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Database: PDB
Entry: 5WZZ
LinkDB: 5WZZ
Original site: 5WZZ 
HEADER    LIGASE                                  19-JAN-17   5WZZ              
TITLE     THE SIAH E3 UBIQUITIN LIGASES PROMOTE WNT/ BETA-CATENIN SIGNALING     
TITLE    2 THROUGH MEDIATING WNT-INDUCED AXIN DEGRADATION                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE SIAH1;                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 93-282;                                       
COMPND   5 SYNONYM: SEVEN IN ABSENTIA HOMOLOG 1,SIAH-1,SIAH-1A;                 
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: AXIN-1;                                                    
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 FRAGMENT: UNP RESIDUES 375-394;                                      
COMPND  12 SYNONYM: AXIS INHIBITION PROTEIN 1,HAXIN;                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SIAH1, HUMSIAH;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K-12;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: AXIN1, AXIN;                                                   
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: K-12                                       
KEYWDS    PROTEIN COMPLEX, WNT PATHWAY, LIGASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.JI,B.JIANG,X.JIANG,O.CHARLAT,A.CHEN,C.MICKANIN,A.BAUER,W.XU,X.-     
AUTHOR   2 X.YAN,F.CONG                                                         
REVDAT   3   30-AUG-17 5WZZ    1       REMARK                                   
REVDAT   2   23-AUG-17 5WZZ    1       TITLE  AUTHOR                            
REVDAT   1   16-AUG-17 5WZZ    0                                                
JRNL        AUTH   L.JI,B.JIANG,X.JIANG,O.CHARLAT,A.CHEN,C.MICKANIN,A.BAUER,    
JRNL        AUTH 2 W.XU,X.-X.YAN,F.CONG                                         
JRNL        TITL   THE SIAH E3 UBIQUITIN LIGASES PROMOTE WNT/ BETA-CATENIN      
JRNL        TITL 2 SIGNALING THROUGH MEDIATING WNT-INDUCED AXIN DEGRADATION     
JRNL        REF    GENES DEV.                    V.  31   904 2017              
JRNL        REFN                   ISSN 1549-5477                               
JRNL        PMID   28546513                                                     
JRNL        DOI    10.1101/GAD.300053.117                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 47337                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2275                            
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 38.7348 -  5.2941    0.97     2831   133  0.1988 0.2358        
REMARK   3     2  5.2941 -  4.2037    0.99     2835   151  0.1539 0.1597        
REMARK   3     3  4.2037 -  3.6728    1.00     2868   140  0.1666 0.2054        
REMARK   3     4  3.6728 -  3.3372    0.99     2835   138  0.1679 0.1753        
REMARK   3     5  3.3372 -  3.0981    1.00     2851   131  0.1763 0.2085        
REMARK   3     6  3.0981 -  2.9155    1.00     2832   138  0.1926 0.2239        
REMARK   3     7  2.9155 -  2.7695    0.99     2812   140  0.1867 0.2184        
REMARK   3     8  2.7695 -  2.6490    1.00     2832   166  0.1912 0.2227        
REMARK   3     9  2.6490 -  2.5471    1.00     2815   145  0.1919 0.2027        
REMARK   3    10  2.5471 -  2.4592    1.00     2846   130  0.1991 0.2270        
REMARK   3    11  2.4592 -  2.3823    1.00     2877   120  0.2070 0.2518        
REMARK   3    12  2.3823 -  2.3142    1.00     2764   153  0.2192 0.2348        
REMARK   3    13  2.3142 -  2.2533    1.00     2854   145  0.2334 0.2494        
REMARK   3    14  2.2533 -  2.1983    1.00     2773   146  0.2399 0.2333        
REMARK   3    15  2.1983 -  2.1483    0.99     2825   153  0.2509 0.3287        
REMARK   3    16  2.1483 -  2.1026    0.94     2612   146  0.2549 0.2790        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.280           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.010           6441                                  
REMARK   3   ANGLE     :  1.371           8718                                  
REMARK   3   CHIRALITY :  0.058            959                                  
REMARK   3   PLANARITY :  0.007           1131                                  
REMARK   3   DIHEDRAL  : 13.819           2342                                  
