  82           
SHEET   20   B20 GLY F  57  ILE F  63 -1  O  GLU F  61   N  PHE F  49           
CISPEP   1 GLN B   54    ASP B   55          0        17.37                     
CISPEP   2 ASP D   11    GLU D   12          0        -0.64                     
CISPEP   3 HIS F   43    ALA F   44          0         0.53                     
CISPEP   4 ALA G   24    PRO G   25          0        10.22                     
CISPEP   5 ASP H   66    ASN H   67          0       -12.24                     
CRYST1   92.687  106.780  265.957  90.00  90.00  90.00 I 21 21 21   64          
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      0.010789  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009365  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003760        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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