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 5WZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002692.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 R CDTE 300K       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92372                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 4CA1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG3350, 200 MM MGCL2, 100     
REMARK 280  MM TRIS-HCL, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  277K                                                                
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       43.22500            
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, 3, 4                                              
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: 1250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 1240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 3                                                       
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: 1370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 4                                                       
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: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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     TYR E   375                                                      
REMARK 465     ARG E   376                                                      
REMARK 465     PHE E   388                                                      
REMARK 465     ALA E   389                                                      
REMARK 465     GLU E   390                                                      
REMARK 465     GLU E   391                                                      
REMARK 465     LEU E   392                                                      
REMARK 465     ILE E   393                                                      
REMARK 465     HIS E   394                                                      
REMARK 465     TYR F   375                                                      
REMARK 465     ARG F   376                                                      
REMARK 465     VAL F   377                                                      
REMARK 465     PRO F   378                                                      
REMARK 465     PHE F   388                                                      
REMARK 465     ALA F   389                                                      
REMARK 465     GLU F   390                                                      
REMARK 465     GLU F   391                                                      
REMARK 465     LEU F   392                                                      
REMARK 465     ILE F   393                                                      
REMARK 465     HIS F   394                                                      
REMARK 465     TYR G   375                                                      
REMARK 465     ARG G   376                                                      
REMARK 465     VAL G   377                                                      
REMARK 465     PHE G   388                                                      
REMARK 465     ALA G   389                                                      
REMARK 465     GLU G   390                                                      
REMARK 465     GLU G   391                                                      
REMARK 465     LEU G   392                                                      
REMARK 465     ILE G   393                                                      
REMARK 465     HIS G   394                                                      
REMARK 465     TYR H   375                                                      
REMARK 465     ARG H   376                                                      
REMARK 465     PHE H   388                                                      
REMARK 465     ALA H   389                                                      
REMARK 465     GLU H   390                                                      
REMARK 465     GLU H   391                                                      
REMARK 465     LEU H   392                                                      
REMARK 465     ILE H   393                                                      
REMARK 465     HIS H   394                                                      
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     HIS A 111    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 200    CG   OD1  OD2                                       
REMARK 470     LYS B 136    CE   NZ                                             
REMARK 470     PRO B 173    CG   CD                                             
REMARK 470     LYS B 198    CD   CE   NZ                                        
REMARK 470     LYS B 216    CD   CE   NZ                                        
REMARK 470     LYS C 136    CE   NZ                                             
REMARK 470     LYS C 198    CG   CD   CE   NZ                                   
REMARK 470     TYR C 199    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP C 200    CG   OD1  OD2                                       
REMARK 470     ARG D 231    CZ   NH1  NH2                                       
REMARK 470     PRO G 378    CG   CD                                             
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   O    HOH B   434     O    HOH B   455              1.95            
REMARK 500   O    HOH B   431     O    HOH D   402              2.02            
REMARK 500   OE1  GLN A   159     O    HOH A   401              2.04            
REMARK 500   OE1  GLU C   226     O    HOH C   401              2.05            
REMARK 500   O    PRO D   173     O    HOH D   401              2.06            
REMARK 500   O    HOH B   423     O    HOH B   455              2.07            
REMARK 500   NH1  ARG B   124     O    HOH B   401              2.08            
REMARK 500   O    HOH D   451     O    HOH D   452              2.11            
REMARK 500   O    SER C   102     O    HOH C   402              2.12            
REMARK 500   O    HOH A   446     O    HOH A   447              2.15            
REMARK 500   NE   ARG A   241     O    HOH A   402              2.17            
REMARK 500   N    ASN B   171     O    HOH B   402              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU A   219     NH1  ARG C   231    21058     2.13            
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    TYR A 199   N   -  CA  -  C   ANGL. DEV. =  19.6 DEGREES          
REMARK 500    ASP A 200   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES          
REMARK 500    ASP A 200   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    LEU B 172   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    PRO B 173   C   -  N   -  CA  ANGL. DEV. =  32.5 DEGREES          
REMARK 500    PRO B 173   CB  -  CA  -  C   ANGL. DEV. = -25.0 DEGREES          
REMARK 500    PRO B 173   N   -  CA  -  C   ANGL. DEV. = -28.9 DEGREES          
REMARK 500    GLY B 174   N   -  CA  -  C   ANGL. DEV. =  25.1 DEGREES          
REMARK 500    CYS C 135   CB  -  CA  -  C   ANGL. DEV. =  11.3 DEGREES          
REMARK 500    TYR C 199   N   -  CA  -  C   ANGL. DEV. = -18.0 DEGREES          
REMARK 500    ASP C 200   CB  -  CA  -  C   ANGL. DEV. = -21.0 DEGREES          
REMARK 500    ASP C 200   N   -  CA  -  C   ANGL. DEV. =  45.1 DEGREES          
REMARK 500    GLY C 201   C   -  N   -  CA  ANGL. DEV. =  23.1 DEGREES          
REMARK 500    SER D 134   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ASN D 228   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    GLY D 229   N   -  CA  -  C   ANGL. DEV. =  25.5 DEGREES          
REMARK 500    HIS D 230   N   -  CA  -  C   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    CYS D 282   CA  -  CB  -  SG  ANGL. DEV. = -12.8 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 106       -2.01     72.76                                   
REMARK 500    LYS A 198     -164.46   -109.97                                   
REMARK 500    TYR A 199      -38.77    -33.91                                   
REMARK 500    ARG A 233      127.79   -171.95                                   
REMARK 500    CYS A 256     -172.33   -176.51                                   
REMARK 500    ASN A 270     -118.89     64.33                                   
REMARK 500    HIS B 230      103.37    -54.94                                   
REMARK 500    CYS B 256     -171.82   -172.33                                   
REMARK 500    PRO C 173      155.67    -45.67                                   
REMARK 500    TYR C 199     -128.46     51.09                                   
REMARK 500    HIS C 230       54.24     39.05                                   
REMARK 500    CYS C 256     -169.70   -176.73                                   
REMARK 500    LYS D 136       16.21     49.21                                   
REMARK 500    ASP D 200      108.63    -46.37                                   
REMARK 500    HIS D 230      -78.04   -126.63                                   
REMARK 500    ALA D 238     -178.83   -171.44                                   
REMARK 500    CYS D 256     -168.81   -174.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU B  172     PRO B  173                 -116.61                    
REMARK 500 ASP C  200     GLY C  201                  137.03                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LEU B 172        -13.91                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  98   SG                                                     
REMARK 620 2 CYS A 105   SG  112.2                                              
REMARK 620 3 HIS A 117   NE2 106.3 110.1                                        
REMARK 620 4 CYS A 121   SG  112.8 108.6 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 128   SG                                                     
REMARK 620 2 CYS A 135   SG  115.1                                              
REMARK 620 3 HIS A 147   NE2 105.5 111.7                                        
REMARK 620 4 HIS A 152   NE2 103.6 116.4 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  98   SG                                                     
REMARK 620 2 CYS B 105   SG  111.3                                              
REMARK 620 3 HIS B 117   NE2 102.2 105.0                                        
REMARK 620 4 CYS B 121   SG  116.1 107.9 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 128   SG                                                     
REMARK 620 2 CYS B 135   SG  114.9                                              
REMARK 620 3 HIS B 147   NE2 102.5 105.4                                        
REMARK 620 4 HIS B 152   NE2 105.8 121.1 105.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  98   SG                                                     
REMARK 620 2 CYS C 105   SG  106.2                                              
REMARK 620 3 HIS C 117   NE2  99.8 102.3                                        
REMARK 620 4 CYS C 121   SG  118.5 115.0 112.9                                  
REMARK 620 5 HOH C 440   O    65.2 106.8 150.0  60.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 128   SG                                                     
REMARK 620 2 CYS C 135   SG  118.6                                              
REMARK 620 3 HIS C 147   NE2 113.3 102.5                                        
REMARK 620 4 HIS C 152   NE2 106.8 111.2 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  98   SG                                                     
REMARK 620 2 CYS D 105   SG  109.2                                              
REMARK 620 3 HIS D 117   NE2 104.0 112.0                                        
REMARK 620 4 CYS D 121   SG  114.4 102.0 115.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 128   SG                                                     
REMARK 620 2 CYS D 135   SG  114.1                                              
REMARK 620 3 HIS D 147   NE2 105.9 112.5                                        
REMARK 620 4 HIS D 152   NE2 104.2 110.8 109.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 302                  
DBREF  5WZZ A   93   282  UNP    Q8IUQ4   SIAH1_HUMAN     93    282             
DBREF  5WZZ B   93   282  UNP    Q8IUQ4   SIAH1_HUMAN     93    282             
DBREF  5WZZ C   93   282  UNP    Q8IUQ4   SIAH1_HUMAN     93    282             
DBREF  5WZZ D   93   282  UNP    Q8IUQ4   SIAH1_HUMAN     93    282             
DBREF  5WZZ E  375   394  UNP    O15169   AXIN1_HUMAN    375    394             
DBREF  5WZZ F  375   394  UNP    O15169   AXIN1_HUMAN    375    394             
DBREF  5WZZ G  375   394  UNP    O15169   AXIN1_HUMAN    375    394             
DBREF  5WZZ H  375   394  UNP    O15169   AXIN1_HUMAN    375    394             
SEQRES   1 A  190  SER VAL LEU PHE PRO CYS LYS TYR ALA SER SER GLY CYS          
SEQRES   2 A  190  GLU ILE THR LEU PRO HIS THR GLU LYS ALA ASP HIS GLU          
SEQRES   3 A  190  GLU LEU CYS GLU PHE ARG PRO TYR SER CYS PRO CYS PRO          
SEQRES   4 A  190  GLY ALA SER CYS LYS TRP GLN GLY SER LEU ASP ALA VAL          
SEQRES   5 A  190  MET PRO HIS LEU MET HIS GLN HIS LYS SER ILE THR THR          
SEQRES   6 A  190  LEU GLN GLY GLU ASP ILE VAL PHE LEU ALA THR ASP ILE          
SEQRES   7 A  190  ASN LEU PRO GLY ALA VAL ASP TRP VAL MET MET GLN SER          
SEQRES   8 A  190  CYS PHE GLY PHE HIS PHE MET LEU VAL LEU GLU LYS GLN          
SEQRES   9 A  190  GLU LYS TYR ASP GLY HIS GLN GLN PHE PHE ALA ILE VAL          
SEQRES  10 A  190  GLN LEU ILE GLY THR ARG LYS GLN ALA GLU ASN PHE ALA          
SEQRES  11 A  190  TYR ARG LEU GLU LEU ASN GLY HIS ARG ARG ARG LEU THR          
SEQRES  12 A  190  TRP GLU ALA THR PRO ARG SER ILE HIS GLU GLY ILE ALA          
SEQRES  13 A  190  THR ALA ILE MET ASN SER ASP CYS LEU VAL PHE ASP THR          
SEQRES  14 A  190  SER ILE ALA GLN LEU PHE ALA GLU ASN GLY ASN LEU GLY          
SEQRES  15 A  190  ILE ASN VAL THR ILE SER MET CYS                              
SEQRES   1 B  190  SER VAL LEU PHE PRO CYS LYS TYR ALA SER SER GLY CYS          
SEQRES   2 B  190  GLU ILE THR LEU PRO HIS THR GLU LYS ALA ASP HIS GLU          
SEQRES   3 B  190  GLU LEU CYS GLU PHE ARG PRO TYR SER CYS PRO CYS PRO          
SEQRES   4 B  190  GLY ALA SER CYS LYS TRP GLN GLY SER LEU ASP ALA VAL          
SEQRES   5 B  190  MET PRO HIS LEU MET HIS GLN HIS LYS SER ILE THR THR          
SEQRES   6 B  190  LEU GLN GLY GLU ASP ILE VAL PHE LEU ALA THR ASP ILE          
SEQRES   7 B  190  ASN LEU PRO GLY ALA VAL ASP TRP VAL MET MET GLN SER          
SEQRES   8 B  190  CYS PHE GLY PHE HIS PHE MET LEU VAL LEU GLU LYS GLN          
SEQRES   9 B  190  GLU LYS TYR ASP GLY HIS GLN GLN PHE PHE ALA ILE VAL          
SEQRES  10 B  190  GLN LEU ILE GLY THR ARG LYS GLN ALA GLU ASN PHE ALA          
SEQRES  11 B  190  TYR ARG LEU GLU LEU ASN GLY HIS ARG ARG ARG LEU THR          
SEQRES  12 B  190  TRP GLU ALA THR PRO ARG SER ILE HIS GLU GLY ILE ALA          
SEQRES  13 B  190  THR ALA ILE MET ASN SER ASP CYS LEU VAL PHE ASP THR          
SEQRES  14 B  190  SER ILE ALA GLN LEU PHE ALA GLU ASN GLY ASN LEU GLY          
SEQRES  15 B  190  ILE ASN VAL THR ILE SER MET CYS                              
SEQRES   1 C  190  SER VAL LEU PHE PRO CYS LYS TYR ALA SER SER GLY CYS          
SEQRES   2 C  190  GLU ILE THR LEU PRO HIS THR GLU LYS ALA ASP HIS GLU          
SEQRES   3 C  190  GLU LEU CYS GLU PHE ARG PRO TYR SER CYS PRO CYS PRO          
SEQRES   4 C  190  GLY ALA SER CYS LYS TRP GLN GLY SER LEU ASP ALA VAL          
SEQRES   5 C  190  MET PRO HIS LEU MET HIS GLN HIS LYS SER ILE THR THR          
SEQRES   6 C  190  LEU GLN GLY GLU ASP ILE VAL PHE LEU ALA THR ASP ILE          
SEQRES   7 C  190  ASN LEU PRO GLY ALA VAL ASP TRP VAL MET MET GLN SER          
SEQRES   8 C  190  CYS PHE GLY PHE HIS PHE MET LEU VAL LEU GLU LYS GLN          
SEQRES   9 C  190  GLU LYS TYR ASP GLY HIS GLN GLN PHE PHE ALA ILE VAL          
SEQRES  10 C  190  GLN LEU ILE GLY THR ARG LYS GLN ALA GLU ASN PHE ALA          
SEQRES  11 C  190  TYR ARG LEU GLU LEU ASN GLY HIS ARG ARG ARG LEU THR          
SEQRES  12 C  190  TRP GLU ALA THR PRO ARG SER ILE HIS GLU GLY ILE ALA          
SEQRES  13 C  190  THR ALA ILE MET ASN SER ASP CYS LEU VAL PHE ASP THR          
SEQRES  14 C  190  SER ILE ALA GLN LEU PHE ALA GLU ASN GLY ASN LEU GLY          
SEQRES  15 C  190  ILE ASN VAL THR ILE SER MET CYS                              
SEQRES   1 D  190  SER VAL LEU PHE PRO CYS LYS TYR ALA SER SER GLY CYS          
SEQRES   2 D  190  GLU ILE THR LEU PRO HIS THR GLU LYS ALA ASP HIS GLU          
SEQRES   3 D  190  GLU LEU CYS GLU PHE ARG PRO TYR SER CYS PRO CYS PRO          
SEQRES   4 D  190  GLY ALA SER CYS LYS TRP GLN GLY SER LEU ASP ALA VAL          
SEQRES   5 D  190  MET PRO HIS LEU MET HIS GLN HIS LYS SER ILE THR THR          
SEQRES   6 D  190  LEU GLN GLY GLU ASP ILE VAL PHE LEU ALA THR ASP ILE          
SEQRES   7 D  190  ASN LEU PRO GLY ALA VAL ASP TRP VAL MET MET GLN SER          
SEQRES   8 D  190  CYS PHE GLY PHE HIS PHE MET LEU VAL LEU GLU LYS GLN          
SEQRES   9 D  190  GLU LYS TYR ASP GLY HIS GLN GLN PHE PHE ALA ILE VAL          
SEQRES  10 D  190  GLN LEU ILE GLY THR ARG LYS GLN ALA GLU ASN PHE ALA          
SEQRES  11 D  190  TYR ARG LEU GLU LEU ASN GLY HIS ARG ARG ARG LEU THR          
SEQRES  12 D  190  TRP GLU ALA THR PRO ARG SER ILE HIS GLU GLY ILE ALA          
SEQRES  13 D  190  THR ALA ILE MET ASN SER ASP CYS LEU VAL PHE ASP THR          
SEQRES  14 D  190  SER ILE ALA GLN LEU PHE ALA GLU ASN GLY ASN LEU GLY          
SEQRES  15 D  190  ILE ASN VAL THR ILE SER MET CYS                              
SEQRES   1 E   20  TYR ARG VAL PRO LYS GLU VAL ARG VAL GLU PRO GLN LYS          
SEQRES   2 E   20  PHE ALA GLU GLU LEU ILE HIS                                  
SEQRES   1 F   20  TYR ARG VAL PRO LYS GLU VAL ARG VAL GLU PRO GLN LYS          
SEQRES   2 F   20  PHE ALA GLU GLU LEU ILE HIS                                  
SEQRES   1 G   20  TYR ARG VAL PRO LYS GLU VAL ARG VAL GLU PRO GLN LYS          
SEQRES   2 G   20  PHE ALA GLU GLU LEU ILE HIS                                  
SEQRES   1 H   20  TYR ARG VAL PRO LYS GLU VAL ARG VAL GLU PRO GLN LYS          
SEQRES   2 H   20  PHE ALA GLU GLU LEU ILE HIS                                  
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET     ZN  B 301       1                                                       
HET     ZN  B 302       1                                                       
HET     ZN  C 301       1                                                       
HET     ZN  C 302       1                                                       
HET     ZN  D 301       1                                                       
HET     ZN  D 302       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   9   ZN    8(ZN 2+)                                                     
FORMUL  17  HOH   *216(H2 O)                                                    
HELIX    1 AA1 TYR A  100  GLY A  104  5                                   5    
HELIX    2 AA2 PRO A  110  CYS A  121  1                                  12    
HELIX    3 AA3 SER A  140  ASP A  142  5                                   3    
HELIX    4 AA4 ALA A  143  HIS A  152  1                                  10    
HELIX    5 AA5 THR A  214  GLU A  219  1                                   6    
HELIX    6 AA6 ILE A  247  ASN A  253  1                                   7    
HELIX    7 AA7 THR A  261  PHE A  267  1                                   7    
HELIX    8 AA8 LYS B   99  GLY B  104  5                                   6    
HELIX    9 AA9 GLU B  113  CYS B  121  1                                   9    
HELIX   10 AB1 SER B  140  ASP B  142  5                                   3    
HELIX   11 AB2 ALA B  143  HIS B  152  1                                  10    
HELIX   12 AB3 THR B  214  GLU B  219  1                                   6    
HELIX   13 AB4 ILE B  247  ASN B  253  1                                   7    
HELIX   14 AB5 THR B  261  ALA B  268  1                                   8    
HELIX   15 AB6 LYS C   99  GLY C  104  5                                   6    
HELIX   16 AB7 PRO C  110  CYS C  121  1                                  12    
HELIX   17 AB8 SER C  140  ASP C  142  5                                   3    
HELIX   18 AB9 ALA C  143  HIS C  152  1                                  10    
HELIX   19 AC1 THR C  214  GLU C  219  1                                   6    
HELIX   20 AC2 ILE C  247  ASN C  253  1                                   7    
HELIX   21 AC3 THR C  261  ALA C  268  1                                   8    
HELIX   22 AC4 LYS D   99  GLY D  104  5                                   6    
HELIX   23 AC5 HIS D  111  CYS D  121  1                                  11    
HELIX   24 AC6 SER D  140  ASP D  142  5                                   3    
HELIX   25 AC7 ALA D  143  HIS D  152  1                                  10    
HELIX   26 AC8 THR D  214  GLU D  219  1                                   6    
HELIX   27 AC9 ILE D  247  ASN D  253  1                                   7    
HELIX   28 AD1 THR D  261  ALA D  268  1                                   8    
SHEET    1 AA1 2 PHE A  96  PRO A  97  0                                        
SHEET    2 AA1 2 THR A 108  LEU A 109 -1  O  LEU A 109   N  PHE A  96           
SHEET    1 AA2 2 TYR A 126  SER A 127  0                                        
SHEET    2 AA2 2 GLN A 138  GLY A 139 -1  O  GLY A 139   N  TYR A 126           
SHEET    1 AA3 5 THR A 157  GLN A 159  0                                        
SHEET    2 AA3 5 VAL A 176  CYS A 184  1  O  SER A 183   N  LEU A 158           
SHEET    3 AA3 5 PHE A 187  GLU A 197 -1  O  LEU A 191   N  MET A 180           
SHEET    4 AA3 5 GLN A 203  LEU A 211 -1  O  GLN A 204   N  GLN A 196           
SHEET    5 AA3 5 ARG A 241  SER A 242  1  O  ARG A 241   N  LEU A 211           
SHEET    1 AA4 5 THR A 157  GLN A 159  0                                        
SHEET    2 AA4 5 VAL A 176  CYS A 184  1  O  SER A 183   N  LEU A 158           
SHEET    3 AA4 5 PHE A 187  GLU A 197 -1  O  LEU A 191   N  MET A 180           
SHEET    4 AA4 5 GLN A 203  LEU A 211 -1  O  GLN A 204   N  GLN A 196           
SHEET    5 AA4 5 LEU A 257  ASP A 260 -1  O  PHE A 259   N  PHE A 205           
SHEET    1 AA5 4 ARG A 232  ALA A 238  0                                        
SHEET    2 AA5 4 PHE A 221  GLY A 229 -1  N  LEU A 225   O  TRP A 236           
SHEET    3 AA5 4 ASN A 272  MET A 281 -1  O  ASN A 276   N  GLU A 226           
SHEET    4 AA5 4 ALA A 268  GLU A 269 -1  N  GLU A 269   O  ASN A 272           
SHEET    1 AA6 5 ARG A 232  ALA A 238  0                                        
SHEET    2 AA6 5 PHE A 221  GLY A 229 -1  N  LEU A 225   O  TRP A 236           
SHEET    3 AA6 5 ASN A 272  MET A 281 -1  O  ASN A 276   N  GLU A 226           
SHEET    4 AA6 5 ASP A 162  ALA A 167 -1  N  PHE A 165   O  ILE A 275           
SHEET    5 AA6 5 GLU G 380  VAL G 383  1  O  VAL G 383   N  LEU A 166           
SHEET    1 AA7 2 LEU B  95  PRO B  97  0                                        
SHEET    2 AA7 2 THR B 108  PRO B 110 -1  O  LEU B 109   N  PHE B  96           
SHEET    1 AA8 2 TYR B 126  SER B 127  0                                        
SHEET    2 AA8 2 GLN B 138  GLY B 139 -1  O  GLY B 139   N  TYR B 126           
SHEET    1 AA9 5 THR B 157  GLN B 159  0                                        
SHEET    2 AA9 5 ASP B 177  CYS B 184  1  O  SER B 183   N  LEU B 158           
SHEET    3 AA9 5 PHE B 187  GLU B 197 -1  O  LEU B 191   N  MET B 180           
SHEET    4 AA9 5 GLN B 203  LEU B 211 -1  O  GLN B 204   N  GLN B 196           
SHEET    5 AA9 5 ARG B 241  SER B 242  1  O  ARG B 241   N  LEU B 211           
SHEET    1 AB1 5 THR B 157  GLN B 159  0                                        
SHEET    2 AB1 5 ASP B 177  CYS B 184  1  O  SER B 183   N  LEU B 158           
SHEET    3 AB1 5 PHE B 187  GLU B 197 -1  O  LEU B 191   N  MET B 180           
SHEET    4 AB1 5 GLN B 203  LEU B 211 -1  O  GLN B 204   N  GLN B 196           
SHEET    5 AB1 5 LEU B 257  ASP B 260 -1  O  PHE B 259   N  PHE B 205           
SHEET    1 AB210 GLU F 380  VAL F 383  0                                        
SHEET    2 AB210 ASP B 162  ALA B 167  1  N  LEU B 166   O  VAL F 383           
SHEET    3 AB210 LEU B 273  MET B 281 -1  O  ILE B 275   N  PHE B 165           
SHEET    4 AB210 PHE B 221  GLY B 229 -1  N  ALA B 222   O  SER B 280           
SHEET    5 AB210 ARG B 232  ALA B 238 -1  O  LEU B 234   N  LEU B 227           
SHEET    6 AB210 ARG D 233  ALA D 238 -1  O  THR D 235   N  THR B 235           
SHEET    7 AB210 PHE D 221  ASN D 228 -1  N  TYR D 223   O  ALA D 238           
SHEET    8 AB210 LEU D 273  MET D 281 -1  O  SER D 280   N  ALA D 222           
SHEET    9 AB210 ASP D 162  ALA D 167 -1  N  ALA D 167   O  LEU D 273           
SHEET   10 AB210 LYS H 379  VAL H 383  1  O  VAL H 383   N  LEU D 166           
SHEET    1 AB3 2 PHE C  96  PRO C  97  0                                        
SHEET    2 AB3 2 THR C 108  LEU C 109 -1  O  LEU C 109   N  PHE C  96           
SHEET    1 AB4 2 TYR C 126  SER C 127  0                                        
SHEET    2 AB4 2 GLN C 138  GLY C 139 -1  O  GLY C 139   N  TYR C 126           
SHEET    1 AB5 5 THR C 157  GLN C 159  0                                        
SHEET    2 AB5 5 VAL C 176  CYS C 184  1  O  SER C 183   N  LEU C 158           
SHEET    3 AB5 5 PHE C 187  LYS C 198 -1  O  LEU C 191   N  MET C 180           
SHEET    4 AB5 5 HIS C 202  LEU C 211 -1  O  ILE C 208   N  VAL C 192           
SHEET    5 AB5 5 ARG C 241  SER C 242  1  O  ARG C 241   N  LEU C 211           
SHEET    1 AB6 5 THR C 157  GLN C 159  0                                        
SHEET    2 AB6 5 VAL C 176  CYS C 184  1  O  SER C 183   N  LEU C 158           
SHEET    3 AB6 5 PHE C 187  LYS C 198 -1  O  LEU C 191   N  MET C 180           
SHEET    4 AB6 5 HIS C 202  LEU C 211 -1  O  ILE C 208   N  VAL C 192           
SHEET    5 AB6 5 LEU C 257  ASP C 260 -1  O  PHE C 259   N  PHE C 205           
SHEET    1 AB7 5 ARG C 232  ALA C 238  0                                        
SHEET    2 AB7 5 PHE C 221  GLY C 229 -1  N  LEU C 225   O  TRP C 236           
SHEET    3 AB7 5 LEU C 273  MET C 281 -1  O  SER C 280   N  ALA C 222           
SHEET    4 AB7 5 ASP C 162  ALA C 167 -1  N  PHE C 165   O  ILE C 275           
SHEET    5 AB7 5 LYS E 379  VAL E 383  1  O  VAL E 383   N  LEU C 166           
SHEET    1 AB8 2 LEU D  95  PRO D  97  0                                        
SHEET    2 AB8 2 THR D 108  PRO D 110 -1  O  LEU D 109   N  PHE D  96           
SHEET    1 AB9 2 TYR D 126  SER D 127  0                                        
SHEET    2 AB9 2 GLN D 138  GLY D 139 -1  O  GLY D 139   N  TYR D 126           
SHEET    1 AC1 5 THR D 157  GLN D 159  0                                        
SHEET    2 AC1 5 VAL D 176  CYS D 184  1  O  MET D 181   N  LEU D 158           
SHEET    3 AC1 5 PHE D 187  TYR D 199 -1  O  LEU D 191   N  MET D 180           
SHEET    4 AC1 5 HIS D 202  LEU D 211 -1  O  GLN D 204   N  GLN D 196           
SHEET    5 AC1 5 ARG D 241  SER D 242  1  O  ARG D 241   N  LEU D 211           
SHEET    1 AC2 5 THR D 157  GLN D 159  0                                        
SHEET    2 AC2 5 VAL D 176  CYS D 184  1  O  MET D 181   N  LEU D 158           
SHEET    3 AC2 5 PHE D 187  TYR D 199 -1  O  LEU D 191   N  MET D 180           
SHEET    4 AC2 5 HIS D 202  LEU D 211 -1  O  GLN D 204   N  GLN D 196           
SHEET    5 AC2 5 LEU D 257  ASP D 260 -1  O  PHE D 259   N  PHE D 205           
LINK         SG  CYS A  98                ZN    ZN A 301     1555   1555  2.42  
LINK         SG  CYS A 105                ZN    ZN A 301     1555   1555  2.31  
LINK         NE2 HIS A 117                ZN    ZN A 301     1555   1555  2.03  
LINK         SG  CYS A 121                ZN    ZN A 301     1555   1555  2.36  
LINK         SG  CYS A 128                ZN    ZN A 302     1555   1555  2.41  
LINK         SG  CYS A 135                ZN    ZN A 302     1555   1555  2.28  
LINK         NE2 HIS A 147                ZN    ZN A 302     1555   1555  2.09  
LINK         NE2 HIS A 152                ZN    ZN A 302     1555   1555  1.98  
LINK         SG  CYS B  98                ZN    ZN B 301     1555   1555  2.34  
LINK         SG  CYS B 105                ZN    ZN B 301     1555   1555  2.25  
LINK         NE2 HIS B 117                ZN    ZN B 301     1555   1555  2.11  
LINK         SG  CYS B 121                ZN    ZN B 301     1555   1555  2.34  
LINK         SG  CYS B 128                ZN    ZN B 302     1555   1555  2.37  
LINK         SG  CYS B 135                ZN    ZN B 302     1555   1555  2.35  
LINK         NE2 HIS B 147                ZN    ZN B 302     1555   1555  2.13  
LINK         NE2 HIS B 152                ZN    ZN B 302     1555   1555  2.01  
LINK         SG  CYS C  98                ZN    ZN C 301     1555   1555  2.35  
LINK         SG  CYS C 105                ZN    ZN C 301     1555   1555  2.29  
LINK         NE2 HIS C 117                ZN    ZN C 301     1555   1555  2.06  
LINK         SG  CYS C 121                ZN    ZN C 301     1555   1555  2.50  
LINK         SG  CYS C 128                ZN    ZN C 302     1555   1555  2.38  
LINK         SG  CYS C 135                ZN    ZN C 302     1555   1555  2.33  
LINK         NE2 HIS C 147                ZN    ZN C 302     1555   1555  2.10  
LINK         NE2 HIS C 152                ZN    ZN C 302     1555   1555  2.06  
LINK         SG  CYS D  98                ZN    ZN D 301     1555   1555  2.36  
LINK         SG  CYS D 105                ZN    ZN D 301     1555   1555  2.27  
LINK         NE2 HIS D 117                ZN    ZN D 301     1555   1555  2.03  
LINK         SG  CYS D 121                ZN    ZN D 301     1555   1555  2.44  
LINK         SG  CYS D 128                ZN    ZN D 302     1555   1555  2.22  
LINK         SG  CYS D 135                ZN    ZN D 302     1555   1555  2.21  
LINK         NE2 HIS D 147                ZN    ZN D 302     1555   1555  2.02  
LINK         NE2 HIS D 152                ZN    ZN D 302     1555   1555  1.99  
LINK        ZN    ZN C 301                 O   HOH C 440     1555   1555  1.99  
SITE     1 AC1  4 CYS A  98  CYS A 105  HIS A 117  CYS A 121                    
SITE     1 AC2  4 CYS A 128  CYS A 135  HIS A 147  HIS A 152                    
SITE     1 AC3  4 CYS B  98  CYS B 105  HIS B 117  CYS B 121                    
SITE     1 AC4  4 CYS B 128  CYS B 135  HIS B 147  HIS B 152                    
SITE     1 AC5  5 CYS C  98  CYS C 105  HIS C 117  CYS C 121                    
SITE     2 AC5  5 HOH C 440                                                     
SITE     1 AC6  4 CYS C 128  CYS C 135  HIS C 147  HIS C 152                    
SITE     1 AC7  4 CYS D  98  CYS D 105  HIS D 117  CYS D 121                    
SITE     1 AC8  4 CYS D 128  CYS D 135  HIS D 147  HIS D 152                    
CRYST1   41.502   86.450  117.454  90.00  98.43  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      0.024095  0.000000  0.003571        0.00000                         
SCALE2      0.000000  0.011567  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008607        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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